ATX1_HUMAN
ID ATX1_HUMAN Reviewed; 815 AA.
AC P54253; Q17S02; Q9UJG2; Q9Y4J1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Ataxin-1;
DE AltName: Full=Spinocerebellar ataxia type 1 protein;
GN Name=ATXN1; Synonyms=ATX1, SCA1;
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], INVOLVEMENT IN SCA1, AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Cerebellum;
RX PubMed=7951322; DOI=10.1038/ng0894-513;
RA Banfi S., Servadio A., Chung M.-Y., Kwiatkowski T.J. Jr., McCall A.E.,
RA Duvick L.A., Shen Y., Roth E.J., Orr H.T., Zoghbi H.Y.;
RT "Identification and characterization of the gene causing type 1
RT spinocerebellar ataxia.";
RL Nat. Genet. 7:513-519(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 189-230, INVOLVEMENT IN SCA1, AND
RP POLYMORPHISM.
RX PubMed=8634720; DOI=10.1093/hmg/4.12.2411;
RA Quan F., Janas J., Popovich B.W.;
RT "A novel CAG repeat configuration in the SCA1 gene: implications for the
RT molecular diagnostics of spinocerebellar ataxia type 1.";
RL Hum. Mol. Genet. 4:2411-2413(1995).
RN [5]
RP INVOLVEMENT IN SCA1, AND SUBCELLULAR LOCATION.
RX PubMed=7647801; DOI=10.1038/ng0595-94;
RA Servadio A., Koshy B., Armstrong D., Antalffy B., Orr H.T., Zoghbi H.Y.;
RT "Expression analysis of the ataxin-1 protein in tissues from normal and
RT spinocerebellar ataxia type 1 individuals.";
RL Nat. Genet. 10:94-98(1995).
RN [6]
RP SUBUNIT.
RX PubMed=9097953; DOI=10.1093/hmg/6.4.513;
RA Burright E.N., Davidson J.D., Duvick L.A., Koshy B., Zoghbi H.Y., Orr H.T.;
RT "Identification of a self-association region within the SCA1 gene product,
RT ataxin-1.";
RL Hum. Mol. Genet. 6:513-518(1997).
RN [7]
RP INTERACTION WITH ANP32A.
RX PubMed=9353121; DOI=10.1038/40159;
RA Matilla A., Koshy B.T., Cummings C.J., Isobe T., Orr H.T., Zoghbi H.Y.;
RT "The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-
RT 1.";
RL Nature 389:974-978(1997).
RN [8]
RP RNA-BINDING DOMAIN.
RX PubMed=11136710; DOI=10.1093/hmg/10.1.25;
RA Yue S., Serra H.G., Zoghbi H.Y., Orr H.T.;
RT "The spinocerebellar ataxia type 1 protein, ataxin-1, has RNA-binding
RT activity that is inversely affected by the length of its polyglutamine
RT tract.";
RL Hum. Mol. Genet. 10:25-30(2001).
RN [9]
RP INTERACTION WITH UBQLN4.
RX PubMed=11001934; DOI=10.1093/oxfordjournals.hmg.a018922;
RA Davidson J.D., Riley B., Burright E.N., Duvick L.A., Zoghbi H.Y., Orr H.T.;
RT "Identification and characterization of an ataxin-1-interacting protein:
RT A1Up, a ubiquitin-like nuclear protein.";
RL Hum. Mol. Genet. 9:2305-2312(2000).
RN [10]
RP INTERACTION WITH PQBP1.
RX PubMed=12062018; DOI=10.1016/s0896-6273(02)00697-9;
RA Okazawa H., Rich T., Chang A., Lin X., Waragai M., Kajikawa M., Enokido Y.,
RA Komuro A., Kato S., Shibata M., Hatanaka H., Mouradian M.M., Sudol M.,
RA Kanazawa I.;
RT "Interaction between mutant ataxin-1 and PQBP-1 affects transcription and
RT cell death.";
RL Neuron 34:701-713(2002).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH USP7.
RX PubMed=12093161; DOI=10.1006/mcne.2002.1103;
RA Hong S., Kim S.J., Ka S., Choi I., Kang S.;
RT "USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1
RT gene product.";
RL Mol. Cell. Neurosci. 20:298-306(2002).
RN [12]
RP PHOSPHORYLATION AT SER-775, AND MUTAGENESIS OF SER-775.
RX PubMed=12741986; DOI=10.1016/s0896-6273(03)00258-7;
RA Emamian E.S., Kaytor M.D., Duvick L.A., Zu T., Tousey S.K., Zoghbi H.Y.,
RA Clark H.B., Orr H.T.;
RT "Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in
RT SCA1 transgenic mice.";
RL Neuron 38:375-387(2003).
RN [13]
RP INTERACTION WITH ATXN1L.
RX PubMed=16121196; DOI=10.1038/sj.emboj.7600785;
RA Mizutani A., Wang L., Rajan H., Vig P.J.S., Alaynick W.A., Thaler J.P.,
RA Tsai C.-C.;
RT "Boat, an AXH domain protein, suppresses the cytotoxicity of mutant ataxin-
RT 1.";
RL EMBO J. 24:3339-3351(2005).
RN [14]
RP SUMOYLATION AT LYS-16; LYS-194; LYS-609; LYS-696 AND LYS-745, AND
RP MUTAGENESIS OF LYS-16; LYS-194; LYS-420; LYS-529; LYS-589; LYS-594;
RP LYS-609; LYS-691; LYS-696; LYS-745 AND LYS-784.
RX PubMed=15824120; DOI=10.1074/jbc.m501677200;
RA Riley B.E., Zoghbi H.Y., Orr H.T.;
RT "SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on
RT a functional nuclear localization signal.";
RL J. Biol. Chem. 280:21942-21948(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION BY
RP 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 [16]
RP FUNCTION, AND INTERACTION WITH RBPJ.
RX PubMed=21475249; DOI=10.1038/embor.2011.49;
RA Tong X., Gui H., Jin F., Heck B.W., Lin P., Ma J., Fondell J.D., Tsai C.C.;
RT "Ataxin-1 and Brother of ataxin-1 are components of the Notch signalling
RT pathway.";
RL EMBO Rep. 12:428-435(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [18]
RP INDUCTION.
RX PubMed=25768905; DOI=10.1016/j.cell.2015.02.012;
RA Gennarino V.A., Singh R.K., White J.J., De Maio A., Han K., Kim J.Y.,
RA Jafar-Nejad P., di Ronza A., Kang H., Sayegh L.S., Cooper T.A., Orr H.T.,
RA Sillitoe R.V., Zoghbi H.Y.;
RT "Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
RT increasing wild-type Ataxin1 levels.";
RL Cell 160:1087-1098(2015).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 563-693, AND SUBUNIT.
RX PubMed=14583607; DOI=10.1074/jbc.m309817200;
RA Chen Y.W., Allen M.D., Veprintsev D.B., Lowe J., Bycroft M.;
RT "The structure of the AXH domain of spinocerebellar ataxin-1.";
RL J. Biol. Chem. 279:3758-3765(2004).
CC -!- FUNCTION: Chromatin-binding factor that repress Notch signaling in the
CC absence of Notch intracellular domain by acting as a CBF1 corepressor.
CC Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-
CC mediated repression. Binds RNA in vitro. May be involved in RNA
CC metabolism (PubMed:21475249). In concert with CIC and ATXN1L, involved
CC in brain development (By similarity). {ECO:0000250|UniProtKB:P54254,
CC ECO:0000269|PubMed:21475249}.
CC -!- SUBUNIT: Homooligomer (PubMed:9097953). Interacts with CIC (By
CC similarity). Interacts with ANP32A, PQBP1, UBQLN4, ATXN1L and USP7
CC (PubMed:9353121, PubMed:11001934, PubMed:12062018, PubMed:12093161,
CC PubMed:16121196). Directly interacts with RBPJ; this interaction is
CC disrupted in the presence of Notch intracellular domain. Competes with
CC ATXN1L for RBPJ-binding (PubMed:21475249). Found in a complex with CIC
CC and ATXN1L (By similarity). {ECO:0000250|UniProtKB:P54254,
CC ECO:0000269|PubMed:11001934, ECO:0000269|PubMed:12062018,
CC ECO:0000269|PubMed:12093161, ECO:0000269|PubMed:14583607,
CC ECO:0000269|PubMed:16121196, ECO:0000269|PubMed:21475249,
CC ECO:0000269|PubMed:9097953, ECO:0000269|PubMed:9353121}.
