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Nuclear receptor corepressor 1 (N-CoR) (N-CoR1) (Retinoid X receptor-interacting protein 13) (RIP13)

 NCOR1_MOUSE             Reviewed;        2453 AA.
Q60974; Q60812;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
20-JUN-2018, entry version 182.
RecName: Full=Nuclear receptor corepressor 1;
Short=N-CoR;
Short=N-CoR1;
AltName: Full=Retinoid X receptor-interacting protein 13;
Short=RIP13;
Name=Ncor1; Synonyms=Rxrip13;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Pituitary;
PubMed=7566114; DOI=10.1038/377397a0;
Hoerlein A.J., Naeaer A.M., Heinzel T., Torchia J., Gloss B.,
Kurokawa R., Ryan A., Kamei Y., Soederstroem M., Glass C.K.,
Rosenfeld M.G.;
"Ligand-independent repression by the thyroid hormone receptor
mediated by a nuclear receptor co-repressor.";
Nature 377:397-404(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1792-2453 (ISOFORM 1).
TISSUE=Liver;
PubMed=7760852; DOI=10.1210/mend.9.1.7760852;
Seol W., Choi H.S., Moore D.D.;
"Isolation of proteins that interact specifically with the retinoid X
receptor: two novel orphan receptors.";
Mol. Endocrinol. 9:72-85(1995).
[3]
INTERACTION WITH RARB; RXRA AND THRB, AND DOMAINS ID1 AND ID2.
PubMed=8961273; DOI=10.1210/mend.10.12.8961273;
Seol W., Mahon M.J., Lee Y.-K., Moore D.D.;
"Two receptor interacting domains in the nuclear hormone receptor
corepressor RIP13/N-CoR.";
Mol. Endocrinol. 10:1646-1655(1996).
[4]
INTERACTION WITH SIN3A AND SIN3B.
PubMed=9139820; DOI=10.1038/387043a0;
Heinzel T., Lavinsky R.M., Mullen T.-M., Soederstroem M.,
Laherty C.D., Torchia J., Yang W.M., Brard G., Ngo S.D., Davie J.R.,
Seto E., Eisenman R.N., Rose D.W., Glass C.K., Rosenfeld M.G.;
"A complex containing N-CoR, mSin3 and histone deacetylase mediates
transcriptional repression.";
Nature 387:43-48(1997).
[5]
INTERACTION WITH C1D.
PubMed=9405624; DOI=10.1073/pnas.94.26.14400;
Zamir I., Dawson J., Lavinsky R.M., Glass C.K., Rosenfeld M.G.,
Lazar M.A.;
"Cloning and characterization of a corepressor and potential component
of the nuclear hormone receptor repression complex.";
Proc. Natl. Acad. Sci. U.S.A. 94:14400-14405(1997).
[6]
INTERACTION WITH SIAH2, AND DEGRADATION.
PubMed=9637679; DOI=10.1101/gad.12.12.1775;
Zhang J., Guenther M.G., Carthew R.W., Lazar M.A.;
"Proteasomal regulation of nuclear receptor corepressor-mediated
repression.";
Genes Dev. 12:1775-1780(1998).
[7]
INTERACTION WITH SAP30 AND SIN3A.
PubMed=9702189; DOI=10.1016/S1097-2765(00)80111-2;
Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C.,
Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K.,
Rosenfeld M.G., Ayer D.E., Eisenman R.N.;
"SAP30, a component of the mSin3 corepressor complex involved in N-
CoR-mediated repression by specific transcription factors.";
Mol. Cell 2:33-42(1998).
[8]
INTERACTION WITH HDAC7.
PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
"Identification of a nuclear domain with deacetylase activity.";
Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
[9]
INTERACTION WITH CBFA2T3.
PubMed=11533236; DOI=10.1128/MCB.21.19.6470-6483.2001;
Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
Downing J.R., Meyers S., Hiebert S.W.;
"ETO, a target of t(8;21) in acute leukemia, makes distinct contacts
with multiple histone deacetylases and binds mSin3A through its
oligomerization domain.";
Mol. Cell. Biol. 21:6470-6483(2001).
[10]
INTERACTION WITH DACH1.
PubMed=12130660; DOI=10.1126/science.1073263;
Li X., Perissi V., Liu F., Rose D.W., Rosenfeld M.G.;
"Tissue-specific regulation of retinal and pituitary precursor cell
proliferation.";
Science 297:1180-1183(2002).
[11]
INTERACTION WITH RARA.
