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   24-JAN-2024, entry version 162.
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, BMAL1, BMAL2, PER1/3, CRY1/2, NR1D1/2 and RORA/C. Positively
CC       regulates the transcriptional activity of CLOCK a core component of the
CC       circadian clock. Regulates transcription through chromatin remodeling
CC       by interacting with other proteins in chromatin as well as proteins in
CC       the basic transcriptional machinery. May be important for embryonic and
CC       postnatal development. May be involved in neuronal differentiation.
CC       {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; 87.
DR   IntAct; Q7Z5J4; 30.
DR   MINT; Q7Z5J4; -.
DR   STRING; 9606.ENSP00000323074; -.
DR   GlyGen; Q7Z5J4; 5 sites, 1 O-linked glycan (5 sites).
DR   iPTMnet; Q7Z5J4; -.
DR   PhosphoSitePlus; Q7Z5J4; -.
DR   SwissPalm; Q7Z5J4; -.
DR   BioMuta; RAI1; -.
DR   DMDM; 50400978; -.
DR   EPD; Q7Z5J4; -.
DR   jPOST; Q7Z5J4; -.
DR   MassIVE; Q7Z5J4; -.
DR   MaxQB; Q7Z5J4; -.
DR   PaxDb; 9606-ENSP00000323074; -.
DR   PeptideAtlas; Q7Z5J4; -.
DR   ProteomicsDB; 69303; -. [Q7Z5J4-1]
DR   ProteomicsDB; 69304; -. [Q7Z5J4-2]
DR   ProteomicsDB; 69305; -. [Q7Z5J4-3]
DR   ProteomicsDB; 69306; -. [Q7Z5J4-4]
DR   Pumba; Q7Z5J4; -.
DR   Antibodypedia; 25487; 108 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   AGR; HGNC:9834; -.
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; DCFPDTA; -.
DR   OrthoDB; 2919570at2759; -.
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; 29 hits in 1171 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 184 other cell types or tissues.
DR   ExpressionAtlas; Q7Z5J4; baseline and differential.
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 DNA-templated transcription; 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   CDD; cd15700; ePHD_RAI1; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR14955; RETINOIC ACID INDUCED 1/TRANSCRIPTION FACTOR 20; 1.
DR   PANTHER; PTHR14955:SF6; RETINOIC ACID-INDUCED PROTEIN 1; 1.
DR   Pfam; PF13771; zf-HC5HC2H; 1.
DR   SMART; SM00249; PHD; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   Genevisible; Q7Z5J4; HS.
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
//