RAI1_HUMAN
ID RAI1_HUMAN Reviewed; 1906 AA.
AC Q7Z5J4; Q8N3B4; Q8ND08; Q8WU64; Q96JK5; Q9H1C1; Q9H1C2; Q9UF69;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Retinoic acid-induced protein 1;
GN Name=RAI1; Synonyms=KIAA1820;
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 [GENOMIC DNA / MRNA] (ISOFORM 2), POLYMORPHISM OF
RP POLY-GLN REGION, AND INVOLVEMENT IN SMITH-MAGENIS SYNDROME.
RX PubMed=11404004; DOI=10.1016/s0378-1119(01)00415-2;
RA Seranski P., Hoff C., Radelof U., Henning S., Reinhard R., Schwartz C.E.,
RA Heiss N., Poustka A.;
RT "RAI1 is a novel polyglutamine encoding gene that is deleted in Smith-
RT Magenis syndrome patients.";
RL Gene 270:69-76(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=12837267; DOI=10.1016/s0888-7543(03)00101-0;
RA Toulouse A., Rochefort D., Roussel J., Joober R., Rouleau G.A.;
RT "Molecular cloning and characterization of human RAI1, a gene associated
RT with schizophrenia.";
RL Genomics 82:162-171(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 622-1906.
RC TISSUE=Melanoma, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP INVOLVEMENT IN SMITH-MAGENIS SYNDROME.
RX PubMed=12652298; DOI=10.1038/ng1126;
RA Slager R.E., Newton T.L., Vlangos C.N., Finucane B., Elsea S.H.;
RT "Mutations in RAI1 associated with Smith-Magenis syndrome.";
RL Nat. Genet. 33:466-468(2003).
RN [7]
RP ROLE OF THE POLY-GLN REGION IN SPINOCEREBELLAR ATAXIA TYPE 2.
RX PubMed=10915763; DOI=10.1093/hmg/9.12.1753;
RA Hayes S., Turecki G., Brisebois K., Lopes-Cendes I., Gaspar C., Riess O.,
RA Ranum L.P., Pulst S.M., Rouleau G.A.;
RT "CAG repeat length in RAI1 is associated with age at onset variability in
RT spinocerebellar ataxia type 2 (SCA2).";
RL Hum. Mol. Genet. 9:1753-1758(2000).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683; THR-696; SER-880;
RP SER-892; SER-1122; SER-1352; SER-1358; SER-1374 AND SER-1431, AND
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683; SER-1064; THR-1068 AND
RP SER-1374, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-683; SER-1352;
RP SER-1358 AND SER-1374, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
RP FUNCTION.
RX PubMed=22578325; DOI=10.1016/j.ajhg.2012.04.013;
RA Williams S.R., Zies D., Mullegama S.V., Grotewiel M.S., Elsea S.H.;
RT "Smith-Magenis syndrome results in disruption of CLOCK gene transcription
RT and reveals an integral role for RAI1 in the maintenance of circadian
RT rhythmicity.";
RL Am. J. Hum. Genet. 90:941-949(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339; SER-345; THR-472;
RP SER-805; SER-1064; SER-1122; SER-1358; SER-1374 AND SER-1431, 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-819 AND LYS-901, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-811; LYS-901 AND LYS-1425, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [17]
RP VARIANT SMS 758-TRP--PRO-1906 DEL.
RX PubMed=24863970; DOI=10.1016/j.ymgme.2014.04.001;
RA Adams D.R., Yuan H., Holyoak T., Arajs K.H., Hakimi P., Markello T.C.,
RA Wolfe L.A., Vilboux T., Burton B.K., Fajardo K.F., Grahame G., Holloman C.,
RA Sincan M., Smith A.C., Wells G.A., Huang Y., Vega H., Snyder J.P.,
RA Golas G.A., Tifft C.J., Boerkoel C.F., Hanson R.W., Traynelis S.F.,
RA Kerr D.S., Gahl W.A.;
RT "Three rare diseases in one sib pair: RAI1, PCK1, GRIN2B mutations
RT associated with Smith-Magenis Syndrome, cytosolic PEPCK deficiency and NMDA
RT receptor glutamate insensitivity.";
RL Mol. Genet. Metab. 113:161-170(2014).
CC -!- FUNCTION: Transcriptional regulator of the circadian clock components:
CC CLOCK, ARNTL/BMAL1, ARNTL2/BMAL2, PER1/3, CRY1/2, NR1D1/2 and RORA/C.
CC Positively regulates the transcriptional activity of CLOCK a core
CC component of the circadian clock. Regulates transcription through
CC chromatin remodeling by interacting with other proteins in chromatin as
CC well as proteins in the basic transcriptional machinery. May be
CC important for embryonic and postnatal development. May be involved in
CC neuronal differentiation. {ECO:0000269|PubMed:22578325}.
