位置:首页 > 蛋白库 > HD_HUMAN
HD_HUMAN
ID   HD_HUMAN                Reviewed;        3142 AA.
AC   P42858; Q9UQB7;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   03-AUG-2022, entry version 218.
DE   RecName: Full=Huntingtin;
DE   AltName: Full=Huntington disease protein;
DE            Short=HD protein;
DE   Contains:
DE     RecName: Full=Huntingtin, myristoylated N-terminal fragment;
GN   Name=HTT; Synonyms=HD, IT15;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN HD.
RC   TISSUE=Retina;
RX   PubMed=8458085; DOI=10.1016/0092-8674(93)90585-e;
RA   Macdonald M., Ambrose C.M., Duyao M.P., Myers R.H., Lin C.S., Srinidhi J.,
RA   Barnes G., Taylor S.A., James M., Groot N., McFarlane H., Jenkins B.,
RA   Anderson M.A., Wexler N.S., Gusella J.F., Bates G.P., Baxendale S.,
RA   Hummerich H., Kirby S., North M., Youngman S., Mott R., Zehetner G.,
RA   Sedlacek Z., Poustka A., Frischauf A.-M., Lehrach H., Buckler A.J.,
RA   Church D., Doucette-Stamm L., O'Donovan M.C., Riba-Ramirez L., Shah M.,
RA   Stanton V.P., Strobel S.A., Draths K.M., Wales J.L., Dervan P.,
RA   Housman D.E., Altherr M., Shiang R., Thompson L., Fielder T., Wasmuth J.J.,
RA   Tagle D., Valdes J., Elmer L., Allard M., Castilla L., Swaroop M.,
RA   Blanchard K., Collins F.S., Snell R., Holloway T., Gillespie K., Datson N.,
RA   Shaw S., Harper P.S.;
RT   "A novel gene containing a trinucleotide repeat that is expanded and
RT   unstable on Huntington's disease chromosomes.";
RL   Cell 72:971-983(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=11013077; DOI=10.1006/geno.2000.6317;
RA   Matsuyama N., Hadano S., Onoe K., Osuga H., Shouguchi-Miyata J., Gondo Y.,
RA   Ikeda J.-E.;
RT   "Identification and characterization of the miniature pig Huntington's
RT   disease gene homolog: evidence for conservation and polymorphism in the CAG
RT   triplet repeat.";
RL   Genomics 69:72-85(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-203.
RX   PubMed=8197474; DOI=10.1007/bf02257483;
RA   Ambrose C.M., Duyao M.P., Barnes G., Bates G.P., Lin C.S., Srinidhi J.,
RA   Baxendale S., Hummerich H., Lehrach H., Altherr M., Wasmuth J., Buckler A.,
RA   Church D., Housman D., Berks M., Micklem G., Durbin R., Dodge A., Read A.,
RA   Gusella J.F., Macdonald M.E.;
RT   "Structure and expression of the Huntington's disease gene: evidence
RT   against simple inactivation due to an expanded CAG repeat.";
RL   Somat. Cell Mol. Genet. 20:27-38(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
RX   PubMed=7759106; DOI=10.1016/0888-7543(95)80014-d;
RA   Lin B., Nasir J., Kalchman M.A., McDonald H., Zeisler J., Goldberg Y.P.,
RA   Hayden M.R.;
RT   "Structural analysis of the 5' region of mouse and human Huntington disease
RT   genes reveals conservation of putative promoter region and di- and
RT   trinucleotide polymorphisms.";
RL   Genomics 25:707-715(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2561-3142, AND VARIANT ILE-2786.
RC   TISSUE=Brain, Caudate nucleus, Frontal cortex, Muscle, and Retina;
RX   PubMed=7903579; DOI=10.1093/hmg/2.10.1541;
RA   Lin B., Rommens J.M., Graham R.K., Kalchman M., Macdonald H., Nasir J.,
RA   Delaney A., Goldberg Y.P., Hayden M.R.;
RT   "Differential 3' polyadenylation of the Huntington disease gene results in
RT   two mRNA species with variable tissue expression.";
RL   Hum. Mol. Genet. 2:1541-1545(1993).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=7647777; DOI=10.1038/ng0595-104;
RA   Trottier Y., Devys D., Imbert G., Saudou F., An I., Lutz Y., Weber C.,
RA   Agid Y., Hirsch E.C., Mandel J.-L.;
RT   "Cellular localization of the Huntington's disease protein and
RT   discrimination of the normal and mutated form.";
RL   Nat. Genet. 10:104-110(1995).
RN   [8]
RP   PROTEOLYTIC CLEAVAGE BY CASPASE-3.
RX   PubMed=8696339; DOI=10.1038/ng0896-442;
RA   Goldberg Y.P., Nicholson D.W., Rasper D.M., Kalchman M.A., Koide H.B.,
RA   Graham R.K., Bromm M., Kazemi-Esfarjani P., Thornberry N.A.,
RA   Vaillancourt J.P., Hayden M.R.;
RT   "Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is
RT   modulated by the polyglutamine tract.";
RL   Nat. Genet. 13:442-449(1996).
RN   [9]
RP   PROTEOLYTIC CLEAVAGE BY CASPASE-3 AT ASP-511, AND MUTAGENESIS OF ASP-511
RP   AND ASP-528.
RX   PubMed=9535906; DOI=10.1074/jbc.273.15.9158;
RA   Wellington C.L., Ellerby L.M., Hackam A.S., Margolis R.L., Trifiro M.A.,
RA   Singaraja R., McCutcheon K., Salvesen G.S., Propp S.S., Bromm M.,
RA   Rowland K.J., Zhang T., Rasper D., Roy S., Thornberry N., Pinsky L.,
RA   Kakizuka A., Ross C.A., Nicholson D.W., Bredesen D.E., Hayden M.R.;
RT   "Caspase cleavage of gene products associated with triplet expansion
RT   disorders generates truncated fragments containing the polyglutamine
RT   tract.";
RL   J. Biol. Chem. 273:9158-9167(1998).
RN   [10]
RP   INTERACTION WITH PRPF40A AND SETD2.
RX   PubMed=9700202; DOI=10.1093/hmg/7.9.1463;
RA   Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F.,
RA   MacDonald M.E.;
RT   "Huntingtin interacts with a family of WW domain proteins.";
RL   Hum. Mol. Genet. 7:1463-1474(1998).
RN   [11]
RP   INTERACTION WITH PQBP1.
RC   TISSUE=Brain;
RX   PubMed=10332029; DOI=10.1093/hmg/8.6.977;
RA   Waragai M., Lammers C.-H., Takeuchi S., Imafuku I., Udagawa Y.,
RA   Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H.;
RT   "PQBP-1, a novel polyglutamine tract binding protein, inhibits
RT   transcription activation by Brn-2 and affects cell survival.";
RL   Hum. Mol. Genet. 8:977-987(1999).
RN   [12]
RP   PROTEOLYTIC CLEAVAGE BY CASPASE-6 AT ASP-584, AND MUTAGENESIS OF ASP-584.
RX   PubMed=10770929; DOI=10.1074/jbc.m001475200;
RA   Wellington C.L., Singaraja R., Ellerby L., Savill J., Roy S., Leavitt B.,
RA   Cattaneo E., Hackam A., Sharp A., Thornberry N., Nicholson D.W.,
RA   Bredesen D.E., Hayden M.R.;
RT   "Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate
RT   formation in neuronal and nonneuronal cells.";
RL   J. Biol. Chem. 275:19831-19838(2000).
RN   [13]
RP   INTERACTION WITH SETD2.
RX   PubMed=10958656; DOI=10.1093/hmg/9.14.2175;
RA   Passani L.A., Bedford M.T., Faber P.W., McGinnis K.M., Sharp A.H.,
RA   Gusella J.F., Vonsattel J.-P., MacDonald M.E.;
RT   "Huntingtin's WW domain partners in Huntington's disease post-mortem brain
RT   fulfill genetic criteria for direct involvement in Huntington's disease
RT   pathogenesis.";
RL   Hum. Mol. Genet. 9:2175-2182(2000).
RN   [14]
RP   INTERACTION WITH SETD2.
RX   PubMed=11461154; DOI=10.1006/mcne.2001.1004;
RA   Rega S., Stiewe T., Chang D.-I., Pollmeier B., Esche H., Bardenheuer W.,
RA   Marquitan G., Puetzer B.M.;
RT   "Identification of the full-length huntingtin-interacting protein
RT   p231HBP/HYPB as a DNA-binding factor.";
RL   Mol. Cell. Neurosci. 18:68-79(2001).
RN   [15]
RP   NUCLEAR EXPORT SIGNAL.
RX   PubMed=12783847; DOI=10.1093/hmg/ddg156;
RA   Xia J., Lee D.H., Taylor J., Vandelft M., Truant R.;
RT   "Huntingtin contains a highly conserved nuclear export signal.";
RL   Hum. Mol. Genet. 12:1393-1403(2003).
RN   [16]
RP   INTERACTION WITH TPR, AND SUBCELLULAR LOCATION.
RX   PubMed=15654337; DOI=10.1038/ng1503;
RA   Cornett J., Cao F., Wang C.E., Ross C.A., Bates G.P., Li S.H., Li X.J.;
RT   "Polyglutamine expansion of huntingtin impairs its nuclear export.";
RL   Nat. Genet. 37:198-204(2005).
RN   [17]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16391387; DOI=10.1385/nmm:7:4:297;
RA   Sayer J.A., Manczak M., Akileswaran L., Reddy P.H., Coghlan V.M.;
RT   "Interaction of the nuclear matrix protein NAKAP with HypA and huntingtin:
RT   implications for nuclear toxicity in Huntington's disease pathogenesis.";
RL   NeuroMolecular Med. 7:297-310(2005).
RN   [18]
RP   SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH
RP   F8A1/F8A2/F8A3 AND RAB5A, AND INTERACTION WITH F8A1/F8A2/F8A3.
RX   PubMed=16476778; DOI=10.1083/jcb.200509091;
RA   Pal A., Severin F., Lommer B., Shevchenko A., Zerial M.;
RT   "Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early
RT   endosome motility and is up-regulated in Huntington's disease.";
RL   J. Cell Biol. 172:605-618(2006).
RN   [19]
RP   INTERACTION WITH SYVN, AND UBIQUITINATION.
RX   PubMed=17141218; DOI=10.1016/j.yexcr.2006.10.031;
RA   Yang H., Zhong X., Ballar P., Luo S., Shen Y., Rubinsztein D.C.,
RA   Monteiro M.J., Fang S.;
RT   "Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity
RT   of polyglutamine-expanded huntingtin.";
RL   Exp. Cell Res. 313:538-550(2007).
RN   [20]
RP   PHOSPHORYLATION AT SER-1179 AND SER-1199.
RX   PubMed=17611284; DOI=10.1523/jneurosci.1831-07.2007;
RA   Anne S.L., Saudou F., Humbert S.;
RT   "Phosphorylation of huntingtin by cyclin-dependent kinase 5 is induced by
RT   DNA damage and regulates wild-type and mutant huntingtin toxicity in
RT   neurons.";
RL   J. Neurosci. 27:7318-7328(2007).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1870, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [23]
RP   INTERACTION WITH PFN1.
RX   PubMed=18573880; DOI=10.1128/mcb.00079-08;
RA   Shao J., Welch W.J., Diprospero N.A., Diamond M.I.;
RT   "Phosphorylation of profilin by ROCK1 regulates polyglutamine
RT   aggregation.";
RL   Mol. Cell. Biol. 28:5196-5208(2008).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-1870 AND SER-1874,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [25]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432 AND SER-1874, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [27]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1870 AND SER-1874, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [28]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [29]
RP   ACETYLATION AT LYS-9; LYS-176; LYS-234; LYS-343 AND LYS-442.
RX   PubMed=21685499; DOI=10.1074/mcp.m111.009829;
RA   Cong X., Held J.M., Degiacomo F., Bonner A., Chen J.M., Schilling B.,
RA   Czerwieniec G.A., Gibson B.W., Ellerby L.M.;
RT   "Mass spectrometric identification of novel lysine acetylation sites in
RT   huntingtin.";
RL   Mol. Cell. Proteomics 0:0-0(2011).
RN   [30]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [31]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640; SER-643; SER-1199 AND
RP   SER-1874, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [32]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [33]
RP   INTERACTION WITH ZDHHC17 AND ZDHHC13, AND MUTAGENESIS OF ILE-495; GLN-498
RP   AND PRO-499.
RX   PubMed=26198635; DOI=10.1074/jbc.m115.657668;
RA   Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
RT   "Identification of a novel sequence motif recognized by the ankyrin repeat
RT   domain of zDHHC17/13 S-acyltransferases.";
RL   J. Biol. Chem. 290:21939-21950(2015).
RN   [34]
RP   INTERACTION WITH ZDHHC17.
RX   PubMed=28882895; DOI=10.1074/jbc.m117.799650;
RA   Lemonidis K., MacLeod R., Baillie G.S., Chamberlain L.H.;
RT   "Peptide array based screening reveals a large number of proteins
RT   interacting with the ankyrin repeat domain of the zDHHC17 S-
RT   acyltransferase.";
RL   J. Biol. Chem. 292:17190-17202(2017).
RN   [35]
RP   INTERACTION WITH ZDHHC17, AND MUTAGENESIS OF 498-GLN-PRO-499.
RX   PubMed=28757145; DOI=10.1016/j.str.2017.06.018;
RA   Verardi R., Kim J.S., Ghirlando R., Banerjee A.;
RT   "Structural basis for substrate recognition by the ankyrin repeat domain of
RT   human DHHC17 palmitoyltransferase.";
RL   Structure 0:0-0(2017).
RN   [36]
RP   FUNCTION, SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-551, AND MUTAGENESIS
RP   OF GLY-551.
RX   PubMed=24459296; DOI=10.1093/hmg/ddu027;
RA   Martin D.D., Heit R.J., Yap M.C., Davidson M.W., Hayden M.R.,
RA   Berthiaume L.G.;
RT   "Identification of a post-translationally myristoylated autophagy-inducing
RT   domain released by caspase cleavage of huntingtin.";
RL   Hum. Mol. Genet. 23:3166-3179(2014).
RN   [37]
RP   PROTEOLYTIC CLEAVAGE AT ASP-550, MYRISTOYLATION AT GLY-551, MUTAGENESIS OF
RP   ASP-550 AND GLY-551, AND CHARACTERIZATION OF VARIANT GLU-551.
RX   PubMed=29802276; DOI=10.1038/s41598-018-25903-w;
RA   Martin D.D.O., Kay C., Collins J.A., Nguyen Y.T., Slama R.A., Hayden M.R.;
RT   "A human huntingtin SNP alters post-translational modification and
RT   pathogenic proteolysis of the protein causing Huntington disease.";
RL   Sci. Rep. 8:8096-8096(2018).
RN   [38] {ECO:0007744|PDB:3IO4, ECO:0007744|PDB:3IO6, ECO:0007744|PDB:3IOR, ECO:0007744|PDB:3IOT, ECO:0007744|PDB:3IOU, ECO:0007744|PDB:3IOV, ECO:0007744|PDB:3IOW}
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-64, AND DOMAIN.
RX   PubMed=19748341; DOI=10.1016/j.str.2009.08.002;
RA   Kim M.W., Chelliah Y., Kim S.W., Otwinowski Z., Bezprozvanny I.;
RT   "Secondary structure of Huntingtin amino-terminal region.";
RL   Structure 17:1205-1212(2009).
RN   [39] {ECO:0007744|PDB:3LRH}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 5-18.
RX   PubMed=21968397; DOI=10.1016/j.jmb.2011.09.034;
RA   Schiefner A., Chatwell L., Korner J., Neumaier I., Colby D.W., Volkmer R.,
RA   Wittrup K.D., Skerra A.;
RT   "A disulfide-free single-domain V(L) intrabody with blocking activity
RT   towards huntingtin reveals a novel mode of epitope recognition.";
RL   J. Mol. Biol. 414:337-355(2011).
RN   [40] {ECO:0007744|PDB:2LD0, ECO:0007744|PDB:2LD2}
RP   STRUCTURE BY NMR OF 1-17.
RX   PubMed=23931318; DOI=10.1016/j.bpj.2013.06.030;
RA   Michalek M., Salnikov E.S., Bechinger B.;
RT   "Structure and topology of the huntingtin 1-17 membrane anchor by a
RT   combined solution and solid-state NMR approach.";
RL   Biophys. J. 105:699-710(2013).
RN   [41] {ECO:0007744|PDB:4FE8, ECO:0007744|PDB:4FEB, ECO:0007744|PDB:4FEC, ECO:0007744|PDB:4FED}
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-64.
RX   PubMed=23370273; DOI=10.4161/pri.23807;
RA   Kim M.;
RT   "Beta conformation of polyglutamine track revealed by a crystal structure
RT   of Huntingtin N-terminal region with insertion of three histidine
RT   residues.";
RL   Prion 7:221-228(2013).
RN   [42] {ECO:0007744|PDB:4RAV}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-17.
RX   PubMed=25861763; DOI=10.1016/j.jmb.2015.03.021;
RA   De Genst E., Chirgadze D.Y., Klein F.A., Butler D.C., Matak-Vinkovic D.,
RA   Trottier Y., Huston J.S., Messer A., Dobson C.M.;
RT   "Structure of a single-chain Fv bound to the 17 N-terminal residues of
RT   huntingtin provides insights into pathogenic amyloid formation and
RT   suppression.";
RL   J. Mol. Biol. 427:2166-2178(2015).
RN   [43] {ECO:0007744|PDB:6EZ8}
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS) IN COMPLEX WITH
RP   F8A1/F8A2/F8A3, AND INTERACTION WITH F8A1/F8A2/F8A3.
RX   PubMed=29466333; DOI=10.1038/nature25502;
RA   Guo Q., Huang B., Cheng J., Seefelder M., Engler T., Pfeifer G., Oeckl P.,
RA   Otto M., Moser F., Maurer M., Pautsch A., Baumeister W.,
RA   Fernandez-Busnadiego R., Kochanek S.;
RT   "The cryo-electron microscopy structure of huntingtin.";
RL   Nature 555:117-120(2018).
RN   [44]
RP   INVOLVEMENT IN LOMARS, AND VARIANT LOMARS LEU-2717.
RX   PubMed=27329733; DOI=10.1038/ejhg.2016.74;
RA   Rodan L.H., Cohen J., Fatemi A., Gillis T., Lucente D., Gusella J.,
RA   Picker J.D.;
RT   "A novel neurodevelopmental disorder associated with compound heterozygous
RT   variants in the huntingtin gene.";
RL   Eur. J. Hum. Genet. 24:1826-1827(2016).
