UBQL1_HUMAN
ID UBQL1_HUMAN Reviewed; 589 AA.
AC Q9UMX0; A0A024R284; Q5T6J5; Q5T6J9; Q8IXS9; Q8N2Q3; Q9H0T8; Q9H3R4; Q9HAZ5;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Ubiquilin-1;
DE AltName: Full=Protein linking IAP with cytoskeleton 1;
DE Short=PLIC-1;
DE Short=hPLIC-1;
GN Name=UBQLN1; Synonyms=DA41, PLIC1;
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] (ISOFORM 1), INTERACTION WITH PSEN1 AND PSEN2,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11076969; DOI=10.1083/jcb.151.4.847;
RA Mah A.L., Perry G., Smith M.A., Monteiro M.J.;
RT "Identification of ubiquilin, a novel presenilin interactor that increases
RT presenilin protein accumulation.";
RL J. Cell Biol. 151:847-862(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Mah A.L., Monteiro M.J.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH UBE3A; BTRC
RP AND THE PROTEASOME.
RC TISSUE=B-cell;
RX PubMed=10983987; DOI=10.1016/s1097-2765(00)00040-x;
RA Kleijnen M.F., Shih A.H., Zhou P., Kumar S., Soccio R.E., Kedersha N.L.,
RA Gill G., Howley P.M.;
RT "The hPLIC proteins may provide a link between the ubiquitination machinery
RT and the proteasome.";
RL Mol. Cell 6:409-419(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=10807547; DOI=10.1007/s100380050209;
RA Hanaoka E., Ozaki T., Ohira M., Nakamura Y., Suzuki M., Takahashi E.,
RA Moriya H., Nakagawara A., Sakiyama S.;
RT "Molecular cloning and expression analysis of the human DA41 gene and its
RT mapping to chromosome 9q21.2-q21.3.";
RL J. Hum. Genet. 45:188-191(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li J.Y.;
RT "Human testis protein.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-316.
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
RP PROTEIN SEQUENCE OF 71-83; 207-236; 244-253 AND 547-582, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [12]
RP PHOSPHORYLATION, INTERACTION WITH MTOR, AND TISSUE SPECIFICITY.
RX PubMed=11853878; DOI=10.1016/s0167-4889(01)00164-1;
RA Wu S., Mikhailov A., Kallo-Hosein H., Hara K., Yonezawa K., Avruch J.;
RT "Characterization of ubiquilin 1, an mTOR-interacting protein.";
RL Biochim. Biophys. Acta 1542:41-56(2002).
RN [13]
RP INTERACTION WITH P4HB.
RX PubMed=12095988; DOI=10.1074/jbc.m203412200;
RA Ko H.S., Uehara T., Nomura Y.;
RT "Role of ubiquilin associated with protein-disulfide isomerase in the
RT endoplasmic reticulum in stress-induced apoptotic cell death.";
RL J. Biol. Chem. 277:35386-35392(2002).
RN [14]
RP FUNCTION, DOMAIN UBIQUITIN-LIKE, DOMAIN UBA, AND INTERACTION WITH UBA52;
RP PSMD3 AND PSMD4.
RX PubMed=15147878; DOI=10.1016/j.febslet.2004.04.031;
RA Ko H.S., Uehara T., Tsuruma K., Nomura Y.;
RT "Ubiquilin interacts with ubiquitylated proteins and proteasome through its
RT ubiquitin-associated and ubiquitin-like domains.";
RL FEBS Lett. 566:110-114(2004).
RN [15]
RP INTERACTION WITH EPS15; EPS15L1; HGS AND STAM2, SUBCELLULAR LOCATION, AND
RP UBIQUITINATION.
RX PubMed=16159959; DOI=10.1242/jcs.02571;
RA Regan-Klapisz E., Sorokina I., Voortman J., de Keizer P., Roovers R.C.,
RA Verheesen P., Urbe S., Fallon L., Fon E.A., Verkleij A., Benmerah A.,
RA van Bergen en Henegouwen P.M.;
RT "Ubiquilin recruits Eps15 into ubiquitin-rich cytoplasmic aggregates via a
RT UIM-UBL interaction.";
RL J. Cell Sci. 118:4437-4450(2005).
RN [16]
RP SUBUNIT, HETERODIMERIZATION WITH UBQLN2, AND INTERACTION WITH PSEN1 AND
RP PSEN2.
RX PubMed=16813565; DOI=10.1042/bj20060441;
RA Ford D.L., Monteiro M.J.;
RT "Dimerization of ubiquilin is dependent upon the central region of the
RT protein: evidence that the monomer, but not the dimer, is involved in
RT binding presenilins.";
RL Biochem. J. 399:397-404(2006).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human 26S
RT proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [18]
RP FUNCTION, AND INTERACTION WITH HERPUD1.
RX PubMed=18307982; DOI=10.1016/j.bbrc.2008.02.086;
RA Kim T.Y., Kim E., Yoon S.K., Yoon J.B.;
RT "Herp enhances ER-associated protein degradation by recruiting
RT ubiquilins.";
RL Biochem. Biophys. Res. Commun. 369:741-746(2008).
RN [19]
RP INTERACTION WITH EPS15.
RX PubMed=18199683; DOI=10.1091/mbc.e07-08-0775;
RA N'Diaye E.N., Hanyaloglu A.C., Kajihara K.K., Puthenveedu M.A., Wu P.,
RA von Zastrow M., Brown E.J.;
RT "The ubiquitin-like protein PLIC-2 is a negative regulator of G protein-
RT coupled receptor endocytosis.";
RL Mol. Biol. Cell 19:1252-1260(2008).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [21]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN UBA.
RX PubMed=19148225; DOI=10.1038/embor.2008.238;
RA N'Diaye E.N., Kajihara K.K., Hsieh I., Morisaki H., Debnath J., Brown E.J.;
RT "PLIC proteins or ubiquilins regulate autophagy-dependent cell survival
RT during nutrient starvation.";
RL EMBO Rep. 10:173-179(2009).
RN [22]
RP FUNCTION, INTERACTION WITH UBXN4, IDENTIFICATION IN A COMPLEX WITH UBXN4
RP AND VCP, AND SUBCELLULAR LOCATION.
RX PubMed=19822669; DOI=10.1083/jcb.200903024;
RA Lim P.J., Danner R., Liang J., Doong H., Harman C., Srinivasan D.,
RA Rothenberg C., Wang H., Ye Y., Fang S., Monteiro M.J.;
RT "Ubiquilin and p97/VCP bind erasin, forming a complex involved in ERAD.";
RL J. Cell Biol. 187:201-217(2009).
RN [23]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18953672; DOI=10.1007/s12031-008-9155-6;
RA Lu A., Hiltunen M., Romano D.M., Soininen H., Hyman B.T., Bertram L.,
RA Tanzi R.E.;
RT "Effects of ubiquilin 1 on the unfolded protein response.";
RL J. Mol. Neurosci. 38:19-30(2009).
RN [24]
RP REVIEW.
RX PubMed=20729634; DOI=10.4161/auto.6.7.13118;
RA Rothenberg C., Monteiro M.J.;
RT "Ubiquilin at a crossroads in protein degradation pathways.";
RL Autophagy 6:979-980(2010).
RN [25]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH UBQLN2 AND
RP MAP1LC3A/B/C, AND PROTEOLYTIC DEGRADATION.
RX PubMed=20529957; DOI=10.1093/hmg/ddq231;
RA Rothenberg C., Srinivasan D., Mah L., Kaushik S., Peterhoff C.M.,
RA Ugolino J., Fang S., Cuervo A.M., Nixon R.A., Monteiro M.J.;
RT "Ubiquilin functions in autophagy and is degraded by chaperone-mediated
RT autophagy.";
RL Hum. Mol. Genet. 19:3219-3232(2010).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [27]
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 [28]
RP REVIEW.
RX PubMed=21966562; DOI=10.4161/cib.4.4.15283;
RA Haapasalo A., Viswanathan J., Kurkinen K.M., Bertram L., Soininen H.,
RA Dantuma N.P., Tanzi R.E., Hiltunen M.;
RT "Involvement of ubiquilin-1 transcript variants in protein degradation and
RT accumulation.";
RL Commun. Integr. Biol. 4:428-432(2011).
RN [29]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TICAM1.
RX PubMed=21695056; DOI=10.1371/journal.pone.0021153;
RA Biswas N., Liu S., Ronni T., Aussenberg S.E., Liu W., Fujita T., Wang T.;
RT "The ubiquitin-like protein PLIC-1 or ubiquilin 1 inhibits TLR3-Trif
RT signaling.";
RL PLoS ONE 6:E21153-E21153(2011).
RN [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PSEN1.
RX PubMed=21143716; DOI=10.1111/j.1600-0854.2010.01149.x;
RA Viswanathan J., Haapasalo A., Bottcher C., Miettinen R., Kurkinen K.M.,
RA Lu A., Thomas A., Maynard C.J., Romano D., Hyman B.T., Berezovska O.,
RA Bertram L., Soininen H., Dantuma N.P., Tanzi R.E., Hiltunen M.;
RT "Alzheimer's disease-associated ubiquilin-1 regulates presenilin-1
RT accumulation and aggresome formation.";
RL Traffic 12:330-348(2011).
RN [32]
RP REVIEW.
RX PubMed=22628307; DOI=10.1515/hsz-2012-0120;
RA Lee D.Y., Brown E.J.;
RT "Ubiquilins in the crosstalk among proteolytic pathways.";
RL Biol. Chem. 393:441-447(2012).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [34]
RP FUNCTION, AND INTERACTION WITH BCL2L10.