CC -!- INTERACTION:
CC P54253; Q969K4: ABTB1; NbExp=3; IntAct=EBI-930964, EBI-7223971;
CC P54253; Q13444-2: ADAM15; NbExp=3; IntAct=EBI-930964, EBI-12137265;
CC P54253; Q5TGY3: AHDC1; NbExp=5; IntAct=EBI-930964, EBI-948813;
CC P54253; P54819: AK2; NbExp=3; IntAct=EBI-930964, EBI-1056291;
CC P54253; P31749: AKT1; NbExp=6; IntAct=EBI-930964, EBI-296087;
CC P54253; Q9H553: ALG2; NbExp=3; IntAct=EBI-930964, EBI-25806804;
CC P54253; Q8IWZ3-2: ANKHD1; NbExp=3; IntAct=EBI-930964, EBI-9641396;
CC P54253; Q8IWZ3-3: ANKHD1; NbExp=6; IntAct=EBI-930964, EBI-25833200;
CC P54253; P39687: ANP32A; NbExp=3; IntAct=EBI-930964, EBI-359234;
CC P54253; P13928: ANXA8; NbExp=6; IntAct=EBI-930964, EBI-2556915;
CC P54253; O43747-2: AP1G1; NbExp=3; IntAct=EBI-930964, EBI-10185819;
CC P54253; P63010-2: AP2B1; NbExp=6; IntAct=EBI-930964, EBI-11529439;
CC P54253; P05067: APP; NbExp=8; IntAct=EBI-930964, EBI-77613;
CC P54253; Q8N6T3-3: ARFGAP1; NbExp=6; IntAct=EBI-930964, EBI-10694449;
CC P54253; Q03989: ARID5A; NbExp=9; IntAct=EBI-930964, EBI-948603;
CC P54253; Q0P5N6: ARL16; NbExp=6; IntAct=EBI-930964, EBI-10186132;
CC P54253; Q8WXK3: ASB13; NbExp=6; IntAct=EBI-930964, EBI-707573;
CC P54253; Q9Y575-3: ASB3; NbExp=6; IntAct=EBI-930964, EBI-14199987;
CC P54253; Q96DX5-3: ASB9; NbExp=6; IntAct=EBI-930964, EBI-25843552;
CC P54253; Q96FT7-4: ASIC4; NbExp=6; IntAct=EBI-930964, EBI-9089489;
CC P54253; P18847: ATF3; NbExp=6; IntAct=EBI-930964, EBI-712767;
CC P54253; Q9H0Y0: ATG10; NbExp=6; IntAct=EBI-930964, EBI-1048913;
CC P54253; P06576: ATP5F1B; NbExp=3; IntAct=EBI-930964, EBI-356231;
CC P54253; P30049: ATP5F1D; NbExp=3; IntAct=EBI-930964, EBI-1049505;
CC P54253; P24539: ATP5PB; NbExp=3; IntAct=EBI-930964, EBI-1044810;
CC P54253; P61421: ATP6V0D1; NbExp=7; IntAct=EBI-930964, EBI-954063;
CC P54253; P15313: ATP6V1B1; NbExp=6; IntAct=EBI-930964, EBI-2891281;
CC P54253; P54253: ATXN1; NbExp=10; IntAct=EBI-930964, EBI-930964;
CC P54253; Q99700: ATXN2; NbExp=4; IntAct=EBI-930964, EBI-697691;
CC P54253; Q99700-5: ATXN2; NbExp=6; IntAct=EBI-930964, EBI-25891409;
CC P54253; O95816: BAG2; NbExp=4; IntAct=EBI-930964, EBI-355275;
CC P54253; Q9UQB8-6: BAIAP2; NbExp=6; IntAct=EBI-930964, EBI-9092016;
CC P54253; Q14457: BECN1; NbExp=6; IntAct=EBI-930964, EBI-949378;
CC P54253; O14503: BHLHE40; NbExp=3; IntAct=EBI-930964, EBI-711810;
CC P54253; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-930964, EBI-1012434;
CC P54253; O43684: BUB3; NbExp=7; IntAct=EBI-930964, EBI-1050987;
CC P54253; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-930964, EBI-12809220;
CC P54253; Q6P1W5: C1orf94; NbExp=18; IntAct=EBI-930964, EBI-946029;
CC P54253; Q9NUB4: C20orf141; NbExp=3; IntAct=EBI-930964, EBI-9088162;
CC P54253; Q9BVC5: C2orf49; NbExp=3; IntAct=EBI-930964, EBI-5458641;
CC P54253; Q5SZD1: C6orf141; NbExp=6; IntAct=EBI-930964, EBI-10697767;
CC P54253; Q14012: CAMK1; NbExp=12; IntAct=EBI-930964, EBI-6380130;
CC P54253; P22681: CBL; NbExp=3; IntAct=EBI-930964, EBI-518228;
CC P54253; Q9ULV8: CBLC; NbExp=6; IntAct=EBI-930964, EBI-2341018;
CC P54253; Q9NPC3: CCNB1IP1; NbExp=6; IntAct=EBI-930964, EBI-745269;
CC P54253; O75909: CCNK; NbExp=2; IntAct=EBI-930964, EBI-739806;
CC P54253; O75909-2: CCNK; NbExp=6; IntAct=EBI-930964, EBI-12010594;
CC P54253; P48643: CCT5; NbExp=3; IntAct=EBI-930964, EBI-355710;
CC P54253; P40227: CCT6A; NbExp=3; IntAct=EBI-930964, EBI-356687;
CC P54253; Q9UJX2: CDC23; NbExp=6; IntAct=EBI-930964, EBI-396137;
CC P54253; Q8NHZ8: CDC26; NbExp=3; IntAct=EBI-930964, EBI-2555941;
CC P54253; Q7Z7K6: CENPV; NbExp=6; IntAct=EBI-930964, EBI-1210604;
CC P54253; Q8NHQ1-3: CEP70; NbExp=3; IntAct=EBI-930964, EBI-11526150;
CC P54253; P23528: CFL1; NbExp=11; IntAct=EBI-930964, EBI-352733;
CC P54253; Q96RK0: CIC; NbExp=8; IntAct=EBI-930964, EBI-945857;
CC P54253; Q14011: CIRBP; NbExp=7; IntAct=EBI-930964, EBI-538850;
CC P54253; Q9NSE2: CISH; NbExp=6; IntAct=EBI-930964, EBI-617866;
CC P54253; P38432: COIL; NbExp=9; IntAct=EBI-930964, EBI-945751;
CC P54253; Q86WV2: COX4I1; NbExp=6; IntAct=EBI-930964, EBI-10260134;
CC P54253; Q8N684: CPSF7; NbExp=2; IntAct=EBI-930964, EBI-746909;
CC P54253; Q8N684-3: CPSF7; NbExp=6; IntAct=EBI-930964, EBI-11523759;
CC P54253; P46108: CRK; NbExp=9; IntAct=EBI-930964, EBI-886;
CC P54253; P46108-2: CRK; NbExp=6; IntAct=EBI-930964, EBI-287559;
CC P54253; Q8IUI8: CRLF3; NbExp=6; IntAct=EBI-930964, EBI-2872414;
CC P54253; O43186: CRX; NbExp=3; IntAct=EBI-930964, EBI-748171;
CC P54253; P53672: CRYBA2; NbExp=7; IntAct=EBI-930964, EBI-750444;
CC P54253; P56545-3: CTBP2; NbExp=3; IntAct=EBI-930964, EBI-10171902;
CC P54253; Q13619: CUL4A; NbExp=6; IntAct=EBI-930964, EBI-456106;
CC P54253; Q9NTM9: CUTC; NbExp=3; IntAct=EBI-930964, EBI-714918;
CC P54253; Q5D0E6-2: DALRD3; NbExp=6; IntAct=EBI-930964, EBI-9090939;
CC P54253; Q13117-3: DAZ2; NbExp=3; IntAct=EBI-930964, EBI-13357576;
CC P54253; Q15038: DAZAP2; NbExp=2; IntAct=EBI-930964, EBI-724310;
CC P54253; Q8WV16-4: DCAF4; NbExp=3; IntAct=EBI-930964, EBI-20852566;
CC P54253; O75935-2: DCTN3; NbExp=6; IntAct=EBI-930964, EBI-12091947;
CC P54253; Q5TDH0-2: DDI2; NbExp=6; IntAct=EBI-930964, EBI-25858598;
CC P54253; Q8NDP9: DKFZp547K2416; NbExp=6; IntAct=EBI-930964, EBI-25842538;