RN   [45]
RP   VARIANT LOMARS LEU-703, AND VARIANT MET-1260.
RX   PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568;
RA   Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I.,
RA   Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P.,
RA   Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C.,
RA   Gyllensten U., Pinto D., Maciel P.;
RT   "Identification of novel genetic causes of Rett syndrome-like phenotypes.";
RL   J. Med. Genet. 53:190-199(2016).
CC   -!- FUNCTION: [Huntingtin]: May play a role in microtubule-mediated
CC       transport or vesicle function.
CC   -!- FUNCTION: [Huntingtin, myristoylated N-terminal fragment]: Promotes the
CC       formation of autophagic vesicles. {ECO:0000269|PubMed:24459296}.
CC   -!- SUBUNIT: Interacts with PFN1 (PubMed:18573880). Interacts through its
CC       N-terminus with PRPF40A (PubMed:9700202). Interacts with PQBP1
CC       (PubMed:10332029). Interacts with SETD2 (PubMed:9700202,
CC       PubMed:10958656, PubMed:11461154). Interacts with SH3GLB1 (By
CC       similarity). Interacts with SYVN (PubMed:17141218). Interacts with TPR;
CC       the interaction is inhibited by forms of Huntingtin with expanded
CC       polyglutamine stretch (PubMed:15654337). Interacts with ZDHHC13 (via
CC       ANK repeats) (PubMed:26198635). Interacts with ZDHHC17 (via ANK
CC       repeats) (PubMed:26198635, PubMed:28882895, PubMed:28757145). Interacts
CC       with F8A1/F8A2/F8A3 (PubMed:29466333, PubMed:16476778). Found in a
CC       complex with F8A1/F8A2/F8A3, HTT and RAB5A; mediates the recruitment of
CC       HTT by RAB5A (PubMed:16476778). {ECO:0000250|UniProtKB:P42859,
CC       ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:10958656,
CC       ECO:0000269|PubMed:11461154, ECO:0000269|PubMed:15654337,
CC       ECO:0000269|PubMed:16476778, ECO:0000269|PubMed:17141218,
CC       ECO:0000269|PubMed:18573880, ECO:0000269|PubMed:26198635,
CC       ECO:0000269|PubMed:28757145, ECO:0000269|PubMed:28882895,
CC       ECO:0000269|PubMed:29466333, ECO:0000269|PubMed:9700202}.
CC   -!- INTERACTION:
CC       P42858; Q9H7C9: AAMDC; NbExp=3; IntAct=EBI-466029, EBI-10308705;
CC       P42858; Q6PCB6: ABHD17C; NbExp=21; IntAct=EBI-466029, EBI-22011868;
CC       P42858; Q9ULW3: ABT1; NbExp=9; IntAct=EBI-466029, EBI-2602396;
CC       P42858; P60709: ACTB; NbExp=3; IntAct=EBI-466029, EBI-353944;
CC       P42858; P63261: ACTG1; NbExp=16; IntAct=EBI-466029, EBI-351292;
CC       P42858; P42025: ACTR1B; NbExp=3; IntAct=EBI-466029, EBI-367493;
CC       P42858; Q15848: ADIPOQ; NbExp=9; IntAct=EBI-466029, EBI-10827839;
CC       P42858; Q9Y4W6: AFG3L2; NbExp=3; IntAct=EBI-466029, EBI-358755;
CC       P42858; Q53H12: AGK; NbExp=3; IntAct=EBI-466029, EBI-2269837;
CC       P42858; Q53H12-2: AGK; NbExp=12; IntAct=EBI-466029, EBI-25944242;
CC       P42858; Q5TGY3: AHDC1; NbExp=12; IntAct=EBI-466029, EBI-948813;
CC       P42858; Q9UIJ7: AK3; NbExp=9; IntAct=EBI-466029, EBI-3916527;
CC       P42858; P14550: AKR1A1; NbExp=6; IntAct=EBI-466029, EBI-372388;
CC       P42858; P31749: AKT1; NbExp=3; IntAct=EBI-466029, EBI-296087;
CC       P42858; Q3SY69: ALDH1L2; NbExp=3; IntAct=EBI-466029, EBI-6916128;
CC       P42858; P04075-2: ALDOA; NbExp=6; IntAct=EBI-466029, EBI-10194102;
CC       P42858; Q9H553: ALG2; NbExp=3; IntAct=EBI-466029, EBI-25806804;
CC       P42858; Q8IWZ3-3: ANKHD1; NbExp=3; IntAct=EBI-466029, EBI-25833200;
CC       P42858; Q6ZTN6-2: ANKRD13D; NbExp=9; IntAct=EBI-466029, EBI-25840993;
CC       P42858; Q5TZF3-1: ANKRD45; NbExp=3; IntAct=EBI-466029, EBI-22011535;
CC       P42858; Q16853: AOC3; NbExp=3; IntAct=EBI-466029, EBI-3921628;
CC       P42858; P63010-2: AP2B1; NbExp=18; IntAct=EBI-466029, EBI-11529439;
CC       P42858; O00203: AP3B1; NbExp=6; IntAct=EBI-466029, EBI-1044383;
CC       P42858; Q9Y2T2: AP3M1; NbExp=3; IntAct=EBI-466029, EBI-2371151;
CC       P42858; P05067: APP; NbExp=6; IntAct=EBI-466029, EBI-77613;
CC       P42858; P48444: ARCN1; NbExp=3; IntAct=EBI-466029, EBI-1044491;
CC       P42858; Q9NP61: ARFGAP3; NbExp=22; IntAct=EBI-466029, EBI-2875816;
CC       P42858; P53365: ARFIP2; NbExp=3; IntAct=EBI-466029, EBI-638194;
CC       P42858; Q8N264: ARHGAP24; NbExp=3; IntAct=EBI-466029, EBI-988764;
CC       P42858; Q52LW3-2: ARHGAP29; NbExp=3; IntAct=EBI-466029, EBI-22012297;
CC       P42858; Q0P5N6: ARL16; NbExp=18; IntAct=EBI-466029, EBI-10186132;
CC       P42858; Q6P1M9: ARMCX5; NbExp=6; IntAct=EBI-466029, EBI-10252512;
CC       P42858; Q86TN1: ARNT2; NbExp=9; IntAct=EBI-466029, EBI-25844820;
CC       P42858; Q9Y575-3: ASB3; NbExp=6; IntAct=EBI-466029, EBI-14199987;
CC       P42858; Q6XD76: ASCL4; NbExp=6; IntAct=EBI-466029, EBI-10254793;
CC       P42858; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-466029, EBI-9089489;
CC       P42858; Q12797-6: ASPH; NbExp=6; IntAct=EBI-466029, EBI-12092171;
CC       P42858; Q12797-7: ASPH; NbExp=3; IntAct=EBI-466029, EBI-25953099;
CC       P42858; Q96DT6: ATG4C; NbExp=15; IntAct=EBI-466029, EBI-3225845;
CC       P42858; Q8WXF7: ATL1; NbExp=18; IntAct=EBI-466029, EBI-2410266;
CC       P42858; P25705: ATP5F1A; NbExp=3; IntAct=EBI-466029, EBI-351437;
CC       P42858; P24539: ATP5PB; NbExp=3; IntAct=EBI-466029, EBI-1044810;
CC       P42858; P48047: ATP5PO; NbExp=6; IntAct=EBI-466029, EBI-355815;
CC       P42858; Q15904: ATP6AP1; NbExp=3; IntAct=EBI-466029, EBI-714667;
CC       P42858; P61421: ATP6V0D1; NbExp=6; IntAct=EBI-466029, EBI-954063;
CC       P42858; P21281: ATP6V1B2; NbExp=3; IntAct=EBI-466029, EBI-4290814;
CC       P42858; Q9UI12: ATP6V1H; NbExp=3; IntAct=EBI-466029, EBI-724719;
CC       P42858; Q9UQB8-3: BAIAP2; NbExp=18; IntAct=EBI-466029, EBI-9091996;
CC       P42858; Q9UQB8-6: BAIAP2; NbExp=18; IntAct=EBI-466029, EBI-9092016;
CC       P42858; Q16520: BATF; NbExp=12; IntAct=EBI-466029, EBI-749503;
CC       P42858; Q9NRL2: BAZ1A; NbExp=4; IntAct=EBI-466029, EBI-927511;
CC       P42858; Q9BUW7: BBLN; NbExp=6; IntAct=EBI-466029, EBI-752084;
CC       P42858; Q8WY36-3: BBX; NbExp=6; IntAct=EBI-466029, EBI-22013474;
CC       P42858; P51572: BCAP31; NbExp=4; IntAct=EBI-466029, EBI-77683;
CC       P42858; Q14457: BECN1; NbExp=14; IntAct=EBI-466029, EBI-949378;
CC       P42858; Q00994: BEX3; NbExp=6; IntAct=EBI-466029, EBI-741753;
CC       P42858; O15392: BIRC5; NbExp=15; IntAct=EBI-466029, EBI-518823;
CC       P42858; Q9GZL8: BPESC1; NbExp=15; IntAct=EBI-466029, EBI-25861458;
CC       P42858; P38398-6: BRCA1; NbExp=3; IntAct=EBI-466029, EBI-25833510;
CC       P42858; Q8WUW1: BRK1; NbExp=6; IntAct=EBI-466029, EBI-2837444;
CC       P42858; Q9H6J7-2: C11orf49; NbExp=6; IntAct=EBI-466029, EBI-13328871;
CC       P42858; Q13901: C1D; NbExp=6; IntAct=EBI-466029, EBI-3844053;
CC       P42858; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-466029, EBI-946029;
CC       P42858; Q9BXJ4: C1QTNF3; NbExp=3; IntAct=EBI-466029, EBI-10697546;
CC       P42858; Q9NUB4: C20orf141; NbExp=6; IntAct=EBI-466029, EBI-9088162;
CC       P42858; Q6P5X5-2: C22orf39; NbExp=3; IntAct=EBI-466029, EBI-10692329;
CC       P42858; Q8N865: C7orf31; NbExp=3; IntAct=EBI-466029, EBI-10174456;
CC       P42858; Q9BRJ6: C7orf50; NbExp=6; IntAct=EBI-466029, EBI-751612;
CC       P42858; Q8IVU9: CABCOCO1; NbExp=3; IntAct=EBI-466029, EBI-21771960;
CC       P42858; P62158: CALM3; NbExp=10; IntAct=EBI-466029, EBI-397435;
CC       P42858; Q14012: CAMK1; NbExp=3; IntAct=EBI-466029, EBI-6380130;
CC       P42858; Q8N5S9-2: CAMKK1; NbExp=9; IntAct=EBI-466029, EBI-25850646;
CC       P42858; Q9HC96: CAPN10; NbExp=12; IntAct=EBI-466029, EBI-3915761;
CC       P42858; P29466-3: CASP1; NbExp=3; IntAct=EBI-466029, EBI-12248206;
CC       P42858; P42574: CASP3; NbExp=9; IntAct=EBI-466029, EBI-524064;
CC       P42858; P55212: CASP6; NbExp=15; IntAct=EBI-466029, EBI-718729;
CC       P42858; P55210: CASP7; NbExp=12; IntAct=EBI-466029, EBI-523958;
CC       P42858; P22681: CBL; NbExp=18; IntAct=EBI-466029, EBI-518228;
CC       P42858; P35520: CBS; NbExp=12; IntAct=EBI-466029, EBI-740135;
CC       P42858; Q5JTY5: CBWD3; NbExp=6; IntAct=EBI-466029, EBI-723434;
CC       P42858; P83916: CBX1; NbExp=15; IntAct=EBI-466029, EBI-78129;
CC       P42858; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-466029, EBI-744556;
CC       P42858; Q96M83-3: CCDC7; NbExp=18; IntAct=EBI-466029, EBI-18211613;
CC       P42858; Q9Y3X0: CCDC9; NbExp=3; IntAct=EBI-466029, EBI-2557532;
CC       P42858; Q13939: CCIN; NbExp=3; IntAct=EBI-466029, EBI-25879469;
CC       P42858; Q9NPC3: CCNB1IP1; NbExp=6; IntAct=EBI-466029, EBI-745269;
CC       P42858; P24863: CCNC; NbExp=9; IntAct=EBI-466029, EBI-395261;
CC       P42858; O96020: CCNE2; NbExp=6; IntAct=EBI-466029, EBI-375033;
CC       P42858; P51959: CCNG1; NbExp=3; IntAct=EBI-466029, EBI-3905829;
CC       P42858; P78371: CCT2; NbExp=6; IntAct=EBI-466029, EBI-357407;
CC       P42858; P48643: CCT5; NbExp=3; IntAct=EBI-466029, EBI-355710;
CC       P42858; P40227: CCT6A; NbExp=10; IntAct=EBI-466029, EBI-356687;
CC       P42858; P50990: CCT8; NbExp=4; IntAct=EBI-466029, EBI-356507;
CC       P42858; P13987: CD59; NbExp=10; IntAct=EBI-466029, EBI-297972;
CC       P42858; Q9H3Q1: CDC42EP4; NbExp=3; IntAct=EBI-466029, EBI-744665;
CC       P42858; Q99459: CDC5L; NbExp=3; IntAct=EBI-466029, EBI-374880;
CC       P42858; O00311: CDC7; NbExp=3; IntAct=EBI-466029, EBI-374980;
CC       P42858; Q9BWT1: CDCA7; NbExp=3; IntAct=EBI-466029, EBI-7054803;
CC       P42858; P55290: CDH13; NbExp=6; IntAct=EBI-466029, EBI-7205595;
CC       P42858; O95674: CDS2; NbExp=9; IntAct=EBI-466029, EBI-3913685;
CC       P42858; Q8N2Z9: CENPS; NbExp=3; IntAct=EBI-466029, EBI-5529649;
CC       P42858; Q7Z7K6: CENPV; NbExp=15; IntAct=EBI-466029, EBI-1210604;
CC       P42858; Q9P2H0: CEP126; NbExp=2; IntAct=EBI-466029, EBI-473176;
CC       P42858; Q53EZ4: CEP55; NbExp=9; IntAct=EBI-466029, EBI-747776;
CC       P42858; Q96MT8-3: CEP63; NbExp=12; IntAct=EBI-466029, EBI-11522539;
CC       P42858; Q8NHQ1-3: CEP70; NbExp=6; IntAct=EBI-466029, EBI-11526150;
CC       P42858; P41208: CETN2; NbExp=13; IntAct=EBI-466029, EBI-1789926;
CC       P42858; Q9Y6H1: CHCHD2; NbExp=10; IntAct=EBI-466029, EBI-2321769;
CC       P42858; Q9NX63: CHCHD3; NbExp=6; IntAct=EBI-466029, EBI-743375;
CC       P42858; Q12873: CHD3; NbExp=3; IntAct=EBI-466029, EBI-523590;
CC       P42858; Q9HD42: CHMP1A; NbExp=12; IntAct=EBI-466029, EBI-1057156;
CC       P42858; O43633: CHMP2A; NbExp=3; IntAct=EBI-466029, EBI-2692789;
CC       P42858; Q9H444: CHMP4B; NbExp=7; IntAct=EBI-466029, EBI-749627;
CC       P42858; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-466029, EBI-7062247;
CC       P42858; P06732: CKM; NbExp=3; IntAct=EBI-466029, EBI-4287089;
CC       P42858; Q9Y240: CLEC11A; NbExp=12; IntAct=EBI-466029, EBI-3957044;
CC       P42858; Q92478: CLEC2B; NbExp=9; IntAct=EBI-466029, EBI-13350535;
CC       P42858; Q16740: CLPP; NbExp=6; IntAct=EBI-466029, EBI-1056029;
CC       P42858; Q8NCR9: CLRN3; NbExp=9; IntAct=EBI-466029, EBI-9091272;
CC       P42858; Q9H9A5: CNOT10; NbExp=4; IntAct=EBI-466029, EBI-1054261;
CC       P42858; Q9H9A5-3: CNOT10; NbExp=3; IntAct=EBI-466029, EBI-25957177;
CC       P42858; Q9UIV1: CNOT7; NbExp=13; IntAct=EBI-466029, EBI-2105113;
CC       P42858; P09543: CNP; NbExp=10; IntAct=EBI-466029, EBI-1059219;
CC       P42858; Q96MW5: COG8; NbExp=12; IntAct=EBI-466029, EBI-720875;
CC       P42858; P53618: COPB1; NbExp=6; IntAct=EBI-466029, EBI-359063;
CC       P42858; Q9UNS2: COPS3; NbExp=22; IntAct=EBI-466029, EBI-350590;
CC       P42858; Q86WV2: COX4I1; NbExp=3; IntAct=EBI-466029, EBI-10260134;
CC       P42858; P10606: COX5B; NbExp=7; IntAct=EBI-466029, EBI-1053725;
CC       P42858; P12074: COX6A1; NbExp=4; IntAct=EBI-466029, EBI-2115950;
CC       P42858; P09669: COX6C; NbExp=4; IntAct=EBI-466029, EBI-715040;
CC       P42858; Q9UKF6: CPSF3; NbExp=3; IntAct=EBI-466029, EBI-1044699;
CC       P42858; A2RRE8: CPT1B; NbExp=6; IntAct=EBI-466029, EBI-25865477;
CC       P42858; Q9BSW2: CRACR2A; NbExp=9; IntAct=EBI-466029, EBI-739773;
CC       P42858; P16220: CREB1; NbExp=3; IntAct=EBI-466029, EBI-711855;
CC       P42858; Q92793: CREBBP; NbExp=2; IntAct=EBI-466029, EBI-81215;
CC       P42858; Q6UXH1-2: CRELD2; NbExp=6; IntAct=EBI-466029, EBI-21670927;
CC       P42858; P46108: CRK; NbExp=3; IntAct=EBI-466029, EBI-886;
CC       P42858; Q14194: CRMP1; NbExp=14; IntAct=EBI-466029, EBI-473101;
CC       P42858; P02489: CRYAA; NbExp=3; IntAct=EBI-466029, EBI-6875961;
CC       P42858; P53672: CRYBA2; NbExp=3; IntAct=EBI-466029, EBI-750444;
CC       P42858; P04141: CSF2; NbExp=15; IntAct=EBI-466029, EBI-1809826;
CC       P42858; P48730-2: CSNK1D; NbExp=15; IntAct=EBI-466029, EBI-9087876;
CC       P42858; P50461: CSRP3; NbExp=3; IntAct=EBI-466029, EBI-5658719;
CC       P42858; P56545-3: CTBP2; NbExp=3; IntAct=EBI-466029, EBI-10171902;
CC       P42858; P35222: CTNNB1; NbExp=14; IntAct=EBI-466029, EBI-491549;
CC       P42858; Q13618: CUL3; NbExp=3; IntAct=EBI-466029, EBI-456129;
CC       P42858; Q93034: CUL5; NbExp=10; IntAct=EBI-466029, EBI-1057139;
CC       P42858; Q8TB03: CXorf38; NbExp=15; IntAct=EBI-466029, EBI-12024320;
CC       P42858; P08574: CYC1; NbExp=7; IntAct=EBI-466029, EBI-1224514;
CC       P42858; P20815: CYP3A5; NbExp=3; IntAct=EBI-466029, EBI-3908011;
CC       P42858; Q5D0E6-2: DALRD3; NbExp=9; IntAct=EBI-466029, EBI-9090939;