RX PubMed=22233804; DOI=10.1073/pnas.1119167109;
RA Beverly L.J., Lockwood W.W., Shah P.P., Erdjument-Bromage H., Varmus H.;
RT "Ubiquitination, localization, and stability of an anti-apoptotic BCL2-like
RT protein, BCL2L10/BCLb, are regulated by Ubiquilin1.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E119-E126(2012).
RN [35]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UBQLN4 AND
RP MAP1LC3A/B/C.
RX PubMed=23459205; DOI=10.1038/embor.2013.22;
RA Lee D.Y., Arnott D., Brown E.J.;
RT "Ubiquilin4 is an adaptor protein that recruits Ubiquilin1 to the autophagy
RT machinery.";
RL EMBO Rep. 14:373-381(2013).
RN [36]
RP REVIEW.
RX PubMed=23600477; DOI=10.1517/14728222.2013.791284;
RA Takalo M., Haapasalo A., Natunen T., Viswanathan J., Kurkinen K.M.,
RA Tanzi R.E., Soininen H., Hiltunen M.;
RT "Targeting ubiquilin-1 in Alzheimer's disease.";
RL Expert Opin. Ther. Targets 17:795-810(2013).
RN [37]
RP INTERACTION WITH TREX1, AND SUBCELLULAR LOCATION.
RX PubMed=23979357; DOI=10.1074/jbc.m113.503391;
RA Orebaugh C.D., Fye J.M., Harvey S., Hollis T., Wilkinson J.C.,
RA Perrino F.W.;
RT "The TREX1 C-terminal region controls cellular localization through
RT ubiquitination.";
RL J. Biol. Chem. 288:28881-28892(2013).
RN [38]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [39]
RP FUNCTION, INTERACTION WITH ORAI1, AND SUBCELLULAR LOCATION.
RX PubMed=23307288; DOI=10.1007/s10059-013-2268-7;
RA Lee J.E., Jeon I.S., Han N.E., Song H.J., Kim E.G., Choi J.W., Song K.D.,
RA Lee H.K., Choi J.K.;
RT "Ubiquilin 1 interacts with Orai1 to regulate calcium mobilization.";
RL Mol. Cells 35:41-46(2013).
RN [40]
RP REVIEW.
RX PubMed=24674348; DOI=10.1186/1471-2148-14-63;
RA Marin I.;
RT "The ubiquilin gene family: evolutionary patterns and functional
RT insights.";
RL BMC Evol. Biol. 14:63-63(2014).
RN [41]
RP STRUCTURE BY NMR OF 541-586 ALONE AND IN COMPLEX WITH UBIQUITIN.
RX PubMed=18241885; DOI=10.1016/j.jmb.2007.12.029;
RA Zhang D., Raasi S., Fushman D.;
RT "Affinity makes the difference: nonselective interaction of the UBA domain
RT of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains.";
RL J. Mol. Biol. 377:162-180(2008).
CC -!- FUNCTION: Plays an important role in the regulation of different
CC protein degradation mechanisms and pathways including ubiquitin-
CC proteasome system (UPS), autophagy and endoplasmic reticulum-associated
CC protein degradation (ERAD) pathway. Mediates the proteasomal targeting
CC of misfolded or accumulated proteins for degradation by binding (via
CC UBA domain) to their polyubiquitin chains and by interacting (via
CC ubiquitin-like domain) with the subunits of the proteasome
CC (PubMed:15147878). Plays a role in the ERAD pathway via its interaction
CC with ER-localized proteins UBXN4, VCP and HERPUD1 and may form a link
CC between the polyubiquitinated ERAD substrates and the proteasome
CC (PubMed:19822669, PubMed:18307982). Involved in the regulation of
CC macroautophagy and autophagosome formation; required for maturation of
CC autophagy-related protein LC3 from the cytosolic form LC3-I to the
CC membrane-bound form LC3-II and may assist in the maturation of
CC autophagosomes to autolysosomes by mediating autophagosome-lysosome
CC fusion (PubMed:19148225, PubMed:20529957, PubMed:23459205). Negatively
CC regulates the TICAM1/TRIF-dependent toll-like receptor signaling
CC pathway by decreasing the abundance of TICAM1 via the autophagic
CC pathway (PubMed:21695056). Promotes the ubiquitination and lysosomal
CC degradation of ORAI1, consequently down-regulating the ORAI1-mediated
CC Ca2+ mobilization (PubMed:23307288). Suppresses the maturation and
CC proteasomal degradation of amyloid beta A4 protein (A4) by stimulating
CC the lysine 63 (K63)-linked polyubiquitination. Delays the maturation of
CC A4 by sequestering it in the Golgi apparatus and preventing its
CC transport to the cell surface for subsequent processing (By
CC similarity). Ubiquitinates BCL2L10 and thereby stabilizes protein
CC abundance (PubMed:22233804). {ECO:0000250|UniProtKB:Q9JJP9,
CC ECO:0000269|PubMed:18307982, ECO:0000269|PubMed:19148225,
CC ECO:0000269|PubMed:19822669, ECO:0000269|PubMed:20529957,
CC ECO:0000269|PubMed:21695056, ECO:0000269|PubMed:22233804,
CC ECO:0000269|PubMed:23307288, ECO:0000269|PubMed:23459205,
CC ECO:0000303|PubMed:15147878}.
CC -!- FUNCTION: [Isoform 1]: Plays a role in unfolded protein response (UPR)
CC by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5
CC and PDIA2 during ER stress (PubMed:18953672). Plays a key role in the
CC regulation of the levels of PSEN1 by targeting its accumulation to
CC aggresomes which may then be removed from cells by autophagocytosis
CC (PubMed:21143716). {ECO:0000269|PubMed:18953672,
CC ECO:0000269|PubMed:21143716}.
CC -!- FUNCTION: [Isoform 2]: Plays a role in unfolded protein response (UPR)
CC by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5
CC and PDIA2 during ER stress. {ECO:0000269|PubMed:18953672}.
CC -!- FUNCTION: [Isoform 3]: Plays a role in unfolded protein response (UPR)
CC by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5
CC and PDIA2 during ER stress (PubMed:18953672). Plays a key role in the
CC regulation of the levels of PSEN1 by targeting its accumulation to
CC aggresomes which may then be removed from cells by autophagocytosis
CC (PubMed:21143716). {ECO:0000269|PubMed:18953672,
CC ECO:0000269|PubMed:21143716}.
CC -!- SUBUNIT: Monomer and homodimer (PubMed:16813565). Heterodimer with
CC UBQLN2 (PubMed:16813565). Binds CD47, NBL1, GABRA1, GABRA2, GABRA3,
CC GABRA6, GABRB1, GABRB2 and GABRB3 (By similarity). Binds UBE3A, BTRC,
CC P4HB and MTOR. Interacts with the proteasome 19S subunit. Interacts
CC (via ubiquitin-like domain) with TREX1; the interaction is direct and
CC may control TREX1 subcellular location. Forms a complex with UBXN4 and
CC VCP. Interacts (via UBA domain) with UBQLN4 (via ubiquitin-like
CC domain). Found in a complex with UBQLN2 and MAP1LC3A/B/C. The monomeric
CC form interacts with PSEN2. The monomeric form interacts with PSEN1
CC (PubMed:11076969, PubMed:21143716). Interacts with ORAI1. Interacts
CC (via UBA domain) with TICAM1. Interacts with EPS15. Interacts (via UBA
CC domain) with UBA52 and (via ubiquitin-like domain) with PSMD3 and
CC PSMD4. Interacts with HERPUD1. Interacts with MAP1LC3A/B/C in the
CC presence of UBQLN4. Interacts (via ubiquitin-like domain) with EPS15
CC (via UIM domains) and both the ubiquitinated and non-ubiquitinated
CC forms can interact with EPS15. Interacts (via ubiquitin-like domain)
CC with EPS15L1, HGS (via UIM domain) and STAM2 (via UIM domain).
CC Interacts with BCL2L10/BCL-B; in the cytoplasm (PubMed:22233804).
CC {ECO:0000250|UniProtKB:Q8R317, ECO:0000250|UniProtKB:Q9JJP9,
CC ECO:0000269|PubMed:10983987, ECO:0000269|PubMed:11076969,
CC ECO:0000269|PubMed:11853878, ECO:0000269|PubMed:12095988,
CC ECO:0000269|PubMed:15147878, ECO:0000269|PubMed:16159959,
CC ECO:0000269|PubMed:16813565, ECO:0000269|PubMed:18199683,
CC ECO:0000269|PubMed:18241885, ECO:0000269|PubMed:18307982,
CC ECO:0000269|PubMed:19822669, ECO:0000269|PubMed:20529957,
CC ECO:0000269|PubMed:21143716, ECO:0000269|PubMed:21695056,
CC ECO:0000269|PubMed:22233804, ECO:0000269|PubMed:23307288,
CC ECO:0000269|PubMed:23459205, ECO:0000269|PubMed:23979357}.
CC -!- SUBUNIT: [Isoform 1]: Monomeric form interacts with PSEN1.
CC {ECO:0000269|PubMed:16813565}.
CC -!- SUBUNIT: [Isoform 3]: Monomeric form interacts with PSEN1.
CC {ECO:0000269|PubMed:16813565}.
