ATX1L_HUMAN
ID ATX1L_HUMAN Reviewed; 689 AA.
AC P0C7T5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ataxin-1-like;
DE AltName: Full=Brother of ataxin-1;
DE Short=Brother of ATXN1;
GN Name=ATXN1L; Synonyms=BOAT, BOAT1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [2]
RP INTERACTION WITH NCOR2 AND ATXN1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-330; SER-361 AND SER-615, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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 (PubMed:21475249). Can suppress ATXN1 cytotoxicity
CC in spinocerebellar ataxia type 1 (SCA1). In concert with CIC and ATXN1,
CC involved in brain development (By similarity).
CC {ECO:0000250|UniProtKB:P0C7T6, ECO:0000269|PubMed:21475249}.
CC -!- SUBUNIT: Homodimer. Interacts with CIC (By similarity). Interacts (via
CC AXH domain) with NCOR2. Interacts with ATXN1 (PubMed:16121196).
CC Directly interacts with RBPJ; this interaction is disrupted in the
CC presence of Notch intracellular domain. Competes with ATXN1 for RBPJ-
CC binding (PubMed:21475249). Found in a complex with CIC and ATXN1 (By
CC similarity). {ECO:0000250|UniProtKB:P0C7T6,
CC ECO:0000269|PubMed:16121196, ECO:0000269|PubMed:21475249}.
CC -!- INTERACTION:
CC P0C7T5; P21549: AGXT; NbExp=3; IntAct=EBI-8624731, EBI-727098;
CC P0C7T5; Q03989: ARID5A; NbExp=3; IntAct=EBI-8624731, EBI-948603;
CC P0C7T5; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-8624731, EBI-946029;
CC P0C7T5; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-8624731, EBI-11978259;
CC P0C7T5; B7ZLH0: FAM22F; NbExp=3; IntAct=EBI-8624731, EBI-10220102;
CC P0C7T5; O75593: FOXH1; NbExp=6; IntAct=EBI-8624731, EBI-1759806;
CC P0C7T5; Q14774: HLX; NbExp=3; IntAct=EBI-8624731, EBI-6678255;
CC P0C7T5; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-8624731, EBI-1052037;
CC P0C7T5; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-8624731, EBI-10241353;
CC P0C7T5; Q3LI59: KRTAP21-2; NbExp=3; IntAct=EBI-8624731, EBI-18395721;
CC P0C7T5; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-8624731, EBI-10261141;
CC P0C7T5; Q92615: LARP4B; NbExp=3; IntAct=EBI-8624731, EBI-1052558;
CC P0C7T5; Q99687-3: MEIS3; NbExp=3; IntAct=EBI-8624731, EBI-18582591;
CC P0C7T5; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-8624731, EBI-8487781;
CC P0C7T5; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-8624731, EBI-5662487;
CC P0C7T5; Q13492-3: PICALM; NbExp=3; IntAct=EBI-8624731, EBI-11031437;
CC P0C7T5; Q9NWB1-5: RBFOX1; NbExp=3; IntAct=EBI-8624731, EBI-12123390;
CC P0C7T5; O43251-10: RBFOX2; NbExp=3; IntAct=EBI-8624731, EBI-11963050;
CC P0C7T5; Q06330: RBPJ; NbExp=7; IntAct=EBI-8624731, EBI-632552;
CC P0C7T5; Q6UWI4: SHISA2; NbExp=3; IntAct=EBI-8624731, EBI-11343474;
CC P0C7T5; Q13207: TBX2; NbExp=3; IntAct=EBI-8624731, EBI-2853051;
CC P0C7T5; Q96LM6: TEX37; NbExp=3; IntAct=EBI-8624731, EBI-743976;
CC P0C7T5; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-8624731, EBI-12817837;
CC P0C7T5; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-8624731, EBI-11975223;
CC P0C7T5; A0A0C4DGF1: ZBTB32; NbExp=3; IntAct=EBI-8624731, EBI-10188476;
CC P0C7T5; A0A1U9X8X8; NbExp=3; IntAct=EBI-8624731, EBI-17234977;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16121196}. Cell
CC projection, dendrite {ECO:0000269|PubMed:16121196}. Note=Forms nuclear
CC foci. Colocalizes with NCOR2 and HDAC3. Distributed beyond the nucleus
CC into the cell body and dendrites in Purkinje cells and in inferior
CC olive cells.
CC -!- TISSUE SPECIFICITY: Expressed in cerebellum and cerebral cortex.
CC {ECO:0000269|PubMed:16121196}.
CC -!- SIMILARITY: Belongs to the ATXN1 family. {ECO:0000305}.
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DR EMBL; AC010653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX537575; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS45523.1; -.
DR RefSeq; NP_001131147.1; NM_001137675.3.
DR AlphaFoldDB; P0C7T5; -.
DR SMR; P0C7T5; -.
DR BioGRID; 131172; 147.
DR IntAct; P0C7T5; 74.
DR MINT; P0C7T5; -.
DR STRING; 9606.ENSP00000415822; -.