CC P54253; O60479: DLX3; NbExp=3; IntAct=EBI-930964, EBI-3908248;
CC P54253; Q09013: DMPK; NbExp=5; IntAct=EBI-930964, EBI-692774;
CC P54253; Q96EY1: DNAJA3; NbExp=7; IntAct=EBI-930964, EBI-356767;
CC P54253; Q96EY1-3: DNAJA3; NbExp=6; IntAct=EBI-930964, EBI-11526226;
CC P54253; Q9UDY4: DNAJB4; NbExp=3; IntAct=EBI-930964, EBI-356960;
CC P54253; Q86Y13: DZIP3; NbExp=7; IntAct=EBI-930964, EBI-948630;
CC P54253; Q3B7T1: EDRF1; NbExp=3; IntAct=EBI-930964, EBI-2870947;
CC P54253; O95967: EFEMP2; NbExp=8; IntAct=EBI-930964, EBI-743414;
CC P54253; O14602: EIF1AY; NbExp=7; IntAct=EBI-930964, EBI-286439;
CC P54253; P20042: EIF2S2; NbExp=3; IntAct=EBI-930964, EBI-711977;
CC P54253; O00303: EIF3F; NbExp=4; IntAct=EBI-930964, EBI-711990;
CC P54253; Q14240-2: EIF4A2; NbExp=3; IntAct=EBI-930964, EBI-10232522;
CC P54253; Q9NRA8: EIF4ENIF1; NbExp=4; IntAct=EBI-930964, EBI-301024;
CC P54253; Q15717: ELAVL1; NbExp=7; IntAct=EBI-930964, EBI-374260;
CC P54253; O00472: ELL2; NbExp=6; IntAct=EBI-930964, EBI-395274;
CC P54253; Q8TE02: ELP5; NbExp=8; IntAct=EBI-930964, EBI-946189;
CC P54253; Q32P44: EML3; NbExp=3; IntAct=EBI-930964, EBI-1046713;
CC P54253; Q8TC29: ENKUR; NbExp=6; IntAct=EBI-930964, EBI-9246952;
CC P54253; O95208-2: EPN2; NbExp=3; IntAct=EBI-930964, EBI-12135243;
CC P54253; Q13216-2: ERCC8; NbExp=3; IntAct=EBI-930964, EBI-16466949;
CC P54253; Q6NXG1: ESRP1; NbExp=12; IntAct=EBI-930964, EBI-10213520;
CC P54253; Q6NXG1-3: ESRP1; NbExp=6; IntAct=EBI-930964, EBI-21567429;
CC P54253; O43909: EXTL3; NbExp=3; IntAct=EBI-930964, EBI-1754679;
CC P54253; P0C7A2-2: FAM153B; NbExp=3; IntAct=EBI-930964, EBI-12940382;
CC P54253; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-930964, EBI-11978259;
CC P54253; Q9NSD9: FARSB; NbExp=3; IntAct=EBI-930964, EBI-353803;
CC P54253; P14324: FDPS; NbExp=4; IntAct=EBI-930964, EBI-948245;
CC P54253; Q9UHY8: FEZ2; NbExp=6; IntAct=EBI-930964, EBI-396453;
CC P54253; P26885: FKBP2; NbExp=3; IntAct=EBI-930964, EBI-719873;
CC P54253; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-930964, EBI-12142257;
CC P54253; Q96NZ1: FOXN4; NbExp=3; IntAct=EBI-930964, EBI-11749712;
CC P54253; P02792: FTL; NbExp=6; IntAct=EBI-930964, EBI-713279;
CC P54253; P06241: FYN; NbExp=8; IntAct=EBI-930964, EBI-515315;
CC P54253; P06241-3: FYN; NbExp=6; IntAct=EBI-930964, EBI-10691738;
CC P54253; Q06547-2: GABPB1; NbExp=6; IntAct=EBI-930964, EBI-618189;
CC P54253; F2Z2M7: GALNT10; NbExp=6; IntAct=EBI-930964, EBI-23893155;
CC P54253; P28676: GCA; NbExp=4; IntAct=EBI-930964, EBI-947242;
CC P54253; Q9UKD1: GMEB2; NbExp=5; IntAct=EBI-930964, EBI-948296;
CC P54253; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-930964, EBI-739467;
CC P54253; Q9UKJ3: GPATCH8; NbExp=4; IntAct=EBI-930964, EBI-948259;
CC P54253; Q93079: H2BC9; NbExp=3; IntAct=EBI-930964, EBI-352469;
CC P54253; P15822: HIVEP1; NbExp=6; IntAct=EBI-930964, EBI-722264;
CC P54253; Q8WVV9-3: HNRNPLL; NbExp=6; IntAct=EBI-930964, EBI-25845242;
CC P54253; P09017: HOXC4; NbExp=6; IntAct=EBI-930964, EBI-3923226;
CC P54253; P37235: HPCAL1; NbExp=7; IntAct=EBI-930964, EBI-749311;
CC P54253; Q9UBD0: HSFX2; NbExp=6; IntAct=EBI-930964, EBI-947253;
CC P54253; Q96LI6: HSFY2; NbExp=3; IntAct=EBI-930964, EBI-3957665;
CC P54253; P0DMV8: HSPA1A; NbExp=3; IntAct=EBI-930964, EBI-11052499;
CC P54253; P11142: HSPA8; NbExp=13; IntAct=EBI-930964, EBI-351896;
CC P54253; P80217-2: IFI35; NbExp=3; IntAct=EBI-930964, EBI-12823003;
CC P54253; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-930964, EBI-9091197;
CC P54253; P29218-3: IMPA1; NbExp=3; IntAct=EBI-930964, EBI-12330251;
CC P54253; Q6DN90-2: IQSEC1; NbExp=6; IntAct=EBI-930964, EBI-21911304;
CC P54253; P53990: IST1; NbExp=2; IntAct=EBI-930964, EBI-945994;
CC P54253; P53990-2: IST1; NbExp=6; IntAct=EBI-930964, EBI-4402971;
CC P54253; P53990-3: IST1; NbExp=9; IntAct=EBI-930964, EBI-12188567;
CC P54253; O14713: ITGB1BP1; NbExp=3; IntAct=EBI-930964, EBI-2127319;
CC P54253; Q92993: KAT5; NbExp=9; IntAct=EBI-930964, EBI-399080;
CC P54253; Q92993-2: KAT5; NbExp=3; IntAct=EBI-930964, EBI-20795332;
CC P54253; Q9NVX7-2: KBTBD4; NbExp=6; IntAct=EBI-930964, EBI-25871195;
CC P54253; Q96SI1-2: KCTD15; NbExp=6; IntAct=EBI-930964, EBI-12382297;
CC P54253; P57682: KLF3; NbExp=4; IntAct=EBI-930964, EBI-8472267;
CC P54253; Q13887: KLF5; NbExp=7; IntAct=EBI-930964, EBI-2696013;
CC P54253; Q53G59: KLHL12; NbExp=8; IntAct=EBI-930964, EBI-740929;
CC P54253; Q6TDP4: KLHL17; NbExp=6; IntAct=EBI-930964, EBI-21328926;
CC P54253; Q9Y2M5: KLHL20; NbExp=6; IntAct=EBI-930964, EBI-714379;
CC P54253; Q8N4N3-2: KLHL36; NbExp=6; IntAct=EBI-930964, EBI-10973851;
CC P54253; P60329: KRTAP12-4; NbExp=3; IntAct=EBI-930964, EBI-10176396;
CC P54253; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-930964, EBI-10241252;
CC P54253; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-930964, EBI-12811111;
CC P54253; Q8IUC2: KRTAP8-1; NbExp=6; IntAct=EBI-930964, EBI-10261141;
CC P54253; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-930964, EBI-1044640;
CC P54253; Q96JM7-2: L3MBTL3; NbExp=6; IntAct=EBI-930964, EBI-11985629;
CC P54253; Q14847-2: LASP1; NbExp=9; IntAct=EBI-930964, EBI-9088686;
CC P54253; O95447: LCA5L; NbExp=3; IntAct=EBI-930964, EBI-8473670;
