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Histone-lysine N-methyltransferase 2B (Lysine N-methyltransferase 2B) (EC 2.1.1.43) (Myeloid/lymphoid or mixed-lineage leukemia protein 4) (Trithorax homolog 2) (WW domain-binding protein 7) (WBP-7)

 KMT2B_HUMAN             Reviewed;        2715 AA.
Q9UMN6; O15022; O95836; Q96GP2; Q96IP3; Q9UK25; Q9Y668; Q9Y669;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
30-AUG-2017, entry version 184.
RecName: Full=Histone-lysine N-methyltransferase 2B;
Short=Lysine N-methyltransferase 2B;
EC=2.1.1.43;
AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia protein 4;
AltName: Full=Trithorax homolog 2;
AltName: Full=WW domain-binding protein 7;
Short=WBP-7;
Name=KMT2B; Synonyms=HRX2, KIAA0304, MLL2, MLL4, TRX2, WBP7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Angrand P.-O., Valvatne H., Jeanmougin F., Adamson A.,
van der Hoeven F., Olsen L., Tekotte H., Huang N., Poch O.,
Lamerdin J., Chambon P., Losson R., Stewart A., Aasland R.;
"Mammalian trithorax- and ASH1-like proteins: putative chromatin
regulators which contain PHD fingers and SET domains.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 111-2715 (ISOFORM 1).
TISSUE=Leukocyte, and Testis;
PubMed=10637508; DOI=10.1038/sj.onc.1203291;
Huntsman D.G., Chin S.-F., Muleris M., Batley S.J., Collins V.P.,
Wiedemann L.M., Aparicio S., Caldas C.;
"MLL2, the second human homolog of the Drosophila trithorax gene, maps
to 19q13.1 and is amplified in solid tumor cell lines.";
Oncogene 18:7975-7984(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 301-2715 (ISOFORM 1).
TISSUE=Brain;
PubMed=9205841; DOI=10.1093/dnares/4.2.141;
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 4:141-150(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1918-2715.
TISSUE=Brain, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Bone marrow, and Placenta;
PubMed=10409430; DOI=10.1006/geno.1999.5860;
FitzGerald K.T., Diaz M.O.;
"MLL2: a new mammalian member of the trx/MLL family of genes.";
Genomics 59:187-192(1999).
[7]
IDENTIFICATION IN THE MEN1-ASSOCIATED HISTONE METHYLTRANSFERASE
COMPLEX, AND INTERACTION OF THE COMPLEX WITH POLR2A AND POLR2B.
PubMed=14992727; DOI=10.1016/S1097-2765(04)00081-4;
Hughes C.M., Rozenblatt-Rosen O., Milne T.A., Copeland T.D.,
Levine S.S., Lee J.C., Hayes D.N., Shanmugam K.S., Bhattacharjee A.,
Biondi C.A., Kay G.F., Hayward N.K., Hess J.L., Meyerson M.;
"Menin associates with a trithorax family histone methyltransferase
complex and with the hoxc8 locus.";
Mol. Cell 13:587-597(2004).
[8]
INTERACTION WITH KDM6B.
PubMed=17825402; DOI=10.1016/j.cell.2007.08.019;
De Santa F., Totaro M.G., Prosperini E., Notarbartolo S., Testa G.,
Natoli G.;
"The histone H3 lysine-27 demethylase Jmjd3 links inflammation to
inhibition of polycomb-mediated gene silencing.";
Cell 130:1083-1094(2007).
[9]
FUNCTION, ENZYME ACTIVITY, AND INTERACTION WITH NFE2.
PubMed=17707229; DOI=10.1016/j.molcel.2007.06.022;
Demers C., Chaturvedi C.-P., Ranish J.A., Juban G., Lai P., Morle F.,
Aebersold R., Dilworth F.J., Groudine M., Brand M.;
"Activator-mediated recruitment of the MLL2 methyltransferase complex
to the beta-globin locus.";
Mol. Cell 27:573-584(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821; SER-844; SER-1032;
SER-1035 AND SER-1930, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2068 AND THR-2083, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-861, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351; SER-821; SER-844;
SER-861; SER-936; SER-1092; SER-1095; SER-1936; THR-2083; SER-2288 AND
SER-2348, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-861 AND THR-2083, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-805 AND LYS-1136, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone
H3. H3 'Lys-4' methylation represents a specific tag for
epigenetic transcriptional activation. Plays a central role in
beta-globin locus transcription regulation by being recruited by
NFE2. Plays an important role in controlling bulk H3K4me during
oocyte growth and preimplantation development. Required during the
transcriptionally active period of oocyte growth for the
establishment and/or maintenance of bulk H3K4 trimethylation
(H3K4me3), global transcriptional silencing that preceeds
resumption of meiosis, oocyte survival and normal zygotic genome
activation. {ECO:0000269|PubMed:17707229}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:17707229}.