DR GlyGen; P0C7T5; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; P0C7T5; -.
DR PhosphoSitePlus; P0C7T5; -.
DR BioMuta; ATXN1L; -.
DR DMDM; 206557834; -.
DR EPD; P0C7T5; -.
DR jPOST; P0C7T5; -.
DR MassIVE; P0C7T5; -.
DR MaxQB; P0C7T5; -.
DR PaxDb; P0C7T5; -.
DR PeptideAtlas; P0C7T5; -.
DR PRIDE; P0C7T5; -.
DR ProteomicsDB; 52365; -.
DR Antibodypedia; 67440; 90 antibodies from 14 providers.
DR DNASU; 342371; -.
DR Ensembl; ENST00000427980.7; ENSP00000415822.2; ENSG00000224470.9.
DR Ensembl; ENST00000683775.1; ENSP00000507897.1; ENSG00000224470.9.
DR GeneID; 342371; -.
DR KEGG; hsa:342371; -.
DR MANE-Select; ENST00000427980.7; ENSP00000415822.2; NM_001137675.4; NP_001131147.1.
DR UCSC; uc002fbd.3; human.
DR CTD; 342371; -.
DR DisGeNET; 342371; -.
DR GeneCards; ATXN1L; -.
DR HGNC; HGNC:33279; ATXN1L.
DR HPA; ENSG00000224470; Low tissue specificity.
DR MIM; 614301; gene.
DR neXtProt; NX_P0C7T5; -.
DR OpenTargets; ENSG00000224470; -.
DR PharmGKB; PA162377321; -.
DR VEuPathDB; HostDB:ENSG00000224470; -.
DR eggNOG; KOG4053; Eukaryota.
DR GeneTree; ENSGT00390000005939; -.
DR HOGENOM; CLU_434497_0_0_1; -.
DR InParanoid; P0C7T5; -.
DR OMA; RGMPVFY; -.
DR OrthoDB; 249631at2759; -.
DR PhylomeDB; P0C7T5; -.
DR TreeFam; TF350643; -.
DR PathwayCommons; P0C7T5; -.
DR SignaLink; P0C7T5; -.
DR BioGRID-ORCS; 342371; 18 hits in 1084 CRISPR screens.
DR ChiTaRS; ATXN1L; human.
DR GenomeRNAi; 342371; -.
DR Pharos; P0C7T5; Tbio.
DR PRO; PR:P0C7T5; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P0C7T5; protein.
DR Bgee; ENSG00000224470; Expressed in endothelial cell and 193 other tissues.
DR Genevisible; P0C7T5; HS.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0007612; P:learning; ISS:UniProtKB.
DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0035176; P:social behavior; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
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 PANTHER; PTHR13392; PTHR13392; 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 Cell projection; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..689
FT /note="Ataxin-1-like"
FT /id="PRO_0000343709"
FT DOMAIN 457..588
FT /note="AXH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00496"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 20..197
FT /note="Interaction with NCOR2 and ATXN1"
FT /evidence="ECO:0000269|PubMed:16121196"
FT REGION 20..197
FT /note="Self-association"
FT REGION 185..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 330
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 313
FT /note="S -> P (in dbSNP:rs7194407)"
FT /id="VAR_044496"
SQ SEQUENCE 689 AA; 73306 MW; 9C5D3938EF91F2C7 CRC64;
MKPVHERSQE CLPPKKRDLP VTSEDMGRTT SCSTNHTPSS DASEWSRGVV VAGQSQAGAR
VSLGGDGAEA ITGLTVDQYG MLYKVAVPPA TFSPTGLPSV VNMSPLPPTF NVASSLIQHP
GIHYPPLHYA QLPSTSLQFI GSPYSLPYAV PPNFLPSPLL SPSANLATSH LPHFVPYASL
LAEGATPPPQ APSPAHSFNK APSATSPSGQ LPHHSSTQPL DLAPGRMPIY YQMSRLPAGY
TLHETPPAGA SPVLTPQESQ SALEAAAANG GQRPRERNLV RRESEALDSP NSKGEGQGLV
PVVECVVDGQ LFSGSQTPRV EVAAPAHRGT PDTDLEVQRV VGALASQDYR VVAAQRKEEP
SPLNLSHHTP DHQGEGRGSA RNPAELAEKS QARGFYPQSH QEPVKHRPLP KAMVVANGNL
VPTGTDSGLL PVGSEILVAS SLDVQARATF PDKEPTPPPI TSSHLPSHFM KGAIIQLATG
ELKRVEDLQT QDFVRSAEVS GGLKIDSSTV VDIQESQWPG FVMLHFVVGE QQSKVSIEVP
PEHPFFVYGQ GWSSCSPGRT TQLFSLPCHR LQVGDVCISI SLQSLNSNSV SQASCAPPSQ
LGPPRERPER TVLGSRELCD SEGKSQPAGE GSRVVEPSQP ESGAQACWPA PSFQRYSMQG
EEARAALLRP SFIPQEVKLS IEGRSNAGK