CC P54253; Q9BYZ2: LDHAL6B; NbExp=6; IntAct=EBI-930964, EBI-1108377;
CC P54253; Q6DKI2: LGALS9C; NbExp=6; IntAct=EBI-930964, EBI-9088829;
CC P54253; Q9UPM6: LHX6; NbExp=6; IntAct=EBI-930964, EBI-10258746;
CC P54253; Q8N0U6: LINC00518; NbExp=6; IntAct=EBI-930964, EBI-10264791;
CC P54253; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-930964, EBI-739832;
CC P54253; Q8N448: LNX2; NbExp=6; IntAct=EBI-930964, EBI-2340947;
CC P54253; Q6UWE0: LRSAM1; NbExp=4; IntAct=EBI-930964, EBI-720984;
CC P54253; Q86VM6: MBNL1; NbExp=6; IntAct=EBI-930964, EBI-10225084;
CC P54253; Q9NR56-5: MBNL1; NbExp=6; IntAct=EBI-930964, EBI-25978262;
CC P54253; Q96RN5-2: MED15; NbExp=6; IntAct=EBI-930964, EBI-11030807;
CC P54253; Q9H7H0: METTL17; NbExp=5; IntAct=EBI-930964, EBI-749353;
CC P54253; Q9H7H0-2: METTL17; NbExp=6; IntAct=EBI-930964, EBI-11098807;
CC P54253; Q8N6F8: METTL27; NbExp=9; IntAct=EBI-930964, EBI-8487781;
CC P54253; Q8TDB4: MGARP; NbExp=6; IntAct=EBI-930964, EBI-4397720;
CC P54253; A4FUJ8: MKL1; NbExp=6; IntAct=EBI-930964, EBI-21250407;
CC P54253; Q9BUB5: MKNK1; NbExp=6; IntAct=EBI-930964, EBI-73837;
CC P54253; O95396: MOCS3; NbExp=6; IntAct=EBI-930964, EBI-373206;
CC P54253; Q8N594: MPND; NbExp=6; IntAct=EBI-930964, EBI-2512452;
CC P54253; Q9Y605: MRFAP1; NbExp=6; IntAct=EBI-930964, EBI-995714;
CC P54253; Q96HT8: MRFAP1L1; NbExp=6; IntAct=EBI-930964, EBI-748896;
CC P54253; O43776: NARS1; NbExp=4; IntAct=EBI-930964, EBI-373505;
CC P54253; O76041: NEBL; NbExp=3; IntAct=EBI-930964, EBI-2880203;
CC P54253; Q86SG6: NEK8; NbExp=3; IntAct=EBI-930964, EBI-1752987;
CC P54253; Q12986: NFX1; NbExp=3; IntAct=EBI-930964, EBI-2130062;
CC P54253; P23511-2: NFYA; NbExp=3; IntAct=EBI-930964, EBI-11061759;
CC P54253; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-930964, EBI-2859639;
CC P54253; Q9UBE8: NLK; NbExp=4; IntAct=EBI-930964, EBI-366978;
CC P54253; O00746: NME4; NbExp=6; IntAct=EBI-930964, EBI-744871;
CC P54253; P56597: NME5; NbExp=3; IntAct=EBI-930964, EBI-740667;
CC P54253; Q15738: NSDHL; NbExp=3; IntAct=EBI-930964, EBI-4280135;
CC P54253; O43809: NUDT21; NbExp=8; IntAct=EBI-930964, EBI-355720;
CC P54253; Q8NFH3: NUP43; NbExp=6; IntAct=EBI-930964, EBI-1059321;
CC P54253; O15381-5: NVL; NbExp=3; IntAct=EBI-930964, EBI-18577082;
CC P54253; Q02218: OGDH; NbExp=3; IntAct=EBI-930964, EBI-747213;
CC P54253; Q96FW1: OTUB1; NbExp=6; IntAct=EBI-930964, EBI-1058491;
CC P54253; Q6GQQ9-2: OTUD7B; NbExp=6; IntAct=EBI-930964, EBI-25830200;
CC P54253; P32243-2: OTX2; NbExp=3; IntAct=EBI-930964, EBI-9087860;
CC P54253; Q6VY07: PACS1; NbExp=6; IntAct=EBI-930964, EBI-2555014;
CC P54253; Q495U3: PANX2; NbExp=3; IntAct=EBI-930964, EBI-17242559;
CC P54253; Q9BR81: PCDHGC3; NbExp=6; IntAct=EBI-930964, EBI-22012354;
CC P54253; P22061-2: PCMT1; NbExp=3; IntAct=EBI-930964, EBI-12386584;
CC P54253; Q9NV79: PCMTD2; NbExp=6; IntAct=EBI-930964, EBI-6309018;
CC P54253; Q96HC4: PDLIM5; NbExp=6; IntAct=EBI-930964, EBI-751267;
CC P54253; Q13113: PDZK1IP1; NbExp=6; IntAct=EBI-930964, EBI-716063;
CC P54253; P12955: PEPD; NbExp=4; IntAct=EBI-930964, EBI-948765;
CC P54253; O00541: PES1; NbExp=3; IntAct=EBI-930964, EBI-1053271;
CC P54253; Q9NRX4: PHPT1; NbExp=8; IntAct=EBI-930964, EBI-740955;
CC P54253; O75925: PIAS1; NbExp=7; IntAct=EBI-930964, EBI-629434;
CC P54253; Q13492-3: PICALM; NbExp=3; IntAct=EBI-930964, EBI-11031437;
CC P54253; P42336: PIK3CA; NbExp=3; IntAct=EBI-930964, EBI-2116585;
CC P54253; Q9P1W9: PIM2; NbExp=4; IntAct=EBI-930964, EBI-720425;
CC P54253; Q96J94: PIWIL1; NbExp=3; IntAct=EBI-930964, EBI-527417;
CC P54253; O15496: PLA2G10; NbExp=3; IntAct=EBI-930964, EBI-726466;
CC P54253; Q9HAU0: PLEKHA5; NbExp=2; IntAct=EBI-930964, EBI-945934;
CC P54253; Q6ZR37: PLEKHG7; NbExp=6; IntAct=EBI-930964, EBI-12891828;
CC P54253; Q494U1-3: PLEKHN1; NbExp=6; IntAct=EBI-930964, EBI-12014286;
CC P54253; O43660-2: PLRG1; NbExp=3; IntAct=EBI-930964, EBI-11743883;
CC P54253; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-930964, EBI-1389308;
CC P54253; Q9P1U0: POLR1H; NbExp=3; IntAct=EBI-930964, EBI-355434;
CC P54253; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-930964, EBI-11956563;
CC P54253; Q6ZMI0-5: PPP1R21; NbExp=6; IntAct=EBI-930964, EBI-25835994;
CC P54253; O60828: PQBP1; NbExp=3; IntAct=EBI-930964, EBI-713867;
CC P54253; Q13162: PRDX4; NbExp=4; IntAct=EBI-930964, EBI-2211957;
CC P54253; P17612: PRKACA; NbExp=3; IntAct=EBI-930964, EBI-476586;
CC P54253; O60260-5: PRKN; NbExp=6; IntAct=EBI-930964, EBI-21251460;
CC P54253; Q6P2Q9: PRPF8; NbExp=6; IntAct=EBI-930964, EBI-538479;
CC P54253; P86479: PRR20C; NbExp=3; IntAct=EBI-930964, EBI-10172814;
CC P54253; P86480: PRR20D; NbExp=3; IntAct=EBI-930964, EBI-12754095;
CC P54253; P48634: PRRC2A; NbExp=4; IntAct=EBI-930964, EBI-347545;
CC P54253; Q5JSZ5: PRRC2B; NbExp=5; IntAct=EBI-930964, EBI-744891;
CC P54253; Q5JSZ5-5: PRRC2B; NbExp=6; IntAct=EBI-930964, EBI-21531669;
CC P54253; P25786: PSMA1; NbExp=3; IntAct=EBI-930964, EBI-359352;
CC P54253; P25789: PSMA4; NbExp=7; IntAct=EBI-930964, EBI-359310;
CC P54253; P28070: PSMB4; NbExp=6; IntAct=EBI-930964, EBI-603350;
CC P54253; P28062-2: PSMB8; NbExp=6; IntAct=EBI-930964, EBI-372312;
CC P54253; P17980: PSMC3; NbExp=7; IntAct=EBI-930964, EBI-359720;