CC       P42858; Q9UN19: DAPP1; NbExp=9; IntAct=EBI-466029, EBI-3918199;
CC       P42858; Q9UER7: DAXX; NbExp=15; IntAct=EBI-466029, EBI-77321;
CC       P42858; Q15038: DAZAP2; NbExp=3; IntAct=EBI-466029, EBI-724310;
CC       P42858; Q9UJU6: DBNL; NbExp=3; IntAct=EBI-466029, EBI-751783;
CC       P42858; P61962: DCAF7; NbExp=10; IntAct=EBI-466029, EBI-359808;
CC       P42858; Q9H816: DCLRE1B; NbExp=9; IntAct=EBI-466029, EBI-3508943;
CC       P42858; Q13561: DCTN2; NbExp=12; IntAct=EBI-466029, EBI-715074;
CC       P42858; Q9UJW0: DCTN4; NbExp=3; IntAct=EBI-466029, EBI-2134033;
CC       P42858; Q9UHI6: DDX20; NbExp=6; IntAct=EBI-466029, EBI-347658;
CC       P42858; Q9NR30: DDX21; NbExp=3; IntAct=EBI-466029, EBI-357942;
CC       P42858; O00148: DDX39A; NbExp=3; IntAct=EBI-466029, EBI-348253;
CC       P42858; Q9UJV9: DDX41; NbExp=6; IntAct=EBI-466029, EBI-1046350;
CC       P42858; Q14154: DELE1; NbExp=18; IntAct=EBI-466029, EBI-2805660;
CC       P42858; P78524: DENND2B; NbExp=3; IntAct=EBI-466029, EBI-962633;
CC       P42858; P17661: DES; NbExp=9; IntAct=EBI-466029, EBI-1055572;
CC       P42858; Q05D60: DEUP1; NbExp=15; IntAct=EBI-466029, EBI-748597;
CC       P42858; Q5T7M9-2: DIPK1A; NbExp=3; IntAct=EBI-466029, EBI-25960650;
CC       P42858; P09622: DLD; NbExp=3; IntAct=EBI-466029, EBI-353366;
CC       P42858; P36957: DLST; NbExp=3; IntAct=EBI-466029, EBI-351007;
CC       P42858; O60479: DLX3; NbExp=3; IntAct=EBI-466029, EBI-3908248;
CC       P42858; P31689: DNAJA1; NbExp=17; IntAct=EBI-466029, EBI-347834;
CC       P42858; Q96EY1: DNAJA3; NbExp=5; IntAct=EBI-466029, EBI-356767;
CC       P42858; Q9UDY4: DNAJB4; NbExp=3; IntAct=EBI-466029, EBI-356960;
CC       P42858; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-466029, EBI-12593112;
CC       P42858; Q9NVH1: DNAJC11; NbExp=3; IntAct=EBI-466029, EBI-1055336;
CC       P42858; Q5F1R6: DNAJC21; NbExp=6; IntAct=EBI-466029, EBI-2654581;
CC       P42858; Q9NNZ3: DNAJC4; NbExp=12; IntAct=EBI-466029, EBI-4397791;
CC       P42858; O14645: DNALI1; NbExp=15; IntAct=EBI-466029, EBI-395638;
CC       P42858; Q05193: DNM1; NbExp=3; IntAct=EBI-466029, EBI-713135;
CC       P42858; P50570-2: DNM2; NbExp=6; IntAct=EBI-466029, EBI-10968534;
CC       P42858; Q9H147: DNTTIP1; NbExp=15; IntAct=EBI-466029, EBI-2795449;
CC       P42858; Q9H3H5: DPAGT1; NbExp=3; IntAct=EBI-466029, EBI-3922860;
CC       P42858; Q16555: DPYSL2; NbExp=3; IntAct=EBI-466029, EBI-1104711;
CC       P42858; Q9BPU6: DPYSL5; NbExp=9; IntAct=EBI-466029, EBI-724653;
CC       P42858; Q14204: DYNC1H1; NbExp=8; IntAct=EBI-466029, EBI-356015;
CC       P42858; P63167: DYNLL1; NbExp=10; IntAct=EBI-466029, EBI-349105;
CC       P42858; A0AVK6: E2F8; NbExp=12; IntAct=EBI-466029, EBI-7779316;
CC       P42858; Q13011: ECH1; NbExp=2; IntAct=EBI-466029, EBI-711968;
CC       P42858; O60869: EDF1; NbExp=6; IntAct=EBI-466029, EBI-781301;
CC       P42858; Q3B7T1: EDRF1; NbExp=18; IntAct=EBI-466029, EBI-2870947;
CC       P42858; Q05639: EEF1A2; NbExp=3; IntAct=EBI-466029, EBI-354943;
CC       P42858; P24534: EEF1B2; NbExp=7; IntAct=EBI-466029, EBI-354334;
CC       P42858; P29692: EEF1D; NbExp=6; IntAct=EBI-466029, EBI-358607;
CC       P42858; P13639: EEF2; NbExp=3; IntAct=EBI-466029, EBI-352560;
CC       P42858; Q12805: EFEMP1; NbExp=3; IntAct=EBI-466029, EBI-536772;
CC       P42858; O14602: EIF1AY; NbExp=6; IntAct=EBI-466029, EBI-286439;
CC       P42858; P20042: EIF2S2; NbExp=12; IntAct=EBI-466029, EBI-711977;
CC       P42858; P41091: EIF2S3; NbExp=3; IntAct=EBI-466029, EBI-1054228;
CC       P42858; O75821: EIF3G; NbExp=4; IntAct=EBI-466029, EBI-366632;
CC       P42858; Q13347: EIF3I; NbExp=13; IntAct=EBI-466029, EBI-354047;
CC       P42858; Q14240-2: EIF4A2; NbExp=3; IntAct=EBI-466029, EBI-10232522;
CC       P42858; O60573: EIF4E2; NbExp=4; IntAct=EBI-466029, EBI-398610;
CC       P42858; P55010: EIF5; NbExp=3; IntAct=EBI-466029, EBI-286450;
CC       P42858; O95163: ELP1; NbExp=4; IntAct=EBI-466029, EBI-347559;
CC       P42858; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-466029, EBI-11748557;
CC       P42858; Q8TC29: ENKUR; NbExp=6; IntAct=EBI-466029, EBI-9246952;
CC       P42858; P06733: ENO1; NbExp=13; IntAct=EBI-466029, EBI-353877;
CC       P42858; Q9Y5L3: ENTPD2; NbExp=3; IntAct=EBI-466029, EBI-3913907;
CC       P42858; O75356: ENTPD5; NbExp=3; IntAct=EBI-466029, EBI-7416931;
CC       P42858; A0A0C4DH22: EPB41L1; NbExp=6; IntAct=EBI-466029, EBI-25865535;
CC       P42858; Q8TE68-3: EPS8L1; NbExp=3; IntAct=EBI-466029, EBI-21574901;
CC       P42858; Q2NKX8: ERCC6L; NbExp=20; IntAct=EBI-466029, EBI-1042535;
CC       P42858; A1L162: ERICH2; NbExp=3; IntAct=EBI-466029, EBI-2682520;
CC       P42858; Q96DN0: ERP27; NbExp=3; IntAct=EBI-466029, EBI-953772;
CC       P42858; Q6NXG1-3: ESRP1; NbExp=6; IntAct=EBI-466029, EBI-21567429;
CC       P42858; Q9UI08-2: EVL; NbExp=20; IntAct=EBI-466029, EBI-6448852;
CC       P42858; Q01844-4: EWSR1; NbExp=3; IntAct=EBI-466029, EBI-25896785;
CC       P42858; O00471: EXOC5; NbExp=3; IntAct=EBI-466029, EBI-949824;
CC       P42858; Q99504: EYA3; NbExp=6; IntAct=EBI-466029, EBI-9089567;
CC       P42858; P15311: EZR; NbExp=4; IntAct=EBI-466029, EBI-1056902;
CC       P42858; P23610: F8A3; NbExp=3; IntAct=EBI-466029, EBI-5663973;
CC       P42858; Q6SJ93: FAM111B; NbExp=12; IntAct=EBI-466029, EBI-6309082;
CC       P42858; Q96GL9: FAM163A; NbExp=12; IntAct=EBI-466029, EBI-11793142;
CC       P42858; Q96KS9: FAM167A; NbExp=6; IntAct=EBI-466029, EBI-10290462;
CC       P42858; Q5HYJ3-3: FAM76B; NbExp=6; IntAct=EBI-466029, EBI-11956087;
CC       P42858; Q5JUQ0: FAM78A; NbExp=3; IntAct=EBI-466029, EBI-21900888;
CC       P42858; Q8IZU1: FAM9A; NbExp=18; IntAct=EBI-466029, EBI-8468186;
CC       P42858; Q9NPI8: FANCF; NbExp=3; IntAct=EBI-466029, EBI-81589;
CC       P42858; Q8TC84: FANK1; NbExp=3; IntAct=EBI-466029, EBI-21975404;
CC       P42858; Q9NSD9: FARSB; NbExp=3; IntAct=EBI-466029, EBI-353803;
CC       P42858; P49327: FASN; NbExp=13; IntAct=EBI-466029, EBI-356658;
CC       P42858; Q53R41: FASTKD1; NbExp=9; IntAct=EBI-466029, EBI-3957005;
CC       P42858; Q8NFZ0: FBH1; NbExp=6; IntAct=EBI-466029, EBI-724767;
CC       P42858; P09467: FBP1; NbExp=3; IntAct=EBI-466029, EBI-712740;
CC       P42858; Q99689: FEZ1; NbExp=6; IntAct=EBI-466029, EBI-396435;
CC       P42858; Q9UHY8: FEZ2; NbExp=18; IntAct=EBI-466029, EBI-396453;
CC       P42858; Q13643: FHL3; NbExp=9; IntAct=EBI-466029, EBI-741101;
CC       P42858; Q9BVA6: FICD; NbExp=3; IntAct=EBI-466029, EBI-3907198;
CC       P42858; P26885: FKBP2; NbExp=6; IntAct=EBI-466029, EBI-719873;
CC       P42858; O75955: FLOT1; NbExp=4; IntAct=EBI-466029, EBI-603643;
CC       P42858; Q8N3X1: FNBP4; NbExp=6; IntAct=EBI-466029, EBI-310600;
CC       P42858; Q3SYB3: FOXD4L6; NbExp=6; IntAct=EBI-466029, EBI-6425864;
CC       P42858; Q6PIV2: FOXR1; NbExp=12; IntAct=EBI-466029, EBI-10253815;
CC       P42858; O95073-2: FSBP; NbExp=3; IntAct=EBI-466029, EBI-10696047;
CC       P42858; P02792: FTL; NbExp=20; IntAct=EBI-466029, EBI-713279;
CC       P42858; P06241-3: FYN; NbExp=12; IntAct=EBI-466029, EBI-10691738;
CC       P42858; Q9ULV1: FZD4; NbExp=9; IntAct=EBI-466029, EBI-2466380;
CC       P42858; Q7L622: G2E3; NbExp=6; IntAct=EBI-466029, EBI-751757;
CC       P42858; Q13283: G3BP1; NbExp=16; IntAct=EBI-466029, EBI-1047359;
CC       P42858; Q9UQC2: GAB2; NbExp=3; IntAct=EBI-466029, EBI-975200;
CC       P42858; Q8N4A0: GALNT4; NbExp=12; IntAct=EBI-466029, EBI-21555925;
CC       P42858; P04406: GAPDH; NbExp=7; IntAct=EBI-466029, EBI-354056;
CC       P42858; P28676: GCA; NbExp=3; IntAct=EBI-466029, EBI-947242;
CC       P42858; P14136: GFAP; NbExp=10; IntAct=EBI-466029, EBI-744302;
CC       P42858; Q9NXC2: GFOD1; NbExp=9; IntAct=EBI-466029, EBI-8799578;
CC       P42858; Q9UG22: GIMAP2; NbExp=6; IntAct=EBI-466029, EBI-15891037;
CC       P42858; Q9Y2X7: GIT1; NbExp=10; IntAct=EBI-466029, EBI-466061;
CC       P42858; P48060: GLIPR1; NbExp=3; IntAct=EBI-466029, EBI-2833130;
CC       P42858; P09471: GNAO1; NbExp=7; IntAct=EBI-466029, EBI-715087;
CC       P42858; P62873: GNB1; NbExp=10; IntAct=EBI-466029, EBI-357130;
CC       P42858; P62879: GNB2; NbExp=10; IntAct=EBI-466029, EBI-356942;
CC       P42858; Q08379: GOLGA2; NbExp=3; IntAct=EBI-466029, EBI-618309;
CC       P42858; Q9H4A5: GOLPH3L; NbExp=20; IntAct=EBI-466029, EBI-4403434;
CC       P42858; Q8IYG2: GPC3; NbExp=3; IntAct=EBI-466029, EBI-25896879;
CC       P42858; P51674: GPM6A; NbExp=4; IntAct=EBI-466029, EBI-7187133;
CC       P42858; Q86YB0: GPM6A; NbExp=3; IntAct=EBI-466029, EBI-25966592;
CC       P42858; Q7Z602: GPR141; NbExp=3; IntAct=EBI-466029, EBI-21649723;
CC       P42858; Q96D09: GPRASP2; NbExp=5; IntAct=EBI-466029, EBI-473189;
CC       P42858; Q96SL4: GPX7; NbExp=3; IntAct=EBI-466029, EBI-749411;
CC       P42858; Q13588: GRAP; NbExp=12; IntAct=EBI-466029, EBI-2847510;
CC       P42858; Q8IY40: GRIK2; NbExp=9; IntAct=EBI-466029, EBI-25832107;
CC       P42858; P49840: GSK3A; NbExp=6; IntAct=EBI-466029, EBI-1044067;
CC       P42858; Q9Y5Q9: GTF3C3; NbExp=12; IntAct=EBI-466029, EBI-1054873;
CC       P42858; Q9BZE4: GTPBP4; NbExp=3; IntAct=EBI-466029, EBI-1056249;
CC       P42858; O75409: H2AP; NbExp=16; IntAct=EBI-466029, EBI-6447217;
CC       P42858; Q93079: H2BC9; NbExp=18; IntAct=EBI-466029, EBI-352469;
CC       P42858; Q6NXT2: H3-5; NbExp=15; IntAct=EBI-466029, EBI-2868501;
CC       P42858; P68431: H3C12; NbExp=20; IntAct=EBI-466029, EBI-79722;
CC       P42858; Q71DI3: H3C15; NbExp=18; IntAct=EBI-466029, EBI-750650;
CC       P42858; P62805: H4C9; NbExp=3; IntAct=EBI-466029, EBI-302023;
CC       P42858; P40939: HADHA; NbExp=3; IntAct=EBI-466029, EBI-356720;
CC       P42858; P54257-2: HAP1; NbExp=8; IntAct=EBI-466029, EBI-9392340;
CC       P42858; Q99871: HAUS7; NbExp=18; IntAct=EBI-466029, EBI-395719;
CC       P42858; O00165: HAX1; NbExp=14; IntAct=EBI-466029, EBI-357001;
CC       P42858; Q8N779: hCG_1998195; NbExp=15; IntAct=EBI-466029, EBI-10267476;
CC       P42858; Q969S8: HDAC10; NbExp=21; IntAct=EBI-466029, EBI-301762;
CC       P42858; Q9UBN7: HDAC6; NbExp=9; IntAct=EBI-466029, EBI-301697;
CC       P42858; Q9HCC6: HES4; NbExp=12; IntAct=EBI-466029, EBI-2680288;
CC       P42858; Q9UBP5: HEY2; NbExp=2; IntAct=EBI-466029, EBI-750630;
CC       P42858; O00291: HIP1; NbExp=7; IntAct=EBI-466029, EBI-473886;
CC       P42858; Q9BW71: HIRIP3; NbExp=6; IntAct=EBI-466029, EBI-723624;
CC       P42858; P52790: HK3; NbExp=3; IntAct=EBI-466029, EBI-2965780;
CC       P42858; P08397: HMBS; NbExp=3; IntAct=EBI-466029, EBI-9090148;
CC       P42858; Q9NP66: HMG20A; NbExp=2; IntAct=EBI-466029, EBI-740641;
CC       P42858; Q9P0W2: HMG20B; NbExp=3; IntAct=EBI-466029, EBI-713401;
CC       P42858; P09429: HMGB1; NbExp=13; IntAct=EBI-466029, EBI-389432;
CC       P42858; P07910: HNRNPC; NbExp=7; IntAct=EBI-466029, EBI-357966;
CC       P42858; P07910-2: HNRNPC; NbExp=9; IntAct=EBI-466029, EBI-5280084;
CC       P42858; P61978: HNRNPK; NbExp=12; IntAct=EBI-466029, EBI-304185;
CC       P42858; P20719: HOXA5; NbExp=9; IntAct=EBI-466029, EBI-8470697;
CC       P42858; O43248: HOXC11; NbExp=7; IntAct=EBI-466029, EBI-2652631;
CC       P42858; P09017: HOXC4; NbExp=16; IntAct=EBI-466029, EBI-3923226;
CC       P42858; P00492: HPRT1; NbExp=15; IntAct=EBI-466029, EBI-748210;
CC       P42858; P0DMV8: HSPA1A; NbExp=9; IntAct=EBI-466029, EBI-11052499;
CC       P42858; P54652: HSPA2; NbExp=3; IntAct=EBI-466029, EBI-356991;
CC       P42858; P11142: HSPA8; NbExp=14; IntAct=EBI-466029, EBI-351896;
CC       P42858; P42858: HTT; NbExp=11; IntAct=EBI-466029, EBI-466029;
CC       P42858; Q12891: HYAL2; NbExp=9; IntAct=EBI-466029, EBI-2806068;
CC       P42858; Q9NX55: HYPK; NbExp=4; IntAct=EBI-466029, EBI-1048743;
CC       P42858; Q02363: ID2; NbExp=6; IntAct=EBI-466029, EBI-713450;
CC       P42858; Q8IY31-2: IFT20; NbExp=6; IntAct=EBI-466029, EBI-11742277;
CC       P42858; Q8IY31-3: IFT20; NbExp=18; IntAct=EBI-466029, EBI-9091197;
CC       P42858; Q9NWB7: IFT57; NbExp=3; IntAct=EBI-466029, EBI-725672;
CC       P42858; P22692: IGFBP4; NbExp=6; IntAct=EBI-466029, EBI-2831948;
CC       P42858; Q14005-2: IL16; NbExp=15; IntAct=EBI-466029, EBI-17178971;
CC       P42858; Q16891: IMMT; NbExp=7; IntAct=EBI-466029, EBI-473801;
CC       P42858; P29218-3: IMPA1; NbExp=6; IntAct=EBI-466029, EBI-12330251;
CC       P42858; Q9UNL4: ING4; NbExp=3; IntAct=EBI-466029, EBI-2866661;
CC       P42858; Q8WYH8-2: ING5; NbExp=18; IntAct=EBI-466029, EBI-21602071;
CC       P42858; Q8NBZ0: INO80E; NbExp=3; IntAct=EBI-466029, EBI-769401;
CC       P42858; Q8TEX9: IPO4; NbExp=7; IntAct=EBI-466029, EBI-395967;
CC       P42858; O00410-3: IPO5; NbExp=3; IntAct=EBI-466029, EBI-9641587;
CC       P42858; Q6DN90-2: IQSEC1; NbExp=18; IntAct=EBI-466029, EBI-21911304;
CC       P42858; Q96N16: JAKMIP1; NbExp=10; IntAct=EBI-466029, EBI-2680803;
CC       P42858; Q92993: KAT5; NbExp=15; IntAct=EBI-466029, EBI-399080;
CC       P42858; Q13303: KCNAB2; NbExp=3; IntAct=EBI-466029, EBI-948729;
CC       P42858; Q9Y691: KCNMB2; NbExp=3; IntAct=EBI-466029, EBI-7932244;
CC       P42858; Q96SI1-2: KCTD15; NbExp=6; IntAct=EBI-466029, EBI-12382297;
CC       P42858; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-466029, EBI-743960;
CC       P42858; A0A384DVV8: KIAA0040; NbExp=3; IntAct=EBI-466029, EBI-20764875;
CC       P42858; Q6ZU52: KIAA0408; NbExp=6; IntAct=EBI-466029, EBI-739493;