CC -!- INTERACTION:
CC Q9UMX0; O00154: ACOT7; NbExp=3; IntAct=EBI-741480, EBI-948905;
CC Q9UMX0; O00154-4: ACOT7; NbExp=3; IntAct=EBI-741480, EBI-12007918;
CC Q9UMX0; Q16186: ADRM1; NbExp=4; IntAct=EBI-741480, EBI-954387;
CC Q9UMX0; Q9NUQ2: AGPAT5; NbExp=6; IntAct=EBI-741480, EBI-6916385;
CC Q9UMX0; O95994: AGR2; NbExp=9; IntAct=EBI-741480, EBI-712648;
CC Q9UMX0; Q8TD06: AGR3; NbExp=4; IntAct=EBI-741480, EBI-3925742;
CC Q9UMX0; P23352: ANOS1; NbExp=3; IntAct=EBI-741480, EBI-5272188;
CC Q9UMX0; D3DTF8: APLN; NbExp=3; IntAct=EBI-741480, EBI-22002556;
CC Q9UMX0; P55056: APOC4; NbExp=3; IntAct=EBI-741480, EBI-18302142;
CC Q9UMX0; P05067: APP; NbExp=3; IntAct=EBI-741480, EBI-77613;
CC Q9UMX0; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-741480, EBI-5280499;
CC Q9UMX0; P50553: ASCL1; NbExp=3; IntAct=EBI-741480, EBI-957042;
CC Q9UMX0; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-741480, EBI-10254793;
CC Q9UMX0; P54252: ATXN3; NbExp=6; IntAct=EBI-741480, EBI-946046;
CC Q9UMX0; P46379-2: BAG6; NbExp=3; IntAct=EBI-741480, EBI-10988864;
CC Q9UMX0; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-741480, EBI-742750;
CC Q9UMX0; Q9UQB8-6: BAIAP2; NbExp=3; IntAct=EBI-741480, EBI-9092016;
CC Q9UMX0; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-741480, EBI-2548012;
CC Q9UMX0; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-741480, EBI-953896;
CC Q9UMX0; Q9ULD4-2: BRPF3; NbExp=3; IntAct=EBI-741480, EBI-23662416;
CC Q9UMX0; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-741480, EBI-10693038;
CC Q9UMX0; Q9BXJ3: C1QTNF4; NbExp=3; IntAct=EBI-741480, EBI-11955105;
CC Q9UMX0; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-741480, EBI-18036948;
CC Q9UMX0; P20807-4: CAPN3; NbExp=3; IntAct=EBI-741480, EBI-11532021;
CC Q9UMX0; P10147: CCL3; NbExp=3; IntAct=EBI-741480, EBI-8459634;
CC Q9UMX0; P80098: CCL7; NbExp=3; IntAct=EBI-741480, EBI-718759;
CC Q9UMX0; Q8TCZ2: CD99L2; NbExp=6; IntAct=EBI-741480, EBI-2824782;
CC Q9UMX0; Q9H305: CDIP1; NbExp=3; IntAct=EBI-741480, EBI-2876678;
CC Q9UMX0; P38936: CDKN1A; NbExp=3; IntAct=EBI-741480, EBI-375077;
CC Q9UMX0; O95674: CDS2; NbExp=3; IntAct=EBI-741480, EBI-3913685;
CC Q9UMX0; Q494V2-2: CFAP100; NbExp=3; IntAct=EBI-741480, EBI-11953200;
CC Q9UMX0; Q8WUX9: CHMP7; NbExp=3; IntAct=EBI-741480, EBI-749253;
CC Q9UMX0; Q03692: COL10A1; NbExp=6; IntAct=EBI-741480, EBI-2528309;
CC Q9UMX0; P08123: COL1A2; NbExp=6; IntAct=EBI-741480, EBI-983038;
CC Q9UMX0; P02458-1: COL2A1; NbExp=3; IntAct=EBI-741480, EBI-12375799;
CC Q9UMX0; Q14055: COL9A2; NbExp=3; IntAct=EBI-741480, EBI-714971;
CC Q9UMX0; Q86WV2: COX4I1; NbExp=3; IntAct=EBI-741480, EBI-10260134;
CC Q9UMX0; P07498: CSN3; NbExp=3; IntAct=EBI-741480, EBI-2602175;
CC Q9UMX0; P33240: CSTF2; NbExp=7; IntAct=EBI-741480, EBI-711360;
CC Q9UMX0; Q9H0L4: CSTF2T; NbExp=7; IntAct=EBI-741480, EBI-747012;
CC Q9UMX0; P78358: CTAG1B; NbExp=6; IntAct=EBI-741480, EBI-1188472;
CC Q9UMX0; O75638-2: CTAG2; NbExp=3; IntAct=EBI-741480, EBI-12265122;
CC Q9UMX0; Q8TB03: CXorf38; NbExp=3; IntAct=EBI-741480, EBI-12024320;
CC Q9UMX0; Q9UHQ9: CYB5R1; NbExp=3; IntAct=EBI-741480, EBI-953870;
CC Q9UMX0; Q15038: DAZAP2; NbExp=3; IntAct=EBI-741480, EBI-724310;
CC Q9UMX0; Q9UJU6: DBNL; NbExp=3; IntAct=EBI-741480, EBI-751783;
CC Q9UMX0; Q01524: DEFA6; NbExp=4; IntAct=EBI-741480, EBI-10222451;
CC Q9UMX0; Q30KQ5: DEFB115; NbExp=3; IntAct=EBI-741480, EBI-12253292;
CC Q9UMX0; Q6ICB0: DESI1; NbExp=6; IntAct=EBI-741480, EBI-2806959;
CC Q9UMX0; O95424: DEXI; NbExp=3; IntAct=EBI-741480, EBI-724515;
CC Q9UMX0; Q8NDP9: DKFZp547K2416; NbExp=3; IntAct=EBI-741480, EBI-25842538;
CC Q9UMX0; O60479: DLX3; NbExp=3; IntAct=EBI-741480, EBI-3908248;
CC Q9UMX0; Q6E0U4: DMKN; NbExp=3; IntAct=EBI-741480, EBI-7943171;
CC Q9UMX0; Q96EY1-3: DNAJA3; NbExp=3; IntAct=EBI-741480, EBI-11526226;
CC Q9UMX0; Q9H147: DNTTIP1; NbExp=3; IntAct=EBI-741480, EBI-2795449;
CC Q9UMX0; A0A0S2Z5Y1: DOLK; NbExp=3; IntAct=EBI-741480, EBI-16431159;
CC Q9UMX0; Q7Z7J5: DPPA2; NbExp=3; IntAct=EBI-741480, EBI-741400;
CC Q9UMX0; Q14117: DPYS; NbExp=3; IntAct=EBI-741480, EBI-12275416;
CC Q9UMX0; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-741480, EBI-724653;
CC Q9UMX0; Q9BVC3: DSCC1; NbExp=3; IntAct=EBI-741480, EBI-11143782;
CC Q9UMX0; Q9Y6W6: DUSP10; NbExp=3; IntAct=EBI-741480, EBI-3443946;
CC Q9UMX0; A0AVK6: E2F8; NbExp=3; IntAct=EBI-741480, EBI-7779316;
CC Q9UMX0; Q16610: ECM1; NbExp=3; IntAct=EBI-741480, EBI-947964;
CC Q9UMX0; Q658K8: EEF1DP3; NbExp=3; IntAct=EBI-741480, EBI-10248874;
CC Q9UMX0; O95967: EFEMP2; NbExp=5; IntAct=EBI-741480, EBI-743414;
CC Q9UMX0; O00472: ELL2; NbExp=3; IntAct=EBI-741480, EBI-395274;
CC Q9UMX0; O43768-8: ENSA; NbExp=3; IntAct=EBI-741480, EBI-25853109;
CC Q9UMX0; P42566: EPS15; NbExp=7; IntAct=EBI-741480, EBI-396684;
CC Q9UMX0; Q96DN0: ERP27; NbExp=4; IntAct=EBI-741480, EBI-953772;
CC Q9UMX0; P30040: ERP29; NbExp=3; IntAct=EBI-741480, EBI-946830;
CC Q9UMX0; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-741480, EBI-10213520;
CC Q9UMX0; Q9HBU6: ETNK1; NbExp=3; IntAct=EBI-741480, EBI-2834493;
CC Q9UMX0; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-741480, EBI-11793142;
CC Q9UMX0; P0C2L3: FAM163B; NbExp=3; IntAct=EBI-741480, EBI-11793223;
CC Q9UMX0; Q8NB25: FAM184A; NbExp=3; IntAct=EBI-741480, EBI-9917523;
CC Q9UMX0; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-741480, EBI-1384254;
CC Q9UMX0; P12318: FCGR2A; NbExp=3; IntAct=EBI-741480, EBI-1395970;
CC Q9UMX0; P26885: FKBP2; NbExp=3; IntAct=EBI-741480, EBI-719873;
CC Q9UMX0; P02751: FN1; NbExp=3; IntAct=EBI-741480, EBI-1220319;
CC Q9UMX0; P41439: FOLR3; NbExp=3; IntAct=EBI-741480, EBI-12893875;
CC Q9UMX0; P15408: FOSL2; NbExp=3; IntAct=EBI-741480, EBI-3893419;
CC Q9UMX0; O75084: FZD7; NbExp=5; IntAct=EBI-741480, EBI-746917;
CC Q9UMX0; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-741480, EBI-618189;