CC -!- INTERACTION:
CC Q7Z5J4; Q13526: PIN1; NbExp=4; IntAct=EBI-743815, EBI-714158;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In neurons, localized to
CC neurites. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q7Z5J4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z5J4-2; Sequence=VSP_010995, VSP_010996, VSP_010999,
CC VSP_011002, VSP_011003;
CC Name=3;
CC IsoId=Q7Z5J4-3; Sequence=VSP_011000, VSP_011001;
CC Name=4;
CC IsoId=Q7Z5J4-4; Sequence=VSP_010997, VSP_010998;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined with higher
CC expression in the heart and brain. No expression was seen in the corpus
CC callosum of the brain. {ECO:0000269|PubMed:12837267}.
CC -!- POLYMORPHISM: The poly-Gln tract is polymorphic and the number of Gln
CC varies from 12 to 14 (PubMed:11404004). The size of the poly-Gln region
CC may influence the age at onset of spinocerebellar ataxia type 2 (SCA2)
CC (PubMed:10915763). {ECO:0000269|PubMed:10915763,
CC ECO:0000269|PubMed:11404004}.
CC -!- DISEASE: Smith-Magenis syndrome (SMS) [MIM:182290]: Characterized by
CC intellectual disability associated with development and growth delays.
CC Affected persons have characteristic behavioral abnormalities,
CC including self-injurious behaviors and sleep disturbance, and distinct
CC craniofacial and skeletal anomalies. {ECO:0000269|PubMed:11404004,
CC ECO:0000269|PubMed:12652298, ECO:0000269|PubMed:24863970}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB47449.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ271790; CAC20423.1; -; mRNA.
DR EMBL; AJ271791; CAC20424.1; -; Genomic_DNA.
DR EMBL; AY172136; AAO31738.1; -; mRNA.
DR EMBL; AB058723; BAB47449.1; ALT_INIT; mRNA.
DR EMBL; BC021209; AAH21209.1; -; mRNA.
DR EMBL; AL133649; CAB63768.1; -; mRNA.
DR EMBL; AL834468; CAD39127.1; -; mRNA.
DR EMBL; AL834486; CAD39144.1; -; mRNA.
DR CCDS; CCDS11188.1; -. [Q7Z5J4-1]
DR PIR; T43490; T43490.
DR RefSeq; NP_109590.3; NM_030665.3. [Q7Z5J4-1]
DR AlphaFoldDB; Q7Z5J4; -.
DR SMR; Q7Z5J4; -.
DR BioGRID; 115966; 60.
DR IntAct; Q7Z5J4; 28.
DR MINT; Q7Z5J4; -.
DR STRING; 9606.ENSP00000323074; -.
DR GlyGen; Q7Z5J4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z5J4; -.
DR PhosphoSitePlus; Q7Z5J4; -.
DR BioMuta; RAI1; -.
DR DMDM; 50400978; -.
DR EPD; Q7Z5J4; -.
DR jPOST; Q7Z5J4; -.
DR MassIVE; Q7Z5J4; -.
DR MaxQB; Q7Z5J4; -.
DR PaxDb; Q7Z5J4; -.
DR PeptideAtlas; Q7Z5J4; -.
DR PRIDE; Q7Z5J4; -.
DR ProteomicsDB; 69303; -. [Q7Z5J4-1]
DR ProteomicsDB; 69304; -. [Q7Z5J4-2]
DR ProteomicsDB; 69305; -. [Q7Z5J4-3]
DR ProteomicsDB; 69306; -. [Q7Z5J4-4]
DR Antibodypedia; 25487; 93 antibodies from 16 providers.
DR DNASU; 10743; -.
DR Ensembl; ENST00000353383.6; ENSP00000323074.4; ENSG00000108557.20. [Q7Z5J4-1]
DR GeneID; 10743; -.
DR KEGG; hsa:10743; -.
DR MANE-Select; ENST00000353383.6; ENSP00000323074.4; NM_030665.4; NP_109590.3.
DR UCSC; uc002grm.4; human. [Q7Z5J4-1]
DR CTD; 10743; -.
DR DisGeNET; 10743; -.
DR GeneCards; RAI1; -.
DR GeneReviews; RAI1; -.
DR HGNC; HGNC:9834; RAI1.
DR HPA; ENSG00000108557; Low tissue specificity.
DR MalaCards; RAI1; -.
DR MIM; 182290; phenotype.
DR MIM; 607642; gene.
DR neXtProt; NX_Q7Z5J4; -.
DR OpenTargets; ENSG00000108557; -.