CC       P42858; Q5T5P2-6: KIAA1217; NbExp=3; IntAct=EBI-466029, EBI-10188326;
CC       P42858; O14901: KLF11; NbExp=7; IntAct=EBI-466029, EBI-948266;
CC       P42858; Q9Y4X4: KLF12; NbExp=3; IntAct=EBI-466029, EBI-750750;
CC       P42858; P57682: KLF3; NbExp=6; IntAct=EBI-466029, EBI-8472267;
CC       P42858; Q53G59: KLHL12; NbExp=3; IntAct=EBI-466029, EBI-740929;
CC       P42858; Q9Y2M5: KLHL20; NbExp=9; IntAct=EBI-466029, EBI-714379;
CC       P42858; O60259: KLK8; NbExp=3; IntAct=EBI-466029, EBI-3915857;
CC       P42858; O15229-2: KMO; NbExp=3; IntAct=EBI-466029, EBI-21870540;
CC       P42858; Q9Y448: KNSTRN; NbExp=3; IntAct=EBI-466029, EBI-373334;
CC       P42858; O00505: KPNA3; NbExp=11; IntAct=EBI-466029, EBI-358297;
CC       P42858; P05783: KRT18; NbExp=6; IntAct=EBI-466029, EBI-297888;
CC       P42858; P08727: KRT19; NbExp=6; IntAct=EBI-466029, EBI-742756;
CC       P42858; P35900: KRT20; NbExp=9; IntAct=EBI-466029, EBI-742094;
CC       P42858; Q14525: KRT33B; NbExp=12; IntAct=EBI-466029, EBI-1049638;
CC       P42858; P60409: KRTAP10-7; NbExp=9; IntAct=EBI-466029, EBI-10172290;
CC       P42858; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-466029, EBI-1052037;
CC       P42858; Q8IUC2: KRTAP8-1; NbExp=6; IntAct=EBI-466029, EBI-10261141;
CC       P42858; Q9BYQ4: KRTAP9-2; NbExp=9; IntAct=EBI-466029, EBI-1044640;
CC       P42858; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-466029, EBI-11985629;
CC       P42858; O43813: LANCL1; NbExp=10; IntAct=EBI-466029, EBI-3046631;
CC       P42858; Q92615: LARP4B; NbExp=3; IntAct=EBI-466029, EBI-1052558;
CC       P42858; O95447: LCA5L; NbExp=18; IntAct=EBI-466029, EBI-8473670;
CC       P42858; Q5T7P3: LCE1B; NbExp=15; IntAct=EBI-466029, EBI-10245913;
CC       P42858; Q86U70-2: LDB1; NbExp=3; IntAct=EBI-466029, EBI-11979761;
CC       P42858; Q9BYZ2: LDHAL6B; NbExp=18; IntAct=EBI-466029, EBI-1108377;
CC       P42858; P07195: LDHB; NbExp=9; IntAct=EBI-466029, EBI-358748;
CC       P42858; O95751: LDOC1; NbExp=5; IntAct=EBI-466029, EBI-740738;
CC       P42858; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-466029, EBI-10274069;
CC       P42858; Q9H2C1: LHX5; NbExp=15; IntAct=EBI-466029, EBI-25835523;
CC       P42858; Q9UPM6: LHX6; NbExp=12; IntAct=EBI-466029, EBI-10258746;
CC       P42858; Q68G74: LHX8; NbExp=12; IntAct=EBI-466029, EBI-8474075;
CC       P42858; Q9H9Z2: LIN28A; NbExp=18; IntAct=EBI-466029, EBI-2462365;
CC       P42858; Q8N0U6: LINC00518; NbExp=6; IntAct=EBI-466029, EBI-10264791;
CC       P42858; Q9H0V9: LMAN2L; NbExp=3; IntAct=EBI-466029, EBI-9091707;
CC       P42858; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-466029, EBI-739832;
CC       P42858; Q8N448: LNX2; NbExp=3; IntAct=EBI-466029, EBI-2340947;
CC       P42858; A2RU56: LOC401296; NbExp=9; IntAct=EBI-466029, EBI-9088215;
CC       P42858; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-466029, EBI-2510853;
CC       P42858; Q14693: LPIN1; NbExp=12; IntAct=EBI-466029, EBI-5278370;
CC       P42858; Q96CN5: LRRC45; NbExp=3; IntAct=EBI-466029, EBI-2805176;
CC       P42858; Q32MZ4: LRRFIP1; NbExp=3; IntAct=EBI-466029, EBI-1369100;
CC       P42858; O95777: LSM8; NbExp=15; IntAct=EBI-466029, EBI-347779;
CC       P42858; Q9Y383: LUC7L2; NbExp=9; IntAct=EBI-466029, EBI-352851;
CC       P42858; Q8N1E2: LYG1; NbExp=3; IntAct=EBI-466029, EBI-13309213;
CC       P42858; Q9H063: MAF1; NbExp=3; IntAct=EBI-466029, EBI-720354;
CC       P42858; P43357: MAGEA3; NbExp=6; IntAct=EBI-466029, EBI-5651459;
CC       P42858; Q96M61: MAGEB18; NbExp=16; IntAct=EBI-466029, EBI-741835;
CC       P42858; Q8N7X4: MAGEB6; NbExp=2; IntAct=EBI-466029, EBI-6447163;
CC       P42858; Q96EH3: MALSU1; NbExp=6; IntAct=EBI-466029, EBI-2339737;
CC       P42858; Q99683: MAP3K5; NbExp=6; IntAct=EBI-466029, EBI-476263;
CC       P42858; Q00266: MAT1A; NbExp=3; IntAct=EBI-466029, EBI-967087;
CC       P42858; P43243: MATR3; NbExp=4; IntAct=EBI-466029, EBI-352602;
CC       P42858; P56270-2: MAZ; NbExp=3; IntAct=EBI-466029, EBI-12068586;
CC       P42858; Q9UIS9: MBD1; NbExp=2; IntAct=EBI-466029, EBI-867196;
CC       P42858; O95243-2: MBD4; NbExp=19; IntAct=EBI-466029, EBI-6448717;
CC       P42858; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-466029, EBI-348259;
CC       P42858; Q9HAF1: MEAF6; NbExp=6; IntAct=EBI-466029, EBI-399266;
CC       P42858; P51608: MECP2; NbExp=18; IntAct=EBI-466029, EBI-1189067;
CC       P42858; Q96RN5: MED15; NbExp=3; IntAct=EBI-466029, EBI-394506;
CC       P42858; Q96RN5-2: MED15; NbExp=6; IntAct=EBI-466029, EBI-11030807;
CC       P42858; Q15528-2: MED22; NbExp=12; IntAct=EBI-466029, EBI-12954271;
CC       P42858; Q9H204: MED28; NbExp=9; IntAct=EBI-466029, EBI-514199;
CC       P42858; Q96HR3: MED30; NbExp=3; IntAct=EBI-466029, EBI-394659;
CC       P42858; Q9Y3C7: MED31; NbExp=9; IntAct=EBI-466029, EBI-394707;
CC       P42858; P50221: MEOX1; NbExp=19; IntAct=EBI-466029, EBI-2864512;
CC       P42858; Q8N6F8: METTL27; NbExp=9; IntAct=EBI-466029, EBI-8487781;
CC       P42858; Q8TDB4: MGARP; NbExp=21; IntAct=EBI-466029, EBI-4397720;
CC       P42858; O94851: MICAL2; NbExp=3; IntAct=EBI-466029, EBI-2804835;
CC       P42858; A4FUJ8: MKL1; NbExp=15; IntAct=EBI-466029, EBI-21250407;
CC       P42858; Q9BUB5: MKNK1; NbExp=18; IntAct=EBI-466029, EBI-73837;
CC       P42858; Q9H000: MKRN2; NbExp=12; IntAct=EBI-466029, EBI-2341005;
CC       P42858; P22033: MMUT; NbExp=12; IntAct=EBI-466029, EBI-2690467;
CC       P42858; P51948: MNAT1; NbExp=9; IntAct=EBI-466029, EBI-716139;
CC       P42858; P41218: MNDA; NbExp=18; IntAct=EBI-466029, EBI-2829677;
CC       P42858; Q16653-13: MOG; NbExp=12; IntAct=EBI-466029, EBI-24226707;
CC       P42858; Q15014: MORF4L2; NbExp=12; IntAct=EBI-466029, EBI-399257;
CC       P42858; Q8N594: MPND; NbExp=3; IntAct=EBI-466029, EBI-2512452;
CC       P42858; P49959: MRE11; NbExp=5; IntAct=EBI-466029, EBI-396513;
CC       P42858; Q9Y605: MRFAP1; NbExp=19; IntAct=EBI-466029, EBI-995714;
CC       P42858; Q96HT8: MRFAP1L1; NbExp=21; IntAct=EBI-466029, EBI-748896;
CC       P42858; Q9BYD1: MRPL13; NbExp=3; IntAct=EBI-466029, EBI-1054936;
CC       P42858; O43196-4: MSH5; NbExp=3; IntAct=EBI-466029, EBI-25860238;
CC       P42858; Q9Y3D2: MSRB2; NbExp=12; IntAct=EBI-466029, EBI-9092052;
CC       P42858; P35548: MSX2; NbExp=12; IntAct=EBI-466029, EBI-6447480;
CC       P42858; P02795: MT2A; NbExp=6; IntAct=EBI-466029, EBI-996616;
CC       P42858; O43312: MTSS1; NbExp=3; IntAct=EBI-466029, EBI-473954;
CC       P42858; Q9ULD2-3: MTUS1; NbExp=3; IntAct=EBI-466029, EBI-18051665;
CC       P42858; Q9ULD2-4: MTUS1; NbExp=9; IntAct=EBI-466029, EBI-25866497;
CC       P42858; O15069: NACAD; NbExp=15; IntAct=EBI-466029, EBI-7108375;
CC       P42858; Q9ULW6: NAP1L2; NbExp=3; IntAct=EBI-466029, EBI-3911716;
CC       P42858; P54920: NAPA; NbExp=3; IntAct=EBI-466029, EBI-749652;
CC       P42858; Q14596: NBR1; NbExp=3; IntAct=EBI-466029, EBI-742698;
CC       P42858; P14598: NCF1; NbExp=6; IntAct=EBI-466029, EBI-395044;
CC       P42858; Q969V3: NCLN; NbExp=9; IntAct=EBI-466029, EBI-1056979;
CC       P42858; O75376: NCOR1; NbExp=3; IntAct=EBI-466029, EBI-347233;
CC       P42858; Q99608: NDN; NbExp=6; IntAct=EBI-466029, EBI-718177;
CC       P42858; Q9P0J0: NDUFA13; NbExp=4; IntAct=EBI-466029, EBI-372742;
CC       P42858; Q16795: NDUFA9; NbExp=7; IntAct=EBI-466029, EBI-1045087;
CC       P42858; O96000: NDUFB10; NbExp=13; IntAct=EBI-466029, EBI-1246371;
CC       P42858; O96000-2: NDUFB10; NbExp=3; IntAct=EBI-466029, EBI-25930682;
CC       P42858; Q9Y6M9: NDUFB9; NbExp=10; IntAct=EBI-466029, EBI-713654;
CC       P42858; P28331-5: NDUFS1; NbExp=6; IntAct=EBI-466029, EBI-25876328;
CC       P42858; O43920: NDUFS5; NbExp=7; IntAct=EBI-466029, EBI-1246091;
CC       P42858; O76041: NEBL; NbExp=18; IntAct=EBI-466029, EBI-2880203;
CC       P42858; I6L9F6: NEFL; NbExp=9; IntAct=EBI-466029, EBI-10178578;
CC       P42858; Q86SG6: NEK8; NbExp=3; IntAct=EBI-466029, EBI-1752987;
CC       P42858; Q13562: NEUROD1; NbExp=6; IntAct=EBI-466029, EBI-3908303;
CC       P42858; P19838-2: NFKB1; NbExp=3; IntAct=EBI-466029, EBI-1452242;
CC       P42858; Q8N5V2: NGEF; NbExp=3; IntAct=EBI-466029, EBI-718372;
CC       P42858; Q9NX24: NHP2; NbExp=3; IntAct=EBI-466029, EBI-1050064;
CC       P42858; Q9UBE8: NLK; NbExp=3; IntAct=EBI-466029, EBI-366978;
CC       P42858; Q96AM0: NLRP1; NbExp=3; IntAct=EBI-466029, EBI-25860999;
CC       P42858; O00746: NME4; NbExp=20; IntAct=EBI-466029, EBI-744871;
CC       P42858; P56597: NME5; NbExp=6; IntAct=EBI-466029, EBI-740667;
CC       P42858; Q9C002: NMES1; NbExp=3; IntAct=EBI-466029, EBI-3905285;
CC       P42858; Q9Y239: NOD1; NbExp=9; IntAct=EBI-466029, EBI-1051262;
CC       P42858; O15130-2: NPFF; NbExp=18; IntAct=EBI-466029, EBI-25840002;
CC       P42858; Q9Y639-1: NPTN; NbExp=6; IntAct=EBI-466029, EBI-12839590;
CC       P42858; Q13133-2: NR1H3; NbExp=3; IntAct=EBI-466029, EBI-12699353;
CC       P42858; Q86WQ0: NR2C2AP; NbExp=3; IntAct=EBI-466029, EBI-10260040;
CC       P42858; Q6X4W1-6: NSMF; NbExp=6; IntAct=EBI-466029, EBI-25842707;
CC       P42858; P36639-4: NUDT1; NbExp=6; IntAct=EBI-466029, EBI-25834643;
CC       P42858; Q9NZJ9: NUDT4; NbExp=6; IntAct=EBI-466029, EBI-4280066;
CC       P42858; Q7Z417: NUFIP2; NbExp=6; IntAct=EBI-466029, EBI-1210753;
CC       P42858; Q9BVL2: NUP58; NbExp=7; IntAct=EBI-466029, EBI-2811583;
CC       P42858; Q9NPJ8-3: NXT2; NbExp=15; IntAct=EBI-466029, EBI-10698339;
CC       P42858; Q96GC1: ODF2L; NbExp=3; IntAct=EBI-466029, EBI-12176953;
CC       P42858; Q02218: OGDH; NbExp=3; IntAct=EBI-466029, EBI-747213;
CC       P42858; Q86WS3: OOSP2; NbExp=9; IntAct=EBI-466029, EBI-25888682;
CC       P42858; Q6B0I4: OPCML; NbExp=3; IntAct=EBI-466029, EBI-25954356;
CC       P42858; Q96CV9: OPTN; NbExp=13; IntAct=EBI-466029, EBI-748974;
CC       P42858; Q96CV9-2: OPTN; NbExp=18; IntAct=EBI-466029, EBI-9091423;
CC       P42858; Q92882: OSTF1; NbExp=5; IntAct=EBI-466029, EBI-1051152;
CC       P42858; Q3ZCN5: OTOGL; NbExp=3; IntAct=EBI-466029, EBI-25954043;
CC       P42858; Q8IVL6-2: P3H3; NbExp=6; IntAct=EBI-466029, EBI-12149899;
CC       P42858; P13674: P4HA1; NbExp=5; IntAct=EBI-466029, EBI-1237386;
CC       P42858; Q6VY07: PACS1; NbExp=18; IntAct=EBI-466029, EBI-2555014;
CC       P42858; Q9BY11: PACSIN1; NbExp=3; IntAct=EBI-466029, EBI-721769;
CC       P42858; Q13177: PAK2; NbExp=2; IntAct=EBI-466029, EBI-1045887;
CC       P42858; Q9P286: PAK5; NbExp=3; IntAct=EBI-466029, EBI-741896;
CC       P42858; Q9NP74: PALMD; NbExp=6; IntAct=EBI-466029, EBI-2811699;
CC       P42858; Q8N3R9: PALS1; NbExp=3; IntAct=EBI-466029, EBI-2513978;
CC       P42858; Q86WK9: PAQR7; NbExp=3; IntAct=EBI-466029, EBI-10694587;
CC       P42858; Q99497: PARK7; NbExp=6; IntAct=EBI-466029, EBI-1164361;
CC       P42858; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-466029, EBI-11022007;
CC       P42858; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-466029, EBI-10302990;
CC       P42858; Q9Y5G3-2: PCDHGB1; NbExp=3; IntAct=EBI-466029, EBI-21584477;
CC       P42858; Q6UW60-2: PCSK4; NbExp=3; IntAct=EBI-466029, EBI-25960845;
CC       P42858; P54750-4: PDE1A; NbExp=3; IntAct=EBI-466029, EBI-25952361;
CC       P42858; Q15119: PDK2; NbExp=10; IntAct=EBI-466029, EBI-726271;
CC       P42858; Q96HC4: PDLIM5; NbExp=9; IntAct=EBI-466029, EBI-751267;
CC       P42858; O15530-4: PDPK1; NbExp=6; IntAct=EBI-466029, EBI-9087775;
CC       P42858; Q13113: PDZK1IP1; NbExp=21; IntAct=EBI-466029, EBI-716063;
CC       P42858; Q96FA3: PELI1; NbExp=3; IntAct=EBI-466029, EBI-448369;
CC       P42858; Q9BRX2: PELO; NbExp=12; IntAct=EBI-466029, EBI-1043580;
CC       P42858; O00541: PES1; NbExp=3; IntAct=EBI-466029, EBI-1053271;
CC       P42858; Q99471: PFDN5; NbExp=3; IntAct=EBI-466029, EBI-357275;
CC       P42858; P35080: PFN2; NbExp=7; IntAct=EBI-466029, EBI-473138;
CC       P42858; O75925: PIAS1; NbExp=19; IntAct=EBI-466029, EBI-629434;
CC       P42858; Q8N2W9: PIAS4; NbExp=6; IntAct=EBI-466029, EBI-473160;
CC       P42858; Q8WXW3: PIBF1; NbExp=3; IntAct=EBI-466029, EBI-2558770;
CC       P42858; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-466029, EBI-79165;
CC       P42858; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-466029, EBI-10232538;
CC       P42858; P42336: PIK3CA; NbExp=3; IntAct=EBI-466029, EBI-2116585;
CC       P42858; P27986: PIK3R1; NbExp=7; IntAct=EBI-466029, EBI-79464;
CC       P42858; P27986-2: PIK3R1; NbExp=18; IntAct=EBI-466029, EBI-9090282;
CC       P42858; O00459: PIK3R2; NbExp=6; IntAct=EBI-466029, EBI-346930;
CC       P42858; Q92569: PIK3R3; NbExp=18; IntAct=EBI-466029, EBI-79893;
CC       P42858; Q9BXM7: PINK1; NbExp=9; IntAct=EBI-466029, EBI-2846068;
CC       P42858; Q96J94: PIWIL1; NbExp=3; IntAct=EBI-466029, EBI-527417;
CC       P42858; P14618: PKM; NbExp=9; IntAct=EBI-466029, EBI-353408;
CC       P42858; Q9BS22: PLA2G1B; NbExp=3; IntAct=EBI-466029, EBI-25961917;
CC       P42858; Q9UP65: PLA2G4C; NbExp=12; IntAct=EBI-466029, EBI-25848809;
CC       P42858; Q15149: PLEC; NbExp=4; IntAct=EBI-466029, EBI-297903;
CC       P42858; Q6ZR37: PLEKHG7; NbExp=12; IntAct=EBI-466029, EBI-12891828;
CC       P42858; Q9HCM2-3: PLXNA4; NbExp=3; IntAct=EBI-466029, EBI-25962330;
CC       P42858; Q6P1K2-3: PMF1; NbExp=3; IntAct=EBI-466029, EBI-12906008;