-!- SUBUNIT: Component of the menin-associated histone
methyltransferase complex, at least composed of KMT2B/MLL4, ASH2L,
RBBP5, WDR5, DPY30, MEN1; the complex interacts with POLR2A and
POLR2B via MEN1. Interacts with NFE2. Interacts with KDM6B.
{ECO:0000269|PubMed:14992727, ECO:0000269|PubMed:17707229,
ECO:0000269|PubMed:17825402}.
-!- INTERACTION:
P16333:NCK1; NbExp=2; IntAct=EBI-765774, EBI-389883;
P61964:WDR5; NbExp=3; IntAct=EBI-765774, EBI-540834;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long;
IsoId=Q9UMN6-1; Sequence=Displayed;
Name=2; Synonyms=Truncated;
IsoId=Q9UMN6-2; Sequence=VSP_006668, VSP_006669;
-!- TISSUE SPECIFICITY: Widely expressed. Highest levels in testis.
Also found in brain, bone marrow, heart, muscle, kidney, placenta,
spleen, thymus, prostate, ovary, intestine, colon, peripheral
blood lymphocytes and pancreas. Often amplified in pancreatic
carcinomas.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. TRX/MLL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
-!- CAUTION: This protein was first named MLL2 by PubMed:10637508 and
PubMed:10409430. MLL2 corresponds to another protein located on
chromosome 12 (see AC O14686). Thus, KMT2B/MLL4 is often referred
to as MLL2 and vice versa in the literature. {ECO:0000305}.
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EMBL; AJ007041; CAB45385.1; -; mRNA.
EMBL; AD000671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF186605; AAD56420.1; -; mRNA.
EMBL; AB002302; BAA20763.3; -; mRNA.
EMBL; BC009337; AAH09337.2; -; mRNA.
EMBL; BC007353; AAH07353.3; -; mRNA.
EMBL; AF104918; AAD17932.1; -; mRNA.
EMBL; AF105279; AAD26113.1; -; mRNA.
EMBL; AF105280; AAD26112.1; -; mRNA.
CCDS; CCDS46055.1; -. [Q9UMN6-1]
RefSeq; NP_055542.1; NM_014727.2. [Q9UMN6-1]
UniGene; Hs.676457; -.
UniGene; Hs.92236; -.
PDB; 3UVM; X-ray; 1.57 A; B=2508-2517.
PDB; 4ERZ; X-ray; 1.75 A; D/E/F=2504-2517.
PDB; 4PZI; X-ray; 2.15 A; A=955-1020.
PDBsum; 3UVM; -.
PDBsum; 4ERZ; -.
PDBsum; 4PZI; -.
ProteinModelPortal; Q9UMN6; -.
SMR; Q9UMN6; -.
BioGrid; 115104; 36.
DIP; DIP-34598N; -.
ELM; Q9UMN6; -.
IntAct; Q9UMN6; 33.
MINT; MINT-1187865; -.
STRING; 9606.ENSP00000222270; -.
BindingDB; Q9UMN6; -.
ChEMBL; CHEMBL2189112; -.
iPTMnet; Q9UMN6; -.
PhosphoSitePlus; Q9UMN6; -.
BioMuta; KMT2B; -.
DMDM; 12643900; -.
EPD; Q9UMN6; -.
PaxDb; Q9UMN6; -.
PeptideAtlas; Q9UMN6; -.
PRIDE; Q9UMN6; -.
Ensembl; ENST00000420124; ENSP00000398837; ENSG00000272333. [Q9UMN6-1]
GeneID; 9757; -.
KEGG; hsa:9757; -.
UCSC; uc021usv.1; human. [Q9UMN6-1]
CTD; 9757; -.
DisGeNET; 9757; -.
GeneCards; KMT2B; -.
HGNC; HGNC:15840; KMT2B.
HPA; HPA006487; -.
MIM; 606834; gene.
neXtProt; NX_Q9UMN6; -.
OpenTargets; ENSG00000272333; -.
eggNOG; KOG1084; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00760000119228; -.
HOVERGEN; HBG100043; -.
InParanoid; Q9UMN6; -.
KO; K14959; -.