CC Q9UMX0; O14764: GABRD; NbExp=4; IntAct=EBI-741480, EBI-744352;
CC Q9UMX0; P22466: GAL; NbExp=3; IntAct=EBI-741480, EBI-6624768;
CC Q9UMX0; Q9UBU3: GHRL; NbExp=3; IntAct=EBI-741480, EBI-10319458;
CC Q9UMX0; Q49A26-4: GLYR1; NbExp=3; IntAct=EBI-741480, EBI-12143817;
CC Q9UMX0; Q16538: GPR162; NbExp=3; IntAct=EBI-741480, EBI-22387200;
CC Q9UMX0; Q02747: GUCA2A; NbExp=3; IntAct=EBI-741480, EBI-12244272;
CC Q9UMX0; Q16661: GUCA2B; NbExp=3; IntAct=EBI-741480, EBI-12349759;
CC Q9UMX0; P06028: GYPB; NbExp=6; IntAct=EBI-741480, EBI-10194756;
CC Q9UMX0; Q5T447-2: HECTD3; NbExp=3; IntAct=EBI-741480, EBI-25854793;
CC Q9UMX0; Q8IV36: HID1; NbExp=3; IntAct=EBI-741480, EBI-743438;
CC Q9UMX0; P52789: HK2; NbExp=4; IntAct=EBI-741480, EBI-741469;
CC Q9UMX0; Q53GQ0: HSD17B12; NbExp=6; IntAct=EBI-741480, EBI-2963255;
CC Q9UMX0; P48723: HSPA13; NbExp=8; IntAct=EBI-741480, EBI-750892;
CC Q9UMX0; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-741480, EBI-725665;
CC Q9UMX0; P24592: IGFBP6; NbExp=3; IntAct=EBI-741480, EBI-947015;
CC Q9UMX0; Q6PIK1: IGL@; NbExp=3; IntAct=EBI-741480, EBI-10253735;
CC Q9UMX0; Q6PIQ7: IGL@; NbExp=3; IntAct=EBI-741480, EBI-6677651;
CC Q9UMX0; Q8N355: IGL@; NbExp=4; IntAct=EBI-741480, EBI-748681;
CC Q9UMX0; Q9NZH6: IL37; NbExp=3; IntAct=EBI-741480, EBI-3862125;
CC Q9UMX0; Q17RA0: IL6ST; NbExp=3; IntAct=EBI-741480, EBI-10238517;
CC Q9UMX0; Q8N8D9: IRF1-AS1; NbExp=3; IntAct=EBI-741480, EBI-18100531;
CC Q9UMX0; P53990: IST1; NbExp=3; IntAct=EBI-741480, EBI-945994;
CC Q9UMX0; P53990-3: IST1; NbExp=3; IntAct=EBI-741480, EBI-12188567;
CC Q9UMX0; Q6GPH6: ITPRIPL1; NbExp=3; IntAct=EBI-741480, EBI-953819;
CC Q9UMX0; Q96JJ6: JPH4; NbExp=3; IntAct=EBI-741480, EBI-2847044;
CC Q9UMX0; Q96MG2: JSRP1; NbExp=3; IntAct=EBI-741480, EBI-11305455;
CC Q9UMX0; P05412: JUN; NbExp=3; IntAct=EBI-741480, EBI-852823;
CC Q9UMX0; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-741480, EBI-743960;
CC Q9UMX0; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-741480, EBI-9089060;
CC Q9UMX0; Q9P2K6: KLHL42; NbExp=4; IntAct=EBI-741480, EBI-739890;
CC Q9UMX0; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-741480, EBI-10261141;
CC Q9UMX0; Q6ISS4: LAIR2; NbExp=3; IntAct=EBI-741480, EBI-10250491;
CC Q9UMX0; P07942: LAMB1; NbExp=3; IntAct=EBI-741480, EBI-949174;
CC Q9UMX0; Q6IAA8: LAMTOR1; NbExp=3; IntAct=EBI-741480, EBI-715385;
CC Q9UMX0; A0A0C4DGV4: LAMTOR5; NbExp=3; IntAct=EBI-741480, EBI-10173304;
CC Q9UMX0; P80188: LCN2; NbExp=3; IntAct=EBI-741480, EBI-11911016;
CC Q9UMX0; A0A0S2Z5S9: LHX4; NbExp=3; IntAct=EBI-741480, EBI-16429099;
CC Q9UMX0; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-741480, EBI-25835523;
CC Q9UMX0; Q68G74: LHX8; NbExp=3; IntAct=EBI-741480, EBI-8474075;
CC Q9UMX0; Q8N0U6: LINC00518; NbExp=3; IntAct=EBI-741480, EBI-10264791;
CC Q9UMX0; Q99732: LITAF; NbExp=4; IntAct=EBI-741480, EBI-725647;
CC Q9UMX0; Q9UIQ6-2: LNPEP; NbExp=3; IntAct=EBI-741480, EBI-12133176;
CC Q9UMX0; P27338: MAOB; NbExp=3; IntAct=EBI-741480, EBI-3911344;
CC Q9UMX0; P21741: MDK; NbExp=3; IntAct=EBI-741480, EBI-722444;
CC Q9UMX0; Q14696: MESD; NbExp=3; IntAct=EBI-741480, EBI-6165891;
CC Q9UMX0; D3DX41: MGC16703; NbExp=3; IntAct=EBI-741480, EBI-25850974;
CC Q9UMX0; Q96C03: MIEF2; NbExp=4; IntAct=EBI-741480, EBI-750153;
CC Q9UMX0; Q6IN84-2: MRM1; NbExp=3; IntAct=EBI-741480, EBI-25835707;
CC Q9UMX0; O60783: MRPS14; NbExp=3; IntAct=EBI-741480, EBI-1045956;
CC Q9UMX0; P01106: MYC; NbExp=3; IntAct=EBI-741480, EBI-447544;
CC Q9UMX0; Q969H8: MYDGF; NbExp=3; IntAct=EBI-741480, EBI-718622;
CC Q9UMX0; Q8IW45: NAXD; NbExp=3; IntAct=EBI-741480, EBI-8650724;
CC Q9UMX0; P41271: NBL1; NbExp=3; IntAct=EBI-741480, EBI-10208650;
CC Q9UMX0; P41271-2: NBL1; NbExp=3; IntAct=EBI-741480, EBI-12135485;
CC Q9UMX0; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-741480, EBI-928842;
CC Q9UMX0; Q9UHB4: NDOR1; NbExp=3; IntAct=EBI-741480, EBI-10249760;
CC Q9UMX0; Q8NC67-2: NETO2; NbExp=3; IntAct=EBI-741480, EBI-25852289;
CC Q9UMX0; Q96IV0: NGLY1; NbExp=7; IntAct=EBI-741480, EBI-6165879;
CC Q9UMX0; Q13232: NME3; NbExp=6; IntAct=EBI-741480, EBI-713684;
CC Q9UMX0; P01160: NPPA; NbExp=3; IntAct=EBI-741480, EBI-953859;
CC Q9UMX0; Q14995: NR1D2; NbExp=3; IntAct=EBI-741480, EBI-6144053;
CC Q9UMX0; F1D8P7: NR1H2; NbExp=3; IntAct=EBI-741480, EBI-10177172;
CC Q9UMX0; Q6PHZ7: NR2C2; NbExp=3; IntAct=EBI-741480, EBI-2802743;
CC Q9UMX0; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-741480, EBI-398874;
CC Q9UMX0; A5D8V7: ODAD3; NbExp=3; IntAct=EBI-741480, EBI-8466445;
CC Q9UMX0; P0C6T2: OST4; NbExp=3; IntAct=EBI-741480, EBI-18397963;
CC Q9UMX0; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-741480, EBI-25830200;
CC Q9UMX0; Q8IVL6-2: P3H3; NbExp=3; IntAct=EBI-741480, EBI-12149899;
CC Q9UMX0; Q8N3R9: PALS1; NbExp=3; IntAct=EBI-741480, EBI-2513978;
CC Q9UMX0; Q495U3: PANX2; NbExp=3; IntAct=EBI-741480, EBI-17242559;
CC Q9UMX0; C3PTT6: PAUF; NbExp=3; IntAct=EBI-741480, EBI-3505892;
CC Q9UMX0; Q9HCL0: PCDH18; NbExp=6; IntAct=EBI-741480, EBI-2949740;
CC Q9UMX0; Q9UN74-2: PCDHA4; NbExp=3; IntAct=EBI-741480, EBI-12184485;
CC Q9UMX0; Q13956: PDE6H; NbExp=3; IntAct=EBI-741480, EBI-10231995;
CC Q9UMX0; O15534: PER1; NbExp=3; IntAct=EBI-741480, EBI-2557276;
CC Q9UMX0; O75928-2: PIAS2; NbExp=3; IntAct=EBI-741480, EBI-348567;
CC Q9UMX0; Q96FE7: PIK3IP1; NbExp=3; IntAct=EBI-741480, EBI-10285708;
CC Q9UMX0; P14618: PKM; NbExp=3; IntAct=EBI-741480, EBI-353408;
CC Q9UMX0; Q9HDD0: PLAAT1; NbExp=3; IntAct=EBI-741480, EBI-12387058;
CC Q9UMX0; Q9NWW9: PLAAT2; NbExp=3; IntAct=EBI-741480, EBI-12253270;
CC Q9UMX0; P53816: PLAAT3; NbExp=7; IntAct=EBI-741480, EBI-746318;
CC Q9UMX0; Q6ZR37: PLEKHG7; NbExp=3; IntAct=EBI-741480, EBI-12891828;
CC Q9UMX0; Q5SXH7-1: PLEKHS1; NbExp=3; IntAct=EBI-741480, EBI-26412802;
CC Q9UMX0; Q96T60: PNKP; NbExp=3; IntAct=EBI-741480, EBI-1045072;
CC Q9UMX0; Q8ND90: PNMA1; NbExp=4; IntAct=EBI-741480, EBI-302345;