CC P54253; P41222: PTGDS; NbExp=5; IntAct=EBI-930964, EBI-948821;
CC P54253; Q15032-2: R3HDM1; NbExp=3; IntAct=EBI-930964, EBI-10966812;
CC P54253; Q9NS91: RAD18; NbExp=6; IntAct=EBI-930964, EBI-2339393;
CC P54253; P54725: RAD23A; NbExp=3; IntAct=EBI-930964, EBI-746453;
CC P54253; Q9Y620: RAD54B; NbExp=3; IntAct=EBI-930964, EBI-740830;
CC P54253; Q8WZA2-3: RAPGEF4; NbExp=3; IntAct=EBI-930964, EBI-25977442;
CC P54253; Q13702-2: RAPSN; NbExp=6; IntAct=EBI-930964, EBI-22012855;
CC P54253; Q09028: RBBP4; NbExp=3; IntAct=EBI-930964, EBI-620823;
CC P54253; Q9BYM8: RBCK1; NbExp=6; IntAct=EBI-930964, EBI-2340624;
CC P54253; Q9NWB1: RBFOX1; NbExp=2; IntAct=EBI-930964, EBI-945906;
CC P54253; Q9NWB1-5: RBFOX1; NbExp=6; IntAct=EBI-930964, EBI-12123390;
CC P54253; O43251: RBFOX2; NbExp=10; IntAct=EBI-930964, EBI-746056;
CC P54253; O43251-10: RBFOX2; NbExp=3; IntAct=EBI-930964, EBI-11963050;
CC P54253; Q96I25: RBM17; NbExp=5; IntAct=EBI-930964, EBI-740272;
CC P54253; Q06330: RBPJ; NbExp=7; IntAct=EBI-930964, EBI-632552;
CC P54253; Q93062: RBPMS; NbExp=6; IntAct=EBI-930964, EBI-740322;
CC P54253; Q93062-3: RBPMS; NbExp=6; IntAct=EBI-930964, EBI-740343;
CC P54253; Q15293: RCN1; NbExp=9; IntAct=EBI-930964, EBI-948278;
CC P54253; Q04864: REL; NbExp=3; IntAct=EBI-930964, EBI-307352;
CC P54253; Q04864-2: REL; NbExp=3; IntAct=EBI-930964, EBI-10829018;
CC P54253; Q8TAI7: RHEBL1; NbExp=3; IntAct=EBI-930964, EBI-746555;
CC P54253; Q9BQY4: RHOXF2; NbExp=4; IntAct=EBI-930964, EBI-372094;
CC P54253; Q9H871: RMND5A; NbExp=6; IntAct=EBI-930964, EBI-2797992;
CC P54253; Q6ZNA4-2: RNF111; NbExp=6; IntAct=EBI-930964, EBI-21535400;
CC P54253; Q9ULX5: RNF112; NbExp=6; IntAct=EBI-930964, EBI-25829984;
CC P54253; Q8WU17: RNF139; NbExp=6; IntAct=EBI-930964, EBI-1551681;
CC P54253; Q96D59: RNF183; NbExp=6; IntAct=EBI-930964, EBI-743938;
CC P54253; Q99496: RNF2; NbExp=6; IntAct=EBI-930964, EBI-722416;
CC P54253; Q96EP0: RNF31; NbExp=4; IntAct=EBI-930964, EBI-948111;
CC P54253; Q9H0F5-2: RNF38; NbExp=6; IntAct=EBI-930964, EBI-25866807;
CC P54253; P27635: RPL10; NbExp=3; IntAct=EBI-930964, EBI-352398;
CC P54253; P61313: RPL15; NbExp=3; IntAct=EBI-930964, EBI-443462;
CC P54253; Q07020: RPL18; NbExp=3; IntAct=EBI-930964, EBI-352694;
CC P54253; P84098: RPL19; NbExp=3; IntAct=EBI-930964, EBI-916524;
CC P54253; P35268: RPL22; NbExp=3; IntAct=EBI-930964, EBI-354533;
CC P54253; P39019: RPS19; NbExp=3; IntAct=EBI-930964, EBI-354451;
CC P54253; P46782: RPS5; NbExp=3; IntAct=EBI-930964, EBI-350569;
CC P54253; Q8N488: RYBP; NbExp=6; IntAct=EBI-930964, EBI-752324;
CC P54253; Q8N6K7-2: SAMD3; NbExp=3; IntAct=EBI-930964, EBI-11528848;
CC P54253; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-930964, EBI-3920694;
CC P54253; O00560: SDCBP; NbExp=6; IntAct=EBI-930964, EBI-727004;
CC P54253; P50454: SERPINH1; NbExp=3; IntAct=EBI-930964, EBI-350723;
CC P54253; Q15637-4: SF1; NbExp=3; IntAct=EBI-930964, EBI-12223157;
CC P54253; Q12874: SF3A3; NbExp=6; IntAct=EBI-930964, EBI-1051880;
CC P54253; Q15393: SF3B3; NbExp=3; IntAct=EBI-930964, EBI-346977;
CC P54253; Q2NKQ1-4: SGSM1; NbExp=6; IntAct=EBI-930964, EBI-10182463;
CC P54253; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-930964, EBI-11522811;
CC P54253; Q8N196: SIX5; NbExp=4; IntAct=EBI-930964, EBI-946167;
CC P54253; P63208: SKP1; NbExp=6; IntAct=EBI-930964, EBI-307486;
CC P54253; Q86UW1: SLC51A; NbExp=7; IntAct=EBI-930964, EBI-945738;
CC P54253; Q9NSD5-3: SLC6A13; NbExp=6; IntAct=EBI-930964, EBI-25831241;
CC P54253; Q96GM5: SMARCD1; NbExp=6; IntAct=EBI-930964, EBI-358489;
CC P54253; O95721: SNAP29; NbExp=3; IntAct=EBI-930964, EBI-490676;
CC P54253; Q96DI7: SNRNP40; NbExp=3; IntAct=EBI-930964, EBI-538492;
CC P54253; P14678: SNRPB; NbExp=3; IntAct=EBI-930964, EBI-372458;
CC P54253; P62316: SNRPD2; NbExp=3; IntAct=EBI-930964, EBI-297993;
CC P54253; P62318: SNRPD3; NbExp=3; IntAct=EBI-930964, EBI-372789;
CC P54253; Q9UPU3: SORCS3; NbExp=3; IntAct=EBI-930964, EBI-7484437;
CC P54253; O95416: SOX14; NbExp=3; IntAct=EBI-930964, EBI-9087806;
CC P54253; P41225: SOX3; NbExp=3; IntAct=EBI-930964, EBI-9078386;
CC P54253; Q99932-2: SPAG8; NbExp=6; IntAct=EBI-930964, EBI-11959123;
CC P54253; Q8IUW3: SPATA2L; NbExp=3; IntAct=EBI-930964, EBI-2510414;
CC P54253; P61009: SPCS3; NbExp=4; IntAct=EBI-930964, EBI-6166040;
CC P54253; Q13501: SQSTM1; NbExp=4; IntAct=EBI-930964, EBI-307104;
CC P54253; P36956: SREBF1; NbExp=5; IntAct=EBI-930964, EBI-948313;
CC P54253; Q969X2: ST6GALNAC6; NbExp=7; IntAct=EBI-930964, EBI-949146;
CC P54253; Q6ZMT1: STAC2; NbExp=4; IntAct=EBI-930964, EBI-948802;
CC P54253; O75886: STAM2; NbExp=8; IntAct=EBI-930964, EBI-373258;
CC P54253; O95630: STAMBP; NbExp=6; IntAct=EBI-930964, EBI-396676;
CC P54253; P55854: SUMO3; NbExp=6; IntAct=EBI-930964, EBI-474067;
CC P54253; Q8NEM7: SUPT20H; NbExp=7; IntAct=EBI-930964, EBI-946984;
CC P54253; Q9NX95: SYBU; NbExp=3; IntAct=EBI-930964, EBI-948293;
CC P54253; Q9NX95-5: SYBU; NbExp=6; IntAct=EBI-930964, EBI-12816095;
CC P54253; Q92609: TBC1D5; NbExp=2; IntAct=EBI-930964, EBI-742381;
CC P54253; Q9BZK7: TBL1XR1; NbExp=6; IntAct=EBI-930964, EBI-765729;
CC P54253; Q16650: TBR1; NbExp=7; IntAct=EBI-930964, EBI-1047158;
CC P54253; Q96SF7: TBX15; NbExp=3; IntAct=EBI-930964, EBI-10191361;