OMA; EEFQGFH; -.
OrthoDB; EOG091G001P; -.
PhylomeDB; Q9UMN6; -.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
GeneWiki; MLL4; -.
GenomeRNAi; 9757; -.
PRO; PR:Q9UMN6; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000272333; -.
CleanEx; HS_MLL2; -.
Genevisible; Q9UMN6; HS.
GO; GO:0035097; C:histone methyltransferase complex; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:MGI.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0048096; P:chromatin-mediated maintenance of transcription; NAS:UniProtKB.
GO; GO:0016458; P:gene silencing; IEA:Ensembl.
GO; GO:0051568; P:histone H3-K4 methylation; IMP:UniProtKB.
GO; GO:0080182; P:histone H3-K4 trimethylation; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0009994; P:oocyte differentiation; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0030728; P:ovulation; IEA:Ensembl.
GO; GO:0051569; P:regulation of histone H3-K4 methylation; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 4.
InterPro; IPR034732; EPHD.
InterPro; IPR003889; FYrich_C.
InterPro; IPR003888; FYrich_N.
InterPro; IPR016569; MeTrfase_trithorax.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR001214; SET_dom.
InterPro; IPR002857; Znf_CXXC.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF05965; FYRC; 1.
Pfam; PF05964; FYRN; 1.
Pfam; PF00628; PHD; 2.
Pfam; PF00856; SET; 1.
Pfam; PF02008; zf-CXXC; 1.
PIRSF; PIRSF010354; Methyltransferase_trithorax; 1.
SMART; SM00542; FYRC; 1.
SMART; SM00541; FYRN; 1.
SMART; SM00249; PHD; 4.
SMART; SM00508; PostSET; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF57903; SSF57903; 2.
PROSITE; PS51805; EPHD; 1.
PROSITE; PS51543; FYRC; 1.
PROSITE; PS51542; FYRN; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50280; SET; 1.
PROSITE; PS51058; ZF_CXXC; 1.
PROSITE; PS01359; ZF_PHD_1; 3.
PROSITE; PS50016; ZF_PHD_2; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
Complete proteome; DNA-binding; Isopeptide bond; Metal-binding;
Methyltransferase; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
Transcription regulation; Transferase; Ubl conjugation; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 2715 Histone-lysine N-methyltransferase 2B.
/FTId=PRO_0000124881.
DOMAIN 1727 1783 FYR N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00875}.
DOMAIN 2411 2492 FYR C-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00876}.
DOMAIN 2575 2691 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 2699 2715 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
DNA_BIND 37 44 A.T hook 1.
DNA_BIND 110 117 A.T hook 2.
DNA_BIND 357 365 A.T hook 3.
ZN_FING 959 1006 CXXC-type. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
ZN_FING 1201 1252 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1249 1303 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1335 1396 PHD-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1578 1618 C2HC pre-PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU01146}.
ZN_FING 1639 1686 PHD-type 4. {ECO:0000255|PROSITE-
ProRule:PRU01146}.
REGION 2652 2653 S-adenosyl-L-methionine binding.
{ECO:0000250}.
COMPBIAS 26 37 Poly-Gly.
COMPBIAS 248 255 Poly-Pro.
COMPBIAS 362 398 Asp/Glu-rich (acidic).
COMPBIAS 402 771 Pro-rich.
COMPBIAS 808 812 Poly-Gln.
COMPBIAS 1963 1970 Poly-Pro.
COMPBIAS 2251 2259 Poly-Pro.
METAL 2655 2655 Zinc. {ECO:0000250}.
METAL 2703 2703 Zinc. {ECO:0000250}.
METAL 2705 2705 Zinc. {ECO:0000250}.
METAL 2710 2710 Zinc. {ECO:0000250}.
BINDING 2585 2585 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 2587 2587 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 2629 2629 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 2704 2704 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000250|UniProtKB:O08550}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000250|UniProtKB:O08550}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000250|UniProtKB:O08550}.
MOD_RES 351 351 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 821 821 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 844 844 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 861 861 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 936 936 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1032 1032 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1035 1035 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1092 1092 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1095 1095 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1930 1930 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1936 1936 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2068 2068 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 2083 2083 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 2288 2288 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2348 2348 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 805 805 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1136 1136 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 532 582 VSARSSRVIKTPRRFMDEDPPKPPKVEVSPVLRPPITTSPP
VPQEPAPVPS -> PLSQSLLLPMTLQLSLSLGQWAAPTTS
ACLDSPLWSPLLLRPRCPLTGLQL (in isoform 2).