CC Q9UMX0; P0DPB6: POLR1D; NbExp=3; IntAct=EBI-741480, EBI-359498;
CC Q9UMX0; P19388: POLR2E; NbExp=3; IntAct=EBI-741480, EBI-395189;
CC Q9UMX0; P23284: PPIB; NbExp=3; IntAct=EBI-741480, EBI-359252;
CC Q9UMX0; P45877: PPIC; NbExp=3; IntAct=EBI-741480, EBI-953909;
CC Q9UMX0; O60927: PPP1R11; NbExp=3; IntAct=EBI-741480, EBI-1048104;
CC Q9UMX0; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-741480, EBI-710402;
CC Q9UMX0; Q96NZ9: PRAP1; NbExp=6; IntAct=EBI-741480, EBI-2116102;
CC Q9UMX0; A5D903: PRB1; NbExp=3; IntAct=EBI-741480, EBI-10173935;
CC Q9UMX0; O43741: PRKAB2; NbExp=3; IntAct=EBI-741480, EBI-1053424;
CC Q9UMX0; Q16378: PRR4; NbExp=3; IntAct=EBI-741480, EBI-738624;
CC Q9UMX0; P55036: PSMD4; NbExp=4; IntAct=EBI-741480, EBI-359318;
CC Q9UMX0; Q15008: PSMD6; NbExp=3; IntAct=EBI-741480, EBI-359701;
CC Q9UMX0; Q06323: PSME1; NbExp=3; IntAct=EBI-741480, EBI-712149;
CC Q9UMX0; Q9UIG4: PSORS1C2; NbExp=3; IntAct=EBI-741480, EBI-11974061;
CC Q9UMX0; P06454-2: PTMA; NbExp=3; IntAct=EBI-741480, EBI-10194874;
CC Q9UMX0; Q8WUD1-2: RAB2B; NbExp=3; IntAct=EBI-741480, EBI-25835884;
CC Q9UMX0; Q9UNT1-2: RABL2B; NbExp=3; IntAct=EBI-741480, EBI-12256104;
CC Q9UMX0; Q9Y5P3: RAI2; NbExp=3; IntAct=EBI-741480, EBI-746228;
CC Q9UMX0; Q04206: RELA; NbExp=3; IntAct=EBI-741480, EBI-73886;
CC Q9UMX0; P47804-3: RGR; NbExp=3; IntAct=EBI-741480, EBI-25834767;
CC Q9UMX0; Q15382: RHEB; NbExp=3; IntAct=EBI-741480, EBI-1055287;
CC Q9UMX0; Q9NPQ8: RIC8A; NbExp=4; IntAct=EBI-741480, EBI-717509;
CC Q9UMX0; Q9NPQ8-4: RIC8A; NbExp=3; IntAct=EBI-741480, EBI-9091816;
CC Q9UMX0; Q9H0X6: RNF208; NbExp=3; IntAct=EBI-741480, EBI-751555;
CC Q9UMX0; P78317: RNF4; NbExp=3; IntAct=EBI-741480, EBI-2340927;
CC Q9UMX0; P62899: RPL31; NbExp=3; IntAct=EBI-741480, EBI-1053664;
CC Q9UMX0; P04843: RPN1; NbExp=4; IntAct=EBI-741480, EBI-355963;
CC Q9UMX0; P62979: RPS27A; NbExp=3; IntAct=EBI-741480, EBI-357375;
CC Q9UMX0; Q7L4I2-2: RSRC2; NbExp=3; IntAct=EBI-741480, EBI-10256202;
CC Q9UMX0; Q9BWD3: RTL8A; NbExp=4; IntAct=EBI-741480, EBI-741643;
CC Q9UMX0; Q17RB0: RTL8B; NbExp=6; IntAct=EBI-741480, EBI-10238588;
CC Q9UMX0; A6ZKI3: RTL8C; NbExp=6; IntAct=EBI-741480, EBI-10174072;
CC Q9UMX0; P13521: SCG2; NbExp=4; IntAct=EBI-741480, EBI-947132;
CC Q9UMX0; P05408: SCG5; NbExp=3; IntAct=EBI-741480, EBI-722635;
CC Q9UMX0; Q96GD3: SCMH1; NbExp=3; IntAct=EBI-741480, EBI-713793;
CC Q9UMX0; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-741480, EBI-9089805;
CC Q9UMX0; P05121: SERPINE1; NbExp=3; IntAct=EBI-741480, EBI-953978;
CC Q9UMX0; O75830: SERPINI2; NbExp=10; IntAct=EBI-741480, EBI-750144;
CC Q9UMX0; Q9BYH1-5: SEZ6L; NbExp=3; IntAct=EBI-741480, EBI-12012146;
CC Q9UMX0; Q9H173: SIL1; NbExp=3; IntAct=EBI-741480, EBI-2840325;
CC Q9UMX0; O15427: SLC16A3; NbExp=3; IntAct=EBI-741480, EBI-7600166;
CC Q9UMX0; P03973: SLPI; NbExp=5; IntAct=EBI-741480, EBI-355293;
CC Q9UMX0; Q96E16: SMIM19; NbExp=3; IntAct=EBI-741480, EBI-17657124;
CC Q9UMX0; Q9BVW6: SMIM2; NbExp=3; IntAct=EBI-741480, EBI-10300146;
CC Q9UMX0; P02814: SMR3B; NbExp=3; IntAct=EBI-741480, EBI-738612;
CC Q9UMX0; Q13573: SNW1; NbExp=3; IntAct=EBI-741480, EBI-632715;
CC Q9UMX0; O14544: SOCS6; NbExp=3; IntAct=EBI-741480, EBI-3929549;
CC Q9UMX0; P08294: SOD3; NbExp=3; IntAct=EBI-741480, EBI-10195782;
CC Q9UMX0; Q02086-2: SP2; NbExp=3; IntAct=EBI-741480, EBI-9088579;
CC Q9UMX0; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-741480, EBI-11959123;
CC Q9UMX0; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-741480, EBI-10696971;
CC Q9UMX0; Q86W54-2: SPATA24; NbExp=3; IntAct=EBI-741480, EBI-12041693;
CC Q9UMX0; Q496A3: SPATS1; NbExp=3; IntAct=EBI-741480, EBI-3923692;
CC Q9UMX0; Q9C004: SPRY4; NbExp=3; IntAct=EBI-741480, EBI-354861;
CC Q9UMX0; P10124: SRGN; NbExp=6; IntAct=EBI-741480, EBI-744915;
CC Q9UMX0; Q99469: STAC; NbExp=3; IntAct=EBI-741480, EBI-2652799;
CC Q9UMX0; O75886: STAM2; NbExp=3; IntAct=EBI-741480, EBI-373258;
CC Q9UMX0; Q13586: STIM1; NbExp=3; IntAct=EBI-741480, EBI-448878;
CC Q9UMX0; O95947: TBX6; NbExp=3; IntAct=EBI-741480, EBI-2824328;
CC Q9UMX0; O15273: TCAP; NbExp=3; IntAct=EBI-741480, EBI-954089;
CC Q9UMX0; Q86WV5: TEN1; NbExp=3; IntAct=EBI-741480, EBI-2562799;
CC Q9UMX0; P54274-2: TERF1; NbExp=3; IntAct=EBI-741480, EBI-711018;
CC Q9UMX0; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-741480, EBI-12090309;
CC Q9UMX0; Q5T0J7-2: TEX35; NbExp=3; IntAct=EBI-741480, EBI-12833746;
CC Q9UMX0; P04155: TFF1; NbExp=6; IntAct=EBI-741480, EBI-743871;
CC Q9UMX0; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-741480, EBI-17438286;
CC Q9UMX0; O60830: TIMM17B; NbExp=3; IntAct=EBI-741480, EBI-2372529;
CC Q9UMX0; Q96DC7: TMCO6; NbExp=7; IntAct=EBI-741480, EBI-746174;
CC Q9UMX0; Q96DC7-2: TMCO6; NbExp=3; IntAct=EBI-741480, EBI-10284552;
CC Q9UMX0; Q96B77: TMEM186; NbExp=3; IntAct=EBI-741480, EBI-9089409;
CC Q9UMX0; P61165: TMEM258; NbExp=3; IntAct=EBI-741480, EBI-12019210;
CC Q9UMX0; Q5JXX7: TMEM31; NbExp=3; IntAct=EBI-741480, EBI-10244617;
CC Q9UMX0; Q8N0U2: TMEM61; NbExp=3; IntAct=EBI-741480, EBI-25830583;
CC Q9UMX0; Q53NU3: tmp_locus_54; NbExp=3; IntAct=EBI-741480, EBI-10242677;
CC Q9UMX0; Q71RG4-4: TMUB2; NbExp=3; IntAct=EBI-741480, EBI-25831574;
CC Q9UMX0; P36406: TRIM23; NbExp=6; IntAct=EBI-741480, EBI-740098;
CC Q9UMX0; Q13049: TRIM32; NbExp=7; IntAct=EBI-741480, EBI-742790;
CC Q9UMX0; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-741480, EBI-17716262;
CC Q9UMX0; Q9Y3Q8: TSC22D4; NbExp=3; IntAct=EBI-741480, EBI-739485;
CC Q9UMX0; O60636: TSPAN2; NbExp=3; IntAct=EBI-741480, EBI-3914288;
CC Q9UMX0; Q6PF05: TTC23L; NbExp=3; IntAct=EBI-741480, EBI-8656864;
CC Q9UMX0; Q9UGJ1-2: TUBGCP4; NbExp=3; IntAct=EBI-741480, EBI-10964469;
CC Q9UMX0; O95881: TXNDC12; NbExp=4; IntAct=EBI-741480, EBI-2564581;
CC Q9UMX0; P62987: UBA52; NbExp=3; IntAct=EBI-741480, EBI-357304;
CC Q9UMX0; Q5U5U6: UBB; NbExp=3; IntAct=EBI-741480, EBI-1642104;