DR Orphanet; 1713; 17p11.2 microduplication syndrome.
DR Orphanet; 477817; PMP22-RAI1 contiguous gene duplication syndrome.
DR Orphanet; 819; Smith-Magenis syndrome.
DR PharmGKB; PA34188; -.
DR VEuPathDB; HostDB:ENSG00000108557; -.
DR eggNOG; KOG1084; Eukaryota.
DR GeneTree; ENSGT00940000156922; -.
DR HOGENOM; CLU_002579_1_0_1; -.
DR InParanoid; Q7Z5J4; -.
DR OMA; CCAAADF; -.
DR PhylomeDB; Q7Z5J4; -.
DR TreeFam; TF331317; -.
DR PathwayCommons; Q7Z5J4; -.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; Q7Z5J4; -.
DR SIGNOR; Q7Z5J4; -.
DR BioGRID-ORCS; 10743; 28 hits in 1092 CRISPR screens.
DR ChiTaRS; RAI1; human.
DR GenomeRNAi; 10743; -.
DR Pharos; Q7Z5J4; Tbio.
DR PRO; PR:Q7Z5J4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q7Z5J4; protein.
DR Bgee; ENSG00000108557; Expressed in pigmented layer of retina and 182 other tissues.
DR ExpressionAtlas; Q7Z5J4; baseline and differential.
DR Genevisible; Q7Z5J4; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00249; PHD; 1.
DR PROSITE; PS51805; EPHD; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Biological rhythms; Cytoplasm;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Triplet repeat expansion; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1906
FT /note="Retinoic acid-induced protein 1"
FT /id="PRO_0000097159"
FT ZN_FING 1780..1835
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 1855..1903
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1613..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..1775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1794..1819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1160..1177
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 1223..1240
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 12..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 472
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 696
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 880
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1068
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 811
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 819
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 901
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 901
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1425
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 207..233
FT /note="THFPQHSQSFPTSSTYSSSVQGGGQGA -> WWAGG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11404004"
FT /id="VSP_010995"
FT VAR_SEQ 407..434
FT /note="VDTQAGNCKPLQKDKLPENLLSDLSLQS -> PAD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11404004"
FT /id="VSP_010996"
FT VAR_SEQ 947..966
FT /note="SHMKPGEEGPDGERAPGDST -> YSVYICIHIHIYNIYEDCKC (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010997"
FT VAR_SEQ 967..1906
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010998"
FT VAR_SEQ 1415..1479
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11404004"
FT /id="VSP_010999"
FT VAR_SEQ 1598..1640
FT /note="FVRVEKRDAFTTICTVVNSPGDAPKPHRKPSSSASSSSSSSSF -> LEPSL
FT GAQNPRSGQNAPPAPADARPLCTTRDRRAYSAREQGQR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11347906"
FT /id="VSP_011000"
FT VAR_SEQ 1641..1906
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11347906"
FT /id="VSP_011001"