CC       P42858; Q8NBT0: POC1A; NbExp=15; IntAct=EBI-466029, EBI-2557132;
CC       P42858; Q9H2U2-3: PPA2; NbExp=3; IntAct=EBI-466029, EBI-25972548;
CC       P42858; Q9H2U2-6: PPA2; NbExp=3; IntAct=EBI-466029, EBI-25972564;
CC       P42858; Q07869: PPARA; NbExp=3; IntAct=EBI-466029, EBI-78615;
CC       P42858; Q03181-2: PPARD; NbExp=3; IntAct=EBI-466029, EBI-10223258;
CC       P42858; P37231: PPARG; NbExp=16; IntAct=EBI-466029, EBI-781384;
CC       P42858; Q59EV6: PPGB; NbExp=10; IntAct=EBI-466029, EBI-14210385;
CC       P42858; O43447: PPIH; NbExp=10; IntAct=EBI-466029, EBI-1055615;
CC       P42858; O60437: PPL; NbExp=8; IntAct=EBI-466029, EBI-368321;
CC       P42858; P62136: PPP1CA; NbExp=10; IntAct=EBI-466029, EBI-357253;
CC       P42858; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-466029, EBI-10293968;
CC       P42858; Q6ZMI0-5: PPP1R21; NbExp=9; IntAct=EBI-466029, EBI-25835994;
CC       P42858; Q16537: PPP2R5E; NbExp=15; IntAct=EBI-466029, EBI-968374;
CC       P42858; O75170-4: PPP6R2; NbExp=3; IntAct=EBI-466029, EBI-11079164;
CC       P42858; O60828: PQBP1; NbExp=3; IntAct=EBI-466029, EBI-713867;
CC       P42858; P49642: PRIM1; NbExp=3; IntAct=EBI-466029, EBI-726050;
CC       P42858; P17612: PRKACA; NbExp=3; IntAct=EBI-466029, EBI-476586;
CC       P42858; P55345: PRMT2; NbExp=3; IntAct=EBI-466029, EBI-78458;
CC       P42858; P04156: PRNP; NbExp=13; IntAct=EBI-466029, EBI-977302;
CC       P42858; Q53TL4: PRO0132; NbExp=3; IntAct=EBI-466029, EBI-25960611;
CC       P42858; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-466029, EBI-1567797;
CC       P42858; O75400: PRPF40A; NbExp=15; IntAct=EBI-466029, EBI-473291;
CC       P42858; O75400-2: PRPF40A; NbExp=9; IntAct=EBI-466029, EBI-5280197;
CC       P42858; Q96M27: PRRC1; NbExp=7; IntAct=EBI-466029, EBI-2560879;
CC       P42858; A0A0C4DFM3: PRUNE2; NbExp=3; IntAct=EBI-466029, EBI-25830870;
CC       P42858; P25786: PSMA1; NbExp=3; IntAct=EBI-466029, EBI-359352;
CC       P42858; P25789: PSMA4; NbExp=4; IntAct=EBI-466029, EBI-359310;
CC       P42858; P60900: PSMA6; NbExp=4; IntAct=EBI-466029, EBI-357793;
CC       P42858; O14818: PSMA7; NbExp=13; IntAct=EBI-466029, EBI-603272;
CC       P42858; P20618: PSMB1; NbExp=7; IntAct=EBI-466029, EBI-372273;
CC       P42858; P49721: PSMB2; NbExp=7; IntAct=EBI-466029, EBI-359335;
CC       P42858; P49720: PSMB3; NbExp=3; IntAct=EBI-466029, EBI-603340;
CC       P42858; P28072: PSMB6; NbExp=3; IntAct=EBI-466029, EBI-359288;
CC       P42858; P28062-2: PSMB8; NbExp=3; IntAct=EBI-466029, EBI-372312;
CC       P42858; P17980: PSMC3; NbExp=6; IntAct=EBI-466029, EBI-359720;
CC       P42858; O00487: PSMD14; NbExp=7; IntAct=EBI-466029, EBI-722193;
CC       P42858; O43242: PSMD3; NbExp=3; IntAct=EBI-466029, EBI-357622;
CC       P42858; P55036: PSMD4; NbExp=5; IntAct=EBI-466029, EBI-359318;
CC       P42858; P51665: PSMD7; NbExp=10; IntAct=EBI-466029, EBI-357659;
CC       P42858; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-466029, EBI-14199621;
CC       P42858; P41222: PTGDS; NbExp=3; IntAct=EBI-466029, EBI-948821;
CC       P42858; Q13882: PTK6; NbExp=4; IntAct=EBI-466029, EBI-1383632;
CC       P42858; Q9UHX1-2: PUF60; NbExp=6; IntAct=EBI-466029, EBI-11529177;
CC       P42858; Q9UHX1-6: PUF60; NbExp=9; IntAct=EBI-466029, EBI-11085298;
CC       P42858; P47897: QARS1; NbExp=6; IntAct=EBI-466029, EBI-347462;
CC       P42858; Q15286: RAB35; NbExp=3; IntAct=EBI-466029, EBI-722275;
CC       P42858; P61020: RAB5B; NbExp=3; IntAct=EBI-466029, EBI-399401;
CC       P42858; P54725: RAD23A; NbExp=3; IntAct=EBI-466029, EBI-746453;
CC       P42858; P78406: RAE1; NbExp=4; IntAct=EBI-466029, EBI-724495;
CC       P42858; P62826: RAN; NbExp=6; IntAct=EBI-466029, EBI-286642;
CC       P42858; P46060: RANGAP1; NbExp=10; IntAct=EBI-466029, EBI-396091;
CC       P42858; Q8WZA2: RAPGEF4; NbExp=3; IntAct=EBI-466029, EBI-948476;
CC       P42858; Q13702-2: RAPSN; NbExp=18; IntAct=EBI-466029, EBI-22012855;
CC       P42858; P20936: RASA1; NbExp=3; IntAct=EBI-466029, EBI-1026476;
CC       P42858; Q6T310: RASL11A; NbExp=3; IntAct=EBI-466029, EBI-4401868;
CC       P42858; Q9NS23-4: RASSF1; NbExp=3; IntAct=EBI-466029, EBI-438710;
CC       P42858; P50749: RASSF2; NbExp=3; IntAct=EBI-466029, EBI-960081;
CC       P42858; Q8WWW0-2: RASSF5; NbExp=3; IntAct=EBI-466029, EBI-960502;
CC       P42858; O43251-3: RBFOX2; NbExp=3; IntAct=EBI-466029, EBI-11531589;
CC       P42858; P57052: RBM11; NbExp=9; IntAct=EBI-466029, EBI-741332;
CC       P42858; P52756: RBM5; NbExp=6; IntAct=EBI-466029, EBI-714003;
CC       P42858; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-466029, EBI-740343;
CC       P42858; Q9UKA8: RCAN3; NbExp=18; IntAct=EBI-466029, EBI-9091952;
CC       P42858; Q15293: RCN1; NbExp=3; IntAct=EBI-466029, EBI-948278;
CC       P42858; Q9GZR2: REXO4; NbExp=3; IntAct=EBI-466029, EBI-2856313;
CC       P42858; Q8IXN7: RIMKLA; NbExp=3; IntAct=EBI-466029, EBI-21890191;
CC       P42858; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-466029, EBI-726876;
CC       P42858; Q5TAB7: RIPPLY2; NbExp=6; IntAct=EBI-466029, EBI-10246897;
CC       P42858; Q6ZNA4-2: RNF111; NbExp=18; IntAct=EBI-466029, EBI-21535400;
CC       P42858; Q9ULX5: RNF112; NbExp=21; IntAct=EBI-466029, EBI-25829984;
CC       P42858; Q96D59: RNF183; NbExp=3; IntAct=EBI-466029, EBI-743938;
CC       P42858; Q5VTR2: RNF20; NbExp=24; IntAct=EBI-466029, EBI-2372238;
CC       P42858; Q9H0F5-2: RNF38; NbExp=21; IntAct=EBI-466029, EBI-25866807;
CC       P42858; O75150: RNF40; NbExp=12; IntAct=EBI-466029, EBI-744408;
CC       P42858; P26373: RPL13; NbExp=10; IntAct=EBI-466029, EBI-356849;
CC       P42858; Q6NZ55: RPL13; NbExp=3; IntAct=EBI-466029, EBI-10252046;
CC       P42858; P61313: RPL15; NbExp=3; IntAct=EBI-466029, EBI-443462;
CC       P42858; Q07020: RPL18; NbExp=12; IntAct=EBI-466029, EBI-352694;
CC       P42858; P84098: RPL19; NbExp=6; IntAct=EBI-466029, EBI-916524;
CC       P42858; P35268: RPL22; NbExp=3; IntAct=EBI-466029, EBI-354533;
CC       P42858; Q9UNX3: RPL26L1; NbExp=3; IntAct=EBI-466029, EBI-2949703;
CC       P42858; P61353: RPL27; NbExp=6; IntAct=EBI-466029, EBI-352760;
CC       P42858; P62899: RPL31; NbExp=3; IntAct=EBI-466029, EBI-1053664;
CC       P42858; P36578: RPL4; NbExp=14; IntAct=EBI-466029, EBI-348313;
CC       P42858; P25398: RPS12; NbExp=3; IntAct=EBI-466029, EBI-354542;
CC       P42858; P62244: RPS15A; NbExp=3; IntAct=EBI-466029, EBI-347895;
CC       P42858; P39019: RPS19; NbExp=3; IntAct=EBI-466029, EBI-354451;
CC       P42858; P62979: RPS27A; NbExp=6; IntAct=EBI-466029, EBI-357375;
CC       P42858; P23396: RPS3; NbExp=3; IntAct=EBI-466029, EBI-351193;
CC       P42858; P46782: RPS5; NbExp=3; IntAct=EBI-466029, EBI-350569;
CC       P42858; Q16799-3: RTN1; NbExp=9; IntAct=EBI-466029, EBI-10180131;
CC       P42858; Q6ZNE9: RUFY4; NbExp=3; IntAct=EBI-466029, EBI-10181525;
CC       P42858; Q66K80: RUSC1-AS1; NbExp=6; IntAct=EBI-466029, EBI-10248967;
CC       P42858; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-466029, EBI-8636004;
CC       P42858; P48443: RXRG; NbExp=18; IntAct=EBI-466029, EBI-712405;
CC       P42858; Q8N488: RYBP; NbExp=9; IntAct=EBI-466029, EBI-752324;
CC       P42858; P25815: S100P; NbExp=9; IntAct=EBI-466029, EBI-743700;
CC       P42858; Q8N6K7-2: SAMD3; NbExp=3; IntAct=EBI-466029, EBI-11528848;
CC       P42858; G3V2R1: SAMD4A; NbExp=3; IntAct=EBI-466029, EBI-21264240;
CC       P42858; O75446: SAP30; NbExp=3; IntAct=EBI-466029, EBI-632609;
CC       P42858; Q6UVJ0: SASS6; NbExp=15; IntAct=EBI-466029, EBI-1570153;
CC       P42858; Q9BY12-3: SCAPER; NbExp=6; IntAct=EBI-466029, EBI-25837959;
CC       P42858; Q8WVM8: SCFD1; NbExp=3; IntAct=EBI-466029, EBI-722569;
CC       P42858; Q96NL6-3: SCLT1; NbExp=3; IntAct=EBI-466029, EBI-25961722;
CC       P42858; Q12765-2: SCRN1; NbExp=3; IntAct=EBI-466029, EBI-12027936;
CC       P42858; O00560: SDCBP; NbExp=12; IntAct=EBI-466029, EBI-727004;
CC       P42858; P55735-3: SEC13; NbExp=15; IntAct=EBI-466029, EBI-12235008;
CC       P42858; Q15437: SEC23B; NbExp=3; IntAct=EBI-466029, EBI-742673;
CC       P42858; Q96T21: SECISBP2; NbExp=3; IntAct=EBI-466029, EBI-954116;
CC       P42858; O43236: SEPTIN4; NbExp=3; IntAct=EBI-466029, EBI-1047513;
CC       P42858; Q14141: SEPTIN6; NbExp=18; IntAct=EBI-466029, EBI-745901;
CC       P42858; Q16181-2: SEPTIN7; NbExp=9; IntAct=EBI-466029, EBI-10176094;
CC       P42858; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-466029, EBI-748601;
CC       P42858; Q9BYW2: SETD2; NbExp=4; IntAct=EBI-466029, EBI-945869;
CC       P42858; Q15047-2: SETDB1; NbExp=15; IntAct=EBI-466029, EBI-9090795;
CC       P42858; Q12874: SF3A3; NbExp=3; IntAct=EBI-466029, EBI-1051880;
CC       P42858; Q15393: SF3B3; NbExp=3; IntAct=EBI-466029, EBI-346977;
CC       P42858; A0A1P0AYU5: SFXN3; NbExp=9; IntAct=EBI-466029, EBI-14193895;
CC       P42858; Q2NKQ1-4: SGSM1; NbExp=12; IntAct=EBI-466029, EBI-10182463;
CC       P42858; Q99961: SH3GL1; NbExp=3; IntAct=EBI-466029, EBI-697911;
CC       P42858; Q99963: SH3GL3; NbExp=9; IntAct=EBI-466029, EBI-473910;
CC       P42858; Q9NR46: SH3GLB2; NbExp=3; IntAct=EBI-466029, EBI-749607;
CC       P42858; Q8IYI0: SHLD1; NbExp=3; IntAct=EBI-466029, EBI-2560428;
CC       P42858; Q9Y2K2-7: SIK3; NbExp=3; IntAct=EBI-466029, EBI-17172855;
CC       P42858; Q96ST3: SIN3A; NbExp=4; IntAct=EBI-466029, EBI-347218;
CC       P42858; P43004: SLC1A2; NbExp=12; IntAct=EBI-466029, EBI-3440986;
CC       P42858; Q02978: SLC25A11; NbExp=6; IntAct=EBI-466029, EBI-359174;
CC       P42858; Q00325-2: SLC25A3; NbExp=3; IntAct=EBI-466029, EBI-5456178;
CC       P42858; Q8NCS7: SLC44A5; NbExp=3; IntAct=EBI-466029, EBI-21504521;
CC       P42858; Q12824: SMARCB1; NbExp=9; IntAct=EBI-466029, EBI-358419;
CC       P42858; Q8TAQ2-2: SMARCC2; NbExp=3; IntAct=EBI-466029, EBI-11990400;
CC       P42858; Q96GM5: SMARCD1; NbExp=12; IntAct=EBI-466029, EBI-358489;
CC       P42858; Q16637-3: SMN2; NbExp=9; IntAct=EBI-466029, EBI-395447;
CC       P42858; Q9HCE7-2: SMURF1; NbExp=6; IntAct=EBI-466029, EBI-9845742;
CC       P42858; P60880-2: SNAP25; NbExp=9; IntAct=EBI-466029, EBI-12177361;
CC       P42858; O95721: SNAP29; NbExp=3; IntAct=EBI-466029, EBI-490676;
CC       P42858; P37840: SNCA; NbExp=4; IntAct=EBI-466029, EBI-985879;
CC       P42858; P62316: SNRPD2; NbExp=3; IntAct=EBI-466029, EBI-297993;
CC       P42858; P62306: SNRPF; NbExp=3; IntAct=EBI-466029, EBI-356900;
CC       P42858; Q13573: SNW1; NbExp=12; IntAct=EBI-466029, EBI-632715;
CC       P42858; Q9UMY4: SNX12; NbExp=3; IntAct=EBI-466029, EBI-1752602;
CC       P42858; O60749: SNX2; NbExp=6; IntAct=EBI-466029, EBI-1046690;
CC       P42858; Q8WV41: SNX33; NbExp=6; IntAct=EBI-466029, EBI-2481535;
CC       P42858; Q8WXH5: SOCS4; NbExp=3; IntAct=EBI-466029, EBI-3942425;
CC       P42858; Q9BX66: SORBS1; NbExp=4; IntAct=EBI-466029, EBI-433642;
CC       P42858; O95416: SOX14; NbExp=12; IntAct=EBI-466029, EBI-9087806;
CC       P42858; Q9BT81: SOX7; NbExp=15; IntAct=EBI-466029, EBI-7239117;
CC       P42858; Q02447: SP3; NbExp=4; IntAct=EBI-466029, EBI-348158;
CC       P42858; Q3SY56: SP6; NbExp=3; IntAct=EBI-466029, EBI-11175533;
CC       P42858; Q99932-2: SPAG8; NbExp=18; IntAct=EBI-466029, EBI-11959123;
CC       P42858; Q9NY87: SPANXC; NbExp=3; IntAct=EBI-466029, EBI-10316585;
CC       P42858; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-466029, EBI-10696971;
CC       P42858; Q8NHS9: SPATA22; NbExp=9; IntAct=EBI-466029, EBI-7067260;
CC       P42858; Q8IUW3: SPATA2L; NbExp=6; IntAct=EBI-466029, EBI-2510414;
CC       P42858; P61009: SPCS3; NbExp=6; IntAct=EBI-466029, EBI-6166040;
CC       P42858; Q01892: SPIB; NbExp=18; IntAct=EBI-466029, EBI-2800992;
CC       P42858; Q1W4C9: SPINK13; NbExp=3; IntAct=EBI-466029, EBI-25953827;
CC       P42858; Q7Z698: SPRED2; NbExp=6; IntAct=EBI-466029, EBI-7082156;
CC       P42858; Q13501: SQSTM1; NbExp=8; IntAct=EBI-466029, EBI-307104;
CC       P42858; P36956: SREBF1; NbExp=3; IntAct=EBI-466029, EBI-948313;
CC       P42858; Q7Z6B7: SRGAP1; NbExp=4; IntAct=EBI-466029, EBI-2481729;
CC       P42858; O75044: SRGAP2; NbExp=3; IntAct=EBI-466029, EBI-1051034;
CC       P42858; O43295: SRGAP3; NbExp=4; IntAct=EBI-466029, EBI-368166;
CC       P42858; Q8IXS7: SRGAP3; NbExp=3; IntAct=EBI-466029, EBI-18616594;
CC       P42858; Q9BXP5: SRRT; NbExp=3; IntAct=EBI-466029, EBI-712721;
CC       P42858; Q9BXP5-3: SRRT; NbExp=6; IntAct=EBI-466029, EBI-25866384;
CC       P42858; Q9BXP5-4: SRRT; NbExp=3; IntAct=EBI-466029, EBI-16701991;
CC       P42858; P05455: SSB; NbExp=3; IntAct=EBI-466029, EBI-358037;
CC       P42858; Q9NP77: SSU72; NbExp=3; IntAct=EBI-466029, EBI-2515416;
CC       P42858; P50502: ST13; NbExp=13; IntAct=EBI-466029, EBI-357285;
CC       P42858; O75886: STAM2; NbExp=6; IntAct=EBI-466029, EBI-373258;
CC       P42858; P49675: STAR; NbExp=3; IntAct=EBI-466029, EBI-722932;
CC       P42858; Q9H668: STN1; NbExp=3; IntAct=EBI-466029, EBI-746930;
CC       P42858; Q9Y3F4: STRAP; NbExp=4; IntAct=EBI-466029, EBI-727414;
CC       P42858; A1L378: STRC; NbExp=6; IntAct=EBI-466029, EBI-22013242;
CC       P42858; Q9UNE7: STUB1; NbExp=12; IntAct=EBI-466029, EBI-357085;
CC       P42858; O14662-5: STX16; NbExp=15; IntAct=EBI-466029, EBI-9089968;
CC       P42858; P61764: STXBP1; NbExp=7; IntAct=EBI-466029, EBI-960169;
CC       P42858; Q9BR01-2: SULT4A1; NbExp=15; IntAct=EBI-466029, EBI-25831443;