CC Q9UMX0; Q96C32: UBC; NbExp=3; IntAct=EBI-741480, EBI-745483;
CC Q9UMX0; P49459: UBE2A; NbExp=3; IntAct=EBI-741480, EBI-2339348;
CC Q9UMX0; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-741480, EBI-10180829;
CC Q9UMX0; Q13404: UBE2V1; NbExp=9; IntAct=EBI-741480, EBI-1050671;
CC Q9UMX0; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-741480, EBI-741480;
CC Q9UMX0; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-741480, EBI-947187;
CC Q9UMX0; Q9NRR5: UBQLN4; NbExp=8; IntAct=EBI-741480, EBI-711226;
CC Q9UMX0; Q04323: UBXN1; NbExp=3; IntAct=EBI-741480, EBI-1058647;
CC Q9UMX0; Q92575: UBXN4; NbExp=6; IntAct=EBI-741480, EBI-723441;
CC Q9UMX0; O94888: UBXN7; NbExp=3; IntAct=EBI-741480, EBI-1993627;
CC Q9UMX0; P22415: USF1; NbExp=3; IntAct=EBI-741480, EBI-1054489;
CC Q9UMX0; Q9P1Q0-4: VPS54; NbExp=3; IntAct=EBI-741480, EBI-25835297;
CC Q9UMX0; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-741480, EBI-11957238;
CC Q9UMX0; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-741480, EBI-10316321;
CC Q9UMX0; Q8WWY7: WFDC12; NbExp=3; IntAct=EBI-741480, EBI-11958577;
CC Q9UMX0; O00755: WNT7A; NbExp=3; IntAct=EBI-741480, EBI-727198;
CC Q9UMX0; Q0VG75: XPO4; NbExp=3; IntAct=EBI-741480, EBI-10226948;
CC Q9UMX0; O43829: ZBTB14; NbExp=3; IntAct=EBI-741480, EBI-10176632;
CC Q9UMX0; Q8NAP8: ZBTB8B; NbExp=3; IntAct=EBI-741480, EBI-17494306;
CC Q9UMX0; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-741480, EBI-14104088;
CC Q9UMX0; Q9NP64: ZCCHC17; NbExp=3; IntAct=EBI-741480, EBI-746345;
CC Q9UMX0; O60844: ZG16; NbExp=10; IntAct=EBI-741480, EBI-746479;
CC Q9UMX0; Q5VZL5: ZMYM4; NbExp=3; IntAct=EBI-741480, EBI-2514659;
CC Q9UMX0; Q9UJ78-2: ZMYM5; NbExp=3; IntAct=EBI-741480, EBI-17634549;
CC Q9UMX0; Q8WUU4: ZNF296; NbExp=3; IntAct=EBI-741480, EBI-8834821;
CC Q9UMX0; Q96JL9-2: ZNF333; NbExp=3; IntAct=EBI-741480, EBI-25835852;
CC Q9UMX0; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-741480, EBI-10252492;
CC Q9UMX0; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-741480, EBI-18036029;
CC Q9UMX0; A0A1U9X8X8; NbExp=3; IntAct=EBI-741480, EBI-17234977;
CC Q9UMX0; B7Z3E8; NbExp=3; IntAct=EBI-741480, EBI-25831617;
CC Q9UMX0; Q8WU02; NbExp=3; IntAct=EBI-741480, EBI-747182;
CC Q9UMX0; P0DTC6: 6; Xeno; NbExp=3; IntAct=EBI-741480, EBI-25475897;
CC Q9UMX0; P0DTD3: 9c; Xeno; NbExp=3; IntAct=EBI-741480, EBI-25475917;
CC Q9UMX0-2; O00154: ACOT7; NbExp=3; IntAct=EBI-10173939, EBI-948905;
CC Q9UMX0-2; O95994: AGR2; NbExp=3; IntAct=EBI-10173939, EBI-712648;
CC Q9UMX0-2; Q8TD06: AGR3; NbExp=3; IntAct=EBI-10173939, EBI-3925742;
CC Q9UMX0-2; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-10173939, EBI-953896;
CC Q9UMX0-2; Q9BXJ5: C1QTNF2; NbExp=3; IntAct=EBI-10173939, EBI-2817707;
CC Q9UMX0-2; O43852: CALU; NbExp=3; IntAct=EBI-10173939, EBI-1171069;
CC Q9UMX0-2; P80098: CCL7; NbExp=3; IntAct=EBI-10173939, EBI-718759;
CC Q9UMX0-2; Q8TCZ2: CD99L2; NbExp=6; IntAct=EBI-10173939, EBI-2824782;
CC Q9UMX0-2; P51788-4: CLCN2; NbExp=3; IntAct=EBI-10173939, EBI-16431116;
CC Q9UMX0-2; Q03692: COL10A1; NbExp=3; IntAct=EBI-10173939, EBI-2528309;
CC Q9UMX0-2; A0A0S2Z3K0: COL1A2; NbExp=3; IntAct=EBI-10173939, EBI-16431143;
CC Q9UMX0-2; P08123: COL1A2; NbExp=6; IntAct=EBI-10173939, EBI-983038;
CC Q9UMX0-2; Q8IYK4: COLGALT2; NbExp=3; IntAct=EBI-10173939, EBI-10263496;
CC Q9UMX0-2; Q86VU5: COMTD1; NbExp=3; IntAct=EBI-10173939, EBI-2836030;
CC Q9UMX0-2; P33240: CSTF2; NbExp=3; IntAct=EBI-10173939, EBI-711360;
CC Q9UMX0-2; Q9H0L4: CSTF2T; NbExp=3; IntAct=EBI-10173939, EBI-747012;
CC Q9UMX0-2; P78358: CTAG1B; NbExp=3; IntAct=EBI-10173939, EBI-1188472;
CC Q9UMX0-2; O75638: CTAG2; NbExp=3; IntAct=EBI-10173939, EBI-10188927;
CC Q9UMX0-2; Q9UHQ9: CYB5R1; NbExp=3; IntAct=EBI-10173939, EBI-953870;
CC Q9UMX0-2; Q01524: DEFA6; NbExp=3; IntAct=EBI-10173939, EBI-10222451;
CC Q9UMX0-2; A0A0S2Z5Y1: DOLK; NbExp=3; IntAct=EBI-10173939, EBI-16431159;
CC Q9UMX0-2; O95967: EFEMP2; NbExp=3; IntAct=EBI-10173939, EBI-743414;
CC Q9UMX0-2; Q96DN0: ERP27; NbExp=3; IntAct=EBI-10173939, EBI-953772;
CC Q9UMX0-2; Q9HBU6: ETNK1; NbExp=3; IntAct=EBI-10173939, EBI-2834493;
CC Q9UMX0-2; P12318: FCGR2A; NbExp=3; IntAct=EBI-10173939, EBI-1395970;
CC Q9UMX0-2; P26885: FKBP2; NbExp=3; IntAct=EBI-10173939, EBI-719873;
CC Q9UMX0-2; O14764: GABRD; NbExp=3; IntAct=EBI-10173939, EBI-744352;
CC Q9UMX0-2; Q9UBU3: GHRL; NbExp=3; IntAct=EBI-10173939, EBI-10319458;
CC Q9UMX0-2; P22352: GPX3; NbExp=3; IntAct=EBI-10173939, EBI-2832946;
CC Q9UMX0-2; Q14416: GRM2; NbExp=3; IntAct=EBI-10173939, EBI-10232876;
CC Q9UMX0-2; P06028: GYPB; NbExp=3; IntAct=EBI-10173939, EBI-10194756;
CC Q9UMX0-2; P52789: HK2; NbExp=3; IntAct=EBI-10173939, EBI-741469;
CC Q9UMX0-2; Q53GQ0: HSD17B12; NbExp=3; IntAct=EBI-10173939, EBI-2963255;
CC Q9UMX0-2; P48723: HSPA13; NbExp=3; IntAct=EBI-10173939, EBI-750892;
CC Q9UMX0-2; Q6PIK1: IGL@; NbExp=3; IntAct=EBI-10173939, EBI-10253735;
CC Q9UMX0-2; Q6PIQ7: IGL@; NbExp=3; IntAct=EBI-10173939, EBI-6677651;
CC Q9UMX0-2; Q8N355: IGL@; NbExp=3; IntAct=EBI-10173939, EBI-748681;
CC Q9UMX0-2; Q17RA0: IL6ST; NbExp=3; IntAct=EBI-10173939, EBI-10238517;
CC Q9UMX0-2; Q9P2K6: KLHL42; NbExp=3; IntAct=EBI-10173939, EBI-739890;
CC Q9UMX0-2; Q99732: LITAF; NbExp=7; IntAct=EBI-10173939, EBI-725647;
CC Q9UMX0-2; Q9NQG1: MANBAL; NbExp=3; IntAct=EBI-10173939, EBI-3867271;
CC Q9UMX0-2; P33993: MCM7; NbExp=3; IntAct=EBI-10173939, EBI-355924;
CC Q9UMX0-2; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-10173939, EBI-740987;
CC Q9UMX0-2; Q96C03: MIEF2; NbExp=3; IntAct=EBI-10173939, EBI-750153;
CC Q9UMX0-2; P55198: MLLT6; NbExp=3; IntAct=EBI-10173939, EBI-740216;
CC Q9UMX0-2; Q8IW45: NAXD; NbExp=3; IntAct=EBI-10173939, EBI-8650724;
CC Q9UMX0-2; P41271: NBL1; NbExp=3; IntAct=EBI-10173939, EBI-10208650;
CC Q9UMX0-2; Q96IV0: NGLY1; NbExp=3; IntAct=EBI-10173939, EBI-6165879;
CC Q9UMX0-2; A0A0S2Z5K2: NLGN3; NbExp=3; IntAct=EBI-10173939, EBI-16431177;