PubMed=17205979; DOI=10.1074/mcp.M600223-MCP200;
Huq M.D., Tsai N.-P., Khan S.A., Wei L.-N.;
"Lysine trimethylation of retinoic acid receptor-alpha: a novel means
to regulate receptor function.";
Mol. Cell. Proteomics 6:677-688(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1481; SER-2449 AND
SER-2451, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[13]
INTERACTION WITH RARA.
PubMed=19078967; DOI=10.1038/emboj.2008.256;
Bruck N., Vitoux D., Ferry C., Duong V., Bauer A., de The H.,
Rochette-Egly C.;
"A coordinated phosphorylation cascade initiated by p38MAPK/MSK1
directs RARalpha to target promoters.";
EMBO J. 28:34-47(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-1481, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2198, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[16]
INTERACTION WITH RXRA.
PubMed=19786558; DOI=10.1124/mol.109.057000;
Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K.,
Kato Y., Makishima M.;
"The basic helix-loop-helix proteins differentiated embryo chondrocyte
(DEC) 1 and DEC2 function as corepressors of retinoid X receptors.";
Mol. Pharmacol. 76:1360-1369(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1011; SER-1122;
THR-1378; SER-1459; SER-1481; SER-1993 AND SER-2198, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[18]
INTERACTION WITH RORA AND RORC.
PubMed=21499262; DOI=10.1038/nature10075;
Solt L.A., Kumar N., Nuhant P., Wang Y., Lauer J.L., Liu J.,
Istrate M.A., Kamenecka T.M., Roush W.R., Vidovic D., Schuerer S.C.,
Xu J., Wagoner G., Drew P.D., Griffin P.R., Burris T.P.;
"Suppression of TH17 differentiation and autoimmunity by a synthetic
ROR ligand.";
Nature 472:491-494(2011).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1347, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[20]
INTERACTION WITH SETD5.
PubMed=27864380; DOI=10.1242/dev.141465;
Osipovich A.B., Gangula R., Vianna P.G., Magnuson M.A.;
"Setd5 is essential for mammalian development and the co-
transcriptional regulation of histone acetylation.";
Development 143:4595-4607(2016).
-!- FUNCTION: Mediates transcriptional repression by certain nuclear
receptors. Part of a complex which promotes histone deacetylation
and the formation of repressive chromatin structures which may
impede the access of basal transcription factors. Participates in
the transcriptional repressor activity produced by BCL6.
-!- SUBUNIT: Forms a large corepressor complex that contains SIN3A/B
and histone deacetylases HDAC1 and HDAC2. This complex associates
with the thyroid receptor (TR) and the retinoid acid receptor
(RAR) in the absence of ligand. Interacts directly with RARA; the
interaction is facilitated with RARA trimethylation. Component of
the N-Cor repressor complex, at least composed of CBFA2T3, HEXIM1,
NCOR1, NCOR2, HDAC3, TBL1X, TBL1XR1, CORO2A and GPS2. Interacts
with ZBTB33; the interaction serves to recruit the N-CoR complex
to promoter regions containing methylated CpG dinucleotides.
Interacts with TRIM28 and KDM3A. Interacts (via the RD1 domain)
with BAZ1A (via its N-terminal); the interaction corepresses a
number of NCOR1-regulated genes. Interacts with BCL6, C1D, DACH1,
HEXIM1, HDAC7, RORA, RORC, SAP30, SIAH2, SIN3A and SIN3B
(PubMed:10984530). May interact with DEAF1. Interacts with RXRA.
Interacts with SETD5 (PubMed:27864380). Interacts with VDR (By
similarity). {ECO:0000250|UniProtKB:O75376,
ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11533236,
ECO:0000269|PubMed:12130660, ECO:0000269|PubMed:17205979,
ECO:0000269|PubMed:19078967, ECO:0000269|PubMed:19786558,
ECO:0000269|PubMed:21499262, ECO:0000269|PubMed:27864380,
ECO:0000269|PubMed:8961273, ECO:0000269|PubMed:9139820,
ECO:0000269|PubMed:9405624, ECO:0000269|PubMed:9637679,
ECO:0000269|PubMed:9702189}.