FT VAR_SEQ 1803..1821
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11404004"
FT /id="VSP_011002"
FT VAR_SEQ 1856..1906
FT /note="MCSSCQEAGATIGCCHKGCLHTYHYPCASDAGCIFIEENFSLKCPKHKRLP
FT -> HGGTVALAPGDFSLPGLRFASLFQGPSWCDCPVLATSTPSSWSRCVPAAKKPGPPL
FT GAATKDASTPTTTRVPAMQVRARPGTGGHWSPSKQSRGTLPGHSSPNPGPISLFSFPPL
FT LPQQFFYPSVCLDLCWAMPGTWK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11404004"
FT /id="VSP_011003"
FT VARIANT 90
FT /note="G -> A (in dbSNP:rs3803763)"
FT /id="VAR_051300"
FT VARIANT 165
FT /note="P -> T (in dbSNP:rs11649804)"
FT /id="VAR_024344"
FT VARIANT 758..1906
FT /note="Missing (in SMS)"
FT /evidence="ECO:0000269|PubMed:24863970"
FT /id="VAR_079636"
FT VARIANT 939
FT /note="Q -> P (in dbSNP:rs1759075)"
FT /id="VAR_051301"
FT CONFLICT 440
FT /note="S -> L (in Ref. 2; AAO31738)"
FT /evidence="ECO:0000305"
FT CONFLICT 1302
FT /note="L -> F (in Ref. 2; AAO31738)"
FT /evidence="ECO:0000305"
FT CONFLICT 1513
FT /note="G -> A (in Ref. 2; AAO31738)"
FT /evidence="ECO:0000305"
FT CONFLICT 1682
FT /note="T -> A (in Ref. 5; CAD39144)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1906 AA; 203352 MW; 8D33A56C33BFE888 CRC64;
MQSFRERCGF HGKQQNYQQT SQETSRLENY RQPSQAGLSC DRQRLLAKDY YNPQPYPSYE
GGAGTPSGTA AAVAADKYHR GSKALPTQQG LQGRPAFPGY GVQDSSPYPG RYAGEESLQA
WGAPQPPPPQ PQPLPAGVAK YDENLMKKTA VPPSRQYAEQ GAQVPFRTHS LHVQQPPPPQ
QPLAYPKLQR QKLQNDIASP LPFPQGTHFP QHSQSFPTSS TYSSSVQGGG QGAHSYKSCT
APTAQPHDRP LTASSSLAPG QRVQNLHAYQ SGRLSYDQQQ QQQQQQQQQQ QALQSRHHAQ
ETLHYQNLAK YQHYGQQGQG YCQPDAAVRT PEQYYQTFSP SSSHSPARSV GRSPSYSSTP
SPLMPNLENF PYSQQPLSTG AFPAGITDHS HFMPLLNPSP TDATSSVDTQ AGNCKPLQKD
KLPENLLSDL SLQSLTALTS QVENISNTVQ QLLLSKAAVP QKKGVKNLVS RTPEQHKSQH
CSPEGSGYSA EPAGTPLSEP PSSTPQSTHA EPQEADYLSG SEDPLERSFL YCNQARGSPA
RVNSNSKAKP ESVSTCSVTS PDDMSTKSDD SFQSLHGSLP LDSFSKFVAG ERDCPRLLLS
ALAQEDLASE ILGLQEAIGE KADKAWAEAP SLVKDSSKPP FSLENHSACL DSVAKSAWPR
PGEPEALPDS LQLDKGGNAK DFSPGLFEDP SVAFATPDPK KTTGPLSFGT KPTLGVPAPD
PTTAAFDCFP DTTAASSADS ANPFAWPEEN LGDACPRWGL HPGELTKGLE QGGKASDGIS
KGDTHEASAC LGFQEEDPPG EKVASLPGDF KQEEVGGVKE EAGGLLQCPE VAKADRWLED
SRHCCSTADF GDLPLLPPTS RKEDLEAEEE YSSLCELLGS PEQRPGMQDP LSPKAPLICT
KEEVEEVLDS KAGWGSPCHL SGESVILLGP TVGTESKVQS WFESSLSHMK PGEEGPDGER
APGDSTTSDA SLAQKPNKPA VPEAPIAKKE PVPRGKSLRS RRVHRGLPEA EDSPCRAPVL
PKDLLLPESC TGPPQGQMEG AGAPGRGASE GLPRMCTRSL TALSEPRTPG PPGLTTTPAP
PDKLGGKQRA AFKSGKRVGK PSPKAASSPS NPAALPVASD SSPMGSKTKE TDSPSTPGKD
QRSMILRSRT KTQEIFHSKR RRPSEGRLPN CRATKKLLDN SHLPATFKVS SSPQKEGRVS
QRARVPKPGA GSKLSDRPLH ALKRKSAFMA PVPTKKRNLV LRSRSSSSSN ASGNGGDGKE
ERPEGSPTLF KRMSSPKKAK PTKGNGEPAT KLPPPETPDA CLKLASRAAF QGAMKTKVLP
PRKGRGLKLE AIVQKITSPS LKKFACKAPG ASPGNPLSPS LSDKDRGLKG AGGSPVGVEE
GLVNVGTGQK LPTSGADPLC RNPTNRSLKG KLMNSKKLSS TDCFKTEAFT SPEALQPGGT
ALAPKKRSRK GRAGAHGLSK GPLEKRPYLG PALLLTPRDR ASGTQGASED NSGGGGKKPK
MEELGLASQP PEGRPCQPQT RAQKQPGHTN YSSYSKRKRL TRGRAKNTTS SPCKGRAKRR
RQQQVLPLDP AEPEIRLKYI SSCKRLRSDS RTPAFSPFVR VEKRDAFTTI CTVVNSPGDA
PKPHRKPSSS ASSSSSSSSF SLDAAGASLA TLPGGSILQP RPSLPLSSTM HLGPVVSKAL
STSCLVCCLC QNPANFKDLG DLCGPYYPEH CLPKKKPKLK EKVRPEGTCE EASLPLERTL
KGPECAAAAT AGKPPRPDGP ADPAKQGPLR TSARGLSRRL QSCYCCDGRE DGGEEAAPAD
KGRKHECSKE APAEPGGEAQ EHWVHEACAV WTGGVYLVAG KLFGLQEAMK VAVDMMCSSC
QEAGATIGCC HKGCLHTYHY PCASDAGCIF IEENFSLKCP KHKRLP