CC Q9UMX0-2; Q13232: NME3; NbExp=3; IntAct=EBI-10173939, EBI-713684;
CC Q9UMX0-2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-10173939, EBI-2811583;
CC Q9UMX0-2; C3PTT6: PAUF; NbExp=3; IntAct=EBI-10173939, EBI-3505892;
CC Q9UMX0-2; Q96AQ6: PBXIP1; NbExp=3; IntAct=EBI-10173939, EBI-740845;
CC Q9UMX0-2; Q96FE7: PIK3IP1; NbExp=3; IntAct=EBI-10173939, EBI-10285708;
CC Q9UMX0-2; P53816: PLAAT3; NbExp=3; IntAct=EBI-10173939, EBI-746318;
CC Q9UMX0-2; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-10173939, EBI-302345;
CC Q9UMX0-2; P23284: PPIB; NbExp=3; IntAct=EBI-10173939, EBI-359252;
CC Q9UMX0-2; P45877: PPIC; NbExp=3; IntAct=EBI-10173939, EBI-953909;
CC Q9UMX0-2; Q96NZ9: PRAP1; NbExp=3; IntAct=EBI-10173939, EBI-2116102;
CC Q9UMX0-2; A5D903: PRB1; NbExp=3; IntAct=EBI-10173939, EBI-10173935;
CC Q9UMX0-2; Q15008: PSMD6; NbExp=3; IntAct=EBI-10173939, EBI-359701;
CC Q9UMX0-2; Q9NPQ8-4: RIC8A; NbExp=3; IntAct=EBI-10173939, EBI-9091816;
CC Q9UMX0-2; P04843: RPN1; NbExp=3; IntAct=EBI-10173939, EBI-355963;
CC Q9UMX0-2; Q9BWD3: RTL8A; NbExp=3; IntAct=EBI-10173939, EBI-741643;
CC Q9UMX0-2; Q17RB0: RTL8B; NbExp=3; IntAct=EBI-10173939, EBI-10238588;
CC Q9UMX0-2; A6ZKI3: RTL8C; NbExp=3; IntAct=EBI-10173939, EBI-10174072;
CC Q9UMX0-2; P05408: SCG5; NbExp=3; IntAct=EBI-10173939, EBI-722635;
CC Q9UMX0-2; Q96GD3: SCMH1; NbExp=3; IntAct=EBI-10173939, EBI-713793;
CC Q9UMX0-2; P05121: SERPINE1; NbExp=3; IntAct=EBI-10173939, EBI-953978;
CC Q9UMX0-2; O75830: SERPINI2; NbExp=3; IntAct=EBI-10173939, EBI-750144;
CC Q9UMX0-2; Q9BVW6: SMIM2; NbExp=3; IntAct=EBI-10173939, EBI-10300146;
CC Q9UMX0-2; P02814: SMR3B; NbExp=3; IntAct=EBI-10173939, EBI-738612;
CC Q9UMX0-2; P10124: SRGN; NbExp=3; IntAct=EBI-10173939, EBI-744915;
CC Q9UMX0-2; Q96DC7-2: TMCO6; NbExp=3; IntAct=EBI-10173939, EBI-10284552;
CC Q9UMX0-2; Q5JXX7: TMEM31; NbExp=3; IntAct=EBI-10173939, EBI-10244617;
CC Q9UMX0-2; A0A0S2Z5T9: TMEM67; NbExp=3; IntAct=EBI-10173939, EBI-16431189;
CC Q9UMX0-2; Q71RG4: TMUB2; NbExp=3; IntAct=EBI-10173939, EBI-2820477;
CC Q9UMX0-2; Q13049: TRIM32; NbExp=3; IntAct=EBI-10173939, EBI-742790;
CC Q9UMX0-2; O95881: TXNDC12; NbExp=3; IntAct=EBI-10173939, EBI-2564581;
CC Q9UMX0-2; Q13404: UBE2V1; NbExp=3; IntAct=EBI-10173939, EBI-1050671;
CC Q9UMX0-2; Q04323: UBXN1; NbExp=3; IntAct=EBI-10173939, EBI-1058647;
CC Q9UMX0-2; Q92575: UBXN4; NbExp=3; IntAct=EBI-10173939, EBI-723441;
CC Q9UMX0-2; Q0VG75: XPO4; NbExp=3; IntAct=EBI-10173939, EBI-10226948;
CC Q9UMX0-2; Q8WV99: ZFAND2B; NbExp=3; IntAct=EBI-10173939, EBI-747823;
CC Q9UMX0-2; O60844: ZG16; NbExp=3; IntAct=EBI-10173939, EBI-746479;
CC Q9UMX0-2; Q5VZL5: ZMYM4; NbExp=3; IntAct=EBI-10173939, EBI-2514659;
CC Q9UMX0-2; Q8WU02; NbExp=3; IntAct=EBI-10173939, EBI-747182;
CC Q9UMX0-2; Q96FB2; NbExp=3; IntAct=EBI-10173939, EBI-2857623;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16159959,
CC ECO:0000269|PubMed:23979357}. Nucleus {ECO:0000269|PubMed:23979357}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:19822669}. Cytoplasmic
CC vesicle, autophagosome {ECO:0000269|PubMed:19148225,
CC ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:21143716,
CC ECO:0000269|PubMed:21695056, ECO:0000269|PubMed:23307288,
CC ECO:0000269|PubMed:23459205}. Cell membrane
CC {ECO:0000269|PubMed:21143716, ECO:0000269|PubMed:23307288}.
CC Note=Detected in neuronal processes and at synapses (By similarity).
CC Recruited to the ER during ER-associated protein degradation (ERAD)
CC (PubMed:19822669). Isoform 1 and isoform 3 colocalize with PSEN1 in the
CC cell membrane and in cytoplasmic juxtanuclear structures called
CC aggresomes (PubMed:21143716). Colocalizes with ORAI1 and TICAM1 in the
CC autophagosome (PubMed:23307288, PubMed:21695056). Colocalizes with
CC EPS15 and HGS in ubiquitin-rich cytoplasmic aggregates that are not
CC endocytic compartments and with EPS15 also in aggresomes
CC (PubMed:16159959). {ECO:0000250|UniProtKB:Q9JJP9,
CC ECO:0000269|PubMed:16159959, ECO:0000269|PubMed:19822669,
CC ECO:0000269|PubMed:21143716, ECO:0000269|PubMed:21695056,
CC ECO:0000269|PubMed:23307288}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UMX0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UMX0-2; Sequence=VSP_009787;
CC Name=3;
CC IsoId=Q9UMX0-3; Sequence=VSP_057689;
CC Name=4;
CC IsoId=Q9UMX0-4; Sequence=VSP_057690, VSP_057691;
CC -!- TISSUE SPECIFICITY: Brain (at protein level) (PubMed:18953672).
CC Ubiquitous. Highly expressed throughout the brain; detected in neurons
CC and in neuropathological lesions, such as neurofibrillary tangles and
CC Lewy bodies. Highly expressed in heart, placenta, pancreas, lung,
CC liver, skeletal muscle and kidney. {ECO:0000269|PubMed:11076969,
CC ECO:0000269|PubMed:11853878, ECO:0000269|PubMed:18953672}.
CC -!- DOMAIN: The UBA domain mediates binding to PSEN1 and PSEN2. It also
CC binds ubiquitin with micromolar affinity, independently of
CC polyubiquitin linkage type. Essential for its association with
CC microtubule-associated protein 1 light chain 3 (MAP1LC3).
CC {ECO:0000269|PubMed:11076969, ECO:0000269|PubMed:15147878,
CC ECO:0000269|PubMed:19148225}.
CC -!- DOMAIN: The ubiquitin-like domain mediates its association with the
CC subunits of the proteasome. {ECO:0000269|PubMed:15147878}.
CC -!- DOMAIN: Dimerization is dependent upon the central region of the
CC protein containing the STI1 domains and is independent of its
CC ubiquitin-like and UBA domains. {ECO:0000269|PubMed:16813565}.
CC -!- PTM: Degraded during both macroautophagy and during chaperone-mediated
CC autophagy (CMA). {ECO:0000269|PubMed:20529957}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:11853878}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:16159959}.
CC -!- MISCELLANEOUS: May be a prognostic marker for lung adenocarcinoma
CC patient clinical outcome. {ECO:0000269|PubMed:22233804}.