-!- INTERACTION:
Q01147:Creb1; NbExp=5; IntAct=EBI-349004, EBI-2291098;
Q9QYB2:Dach1; NbExp=2; IntAct=EBI-349004, EBI-348961;
O15379:HDAC3 (xeno); NbExp=2; IntAct=EBI-349004, EBI-607682;
Q9UKV0-3:HDAC9 (xeno); NbExp=2; IntAct=EBI-349004, EBI-765476;
Q9UKV0-7:HDAC9 (xeno); NbExp=3; IntAct=EBI-349004, EBI-1372717;
P51608:MECP2 (xeno); NbExp=4; IntAct=EBI-349004, EBI-1189067;
O88574:Sap30; NbExp=3; IntAct=EBI-349004, EBI-593511;
Q96EB6:SIRT1 (xeno); NbExp=2; IntAct=EBI-349004, EBI-1802965;
Q923E4:Sirt1; NbExp=3; IntAct=EBI-349004, EBI-1802585;
P12755:SKI (xeno); NbExp=5; IntAct=EBI-349004, EBI-347281;
P12757:SKIL (xeno); NbExp=2; IntAct=EBI-349004, EBI-2902468;
Q13573:SNW1 (xeno); NbExp=3; IntAct=EBI-349004, EBI-632715;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q60974-1; Sequence=Displayed;
Name=2;
IsoId=Q60974-2; Sequence=VSP_003411;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The N-terminal region contains three independent domains
that are capable of mediating transcriptional repression (RD1, RD2
and RD3). {ECO:0000269|PubMed:8961273}.
-!- DOMAIN: The C-terminal region contains two separate nuclear
receptor-interacting domains (ID1 and ID2), each of which contains
a conserved sequence referred to as the CORNR box. This motif is
necessary and sufficient for binding to unligated nuclear hormone
receptors, while sequences flanking the CORNR box determine the
precise nuclear hormone receptor specificity.
{ECO:0000269|PubMed:8961273}.
-!- PTM: Ubiquitinated; mediated by SIAH2 and leading to its
subsequent proteasomal degradation. {ECO:0000305}.
-!- SIMILARITY: Belongs to the N-CoR nuclear receptor corepressors
family. {ECO:0000305}.
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EMBL; U35312; AAB17125.1; -; mRNA.
EMBL; U22016; AAC52168.1; -; mRNA.
PIR; S60254; S60254.
UniGene; Mm.271814; -.
UniGene; Mm.460227; -.
ProteinModelPortal; Q60974; -.
SMR; Q60974; -.
CORUM; Q60974; -.
DIP; DIP-32548N; -.
IntAct; Q60974; 26.
MINT; Q60974; -.
STRING; 10090.ENSMUSP00000018645; -.
iPTMnet; Q60974; -.
PhosphoSitePlus; Q60974; -.
PaxDb; Q60974; -.
PeptideAtlas; Q60974; -.
PRIDE; Q60974; -.
MGI; MGI:1349717; Ncor1.
eggNOG; KOG1878; Eukaryota.
eggNOG; ENOG410YDXP; LUCA.
HOVERGEN; HBG052587; -.
InParanoid; Q60974; -.
ChiTaRS; Ncor1; mouse.
PRO; PR:Q60974; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_NCOR1; -.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0016580; C:Sin3 complex; IBA:GO_Central.
GO; GO:0005876; C:spindle microtubule; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IPI:MGI.
GO; GO:0017053; C:transcriptional repressor complex; IPI:MGI.
GO; GO:0003682; F:chromatin binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:MGI.
GO; GO:0030331; F:estrogen receptor binding; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0035033; F:histone deacetylase regulator activity; IDA:MGI.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; IBA:GO_Central.
GO; GO:0035257; F:nuclear hormone receptor binding; ISO:MGI.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
GO; GO:0042974; F:retinoic acid receptor binding; IDA:MGI.
GO; GO:0046965; F:retinoid X receptor binding; IDA:MGI.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISO:MGI.
GO; GO:0001012; F:RNA polymerase II regulatory region DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0046966; F:thyroid hormone receptor binding; IDA:MGI.
GO; GO:0003714; F:transcription corepressor activity; IGI:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IMP:MGI.
GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IGI:MGI.
GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0032922; P:circadian regulation of gene expression; IGI:MGI.
GO; GO:0060318; P:definitive erythrocyte differentiation; IMP:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0046329; P:negative regulation of JNK cascade; ISO:MGI.
GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:MGI.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0031065; P:positive regulation of histone deacetylation; IDA:MGI.
GO; GO:0072362; P:regulation of glycolytic process by negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0072368; P:regulation of lipid transport by negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0040014; P:regulation of multicellular organism growth; IGI:MGI.
GO; GO:0002155; P:regulation of thyroid hormone mediated signaling pathway; IGI:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:MGI.
GO; GO:0051225; P:spindle assembly; ISO:MGI.
GO; GO:0021794; P:thalamus development; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00167; SANT; 2.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR031557; N-CoR_GPS2_interact.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR017884; SANT_dom.