CC       P42858; Q8NBJ7: SUMF2; NbExp=6; IntAct=EBI-466029, EBI-723091;
CC       P42858; P63165: SUMO1; NbExp=3; IntAct=EBI-466029, EBI-80140;
CC       P42858; P55854: SUMO3; NbExp=9; IntAct=EBI-466029, EBI-474067;
CC       P42858; A1L190: SYCE3; NbExp=15; IntAct=EBI-466029, EBI-10283466;
CC       P42858; Q92797: SYMPK; NbExp=3; IntAct=EBI-466029, EBI-1051992;
CC       P42858; Q92797-2: SYMPK; NbExp=9; IntAct=EBI-466029, EBI-21560407;
CC       P42858; P08247: SYP; NbExp=13; IntAct=EBI-466029, EBI-9071725;
CC       P42858; Q9BQS2-2: SYT15; NbExp=3; IntAct=EBI-466029, EBI-13373352;
CC       P42858; Q8N9I0: SYT2; NbExp=10; IntAct=EBI-466029, EBI-8032987;
CC       P42858; Q9BQG1: SYT3; NbExp=12; IntAct=EBI-466029, EBI-17284568;
CC       P42858; Q5T7P8-2: SYT6; NbExp=3; IntAct=EBI-466029, EBI-10246152;
CC       P42858; O75410: TACC1; NbExp=4; IntAct=EBI-466029, EBI-624237;
CC       P42858; O75410-7: TACC1; NbExp=12; IntAct=EBI-466029, EBI-12007872;
CC       P42858; Q86TJ2-3: TADA2B; NbExp=3; IntAct=EBI-466029, EBI-18173581;
CC       P42858; P37802: TAGLN2; NbExp=3; IntAct=EBI-466029, EBI-1056740;
CC       P42858; P37837: TALDO1; NbExp=3; IntAct=EBI-466029, EBI-1056712;
CC       P42858; Q6NW12: TANK; NbExp=9; IntAct=EBI-466029, EBI-25948253;
CC       P42858; Q92844: TANK; NbExp=3; IntAct=EBI-466029, EBI-356349;
CC       P42858; Q92844-3: TANK; NbExp=3; IntAct=EBI-466029, EBI-25967460;
CC       P42858; Q9H2K8: TAOK3; NbExp=3; IntAct=EBI-466029, EBI-1384100;
CC       P42858; Q5VWN6: TASOR2; NbExp=12; IntAct=EBI-466029, EBI-745958;
CC       P42858; Q92609: TBC1D5; NbExp=3; IntAct=EBI-466029, EBI-742381;
CC       P42858; Q32MN6: TBP; NbExp=9; IntAct=EBI-466029, EBI-10239991;
CC       P42858; Q16650: TBR1; NbExp=12; IntAct=EBI-466029, EBI-1047158;
CC       P42858; Q9Y458: TBX22; NbExp=12; IntAct=EBI-466029, EBI-6427217;
CC       P42858; O14776: TCERG1; NbExp=9; IntAct=EBI-466029, EBI-473271;
CC       P42858; P17987: TCP1; NbExp=3; IntAct=EBI-466029, EBI-356553;
CC       P42858; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-466029, EBI-3923210;
CC       P42858; P28347-2: TEAD1; NbExp=18; IntAct=EBI-466029, EBI-12151837;
CC       P42858; Q86WV5: TEN1; NbExp=9; IntAct=EBI-466029, EBI-2562799;
CC       P42858; Q96A09: TENT5B; NbExp=6; IntAct=EBI-466029, EBI-752030;
CC       P42858; Q15554-4: TERF2; NbExp=15; IntAct=EBI-466029, EBI-25840535;
CC       P42858; Q96M34: TEX55; NbExp=3; IntAct=EBI-466029, EBI-25961624;
CC       P42858; Q03403: TFF2; NbExp=18; IntAct=EBI-466029, EBI-4314702;
CC       P42858; Q92734: TFG; NbExp=3; IntAct=EBI-466029, EBI-357061;
CC       P42858; O95455: TGDS; NbExp=3; IntAct=EBI-466029, EBI-1761487;
CC       P42858; P37173: TGFBR2; NbExp=3; IntAct=EBI-466029, EBI-296151;
CC       P42858; P21980-2: TGM2; NbExp=6; IntAct=EBI-466029, EBI-25842075;
CC       P42858; Q96MW7: TIGD1; NbExp=9; IntAct=EBI-466029, EBI-9091586;
CC       P42858; O60220: TIMM8A; NbExp=15; IntAct=EBI-466029, EBI-1049822;
CC       P42858; Q08117: TLE5; NbExp=3; IntAct=EBI-466029, EBI-717810;
CC       P42858; Q9BZW5-2: TM6SF1; NbExp=3; IntAct=EBI-466029, EBI-25852210;
CC       P42858; Q96EY4: TMA16; NbExp=3; IntAct=EBI-466029, EBI-1045338;
CC       P42858; Q9NUM4: TMEM106B; NbExp=3; IntAct=EBI-466029, EBI-10490807;
CC       P42858; Q12893: TMEM115; NbExp=3; IntAct=EBI-466029, EBI-8633987;
CC       P42858; Q6UW68: TMEM205; NbExp=3; IntAct=EBI-466029, EBI-6269551;
CC       P42858; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-466029, EBI-11528917;
CC       P42858; Q9NV96-2: TMEM30A; NbExp=3; IntAct=EBI-466029, EBI-12921610;
CC       P42858; Q9BTV4: TMEM43; NbExp=3; IntAct=EBI-466029, EBI-721293;
CC       P42858; Q9BQJ4: TMEM47; NbExp=3; IntAct=EBI-466029, EBI-13370320;
CC       P42858; Q8IUR5-4: TMTC1; NbExp=6; IntAct=EBI-466029, EBI-9089156;
CC       P42858; Q71RG4-4: TMUB2; NbExp=6; IntAct=EBI-466029, EBI-25831574;
CC       P42858; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-466029, EBI-2505861;
CC       P42858; O00300: TNFRSF11B; NbExp=3; IntAct=EBI-466029, EBI-15481185;
CC       P42858; O95150: TNFSF15; NbExp=3; IntAct=EBI-466029, EBI-16355546;
CC       P42858; Q96KP6: TNIP3; NbExp=9; IntAct=EBI-466029, EBI-2509913;
CC       P42858; P22105-1: TNXB; NbExp=3; IntAct=EBI-466029, EBI-20753895;
CC       P42858; Q9NS69: TOMM22; NbExp=6; IntAct=EBI-466029, EBI-1047508;
CC       P42858; P04637: TP53; NbExp=19; IntAct=EBI-466029, EBI-366083;
CC       P42858; P60174: TPI1; NbExp=6; IntAct=EBI-466029, EBI-717475;
CC       P42858; Q12933: TRAF2; NbExp=3; IntAct=EBI-466029, EBI-355744;
CC       P42858; O14545: TRAFD1; NbExp=5; IntAct=EBI-466029, EBI-1396921;
CC       P42858; P19474: TRIM21; NbExp=21; IntAct=EBI-466029, EBI-81290;
CC       P42858; Q9UPQ4-2: TRIM35; NbExp=9; IntAct=EBI-466029, EBI-17716262;
CC       P42858; P0CI25: TRIM49; NbExp=9; IntAct=EBI-466029, EBI-6427421;
CC       P42858; Q15642-2: TRIP10; NbExp=18; IntAct=EBI-466029, EBI-6550597;
CC       P42858; Q15654: TRIP6; NbExp=3; IntAct=EBI-466029, EBI-742327;
CC       P42858; Q99614: TTC1; NbExp=9; IntAct=EBI-466029, EBI-742074;
CC       P42858; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-466029, EBI-948354;
CC       P42858; Q5W5X9-3: TTC23; NbExp=18; IntAct=EBI-466029, EBI-9090990;
CC       P42858; Q71U36: TUBA1A; NbExp=3; IntAct=EBI-466029, EBI-302552;
CC       P42858; P07437: TUBB; NbExp=9; IntAct=EBI-466029, EBI-350864;
CC       P42858; Q9BUF5: TUBB6; NbExp=3; IntAct=EBI-466029, EBI-356735;
CC       P42858; Q9UGJ1-2: TUBGCP4; NbExp=6; IntAct=EBI-466029, EBI-10964469;
CC       P42858; Q15672: TWIST1; NbExp=3; IntAct=EBI-466029, EBI-1797287;
CC       P42858; Q8WVJ9: TWIST2; NbExp=15; IntAct=EBI-466029, EBI-1797313;
CC       P42858; Q99757: TXN2; NbExp=3; IntAct=EBI-466029, EBI-2932492;
CC       P42858; Q6PKC3: TXNDC11; NbExp=7; IntAct=EBI-466029, EBI-749812;
CC       P42858; Q01081: U2AF1; NbExp=3; IntAct=EBI-466029, EBI-632461;
CC       P42858; P22314: UBA1; NbExp=3; IntAct=EBI-466029, EBI-709688;
CC       P42858; Q9BSL1: UBAC1; NbExp=26; IntAct=EBI-466029, EBI-749370;
CC       P42858; P0CG48: UBC; NbExp=3; IntAct=EBI-466029, EBI-3390054;
CC       P42858; Q9Y2X8: UBE2D4; NbExp=3; IntAct=EBI-466029, EBI-745527;
CC       P42858; P62256: UBE2H; NbExp=3; IntAct=EBI-466029, EBI-2129909;
CC       P42858; P63279: UBE2I; NbExp=3; IntAct=EBI-466029, EBI-80168;
CC       P42858; P61086: UBE2K; NbExp=24; IntAct=EBI-466029, EBI-473850;
CC       P42858; Q9UHD9: UBQLN2; NbExp=12; IntAct=EBI-466029, EBI-947187;
CC       P42858; Q92890: UFD1; NbExp=7; IntAct=EBI-466029, EBI-1994090;
CC       P42858; O75385: ULK1; NbExp=8; IntAct=EBI-466029, EBI-908831;
CC       P42858; Q495M9: USH1G; NbExp=3; IntAct=EBI-466029, EBI-8601749;
CC       P42858; Q9UMW8: USP18; NbExp=3; IntAct=EBI-466029, EBI-356206;
CC       P42858; O75604-3: USP2; NbExp=6; IntAct=EBI-466029, EBI-10696113;
CC       P42858; Q9UPU5: USP24; NbExp=21; IntAct=EBI-466029, EBI-1642365;
CC       P42858; Q8NFA0-2: USP32; NbExp=18; IntAct=EBI-466029, EBI-12220239;
CC       P42858; Q93008: USP9X; NbExp=8; IntAct=EBI-466029, EBI-302524;
CC       P42858; Q9BVJ6: UTP14A; NbExp=4; IntAct=EBI-466029, EBI-473284;
CC       P42858; Q9NYH9: UTP6; NbExp=3; IntAct=EBI-466029, EBI-749211;
CC       P42858; Q08AM6: VAC14; NbExp=3; IntAct=EBI-466029, EBI-2107455;
CC       P42858; Q9HCJ6: VAT1L; NbExp=3; IntAct=EBI-466029, EBI-10234766;
CC       P42858; P55072: VCP; NbExp=10; IntAct=EBI-466029, EBI-355164;
CC       P42858; P45880: VDAC2; NbExp=22; IntAct=EBI-466029, EBI-354022;
CC       P42858; P40337-2: VHL; NbExp=12; IntAct=EBI-466029, EBI-12157263;
CC       P42858; P09327-2: VIL1; NbExp=3; IntAct=EBI-466029, EBI-25958818;
CC       P42858; P08670: VIM; NbExp=4; IntAct=EBI-466029, EBI-353844;
CC       P42858; Q9UK41: VPS28; NbExp=16; IntAct=EBI-466029, EBI-727424;
CC       P42858; Q8NEZ2: VPS37A; NbExp=6; IntAct=EBI-466029, EBI-2850578;
CC       P42858; O75351: VPS4B; NbExp=3; IntAct=EBI-466029, EBI-2514459;
CC       P42858; Q9BTA9: WAC; NbExp=5; IntAct=EBI-466029, EBI-749118;
CC       P42858; Q9BTA9-5: WAC; NbExp=3; IntAct=EBI-466029, EBI-25956668;
CC       P42858; O75554: WBP4; NbExp=3; IntAct=EBI-466029, EBI-7251981;
CC       P42858; Q8IZQ1: WDFY3; NbExp=10; IntAct=EBI-466029, EBI-1569256;
CC       P42858; Q9GZS3: WDR61; NbExp=22; IntAct=EBI-466029, EBI-358545;
CC       P42858; A4D1P6: WDR91; NbExp=16; IntAct=EBI-466029, EBI-718046;
CC       P42858; Q15007-2: WTAP; NbExp=3; IntAct=EBI-466029, EBI-25840023;
CC       P42858; O00308: WWP2; NbExp=9; IntAct=EBI-466029, EBI-743923;
CC       P42858; Q9HCS7: XAB2; NbExp=3; IntAct=EBI-466029, EBI-295232;
CC       P42858; Q8WTP9: XAGE3; NbExp=3; IntAct=EBI-466029, EBI-6448284;
CC       P42858; P12956: XRCC6; NbExp=21; IntAct=EBI-466029, EBI-353208;
CC       P42858; O95070: YIF1A; NbExp=12; IntAct=EBI-466029, EBI-2799703;
CC       P42858; P31946: YWHAB; NbExp=11; IntAct=EBI-466029, EBI-359815;
CC       P42858; Q9H869-2: YY1AP1; NbExp=3; IntAct=EBI-466029, EBI-12150045;
CC       P42858; Q9H171: ZBP1; NbExp=6; IntAct=EBI-466029, EBI-6264672;
CC       P42858; Q05516: ZBTB16; NbExp=4; IntAct=EBI-466029, EBI-711925;
CC       P42858; O43167-2: ZBTB24; NbExp=9; IntAct=EBI-466029, EBI-25842419;
CC       P42858; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-466029, EBI-14104088;
CC       P42858; Q6PEW1: ZCCHC12; NbExp=3; IntAct=EBI-466029, EBI-748373;
CC       P42858; Q8IUH5: ZDHHC17; NbExp=30; IntAct=EBI-466029, EBI-524753;
CC       P42858; Q8WVZ1-3: ZDHHC19; NbExp=3; IntAct=EBI-466029, EBI-25961277;
CC       P42858; G3V1X1: ZFC3H1; NbExp=5; IntAct=EBI-466029, EBI-6448783;
CC       P42858; Q6ZN57: ZFP2; NbExp=12; IntAct=EBI-466029, EBI-7236323;
CC       P42858; Q96K21: ZFYVE19; NbExp=21; IntAct=EBI-466029, EBI-6448240;
CC       P42858; Q9UKY1: ZHX1; NbExp=6; IntAct=EBI-466029, EBI-347767;
CC       P42858; Q96EF9: ZHX1-C8orf76; NbExp=18; IntAct=EBI-466029, EBI-25830993;
CC       P42858; Q9BRR0: ZKSCAN3; NbExp=3; IntAct=EBI-466029, EBI-1965777;
CC       P42858; Q15776: ZKSCAN8; NbExp=9; IntAct=EBI-466029, EBI-2602314;
CC       P42858; Q96NC0: ZMAT2; NbExp=20; IntAct=EBI-466029, EBI-2682299;
CC       P42858; O95789-4: ZMYM6; NbExp=3; IntAct=EBI-466029, EBI-12949277;
CC       P42858; P52744: ZNF138; NbExp=9; IntAct=EBI-466029, EBI-10746567;
CC       P42858; Q9UJW8-4: ZNF180; NbExp=9; IntAct=EBI-466029, EBI-12055755;
CC       P42858; P17023: ZNF19; NbExp=3; IntAct=EBI-466029, EBI-12884200;
CC       P42858; Q9BSG1: ZNF2; NbExp=3; IntAct=EBI-466029, EBI-8489229;
CC       P42858; Q9Y2X9: ZNF281; NbExp=3; IntAct=EBI-466029, EBI-396200;
CC       P42858; Q9HBT8: ZNF286A; NbExp=9; IntAct=EBI-466029, EBI-10754950;
CC       P42858; Q9NR11-2: ZNF302; NbExp=3; IntAct=EBI-466029, EBI-12988373;
CC       P42858; Q8N895: ZNF366; NbExp=15; IntAct=EBI-466029, EBI-2813661;
CC       P42858; Q9C0F3: ZNF436; NbExp=15; IntAct=EBI-466029, EBI-8489702;
CC       P42858; Q8N0Y2-2: ZNF444; NbExp=9; IntAct=EBI-466029, EBI-12010736;
CC       P42858; Q6ZNH5: ZNF497; NbExp=9; IntAct=EBI-466029, EBI-10486136;
CC       P42858; O60304: ZNF500; NbExp=6; IntAct=EBI-466029, EBI-18234077;
CC       P42858; Q8N988-2: ZNF557; NbExp=12; IntAct=EBI-466029, EBI-10699005;
CC       P42858; Q68EA5: ZNF57; NbExp=15; IntAct=EBI-466029, EBI-8490788;
CC       P42858; Q7Z3I7: ZNF572; NbExp=9; IntAct=EBI-466029, EBI-10172590;
CC       P42858; Q96N77-2: ZNF641; NbExp=18; IntAct=EBI-466029, EBI-12939666;
CC       P42858; Q8N720: ZNF655; NbExp=14; IntAct=EBI-466029, EBI-625509;
CC       P42858; Q5TEC3: ZNF697; NbExp=3; IntAct=EBI-466029, EBI-25845217;
CC       P42858; Q3KNS6-3: ZNF829; NbExp=6; IntAct=EBI-466029, EBI-18036029;
CC       P42858; O15535: ZSCAN9; NbExp=9; IntAct=EBI-466029, EBI-751531;
CC       P42858; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-466029, EBI-1538838;
CC       P42858; A8K3Q9; NbExp=3; IntAct=EBI-466029, EBI-10174314;
CC       P42858; A8K878; NbExp=21; IntAct=EBI-466029, EBI-25831303;
CC       P42858; B7Z3E8; NbExp=6; IntAct=EBI-466029, EBI-25831617;
CC       P42858; Q0VG73; NbExp=6; IntAct=EBI-466029, EBI-25953074;
CC       P42858; Q7L8T7; NbExp=6; IntAct=EBI-466029, EBI-25831943;
CC       P42858; Q86V28; NbExp=6; IntAct=EBI-466029, EBI-10259496;
CC       P42858; Q96IQ6; NbExp=6; IntAct=EBI-466029, EBI-10295632;
CC       P42858; O88485: Dync1i1; Xeno; NbExp=2; IntAct=EBI-466029, EBI-492834;
CC       P42858; P54256: Hap1; Xeno; NbExp=3; IntAct=EBI-466029, EBI-994539;
CC       P42858; P51660: Hsd17b4; Xeno; NbExp=15; IntAct=EBI-466029, EBI-8328056;
CC       P42858; P29994: Itpr1; Xeno; NbExp=2; IntAct=EBI-466029, EBI-8614640;
CC       P42858; Q99KR7: Ppif; Xeno; NbExp=3; IntAct=EBI-466029, EBI-6455001;
CC   -!- SUBCELLULAR LOCATION: [Huntingtin]: Cytoplasm
CC       {ECO:0000269|PubMed:15654337, ECO:0000269|PubMed:16476778,
CC       ECO:0000269|PubMed:7647777}. Nucleus {ECO:0000269|PubMed:15654337,
CC       ECO:0000269|PubMed:16391387}. Early endosome
CC       {ECO:0000269|PubMed:16476778}. Note=The mutant Huntingtin protein
CC       colocalizes with AKAP8L in the nuclear matrix of Huntington disease
CC       neurons. Shuttles between cytoplasm and nucleus in a Ran GTPase-
CC       independent manner (PubMed:15654337). Recruits onto early endosomes in
CC       a Rab5- and HAP40-dependent fashion (PubMed:16476778).