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; AF176069; AAD49751.3; -; mRNA.
DR EMBL; AF293384; AAG02473.1; -; mRNA.
DR EMBL; AB035275; BAB20436.1; -; mRNA.
DR EMBL; HM005532; AEE61129.1; -; mRNA.
DR EMBL; AL136643; CAB66578.1; -; mRNA.
DR EMBL; AL354920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62659.1; -; Genomic_DNA.
DR EMBL; CH471089; EAW62661.1; -; Genomic_DNA.
DR EMBL; CH471089; EAW62664.1; -; Genomic_DNA.
DR EMBL; BC010066; AAH10066.1; -; mRNA.
DR EMBL; BC039294; AAH39294.1; -; mRNA.
DR EMBL; AK074535; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS6663.1; -. [Q9UMX0-1]
DR CCDS; CCDS6664.1; -. [Q9UMX0-2]
DR RefSeq; NP_038466.2; NM_013438.4. [Q9UMX0-1]
DR RefSeq; NP_444295.1; NM_053067.2. [Q9UMX0-2]
DR PDB; 2JY5; NMR; -; A=541-586.
DR PDB; 2JY6; NMR; -; B=541-586.
DR PDB; 2KLC; NMR; -; A=34-112.
DR PDBsum; 2JY5; -.
DR PDBsum; 2JY6; -.
DR PDBsum; 2KLC; -.
DR AlphaFoldDB; Q9UMX0; -.
DR BMRB; Q9UMX0; -.
DR SMR; Q9UMX0; -.
DR BioGRID; 119007; 405.
DR CORUM; Q9UMX0; -.
DR DIP; DIP-41629N; -.
DR IntAct; Q9UMX0; 345.
DR MINT; Q9UMX0; -.
DR STRING; 9606.ENSP00000365576; -.
DR GlyGen; Q9UMX0; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; Q9UMX0; -.
DR MetOSite; Q9UMX0; -.
DR PhosphoSitePlus; Q9UMX0; -.
DR BioMuta; UBQLN1; -.
DR DMDM; 48475013; -.
DR REPRODUCTION-2DPAGE; IPI00071180; -.
DR EPD; Q9UMX0; -.
DR jPOST; Q9UMX0; -.
DR MassIVE; Q9UMX0; -.
DR MaxQB; Q9UMX0; -.
DR PaxDb; Q9UMX0; -.
DR PeptideAtlas; Q9UMX0; -.
DR PRIDE; Q9UMX0; -.
DR ProteomicsDB; 85215; -. [Q9UMX0-1]
DR ProteomicsDB; 85216; -. [Q9UMX0-2]
DR Antibodypedia; 27540; 350 antibodies from 32 providers.
DR DNASU; 29979; -.
DR Ensembl; ENST00000257468.11; ENSP00000257468.7; ENSG00000135018.14. [Q9UMX0-2]
DR Ensembl; ENST00000376395.9; ENSP00000365576.4; ENSG00000135018.14. [Q9UMX0-1]
DR GeneID; 29979; -.
DR KEGG; hsa:29979; -.
DR MANE-Select; ENST00000376395.9; ENSP00000365576.4; NM_013438.5; NP_038466.2.
DR UCSC; uc004amv.4; human. [Q9UMX0-1]
DR CTD; 29979; -.
DR DisGeNET; 29979; -.
DR GeneCards; UBQLN1; -.
DR HGNC; HGNC:12508; UBQLN1.
DR HPA; ENSG00000135018; Low tissue specificity.
DR MIM; 605046; gene.
DR neXtProt; NX_Q9UMX0; -.
DR OpenTargets; ENSG00000135018; -.
DR PharmGKB; PA37155; -.
DR VEuPathDB; HostDB:ENSG00000135018; -.
DR eggNOG; KOG0010; Eukaryota.
DR GeneTree; ENSGT00940000156437; -.
DR HOGENOM; CLU_024293_4_0_1; -.
DR InParanoid; Q9UMX0; -.
DR OMA; GMDMFGP; -.
DR OrthoDB; 1553668at2759; -.
DR PhylomeDB; Q9UMX0; -.
DR TreeFam; TF314412; -.
DR PathwayCommons; Q9UMX0; -.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR SignaLink; Q9UMX0; -.
DR BioGRID-ORCS; 29979; 22 hits in 1084 CRISPR screens.
DR ChiTaRS; UBQLN1; human.
DR EvolutionaryTrace; Q9UMX0; -.
DR GeneWiki; UBQLN1; -.
DR GenomeRNAi; 29979; -.
DR Pharos; Q9UMX0; Tbio.
DR PRO; PR:Q9UMX0; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9UMX0; protein.
DR Bgee; ENSG00000135018; Expressed in ileal mucosa and 194 other tissues.
DR ExpressionAtlas; Q9UMX0; baseline and differential.
DR Genevisible; Q9UMX0; HS.
DR GO; GO:0016235; C:aggresome; IDA:UniProtKB.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IDA:LIFEdb.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0035973; P:aggrephagy; IDA:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IMP:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; IMP:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; IMP:BHF-UCL.
DR GO; GO:0016236; P:macroautophagy; IMP:GO_Central.
DR GO; GO:1901340; P:negative regulation of store-operated calcium channel activity; IMP:UniProtKB.
DR GO; GO:0034140; P:negative regulation of toll-like receptor 3 signaling pathway; IEA:Ensembl.
DR GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0016241; P:regulation of macroautophagy; IBA:GO_Central.
DR GO; GO:1902175; P:regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:BHF-UCL.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IDA:HGNC-UCL.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:BHF-UCL.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR028430; Ubiquilin-1/2.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10677:SF5; PTHR10677:SF5; 2.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00727; STI1; 4.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Autophagy; Cell membrane;
KW Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
KW Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..589
FT /note="Ubiquilin-1"
FT /id="PRO_0000211008"
FT DOMAIN 37..111
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 182..210
FT /note="STI1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 212..251
FT /note="STI1 2"
FT /evidence="ECO:0000255"
FT DOMAIN 387..434
FT /note="STI1 3"
FT /evidence="ECO:0000255"
FT DOMAIN 438..470
FT /note="STI1 4"
FT /evidence="ECO:0000255"
FT DOMAIN 546..586
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..428
FT /note="Interaction with UBXN4"
FT /evidence="ECO:0000269|PubMed:19822669"
FT REGION 295..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895"
FT VAR_SEQ 61..237
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18953672"
FT /id="VSP_057689"
FT VAR_SEQ 150..181
FT /note="GGLGGLAGLSSLGLNTTNFSELQSQMQRQLLS -> DVGTCQESSNDAGDDE
FT EPGPSFEQPRKHPRGI (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:18953672"
FT /id="VSP_057690"
FT VAR_SEQ 182..589
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:18953672"
FT /id="VSP_057691"
FT VAR_SEQ 417..444
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:18953672"
FT /id="VSP_009787"
FT CONFLICT 25
FT /note="A -> T (in Ref. 9; AAH39294)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="V -> A (in Ref. 4; BAB20436)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="F -> S (in Ref. 4; BAB20436)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="L -> S (in Ref. 4; BAB20436)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="S -> G (in Ref. 6; CAB66578)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="P -> H (in Ref. 9; AAH39294)"
FT /evidence="ECO:0000305"
FT CONFLICT 537..538
FT /note="NP -> YS (in Ref. 4; BAB20436)"
FT /evidence="ECO:0000305"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:2KLC"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:2KLC"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:2KLC"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2KLC"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2KLC"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2KLC"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:2KLC"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:2KLC"
FT TURN 543..547
FT /evidence="ECO:0007829|PDB:2JY5"
FT HELIX 548..556
FT /evidence="ECO:0007829|PDB:2JY5"
FT HELIX 562..572
FT /evidence="ECO:0007829|PDB:2JY5"
FT HELIX 576..583
FT /evidence="ECO:0007829|PDB:2JY5"
SQ SEQUENCE 589 AA; 62519 MW; 8B4756B6113B7025 CRC64;
MAESGESGGP PGSQDSAAGA EGAGAPAAAA SAEPKIMKVT VKTPKEKEEF AVPENSSVQQ
FKEEISKRFK SHTDQLVLIF AGKILKDQDT LSQHGIHDGL TVHLVIKTQN RPQDHSAQQT
NTAGSNVTTS STPNSNSTSG SATSNPFGLG GLGGLAGLSS LGLNTTNFSE LQSQMQRQLL
SNPEMMVQIM ENPFVQSMLS NPDLMRQLIM ANPQMQQLIQ RNPEISHMLN NPDIMRQTLE
LARNPAMMQE MMRNQDRALS NLESIPGGYN ALRRMYTDIQ EPMLSAAQEQ FGGNPFASLV
SNTSSGEGSQ PSRTENRDPL PNPWAPQTSQ SSSASSGTAS TVGGTTGSTA SGTSGQSTTA
PNLVPGVGAS MFNTPGMQSL LQQITENPQL MQNMLSAPYM RSMMQSLSQN PDLAAQMMLN
NPLFAGNPQL QEQMRQQLPT FLQQMQNPDT LSAMSNPRAM QALLQIQQGL QTLATEAPGL
IPGFTPGLGA LGSTGGSSGT NGSNATPSEN TSPTAGTTEP GHQQFIQQML QALAGVNPQL
QNPEVRFQQQ LEQLSAMGFL NREANLQALI ATGGDINAAI ERLLGSQPS