Pfam; PF15784; GPS2_interact; 1.
Pfam; PF00249; Myb_DNA-binding; 1.
SMART; SM00717; SANT; 2.
SUPFAM; SSF46689; SSF46689; 2.
PROSITE; PS51293; SANT; 2.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chromatin regulator; Coiled coil;
Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 2453 Nuclear receptor corepressor 1.
/FTId=PRO_0000055618.
DOMAIN 435 486 SANT 1. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
DOMAIN 622 673 SANT 2. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
REGION 1 373 Interaction with ZBTB33 and HEXIM1.
{ECO:0000250}.
REGION 254 312 Interaction with SIN3A/B.
REGION 1510 2453 Interaction with C1D.
{ECO:0000269|PubMed:9405624}.
REGION 2050 2129 ID1.
REGION 2065 2068 Required for interaction with RARA in the
absence of its ligand. {ECO:0000250}.
REGION 2226 2287 ID2.
COILED 174 216 {ECO:0000255}.
COILED 299 328 {ECO:0000255}.
COILED 501 550 {ECO:0000255}.
MOTIF 1949 1953 CORNR box 1.
MOTIF 2073 2077 CORNR box 2.
MOTIF 2277 2281 CORNR box 3.
COMPBIAS 58 64 Poly-Gln.
COMPBIAS 593 602 Poly-Ala.
COMPBIAS 606 616 Pro-rich.
COMPBIAS 1044 1047 Poly-Pro.
COMPBIAS 1713 1718 Poly-Ala.
COMPBIAS 1968 1979 Poly-Ser.
MOD_RES 172 172 Phosphoserine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 1011 1011 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1122 1122 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1206 1206 Phosphoserine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 1207 1207 Phosphoserine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 1274 1274 Phosphoserine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 1292 1292 Phosphoserine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 1333 1333 Phosphoserine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 1347 1347 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1378 1378 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1423 1423 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 1459 1459 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1481 1481 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 1598 1598 Phosphoserine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 1993 1993 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1997 1997 Phosphoserine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 2116 2116 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WUB5}.
MOD_RES 2134 2134 Phosphoserine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 2150 2150 Phosphoserine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 2165 2165 Phosphoserine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 2198 2198 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 2412 2412 Phosphothreonine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 2449 2449 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 2451 2451 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
CROSSLNK 1117 1117 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:O75376}.
CROSSLNK 1117 1117 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:O75376}.
CROSSLNK 1195 1195 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O75376}.
CROSSLNK 1400 1400 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O75376}.