CC P54253; Q9Y458: TBX22; NbExp=3; IntAct=EBI-930964, EBI-6427217;
CC P54253; O15273: TCAP; NbExp=8; IntAct=EBI-930964, EBI-954089;
CC P54253; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-930964, EBI-11955057;
CC P54253; P28347-2: TEAD1; NbExp=3; IntAct=EBI-930964, EBI-12151837;
CC P54253; Q96IP4: TENT5A; NbExp=5; IntAct=EBI-930964, EBI-954084;
CC P54253; Q96A09: TENT5B; NbExp=11; IntAct=EBI-930964, EBI-752030;
CC P54253; Q15554-4: TERF2; NbExp=6; IntAct=EBI-930964, EBI-25840535;
CC P54253; P37173: TGFBR2; NbExp=3; IntAct=EBI-930964, EBI-296151;
CC P54253; O95411: TIAF1; NbExp=3; IntAct=EBI-930964, EBI-302378;
CC P54253; Q08117: TLE5; NbExp=3; IntAct=EBI-930964, EBI-717810;
CC P54253; Q9NV96-2: TMEM30A; NbExp=6; IntAct=EBI-930964, EBI-12921610;
CC P54253; Q71RG4-4: TMUB2; NbExp=3; IntAct=EBI-930964, EBI-25831574;
CC P54253; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-930964, EBI-2505861;
CC P54253; Q9H0E2: TOLLIP; NbExp=7; IntAct=EBI-930964, EBI-74615;
CC P54253; O94842: TOX4; NbExp=7; IntAct=EBI-930964, EBI-948613;
CC P54253; P06753: TPM3; NbExp=4; IntAct=EBI-930964, EBI-355607;
CC P54253; P06753-2: TPM3; NbExp=3; IntAct=EBI-930964, EBI-10977875;
CC P54253; Q8N7U7-2: TPRX1; NbExp=3; IntAct=EBI-930964, EBI-14115717;
CC P54253; Q12933: TRAF2; NbExp=14; IntAct=EBI-930964, EBI-355744;
CC P54253; P36406: TRIM23; NbExp=6; IntAct=EBI-930964, EBI-740098;
CC P54253; Q13049: TRIM32; NbExp=5; IntAct=EBI-930964, EBI-742790;
CC P54253; O00635: TRIM38; NbExp=5; IntAct=EBI-930964, EBI-2130415;
CC P54253; L8E9Q5: TRIM65; NbExp=6; IntAct=EBI-930964, EBI-25843781;
CC P54253; Q86WT6-2: TRIM69; NbExp=6; IntAct=EBI-930964, EBI-11525489;
CC P54253; Q86UV6-2: TRIM74; NbExp=6; IntAct=EBI-930964, EBI-10259086;
CC P54253; Q9C026: TRIM9; NbExp=6; IntAct=EBI-930964, EBI-720828;
CC P54253; Q15654: TRIP6; NbExp=7; IntAct=EBI-930964, EBI-742327;
CC P54253; Q86WV8: TSC1; NbExp=3; IntAct=EBI-930964, EBI-12806590;
CC P54253; Q6DKK2: TTC19; NbExp=7; IntAct=EBI-930964, EBI-948354;
CC P54253; Q8WVJ9: TWIST2; NbExp=6; IntAct=EBI-930964, EBI-1797313;
CC P54253; Q01081: U2AF1; NbExp=4; IntAct=EBI-930964, EBI-632461;
CC P54253; P26368: U2AF2; NbExp=5; IntAct=EBI-930964, EBI-742339;
CC P54253; Q9BSL1: UBAC1; NbExp=6; IntAct=EBI-930964, EBI-749370;
CC P54253; Q969T4: UBE2E3; NbExp=7; IntAct=EBI-930964, EBI-348496;
CC P54253; P63279: UBE2I; NbExp=7; IntAct=EBI-930964, EBI-80168;
CC P54253; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-930964, EBI-10180829;
CC P54253; Q13404: UBE2V1; NbExp=6; IntAct=EBI-930964, EBI-1050671;
CC P54253; O94941: UBOX5; NbExp=6; IntAct=EBI-930964, EBI-751901;
CC P54253; Q9NRR5: UBQLN4; NbExp=6; IntAct=EBI-930964, EBI-711226;
CC P54253; O75604-3: USP2; NbExp=6; IntAct=EBI-930964, EBI-10696113;
CC P54253; Q70CQ3: USP30; NbExp=3; IntAct=EBI-930964, EBI-2512374;
CC P54253; P62068: USP46; NbExp=6; IntAct=EBI-930964, EBI-2512753;
CC P54253; Q70EL1: USP54; NbExp=3; IntAct=EBI-930964, EBI-946185;
CC P54253; Q70EL1-9: USP54; NbExp=6; IntAct=EBI-930964, EBI-11975223;
CC P54253; P55072: VCP; NbExp=3; IntAct=EBI-930964, EBI-355164;
CC P54253; O75351: VPS4B; NbExp=3; IntAct=EBI-930964, EBI-2514459;
CC P54253; P62760: VSNL1; NbExp=7; IntAct=EBI-930964, EBI-740943;
CC P54253; Q96N03: VSTM2L; NbExp=9; IntAct=EBI-930964, EBI-948213;
CC P54253; Q9GZS3: WDR61; NbExp=6; IntAct=EBI-930964, EBI-358545;
CC P54253; Q9BRX9: WDR83; NbExp=6; IntAct=EBI-930964, EBI-7705033;
CC P54253; P31946: YWHAB; NbExp=4; IntAct=EBI-930964, EBI-359815;
CC P54253; P62258: YWHAE; NbExp=8; IntAct=EBI-930964, EBI-356498;
CC P54253; Q04917: YWHAH; NbExp=8; IntAct=EBI-930964, EBI-306940;
CC P54253; P27348: YWHAQ; NbExp=4; IntAct=EBI-930964, EBI-359854;
CC P54253; P63104: YWHAZ; NbExp=8; IntAct=EBI-930964, EBI-347088;
CC P54253; Q9H869: YY1AP1; NbExp=4; IntAct=EBI-930964, EBI-946122;
CC P54253; Q9H869-2: YY1AP1; NbExp=15; IntAct=EBI-930964, EBI-12150045;
CC P54253; A0A0C4DGF1: ZBTB32; NbExp=3; IntAct=EBI-930964, EBI-10188476;
CC P54253; O43298: ZBTB43; NbExp=7; IntAct=EBI-930964, EBI-740718;
CC P54253; Q96K80: ZC3H10; NbExp=7; IntAct=EBI-930964, EBI-742550;
CC P54253; Q86WB0-2: ZC3HC1; NbExp=6; IntAct=EBI-930964, EBI-25894765;
CC P54253; Q9UKY1: ZHX1; NbExp=11; IntAct=EBI-930964, EBI-347767;
CC P54253; Q9H4I2-2: ZHX3; NbExp=6; IntAct=EBI-930964, EBI-10693326;
CC P54253; Q96NC0: ZMAT2; NbExp=6; IntAct=EBI-930964, EBI-2682299;
CC P54253; O95789-4: ZMYM6; NbExp=6; IntAct=EBI-930964, EBI-12949277;
CC P54253; Q8N554: ZNF276; NbExp=4; IntAct=EBI-930964, EBI-750821;
CC P54253; Q8N895: ZNF366; NbExp=6; IntAct=EBI-930964, EBI-2813661;
CC P54253; Q96MN9: ZNF488; NbExp=9; IntAct=EBI-930964, EBI-948288;
CC P54253; Q96MN9-2: ZNF488; NbExp=6; IntAct=EBI-930964, EBI-25831733;
CC P54253; Q8N988-2: ZNF557; NbExp=3; IntAct=EBI-930964, EBI-10699005;
CC P54253; Q8NBB4-2: ZSCAN1; NbExp=6; IntAct=EBI-930964, EBI-12021938;
CC P54253; Q2QGD7: ZXDC; NbExp=7; IntAct=EBI-930964, EBI-1538838;
CC P54253; Q9H669; NbExp=3; IntAct=EBI-930964, EBI-10307430;
CC P54253; Q9Y649; NbExp=3; IntAct=EBI-930964, EBI-25900580;
CC P54253-1; P38432: COIL; NbExp=6; IntAct=EBI-930975, EBI-945751;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7647801}. Nucleus
CC {ECO:0000269|PubMed:12093161, ECO:0000269|PubMed:7647801}.