{ECO:0000305}.
/FTId=VSP_006668.
VAR_SEQ 583 2715 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_006669.
VARIANT 172 172 T -> I (in dbSNP:rs60207923).
/FTId=VAR_061913.
VARIANT 587 587 P -> R (in dbSNP:rs2242519).
/FTId=VAR_046563.
VARIANT 754 754 P -> L (in dbSNP:rs179686).
/FTId=VAR_046564.
VARIANT 1097 1097 P -> L (in dbSNP:rs34014681).
/FTId=VAR_046565.
VARIANT 1829 1829 P -> L (in dbSNP:rs16970649).
/FTId=VAR_052653.
VARIANT 2364 2364 D -> G (in dbSNP:rs231591).
/FTId=VAR_052654.
VARIANT 2408 2408 K -> N (in dbSNP:rs36062432).
/FTId=VAR_052655.
CONFLICT 834 834 K -> E (in Ref. 6; AAD17932).
{ECO:0000305}.
CONFLICT 941 941 S -> Y (in Ref. 6; AAD17932).
{ECO:0000305}.
CONFLICT 1317 1317 E -> Q (in Ref. 6; AAD17932).
{ECO:0000305}.
CONFLICT 1362 1362 H -> Y (in Ref. 6; AAD17932).
{ECO:0000305}.
CONFLICT 1438 1438 D -> N (in Ref. 6; AAD17932).
{ECO:0000305}.
CONFLICT 1918 1920 PLA -> GTR (in Ref. 5; AAH09337).
{ECO:0000305}.
CONFLICT 2622 2622 D -> H (in Ref. 6; AAD26112).
{ECO:0000305}.
HELIX 970 973 {ECO:0000244|PDB:4PZI}.
STRAND 979 981 {ECO:0000244|PDB:4PZI}.
HELIX 982 985 {ECO:0000244|PDB:4PZI}.
HELIX 988 990 {ECO:0000244|PDB:4PZI}.
HELIX 1001 1003 {ECO:0000244|PDB:4PZI}.
HELIX 1006 1015 {ECO:0000244|PDB:4PZI}.
HELIX 2510 2512 {ECO:0000244|PDB:3UVM}.
SEQUENCE 2715 AA; 293515 MW; C0615B981BBEB7BF CRC64;
MAAAAGGGSC PGPGSARGRF PGRPRGAGGG GGRGGRGNGA ERVRVALRRG GGATGPGGAE
PGEDTALLRL LGLRRGLRRL RRLWAGPRVQ RGRGRGRGRG WGPSRGCVPE EESSDGESDE
EEFQGFHSDE DVAPSSLRSA LRSQRGRAPR GRGRKHKTTP LPPPRLADVA PTPPKTPARK
RGEEGTERMV QALTELLRRA QAPQAPRSRA CEPSTPRRSR GRPPGRPAGP CRRKQQAVVV
AEAAVTIPKP EPPPPVVPVK HQTGSWKCKE GPGPGPGTPR RGGQSSRGGR GGRGRGRGGG
LPFVIKFVSR AKKVKMGQLS LGLESGQGQG QHEESWQDVP QRRVGSGQGG SPCWKKQEQK
LDDEEEEKKE EEEKDKEGEE KEERAVAEEM MPAAEKEEAK LPPPPLTPPA PSPPPPLPPP
STSPPPPLCP PPPPPVSPPP LPSPPPPPAQ EEQEESPPPV VPATCSRKRG RPPLTPSQRA
EREAARAGPE GTSPPTPTPS TATGGPPEDS PTVAPKSTTF LKNIRQFIMP VVSARSSRVI
KTPRRFMDED PPKPPKVEVS PVLRPPITTS PPVPQEPAPV PSPPRAPTPP STPVPLPEKR
RSILREPTFR WTSLTRELPP PPPAPPPPPA PSPPPAPATS SRRPLLLRAP QFTPSEAHLK
IYESVLTPPP LGAPEAPEPE PPPADDSPAE PEPRAVGRTN HLSLPRFAPV VTTPVKAEVS
PHGAPALSNG PQTQAQLLQP LQALQTQLLP QALPPPQPQL QPPPSPQQMP PLEKARIAGV