CROSSLNK 1423 1423 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:O75376}.
CROSSLNK 1525 1525 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O75376}.
VAR_SEQ 2333 2371 Missing (in isoform 2).
{ECO:0000303|PubMed:7566114}.
/FTId=VSP_003411.
CONFLICT 1952 1952 I -> T (in Ref. 2; AAC52168).
{ECO:0000305}.
CONFLICT 2090 2090 A -> P (in Ref. 2; AAC52168).
{ECO:0000305}.
SEQUENCE 2453 AA; 270642 MW; 52208B40382F7E6A CRC64;
MSSSGYPPNQ GAFSTEQSRY PSHSVQYTFP SARHQQEFAV PDYRSSHLEV SQASQLLQQQ
QQQQLRRRPS LLSEFHPGSD RPQERRSGYE QFHPGPSPVD HDSLESKRPR LEQVSDSHFQ
RISAAVLPLV HTLPEGLRSS ANAKKDPAFG VKHEAPSSPL SGQPCGDDQN ASPSKLSKEE
LIQSMDRVDR EIAKVEQQIL KLKKKQQQLE EEAAKPPEPE KPVSPPPVEQ KHRSIVQIIY
DENRKKAEEA HKIFEGLGPK VELPLYNQPS DTKVYHENIK TNQVMRKKLI LFFKRRNHAR
KQREQKICQR YDQLMEAWEK KVDRIENNPR RKAKESKTRE YYEKQFPEIR KQREQQERFQ
RVGQRGAGLS ATIARSEHEI SEIIDGLSEQ ENNEKQMRQL SVIPPMMFDA EQRRVKFINM
NGLMEDPMKV YKDRQFMNVW TDHEKEIFKD KFIQHPKNFG LIASYLERKS VPDCVLYYYL
TKKNENYKAL VRRNYGKRRG RNQQIARPSQ EEKVEEKEED KAEKTEKKEE EKKDDEEKDD
KEDSKETTKE KDRTEATAEE PEEREQVTPR GRKTANSQGR GKGRVTRSMT SEAAAANAAA
AATEEPPPPL PPPPEPISTE PVETSRWTEE EMEVAKKGLV EHGRNWAAIA KMVGTKSEAQ
CKNFYFNYKR RHNLDNLLQQ HKQKASRKPR EERDVSQCES VASTVSAQED EDIEASNEEE
NPEDSEGAEN SSDTESAPSP SPVEAAKSSE DSSENAASRG NTEPVAELEA TTDPAPCASP
SSAVPTTKPA ERESVEAQVT DSASAETAEP MDVDHEECGA EGSSVLDPPA PTKADSVDPE
MQVPENTASK GEGDAKERDL ESTSEKTEAR DEDVVVAEQI ERPEPQSDDD SSATCSADEG
VDGEPERQRV FPMDAKPSLL TPPGSILISS PIKPNLLDLP QLQHRAAVIP PMVSCTPCNI
PIGTPVSGYA LYQRHIKAMH ESALLEEQRQ RQEQVDLECR SSTSPCSTSK SPNREWEVLQ
PAPHQVITNL PEGVRLPTTR PTRPPPPLIP SSKTTVASEK PSFIMGGSIS QGTPGTYLSS
HNQAYPQEAP KPSVGSISLG LPRQQESTKA APLTYIKQEE FSPRSQNSQP EGLLVRAQHE
GVVRGTAGAV QEGSITRGTP ASKISVETIS SLRGSITQGT PALPQAGIPT EALVKGPVSR
MPIEESSPEK VREEAASKGH VIYEGKSGHI LSYDNIKNAR EGTRSPRTAH EMSLKRSYEA
VEGSIKQGMS MRESPVSAPL EGLICRALPR GSPHSDLKER TVLSGSIMQG TPRATAESFE
DGLKYPKQIK RESPPIRAFE GAITKGKPYD GITTIKEMGR SIHEIPRQDI LTQESRKTPE
VVQSTRPIIE GSISQGTPIK FDNNSGQSAI KHNVKSLITG PSKLPRGMLE IVPENIKVVE
RGKYEDVKAG EPVRARHTSV VSSGPSVLRS TLHEAPKAQL SPGLYDDSSA RRTPVSYQNT
ISRGSPMMNR TSDVSSSKSA SHERKSTLTP TQRESIPAKS PVPGVDPIVS HSPFDPHHRS
SAAGEVYRSH LPTHLDPAMP FHRALDPAAA YLLQRQLSPT PGYPSQYQLY AMENTRQTIL
NDYITSQQMQ VNLRPDVTRG LSPREQPLGL PYPATRGIID LTNMPPTILV PHAGGTSTPP
MDRITYIPGT QVTFPPRPYN AASLSPGHPT HLAAAASAER EREREREKER ERERERERER
ERERIAAAPA DLYLRPGSEQ PGRPGSHGYV RSPSPSVRTQ ETILQQRPSV FQGTNGTSVI
TPLDPTAQLR IMPLPSGGPS ISQGLPASRY NTAADALAAL VDAAASAPQM DVSKTKESKH
EAARLEENLR SRSAAVSEQQ QLEQKNLEVE KRSVQCVCTS SALPSGKAQP HASVVYSEAG
KDKGPPPKSR YEEELRTRGK TTITAANFID VIITRQIASD KDARERGSQS SDSSSSLSSH
RYETASDAIE VISPASSPAP PQEKPQAYQP DMVKANQAEN ESTRQYEGPL HHYRSQQESP
SPQQQPPLPP SSQSEGMGQV PRTHRLITLA DHICQIITQD FARNQVPSQA STSTFQTSPS
ALSSTPVRTK TSSRYSPESQ SQTVLHPRPG PRVSPENLVD KSRGSRPGKS PERSHIPSEP
YEPISPPQGP AVHEKQDSML LLSQRGVDPA EQRSDSRSPG SISYLPSFFT KLESTSPMVK
SKKQEIFRKL NSSGGGDSDM AAAQPGTEIF NLPAVTTSGA VSSRSHSFAD PASNLGLEDI
IRKALMGSFD DKVEDHGVVM SHPVGIMPGS ASTSVVTSSE ARRDEGEPSP HAGVCKPKLI
NKSNSRKSKS PIPGQSYLGT ERPSSVSSVH SEGDYHRQTP GWAWEDRPSS TGSTQFPYNP
LTIRMLSSTP PTQIACAPSA ITQAAPHQQN RIWEREPAPL LSAQYETLSD SDD


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