CC       {ECO:0000269|PubMed:15654337, ECO:0000269|PubMed:16476778}.
CC   -!- SUBCELLULAR LOCATION: [Huntingtin, myristoylated N-terminal fragment]:
CC       Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:24459296}.
CC   -!- TISSUE SPECIFICITY: Expressed in the brain cortex (at protein level).
CC       Widely expressed with the highest level of expression in the brain
CC       (nerve fibers, varicosities, and nerve endings). In the brain, the
CC       regions where it can be mainly found are the cerebellar cortex, the
CC       neocortex, the striatum, and the hippocampal formation.
CC       {ECO:0000269|PubMed:16391387}.
CC   -!- DOMAIN: The N-terminal Gln-rich and Pro-rich domain has great
CC       conformational flexibility and is likely to exist in a fluctuating
CC       equilibrium of alpha-helical, random coil, and extended conformations.
CC       {ECO:0000269|PubMed:19748341}.
CC   -!- PTM: [Huntingtin]: Cleaved by caspases downstream of the polyglutamine
CC       stretch (PubMed:8696339, PubMed:9535906, PubMed:10770929,
CC       PubMed:29802276). The resulting N-terminal fragments are cytotoxic and
CC       provokes apoptosis (PubMed:10770929). {ECO:0000269|PubMed:10770929,
CC       ECO:0000269|PubMed:29802276, ECO:0000269|PubMed:8696339,
CC       ECO:0000269|PubMed:9535906}.
CC   -!- PTM: [Huntingtin]: Forms with expanded polyglutamine expansion are
CC       specifically ubiquitinated by SYVN1, which promotes their proteasomal
CC       degradation. {ECO:0000269|PubMed:17141218}.
CC   -!- PTM: [Huntingtin]: Phosphorylation at Ser-1179 and Ser-1199 by CDK5 in
CC       response to DNA damage in nuclei of neurons protects neurons against
CC       polyglutamine expansion as well as DNA damage mediated toxicity.
CC       {ECO:0000269|PubMed:17611284}.
CC   -!- PTM: [Huntingtin, myristoylated N-terminal fragment]: Myristoylated at
CC       Gly-551, following proteolytic cleavage at Asp-550.
CC       {ECO:0000269|PubMed:24459296, ECO:0000269|PubMed:29802276}.
CC   -!- POLYMORPHISM: The poly-Gln region of HTT is highly polymorphic (10 to
CC       35 repeats) in the normal population and is expanded to about 36-120
CC       repeats in Huntington disease patients. The repeat length usually
CC       increases in successive generations, but contracts also on occasion.
CC       The adjacent poly-Pro region is also polymorphic and varies between 7-
CC       12 residues. Polyglutamine expansion leads to elevated susceptibility
CC       to apopain cleavage and likely result in accelerated neuronal apoptosis
CC       (PubMed:8696339). {ECO:0000269|PubMed:8696339}.
CC   -!- DISEASE: Huntington disease (HD) [MIM:143100]: A neurodegenerative
CC       disorder characterized by involuntary movements (chorea), general motor
CC       impairment, psychiatric disorders and dementia. Onset of the disease
CC       occurs usually in the third or fourth decade of life. Onset and
CC       clinical course depend on the degree of poly-Gln repeat expansion,
CC       longer expansions resulting in earlier onset and more severe clinical
CC       manifestations. Neuropathology of Huntington disease displays a
CC       distinctive pattern with loss of neurons, especially in the caudate and
CC       putamen. {ECO:0000269|PubMed:8458085}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- DISEASE: Lopes-Maciel-Rodan syndrome (LOMARS) [MIM:617435]: An
CC       autosomal recessive neurodevelopmental disorder characterized by
CC       developmental regression in infancy, delayed psychomotor development,
CC       severe intellectual disability, and cerebral and cerebellar atrophy.
CC       Additional features include swallowing problems, dystonia,
CC       bradykinesia, and continuous manual stereotypies without chorea. Some
CC       patients manifest seizures. {ECO:0000269|PubMed:26740508,
CC       ECO:0000269|PubMed:27329733}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the huntingtin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Huntingtin entry;
CC       URL="https://en.wikipedia.org/wiki/Huntingtin";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L12392; AAB38240.1; -; mRNA.
DR   EMBL; AB016794; BAA36753.1; -; mRNA.
DR   EMBL; Z49154; CAA89024.1; -; Genomic_DNA.
DR   EMBL; Z49155; CAA89025.1; -; Genomic_DNA.
DR   EMBL; Z49208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z49769; CAA89839.1; -; Genomic_DNA.
DR   EMBL; Z68756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z69649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L27350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L27351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L27352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L27353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L27354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L34020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L20431; AAA52702.1; -; mRNA.
DR   PIR; A46068; A46068.
DR   RefSeq; NP_002102.4; NM_002111.8.
DR   PDB; 2LD0; NMR; -; A=1-17.
DR   PDB; 2LD2; NMR; -; A=1-17.
DR   PDB; 3IO4; X-ray; 3.63 A; A/B/C=1-64.
DR   PDB; 3IO6; X-ray; 3.70 A; A/B/C=1-64.
DR   PDB; 3IOR; X-ray; 3.60 A; A/B/C=1-64.
DR   PDB; 3IOT; X-ray; 3.50 A; A/B/C=1-64.
DR   PDB; 3IOU; X-ray; 3.70 A; A/B/C=1-64.
DR   PDB; 3IOV; X-ray; 3.70 A; A/B/C=1-64.
DR   PDB; 3IOW; X-ray; 3.50 A; A/B/C=1-64.
DR   PDB; 3LRH; X-ray; 2.60 A; B/D/F/H/J/L/N/P=5-18.
DR   PDB; 4FE8; X-ray; 3.00 A; A/B/C=1-64.
DR   PDB; 4FEB; X-ray; 2.80 A; A/B/C=1-64.
DR   PDB; 4FEC; X-ray; 3.00 A; A/B/C=1-64.
DR   PDB; 4FED; X-ray; 2.81 A; A/B/C=1-64.
DR   PDB; 4RAV; X-ray; 2.50 A; E/F=1-17.
DR   PDB; 6EZ8; EM; 4.00 A; A=1-3142.
DR   PDB; 6N8C; NMR; -; A/B/C/D=2-24.
DR   PDB; 6RMH; EM; 9.60 A; A=1-3142.
DR   PDB; 6X9O; EM; 2.60 A; A=1-3142.
DR   PDB; 6YEJ; EM; 18.20 A; A=18-3142.
DR   PDB; 7DXJ; EM; 3.60 A; A=1-3142.
DR   PDB; 7DXK; EM; 4.10 A; A=18-3142.
DR   PDBsum; 2LD0; -.
DR   PDBsum; 2LD2; -.
DR   PDBsum; 3IO4; -.
DR   PDBsum; 3IO6; -.
DR   PDBsum; 3IOR; -.
DR   PDBsum; 3IOT; -.
DR   PDBsum; 3IOU; -.
DR   PDBsum; 3IOV; -.
DR   PDBsum; 3IOW; -.
DR   PDBsum; 3LRH; -.
DR   PDBsum; 4FE8; -.
DR   PDBsum; 4FEB; -.
DR   PDBsum; 4FEC; -.
DR   PDBsum; 4FED; -.
DR   PDBsum; 4RAV; -.
DR   PDBsum; 6EZ8; -.
DR   PDBsum; 6N8C; -.
DR   PDBsum; 6RMH; -.
DR   PDBsum; 6X9O; -.
DR   PDBsum; 6YEJ; -.
DR   PDBsum; 7DXJ; -.
DR   PDBsum; 7DXK; -.
DR   BMRB; P42858; -.
DR   SMR; P42858; -.
DR   BioGRID; 109314; 437.
DR   CORUM; P42858; -.
DR   DIP; DIP-32492N; -.
DR   ELM; P42858; -.
DR   IntAct; P42858; 1109.
DR   MINT; P42858; -.
DR   STRING; 9606.ENSP00000347184; -.
DR   BindingDB; P42858; -.
DR   ChEMBL; CHEMBL5514; -.
DR   DrugBank; DB09130; Copper.
DR   MoonDB; P42858; Predicted.
DR   GlyGen; P42858; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P42858; -.
DR   MetOSite; P42858; -.
DR   PhosphoSitePlus; P42858; -.
DR   SwissPalm; P42858; -.
DR   BioMuta; HTT; -.
DR   DMDM; 296434520; -.
DR   EPD; P42858; -.
DR   jPOST; P42858; -.
DR   MassIVE; P42858; -.
DR   MaxQB; P42858; -.
DR   PaxDb; P42858; -.
DR   PeptideAtlas; P42858; -.
DR   PRIDE; P42858; -.
DR   ProteomicsDB; 55561; -.
DR   ABCD; P42858; 2 sequenced antibodies.
DR   Antibodypedia; 3449; 780 antibodies from 41 providers.
DR   DNASU; 3064; -.
DR   Ensembl; ENST00000355072.11; ENSP00000347184.5; ENSG00000197386.14.
DR   GeneID; 3064; -.
DR   KEGG; hsa:3064; -.
DR   MANE-Select; ENST00000355072.11; ENSP00000347184.5; NM_001388492.1; NP_001375421.1.
DR   UCSC; uc062uto.1; human.
DR   CTD; 3064; -.
DR   DisGeNET; 3064; -.
DR   GeneCards; HTT; -.
DR   GeneReviews; HTT; -.
DR   HGNC; HGNC:4851; HTT.
DR   HPA; ENSG00000197386; Low tissue specificity.
DR   MalaCards; HTT; -.
DR   MIM; 143100; phenotype.
DR   MIM; 613004; gene.
DR   MIM; 617435; phenotype.
DR   neXtProt; NX_P42858; -.
DR   OpenTargets; ENSG00000197386; -.
DR   Orphanet; 399; Huntington disease.
DR   Orphanet; 248111; Juvenile Huntington disease.
DR   Orphanet; 528084; Non-specific syndromic intellectual disability.
DR   PharmGKB; PA164741646; -.
DR   VEuPathDB; HostDB:ENSG00000197386; -.
DR   eggNOG; ENOG502QR1D; Eukaryota.
DR   GeneTree; ENSGT00390000015863; -.
DR   HOGENOM; CLU_000428_0_0_1; -.
DR   InParanoid; P42858; -.
DR   OMA; HTCSLIY; -.
DR   OrthoDB; 33894at2759; -.
DR   PhylomeDB; P42858; -.
DR   TreeFam; TF323608; -.
DR   PathwayCommons; P42858; -.
DR   Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity.
DR   SignaLink; P42858; -.
DR   SIGNOR; P42858; -.
DR   BioGRID-ORCS; 3064; 34 hits in 1086 CRISPR screens.
DR   ChiTaRS; HTT; human.
DR   EvolutionaryTrace; P42858; -.
DR   GeneWiki; Huntingtin; -.
DR   GenomeRNAi; 3064; -.
DR   Pharos; P42858; Tchem.
DR   PRO; PR:P42858; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; P42858; protein.
DR   Bgee; ENSG00000197386; Expressed in sural nerve and 132 other tissues.
DR   ExpressionAtlas; P42858; baseline and differential.
DR   Genevisible; P42858; HS.
DR   GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR   GO; GO:0030424; C:axon; IDA:UniProtKB.
DR   GO; GO:0005814; C:centriole; IDA:SYSCILIA_CCNET.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR   GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0016234; C:inclusion body; IMP:CAFA.
DR   GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:CAFA.
DR   GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR   GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
DR   GO; GO:0034452; F:dynactin binding; IPI:UniProtKB.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IDA:UniProtKB.
DR   GO; GO:0031072; F:heat shock protein binding; IPI:CAFA.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0019900; F:kinase binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR   GO; GO:0005522; F:profilin binding; IPI:UniProtKB.
DR   GO; GO:0044325; F:transmembrane transporter binding; IDA:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR   GO; GO:0099111; P:microtubule-based transport; IBA:GO_Central.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR   GO; GO:1905337; P:positive regulation of aggrephagy; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IDA:CAFA.
DR   GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0045724; P:positive regulation of cilium assembly; IMP:SYSCILIA_CCNET.
DR   GO; GO:0031587; P:positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:UniProtKB.
DR   GO; GO:1904504; P:positive regulation of lipophagy; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0031648; P:protein destabilization; IMP:CAFA.
DR   GO; GO:1905289; P:regulation of CAMKK-AMPK signaling cascade; IMP:ARUK-UCL.
DR   GO; GO:2000479; P:regulation of cAMP-dependent protein kinase activity; IMP:ARUK-UCL.
DR   GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IMP:dictyBase.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:UniProtKB.
DR   GO; GO:0047496; P:vesicle transport along microtubule; IMP:UniProtKB.
DR   GO; GO:0042297; P:vocal learning; IMP:AgBase.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000091; Huntingtin.
DR   InterPro; IPR028426; Huntingtin_fam.
DR   InterPro; IPR024613; Huntingtin_middle-repeat.
DR   PANTHER; PTHR10170; PTHR10170; 1.
DR   Pfam; PF12372; DUF3652; 1.
DR   PRINTS; PR00375; HUNTINGTIN.