CC Note=Colocalizes with USP7 in the nucleus.
CC {ECO:0000269|PubMed:12093161}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=At least 2 isoforms are produced.;
CC Name=1;
CC IsoId=P54253-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Widely expressed throughout the body.
CC {ECO:0000269|PubMed:12062018}.
CC -!- INDUCTION: ATXN1 protein levels are directly regulated by PUM1 protein:
CC PUM1 acts by binding to the 3'-UTR of ATXN1 mRNA, affecting ATXN1 mRNA
CC stability and leading to reduced ATXN1 protein levels.
CC {ECO:0000269|PubMed:25768905}.
CC -!- DOMAIN: The AXH domain is required for interaction with CIC.
CC {ECO:0000250|UniProtKB:P54254}.
CC -!- PTM: Ubiquitinated by UBE3A, leading to its degradation by the
CC proteasome. The presence of expanded poly-Gln repeats in
CC spinocerebellar ataxia 1 (SCA1) patients impairs ubiquitination and
CC degradation, leading to accumulation of ATXN1 in neurons and subsequent
CC toxicity. {ECO:0000250|UniProtKB:P54254}.
CC -!- PTM: Phosphorylation at Ser-775 increases the pathogenicity of proteins
CC with an expanded polyglutamine tract. {ECO:0000269|PubMed:12741986}.
CC -!- PTM: Sumoylation is dependent on nuclear localization and
CC phosphorylation at Ser-775. It is reduced in the presence of an
CC expanded polyglutamine tract. {ECO:0000269|PubMed:12741986,
CC ECO:0000269|PubMed:15824120}.
CC -!- POLYMORPHISM: The poly-Gln region of ATXN1 is highly polymorphic (4 to
CC 39 repeats) in the normal population and is expanded to about 40-83
CC repeats in spinocerebellar ataxia 1 (SCA1) patients.
CC {ECO:0000269|PubMed:8634720}.
CC -!- DISEASE: Spinocerebellar ataxia 1 (SCA1) [MIM:164400]: Spinocerebellar
CC ataxia is a clinically and genetically heterogeneous group of
CC cerebellar disorders. Patients show progressive incoordination of gait
CC and often poor coordination of hands, speech and eye movements, due to
CC cerebellum degeneration with variable involvement of the brainstem and
CC spinal cord. SCA1 belongs to the autosomal dominant cerebellar ataxias
CC type I (ADCA I) which are characterized by cerebellar ataxia in
CC combination with additional clinical features like optic atrophy,
CC ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy
CC and dementia. SCA1 is caused by expansion of a CAG repeat in the coding
CC region of ATXN1. Longer expansions result in earlier onset and more
CC severe clinical manifestations of the disease.
CC {ECO:0000269|PubMed:7647801, ECO:0000269|PubMed:7951322,
CC ECO:0000269|PubMed:8634720}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. The disease is caused by
CC expansion of the polyglutamine tract to about 40-83 repeats, causing
CC accumulation in neurons and exerting toxicity.
CC {ECO:0000269|PubMed:7647801, ECO:0000269|PubMed:8634720}.
CC -!- MISCELLANEOUS: Self-association seems to be necessary for formation of
CC nuclear aggregates which are associated with pathogenesis.
CC -!- SIMILARITY: Belongs to the ATXN1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ataxin-1 entry;
CC URL="https://en.wikipedia.org/wiki/Ataxin_1";
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DR EMBL; X79204; CAA55793.1; -; mRNA.
DR EMBL; AL009031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117125; AAI17126.1; -; mRNA.
DR EMBL; S82497; AAD14401.1; -; Genomic_DNA.
DR CCDS; CCDS34342.1; -. [P54253-1]
DR PIR; S46268; S46268.
DR RefSeq; NP_000323.2; NM_000332.3. [P54253-1]
DR RefSeq; NP_001121636.1; NM_001128164.1. [P54253-1]
DR PDB; 1OA8; X-ray; 1.70 A; A/B/C/D=562-693.
DR PDB; 2M41; NMR; -; B=566-688.
DR PDB; 4APT; X-ray; 2.50 A; A/B/C/D=566-688.
DR PDB; 4AQP; X-ray; 2.45 A; A/B/C/D=566-688.
DR PDB; 4J2J; X-ray; 2.50 A; A/B/C=562-688.
DR PDB; 4J2L; X-ray; 3.15 A; A/B=562-688.
DR PDB; 6QIU; X-ray; 1.80 A; P=771-780.
DR PDBsum; 1OA8; -.
DR PDBsum; 2M41; -.
DR PDBsum; 4APT; -.
DR PDBsum; 4AQP; -.
DR PDBsum; 4J2J; -.
DR PDBsum; 4J2L; -.
DR PDBsum; 6QIU; -.
DR AlphaFoldDB; P54253; -.
DR BMRB; P54253; -.
DR SASBDB; P54253; -.
DR SMR; P54253; -.
DR BioGRID; 112217; 396.
DR CORUM; P54253; -.
DR DIP; DIP-35353N; -.
DR IntAct; P54253; 566.
DR MINT; P54253; -.
DR STRING; 9606.ENSP00000244769; -.
DR BindingDB; P54253; -.
DR MoonDB; P54253; Predicted.
DR GlyGen; P54253; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P54253; -.
DR PhosphoSitePlus; P54253; -.
DR BioMuta; ATXN1; -.
DR DMDM; 206729854; -.
DR EPD; P54253; -.
DR jPOST; P54253; -.
DR MassIVE; P54253; -.
DR MaxQB; P54253; -.
DR PaxDb; P54253; -.
DR PeptideAtlas; P54253; -.
DR PRIDE; P54253; -.
DR ProteomicsDB; 56658; -. [P54253-1]
DR ABCD; P54253; 2 sequenced antibodies.
DR Antibodypedia; 1922; 857 antibodies from 42 providers.
DR DNASU; 6310; -.
DR Ensembl; ENST00000244769.8; ENSP00000244769.3; ENSG00000124788.19. [P54253-1]
DR Ensembl; ENST00000436367.6; ENSP00000416360.1; ENSG00000124788.19. [P54253-1]
DR GeneID; 6310; -.
DR KEGG; hsa:6310; -.
DR MANE-Select; ENST00000436367.6; ENSP00000416360.1; NM_001128164.2; NP_001121636.1.
DR UCSC; uc003nbt.4; human. [P54253-1]
DR CTD; 6310; -.
DR DisGeNET; 6310; -.
DR GeneCards; ATXN1; -.
DR GeneReviews; ATXN1; -.
DR HGNC; HGNC:10548; ATXN1.
DR HPA; ENSG00000124788; Low tissue specificity.
DR MalaCards; ATXN1; -.
DR MIM; 164400; phenotype.
DR MIM; 601556; gene.
DR neXtProt; NX_P54253; -.
DR OpenTargets; ENSG00000124788; -.
DR Orphanet; 98755; Spinocerebellar ataxia type 1.
DR PharmGKB; PA34958; -.
DR VEuPathDB; HostDB:ENSG00000124788; -.
DR eggNOG; KOG4053; Eukaryota.
DR GeneTree; ENSGT00390000005939; -.
DR HOGENOM; CLU_019983_0_0_1; -.