GSLPLSGVEE KMFSLLKRAK VQLFKIDQQQ QQKVAASMPL SPGGQMEEVA GAVKQISDRG
PVRSEDESVE AKRERPSGPE SPVQGPRIKH VCRHAAVALG QARAMVPEDV PRLSALPLRD
RQDLATEDTS SASETESVPS RSRRGKVEAA GPGGESEPTG SGGTLAHTPR RSLPSHHGKK
MRMARCGHCR GCLRVQDCGS CVNCLDKPKF GGPNTKKQCC VYRKCDKIEA RKMERLAKKG
RTIVKTLLPW DSDESPEASP GPPGPRRGAG AGGPREEVVA HPGPEEQDSL LQRKSARRCV
KQRPSYDIFE DSDDSEPGGP PAPRRRTPRE NELPLPEPEE QSRPRKPTLQ PVLQLKARRR
LDKDALAPGP FASFPNGWTG KQKSPDGVHR VRVDFKEDCD LENVWLMGGL SVLTSVPGGP
PMVCLLCASK GLHELVFCQV CCDPFHPFCL EEAERPLPQH HDTWCCRRCK FCHVCGRKGR
GSKHLLECER CRHAYHPACL GPSYPTRATR KRRHWICSAC VRCKSCGATP GKNWDVEWSG
DYSLCPRCTQ LYEKGNYCPI CTRCYEDNDY ESKMMQCAQC DHWVHAKCEG LSDEDYEILS
GLPDSVLYTC GPCAGAAQPR WREALSGALQ GGLRQVLQGL LSSKVVGPLL LCTQCGPDGK
QLHPGPCGLQ AVSQRFEDGH YKSVHSFMED MVGILMRHSE EGETPDRRAG GQMKGLLLKL
LESAFGWFDA HDPKYWRRST RLPNGVLPNA VLPPSLDHVY AQWRQQEPET PESGQPPGDP
SAAFQGKDPA AFSHLEDPRQ CALCLKYGDA DSKEAGRLLY IGQNEWTHVN CAIWSAEVFE
ENDGSLKNVH AAVARGRQMR CELCLKPGAT VGCCLSSCLS NFHFMCARAS YCIFQDDKKV
FCQKHTDLLD GKEIVNPDGF DVLRRVYVDF EGINFKRKFL TGLEPDAINV LIGSIRIDSL
GTLSDLSDCE GRLFPIGYQC SRLYWSTVDA RRRCWYRCRI LEYRPWGPRE EPAHLEAAEE
NQTIVHSPAP SSEPPGGEDP PLDTDVLVPG APERHSPIQN LDPPLRPDSG SAPPPAPRSF
SGARIKVPNY SPSRRPLGGV SFGPLPSPGS PSSLTHHIPT VGDPDFPAPP RRSRRPSPLA
PRPPPSRWAS PPLKTSPQLR VPPPTSVVTA LTPTSGELAP PGPAPSPPPP EDLGPDFEDM
EVVSGLSAAD LDFAASLLGT EPFQEEIVAA GAMGSSHGGP GDSSEEESSP TSRYIHFPVT
VVSAPGLAPS ATPGAPRIEQ LDGVDDGTDS EAEAVQQPRG QGTPPSGPGV VRAGVLGAAG
DRARPPEDLP SEIVDFVLKN LGGPGDGGAG PREESLPPAP PLANGSQPSQ GLTASPADPT
RTFAWLPGAP GVRVLSLGPA PEPPKPATSK IILVNKLGQV FVKMAGEGEP VPPPVKQPPL
PPTISPTAPT SWTLPPGPLL GVLPVVGVVR PAPPPPPPPL TLVLSSGPAS PPRQAIRVKR
VSTFSGRSPP APPPYKAPRL DEDGEASEDT PQVPGLGSGG FSRVRMKTPT VRGVLDLDRP
GEPAGEESPG PLQERSPLLP LPEDGPPQVP DGPPDLLLES QWHHYSGEAS SSEEEPPSPD
DKENQAPKRT GPHLRFEISS EDGFSVEAES LEGAWRTLIE KVQEARGHAR LRHLSFSGMS
GARLLGIHHD AVIFLAEQLP GAQRCQHYKF RYHQQGEGQE EPPLNPHGAA RAEVYLRKCT
FDMFNFLASQ HRVLPEGATC DEEEDEVQLR STRRATSLEL PMAMRFRHLK KTSKEAVGVY
RSAIHGRGLF CKRNIDAGEM VIEYSGIVIR SVLTDKREKF YDGKGIGCYM FRMDDFDVVD
ATMHGNAARF INHSCEPNCF SRVIHVEGQK HIVIFALRRI LRGEELTYDY KFPIEDASNK
LPCNCGAKRC RRFLN


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