DR   SUPFAM; SSF48371; SSF48371; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Apoptosis; Cytoplasm; Cytoplasmic vesicle;
KW   Disease variant; Endosome; Intellectual disability; Lipoprotein; Myristate;
KW   Neurodegeneration; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Triplet repeat expansion; Ubl conjugation.
FT   CHAIN           1..3142
FT                   /note="Huntingtin"
FT                   /id="PRO_0000083942"
FT   CHAIN           551..584
FT                   /note="Huntingtin, myristoylated N-terminal fragment"
FT                   /id="PRO_0000447477"
FT   REPEAT          204..241
FT                   /note="HEAT 1"
FT   REPEAT          246..283
FT                   /note="HEAT 2"
FT   REPEAT          316..360
FT                   /note="HEAT 3"
FT   REPEAT          802..839
FT                   /note="HEAT 4"
FT   REPEAT          902..940
FT                   /note="HEAT 5"
FT   REGION          3..13
FT                   /note="Sufficient for interaction with TPR"
FT                   /evidence="ECO:0000269|PubMed:15654337"
FT   REGION          14..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..502
FT                   /note="Interaction with ZDHHC17"
FT                   /evidence="ECO:0000269|PubMed:28757145"
FT   REGION          517..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1176..1225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2330..2351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2633..2662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2395..2404
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        14..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..82
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..583
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1205..1225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2335..2349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            511..512
FT                   /note="Cleavage; by caspase-3"
FT                   /evidence="ECO:0000269|PubMed:9535906"
FT   SITE            528..529
FT                   /note="Cleavage; by caspase-3"
FT                   /evidence="ECO:0000255"
FT   SITE            550..551
FT                   /note="Cleavage; by caspase-3"
FT                   /evidence="ECO:0000269|PubMed:29802276"
FT   SITE            584..585
FT                   /note="Cleavage; by caspase-6"
FT                   /evidence="ECO:0000269|PubMed:10770929"
FT   SITE            587..588
FT                   /note="Cleavage; by caspase-3"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         9
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21685499"
FT   MOD_RES         176
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21685499"
FT   MOD_RES         234
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21685499"
FT   MOD_RES         343
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21685499"
FT   MOD_RES         411
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42859"
FT   MOD_RES         419
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42859"
FT   MOD_RES         432
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         442
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:21685499"
FT   MOD_RES         640
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         643
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1179
FT                   /note="Phosphoserine; by CDK5"
FT                   /evidence="ECO:0000269|PubMed:17611284"
FT   MOD_RES         1199
FT                   /note="Phosphoserine; by CDK5"
FT                   /evidence="ECO:0000269|PubMed:17611284,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1870
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231"
FT   MOD_RES         1874
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   LIPID           551
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000269|PubMed:24459296,
FT                   ECO:0000269|PubMed:29802276"
FT   VARIANT         18
FT                   /note="Q -> QQQ"
FT                   /id="VAR_005268"
FT   VARIANT         551
FT                   /note="G -> E (inhibits proteolytic cleavage at D-550;
FT                   abolishes post-translational myristoylation; results in
FT                   increased cleavage at D-511; dbSNP:rs118005095)"
FT                   /evidence="ECO:0000269|PubMed:29802276"
FT                   /id="VAR_081737"
FT   VARIANT         703
FT                   /note="P -> L (in LOMARS; dbSNP:rs768047421)"
FT                   /evidence="ECO:0000269|PubMed:26740508"
FT                   /id="VAR_079026"
FT   VARIANT         893
FT                   /note="G -> R (in dbSNP:rs363075)"
FT                   /id="VAR_060170"
FT   VARIANT         1064
FT                   /note="V -> I (in dbSNP:rs35892913)"
FT                   /id="VAR_060171"
FT   VARIANT         1091
FT                   /note="I -> M (in dbSNP:rs1143646)"
FT                   /id="VAR_060172"
FT   VARIANT         1173
FT                   /note="T -> A (in dbSNP:rs3025843)"
FT                   /id="VAR_060173"
FT   VARIANT         1260
FT                   /note="T -> M (found in a patient with Rett syndrome-like
FT                   phenotype; unknown pathological significance;
FT                   dbSNP:rs34315806)"
FT                   /evidence="ECO:0000269|PubMed:26740508"
FT                   /id="VAR_060174"
FT   VARIANT         1382
FT                   /note="E -> A (in dbSNP:rs3025837)"
FT                   /id="VAR_054017"
FT   VARIANT         1385
FT                   /note="N -> H (in dbSNP:rs3025837)"
FT                   /id="VAR_060175"
FT   VARIANT         1720
FT                   /note="T -> N (in dbSNP:rs363125)"
FT                   /id="VAR_060176"
FT   VARIANT         2113
FT                   /note="D -> Y (in dbSNP:rs1143648)"
FT                   /id="VAR_060177"
FT   VARIANT         2309
FT                   /note="Y -> H (in dbSNP:rs362331)"
FT                   /id="VAR_060178"
FT   VARIANT         2717
FT                   /note="F -> L (in LOMARS; dbSNP:rs1085307052)"
FT                   /evidence="ECO:0000269|PubMed:27329733"
FT                   /id="VAR_079027"
FT   VARIANT         2786
FT                   /note="V -> I (in dbSNP:rs362272)"
FT                   /evidence="ECO:0000269|PubMed:7903579"
FT                   /id="VAR_060179"
FT   MUTAGEN         495
FT                   /note="I->A: Inhibits interaction with ZDHHC13 and
FT                   ZDHHC17."
FT                   /evidence="ECO:0000269|PubMed:26198635"
FT   MUTAGEN         498..499
FT                   /note="QP->AA: Abolishes interaction with ZDHHC17."
FT                   /evidence="ECO:0000269|PubMed:28757145"
FT   MUTAGEN         498
FT                   /note="Q->A: Inhibits interaction with ZDHHC13 and
FT                   ZDHHC17."
FT                   /evidence="ECO:0000269|PubMed:26198635"
FT   MUTAGEN         499
FT                   /note="P->A: Inhibits interaction with ZDHHC13 and
FT                   ZDHHC17."
FT                   /evidence="ECO:0000269|PubMed:26198635"
FT   MUTAGEN         511
FT                   /note="D->A: Loss of proteolytic cleavage."
FT                   /evidence="ECO:0000269|PubMed:9535906"
FT   MUTAGEN         528
FT                   /note="D->A: No effect on proteolytic cleavage."
FT                   /evidence="ECO:0000269|PubMed:9535906"
FT   MUTAGEN         550
FT                   /note="D->E: Loss of proteolytic cleavage. Loss of
FT                   myristoylation."
FT                   /evidence="ECO:0000269|PubMed:29802276"
FT   MUTAGEN         551
FT                   /note="G->A: Loss of myristoylation."
FT                   /evidence="ECO:0000269|PubMed:24459296,
FT                   ECO:0000269|PubMed:29802276"
FT   MUTAGEN         551
FT                   /note="G->S: Loss of myristoylation."
FT                   /evidence="ECO:0000269|PubMed:29802276"
FT   MUTAGEN         584
FT                   /note="D->A: Loss of proteolytic cleavage."
FT                   /evidence="ECO:0000269|PubMed:10770929"
FT   CONFLICT        823
FT                   /note="C -> S (in Ref. 2; BAA36753)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..10
FT                   /evidence="ECO:0007829|PDB:4RAV"
FT   STRAND          13..15
FT                   /evidence="ECO:0007829|PDB:4RAV"
FT   HELIX           23..26
FT                   /evidence="ECO:0007829|PDB:3IOT"
FT   TURN            30..32
FT                   /evidence="ECO:0007829|PDB:3IOT"
FT   HELIX           97..109
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           119..132
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           135..137
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          139..141
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           142..157
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           159..175
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           180..191
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           192..196
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           202..217
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           222..239
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           240..242
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           245..256
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           257..260
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           264..279
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          281..283
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           284..297
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          302..304
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           309..321
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           322..324
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           351..364
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           370..385
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           389..396
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          397..399
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           400..403
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          676..678
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           680..692
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          696..699
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            704..706
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           709..725
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           727..731
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          732..734
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            741..743
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           750..758
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            762..764
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           765..782
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           787..797
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           804..806
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           808..815
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           820..838
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           843..853
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           854..858
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           862..873
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           877..886
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            890..893
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           894..896
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           903..910
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            911..913
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           914..917
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           921..934
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           935..937
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           949..961
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           996..1014
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1019..1035
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            1038..1040
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            1042..1045
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1065..1074
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          1076..1078
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1079..1081
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1083..1098
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1101..1103
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1135..1156
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1234..1250
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1262..1277
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1278..1280
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1283..1286
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            1287..1289
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1290..1300
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            1301..1303
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1305..1319
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            1324..1326
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            1356..1359
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1360..1372
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1422..1425
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1426..1438
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1442..1457
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1462..1465
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          1467..1469
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1470..1484
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            1491..1493
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1494..1506
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          1508..1515
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1517..1529
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          1530..1532
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            1534..1537
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1538..1550
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1563..1577
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            1578..1580
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1582..1598
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1602..1620
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1628..1640
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1643..1646
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1650..1656
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          1663..1665
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1666..1686
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1689..1698
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1703..1706
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1708..1715
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1736..1756
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            1760..1763
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1766..1788
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          1789..1791
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1793..1803
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          1808..1812
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1815..1823
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            1824..1828
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1830..1842
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            1848..1850
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1851..1854
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1889..1908
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1914..1929
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            1930..1932
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1934..1944
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1947..1958
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            1959..1965
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1967..1978
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1982..1984
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           1987..1994
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2002..2021
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2024..2030
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2033..2045
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2048..2051
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2053..2066
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2097..2108
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2116..2123
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2128..2130
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            2131..2136
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2142..2144
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2145..2156
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            2157..2159
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2163..2181
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2201..2208
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2215..2217
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2218..2229
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2232..2234
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2237..2239
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2245..2266
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          2267..2269
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2272..2285
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2289..2295
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2301..2319
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2354..2368
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            2369..2374
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2379..2381
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          2386..2388
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2389..2400
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2403..2409
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2413..2417
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          2426..2429
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2437..2439
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2443..2456
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2461..2475
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2498..2512
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          2516..2518
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            2522..2524
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          2537..2542
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2543..2562
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2594..2596
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            2598..2600
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2619..2625
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          2663..2666
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2668..2680
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2694..2707
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            2708..2710
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2714..2730
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          2736..2738
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2739..2752
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          2757..2760
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2763..2771
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2776..2790
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2802..2816
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          2821..2824
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2826..2842
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            2844..2846
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            2851..2853
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2854..2863
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            2867..2869
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2872..2887
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2897..2900
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            2904..2906
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2912..2928
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2952..2967
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2970..2987
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2990..2992
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           2994..3001
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           3009..3023
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            3024..3027
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           3031..3037
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   STRAND          3040..3042
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           3049..3062
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            3067..3069
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           3070..3072
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           3073..3077
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           3085..3100
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            3101..3103
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           3106..3116
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           3117..3119
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   TURN            3122..3126
FT                   /evidence="ECO:0007829|PDB:6X9O"
FT   HELIX           3127..3135
FT                   /evidence="ECO:0007829|PDB:6X9O"
SQ   SEQUENCE   3142 AA;  347603 MW;  A267509E84D52F0D CRC64;
     MATLEKLMKA FESLKSFQQQ QQQQQQQQQQ QQQQQQQQPP PPPPPPPPPQ LPQPPPQAQP
     LLPQPQPPPP PPPPPPGPAV AEEPLHRPKK ELSATKKDRV NHCLTICENI VAQSVRNSPE
     FQKLLGIAME LFLLCSDDAE SDVRMVADEC LNKVIKALMD SNLPRLQLEL YKEIKKNGAP
     RSLRAALWRF AELAHLVRPQ KCRPYLVNLL PCLTRTSKRP EESVQETLAA AVPKIMASFG
     NFANDNEIKV LLKAFIANLK SSSPTIRRTA AGSAVSICQH SRRTQYFYSW LLNVLLGLLV
     PVEDEHSTLL ILGVLLTLRY LVPLLQQQVK DTSLKGSFGV TRKEMEVSPS AEQLVQVYEL
     TLHHTQHQDH NVVTGALELL QQLFRTPPPE LLQTLTAVGG IGQLTAAKEE SGGRSRSGSI
     VELIAGGGSS CSPVLSRKQK GKVLLGEEEA LEDDSESRSD VSSSALTASV KDEISGELAA
     SSGVSTPGSA GHDIITEQPR SQHTLQADSV DLASCDLTSS ATDGDEEDIL SHSSSQVSAV
     PSDPAMDLND GTQASSPISD SSQTTTEGPD SAVTPSDSSE IVLDGTDNQY LGLQIGQPQD
     EDEEATGILP DEASEAFRNS SMALQQAHLL KNMSHCRQPS DSSVDKFVLR DEATEPGDQE
     NKPCRIKGDI GQSTDDDSAP LVHCVRLLSA SFLLTGGKNV LVPDRDVRVS VKALALSCVG
     AAVALHPESF FSKLYKVPLD TTEYPEEQYV SDILNYIDHG DPQVRGATAI LCGTLICSIL
     SRSRFHVGDW MGTIRTLTGN TFSLADCIPL LRKTLKDESS VTCKLACTAV RNCVMSLCSS
     SYSELGLQLI IDVLTLRNSS YWLVRTELLE TLAEIDFRLV SFLEAKAENL HRGAHHYTGL
     LKLQERVLNN VVIHLLGDED PRVRHVAAAS LIRLVPKLFY KCDQGQADPV VAVARDQSSV
     YLKLLMHETQ PPSHFSVSTI TRIYRGYNLL PSITDVTMEN NLSRVIAAVS HELITSTTRA
     LTFGCCEALC LLSTAFPVCI WSLGWHCGVP PLSASDESRK SCTVGMATMI LTLLSSAWFP
     LDLSAHQDAL ILAGNLLAAS APKSLRSSWA SEEEANPAAT KQEEVWPALG DRALVPMVEQ
     LFSHLLKVIN ICAHVLDDVA PGPAIKAALP SLTNPPSLSP IRRKGKEKEP GEQASVPLSP
     KKGSEASAAS RQSDTSGPVT TSKSSSLGSF YHLPSYLKLH DVLKATHANY KVTLDLQNST
     EKFGGFLRSA LDVLSQILEL ATLQDIGKCV EEILGYLKSC FSREPMMATV CVQQLLKTLF
     GTNLASQFDG LSSNPSKSQG RAQRLGSSSV RPGLYHYCFM APYTHFTQAL ADASLRNMVQ
     AEQENDTSGW FDVLQKVSTQ LKTNLTSVTK NRADKNAIHN HIRLFEPLVI KALKQYTTTT
     CVQLQKQVLD LLAQLVQLRV NYCLLDSDQV FIGFVLKQFE YIEVGQFRES EAIIPNIFFF
     LVLLSYERYH SKQIIGIPKI IQLCDGIMAS GRKAVTHAIP ALQPIVHDLF VLRGTNKADA
     GKELETQKEV VVSMLLRLIQ YHQVLEMFIL VLQQCHKENE DKWKRLSRQI ADIILPMLAK
     QQMHIDSHEA LGVLNTLFEI LAPSSLRPVD MLLRSMFVTP NTMASVSTVQ LWISGILAIL
     RVLISQSTED IVLSRIQELS FSPYLISCTV INRLRDGDST STLEEHSEGK QIKNLPEETF
     SRFLLQLVGI LLEDIVTKQL KVEMSEQQHT FYCQELGTLL MCLIHIFKSG MFRRITAAAT
     RLFRSDGCGG SFYTLDSLNL RARSMITTHP ALVLLWCQIL LLVNHTDYRW WAEVQQTPKR
     HSLSSTKLLS PQMSGEEEDS DLAAKLGMCN REIVRRGALI LFCDYVCQNL HDSEHLTWLI
     VNHIQDLISL SHEPPVQDFI SAVHRNSAAS GLFIQAIQSR CENLSTPTML KKTLQCLEGI
     HLSQSGAVLT LYVDRLLCTP FRVLARMVDI LACRRVEMLL AANLQSSMAQ LPMEELNRIQ
     EYLQSSGLAQ RHQRLYSLLD RFRLSTMQDS LSPSPPVSSH PLDGDGHVSL ETVSPDKDWY
     VHLVKSQCWT RSDSALLEGA ELVNRIPAED MNAFMMNSEF NLSLLAPCLS LGMSEISGGQ
     KSALFEAARE VTLARVSGTV QQLPAVHHVF QPELPAEPAA YWSKLNDLFG DAALYQSLPT
     LARALAQYLV VVSKLPSHLH LPPEKEKDIV KFVVATLEAL SWHLIHEQIP LSLDLQAGLD
     CCCLALQLPG LWSVVSSTEF VTHACSLIYC VHFILEAVAV QPGEQLLSPE RRTNTPKAIS
     EEEEEVDPNT QNPKYITAAC EMVAEMVESL QSVLALGHKR NSGVPAFLTP LLRNIIISLA
     RLPLVNSYTR VPPLVWKLGW SPKPGGDFGT AFPEIPVEFL QEKEVFKEFI YRINTLGWTS
     RTQFEETWAT LLGVLVTQPL VMEQEESPPE EDTERTQINV LAVQAITSLV LSAMTVPVAG
     NPAVSCLEQQ PRNKPLKALD TRFGRKLSII RGIVEQEIQA MVSKRENIAT HHLYQAWDPV
     PSLSPATTGA LISHEKLLLQ INPERELGSM SYKLGQVSIH SVWLGNSITP LREEEWDEEE
     EEEADAPAPS SPPTSPVNSR KHRAGVDIHS CSQFLLELYS RWILPSSSAR RTPAILISEV
     VRSLLVVSDL FTERNQFELM YVTLTELRRV HPSEDEILAQ YLVPATCKAA AVLGMDKAVA
     EPVSRLLEST LRSSHLPSRV GALHGVLYVL ECDLLDDTAK QLIPVISDYL LSNLKGIAHC
     VNIHSQQHVL VMCATAFYLI ENYPLDVGPE FSASIIQMCG VMLSGSEEST PSIIYHCALR
     GLERLLLSEQ LSRLDAESLV KLSVDRVNVH SPHRAMAALG LMLTCMYTGK EKVSPGRTSD
     PNPAAPDSES VIVAMERVSV LFDRIRKGFP CEARVVARIL PQFLDDFFPP QDIMNKVIGE
     FLSNQQPYPQ FMATVVYKVF QTLHSTGQSS MVRDWVMLSL SNFTQRAPVA MATWSLSCFF
     VSASTSPWVA AILPHVISRM GKLEQVDVNL FCLVATDFYR HQIEEELDRR AFQSVLEVVA
     APGSPYHRLL TCLRNVHKVT TC
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024