DR InParanoid; P54253; -.
DR OMA; ENHRADN; -.
DR PhylomeDB; P54253; -.
DR TreeFam; TF350643; -.
DR PathwayCommons; P54253; -.
DR SignaLink; P54253; -.
DR SIGNOR; P54253; -.
DR BioGRID-ORCS; 6310; 25 hits in 1075 CRISPR screens.
DR ChiTaRS; ATXN1; human.
DR EvolutionaryTrace; P54253; -.
DR GeneWiki; Ataxin_1; -.
DR GenomeRNAi; 6310; -.
DR Pharos; P54253; Tbio.
DR PRO; PR:P54253; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P54253; protein.
DR Bgee; ENSG00000124788; Expressed in endothelial cell and 210 other tissues.
DR ExpressionAtlas; P54253; baseline and differential.
DR Genevisible; P54253; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0034046; F:poly(G) binding; IDA:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0007612; P:learning; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0051168; P:nuclear export; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; NAS:UniProtKB.
DR GO; GO:0035176; P:social behavior; ISS:UniProtKB.
DR InterPro; IPR020997; Ataxin-1_N.
DR InterPro; IPR043404; ATAXIN1-like.
DR InterPro; IPR003652; Ataxin_AXH_dom.
DR InterPro; IPR036096; Ataxin_AXH_dom_sf.
DR InterPro; IPR040172; ATXN1.
DR PANTHER; PTHR13392; PTHR13392; 1.
DR PANTHER; PTHR13392:SF5; PTHR13392:SF5; 1.
DR Pfam; PF12547; ATXN-1_C; 1.
DR Pfam; PF08517; AXH; 1.
DR SMART; SM00536; AXH; 1.
DR SUPFAM; SSF102031; SSF102031; 1.
DR PROSITE; PS51148; AXH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA-binding;
KW Isopeptide bond; Neurodegeneration; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; RNA-binding; Spinocerebellar ataxia;
KW Transcription; Transcription regulation; Triplet repeat expansion;
KW Ubl conjugation.
FT CHAIN 1..815
FT /note="Ataxin-1"
FT /id="PRO_0000064751"
FT DOMAIN 562..693
FT /note="AXH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00496"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..604
FT /note="Self-association"
FT /evidence="ECO:0000269|PubMed:9097953"
FT REGION 538..815
FT /note="Interaction with USP7"
FT /evidence="ECO:0000269|PubMed:12093161"
FT REGION 540..766
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:11136710"
FT REGION 762..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 794..797
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P54254"
FT COMPBIAS 185..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54254"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54254"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12741986"
FT CROSSLNK 16
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15824120"
FT CROSSLNK 194
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15824120"
FT CROSSLNK 609
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15824120"
FT CROSSLNK 696
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15824120"
FT CROSSLNK 745
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15824120"
FT VARIANT 209
FT /note="H -> Q (in dbSNP:rs11969612)"
FT /id="VAR_046616"
FT VARIANT 753
FT /note="P -> S (in dbSNP:rs16885)"
FT /id="VAR_046617"
FT MUTAGEN 16
FT /note="K->R: Sumoylation reduced to 40% of wild-type."
FT /evidence="ECO:0000269|PubMed:15824120"
FT MUTAGEN 194
FT /note="K->R: Sumoylation reduced to 46% of wild-type."
FT /evidence="ECO:0000269|PubMed:15824120"
FT MUTAGEN 420
FT /note="K->R: No effect on sumoylation."
FT /evidence="ECO:0000269|PubMed:15824120"
FT MUTAGEN 529
FT /note="K->R: Sumoylation reduced to 57% of wild-type."
FT /evidence="ECO:0000269|PubMed:15824120"
FT MUTAGEN 589
FT /note="K->R: Sumoylation reduced to 53% of wild-type."
FT /evidence="ECO:0000269|PubMed:15824120"
FT MUTAGEN 594
FT /note="K->R: Sumoylation reduced to 68% of wild-type."
FT /evidence="ECO:0000269|PubMed:15824120"
FT MUTAGEN 609
FT /note="K->R: Sumoylation reduced to 43% of wild-type."
FT /evidence="ECO:0000269|PubMed:15824120"
FT MUTAGEN 691
FT /note="K->R: No effect on sumoylation."
FT /evidence="ECO:0000269|PubMed:15824120"
FT MUTAGEN 696
FT /note="K->R: Sumoylation reduced to 42% of wild-type."
FT /evidence="ECO:0000269|PubMed:15824120"
FT MUTAGEN 745
FT /note="K->R: Sumoylation reduced to 44% of wild-type."
FT /evidence="ECO:0000269|PubMed:15824120"
FT MUTAGEN 775
FT /note="S->A: Reduces phosphorylation but does not affect
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:12741986"
FT MUTAGEN 784
FT /note="K->R: Sumoylation reduced to 62% of wild-type."
FT /evidence="ECO:0000269|PubMed:15824120"
FT CONFLICT 211
FT /note="H -> HQ (in Ref. 1; CAA55793)"
FT /evidence="ECO:0000305"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:2M41"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:1OA8"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:1OA8"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:1OA8"
FT HELIX 590..592
FT /evidence="ECO:0007829|PDB:1OA8"
FT HELIX 595..604
FT /evidence="ECO:0007829|PDB:1OA8"
FT STRAND 606..620
FT /evidence="ECO:0007829|PDB:1OA8"
FT STRAND 626..633
FT /evidence="ECO:0007829|PDB:1OA8"
FT TURN 634..637
FT /evidence="ECO:0007829|PDB:1OA8"
FT STRAND 638..645
FT /evidence="ECO:0007829|PDB:1OA8"
FT STRAND 650..652
FT /evidence="ECO:0007829|PDB:1OA8"
FT TURN 653..655
FT /evidence="ECO:0007829|PDB:1OA8"
FT STRAND 656..660
FT /evidence="ECO:0007829|PDB:1OA8"
FT HELIX 662..669
FT /evidence="ECO:0007829|PDB:1OA8"
FT STRAND 673..675
FT /evidence="ECO:0007829|PDB:4J2L"
FT STRAND 681..687
FT /evidence="ECO:0007829|PDB:1OA8"
SQ SEQUENCE 815 AA; 86923 MW; 657876F8FD19ECB2 CRC64;
MKSNQERSNE CLPPKKREIP ATSRSSEEKA PTLPSDNHRV EGTAWLPGNP GGRGHGGGRH
GPAGTSVELG LQQGIGLHKA LSTGLDYSPP SAPRSVPVAT TLPAAYATPQ PGTPVSPVQY
AHLPHTFQFI GSSQYSGTYA SFIPSQLIPP TANPVTSAVA SAAGATTPSQ RSQLEAYSTL
LANMGSLSQT PGHKAEQQQQ QQQQQQQQHQ HQQQQQQQQQ QQQQQHLSRA PGLITPGSPP
PAQQNQYVHI SSSPQNTGRT ASPPAIPVHL HPHQTMIPHT LTLGPPSQVV MQYADSGSHF
VPREATKKAE SSRLQQAIQA KEVLNGEMEK SRRYGAPSSA DLGLGKAGGK SVPHPYESRH
VVVHPSPSDY SSRDPSGVRA SVMVLPNSNT PAADLEVQQA THREASPSTL NDKSGLHLGK
PGHRSYALSP HTVIQTTHSA SEPLPVGLPA TAFYAGTQPP VIGYLSGQQQ AITYAGSLPQ
HLVIPGTQPL LIPVGSTDME ASGAAPAIVT SSPQFAAVPH TFVTTALPKS ENFNPEALVT
QAAYPAMVQA QIHLPVVQSV ASPAAAPPTL PPYFMKGSII QLANGELKKV EDLKTEDFIQ
SAEISNDLKI DSSTVERIED SHSPGVAVIQ FAVGEHRAQV SVEVLVEYPF FVFGQGWSSC
CPERTSQLFD LPCSKLSVGD VCISLTLKNL KNGSVKKGQP VDPASVLLKH SKADGLAGSR
HRYAEQENGI NQGSAQMLSE NGELKFPEKM GLPAAPFLTK IEPSKPAATR KRRWSAPESR
KLEKSEDEPP LTLPKPSLIP QEVKICIEGR SNVGK
