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Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.43) (Lysine N-methyltransferase 3A) (SET domain-containing protein 2)

 SETD2_MOUSE             Reviewed;        2537 AA.
E9Q5F9; Q69ZC0; Q6PCY9; Q8K0F3;
18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
05-APR-2011, sequence version 1.
22-NOV-2017, entry version 60.
RecName: Full=Histone-lysine N-methyltransferase SETD2 {ECO:0000305};
EC=2.1.1.43 {ECO:0000269|PubMed:18157086};
AltName: Full=Lysine N-methyltransferase 3A {ECO:0000250|UniProtKB:Q9BYW2};
AltName: Full=Protein-lysine N-methyltransferase SETD2 {ECO:0000305};
EC=2.1.1.- {ECO:0000269|PubMed:27518565};
AltName: Full=SET domain-containing protein 2 {ECO:0000303|PubMed:18157086};
Name=Setd2 {ECO:0000303|PubMed:18157086, ECO:0000312|MGI:MGI:1918177};
Synonyms=Kiaa1732 {ECO:0000303|PubMed:15368895},
Kmt3a {ECO:0000250|UniProtKB:Q9BYW2};
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 [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2121-2537 AND 1800-2537
(ISOFORM 2).
TISSUE=Mammary tumor;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1834-2537 (ISOFORM 1).
TISSUE=Thymus;
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
PubMed=18157086; DOI=10.1038/sj.emboj.7601967;
Edmunds J.W., Mahadevan L.C., Clayton A.L.;
"Dynamic histone H3 methylation during gene induction: HYPB/Setd2
mediates all H3K36 trimethylation.";
EMBO J. 27:406-420(2008).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1387; SER-1389 AND
SER-1391, 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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-242; SER-322;
SER-324; SER-624; SER-633; SER-697; SER-1818; SER-1819; THR-1827;
SER-1954; SER-1962 AND SER-1969, 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).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20133625; DOI=10.1073/pnas.0915033107;
Hu M., Sun X.J., Zhang Y.L., Kuang Y., Hu C.Q., Wu W.L., Shen S.H.,
Du T.T., Li H., He F., Xiao H.S., Wang Z.G., Liu T.X., Lu H.,
Huang Q.H., Chen S.J., Chen Z.;
"Histone H3 lysine 36 methyltransferase Hypb/Setd2 is required for
embryonic vascular remodeling.";
Proc. Natl. Acad. Sci. U.S.A. 107:2956-2961(2010).
[8]
FUNCTION.
PubMed=25242323; DOI=10.1016/j.celrep.2014.08.031;
Zhang Y., Xie S., Zhou Y., Xie Y., Liu P., Sun M., Xiao H., Jin Y.,
Sun X., Chen Z., Huang Q., Chen S.;
"H3K36 histone methyltransferase Setd2 is required for murine
embryonic stem cell differentiation toward endoderm.";
Cell Rep. 8:1989-2002(2014).
[9]
FUNCTION AS ALPHA-TUBULIN METHYLTRANSFERASE.
PubMed=27518565; DOI=10.1016/j.cell.2016.07.005;
Park I.Y., Powell R.T., Tripathi D.N., Dere R., Ho T.H., Blasius T.L.,
Chiang Y.C., Davis I.J., Fahey C.C., Hacker K.E., Verhey K.J.,
Bedford M.T., Jonasch E., Rathmell W.K., Walker C.L.;
"Dual chromatin and cytoskeletal remodeling by SETD2.";
Cell 166:950-962(2016).
-!- FUNCTION: Histone methyltransferase that specifically
trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated
'Lys-36' (H3K36me2) as substrate (PubMed:18157086,
PubMed:20133625). Represents the main enzyme generating H3K36me3,
a specific tag for epigenetic transcriptional activation
(PubMed:18157086, PubMed:20133625). Plays a role in chromatin
structure modulation during elongation by coordinating recruitment
of the FACT complex and by interacting with hyperphosphorylated
POLR2A (By similarity). Acts as a key regulator of DNA mismatch
repair in G1 and early S phase by generating H3K36me3, a mark
required to recruit MSH6 subunit of the MutS alpha complex: early
recruitment of the MutS alpha complex to chromatin to be
replicated allows a quick identification of mismatch DNA to
initiate the mismatch repair reaction (By similarity). Required
for DNA double-strand break repair in response to DNA damage: acts
by mediating formation of H3K36me3, promoting recruitment of RAD51
and DNA repair via homologous recombination (HR) (By similarity).
Acts as a tumor suppressor (By similarity). H3K36me3 also plays an
essential role in the maintenance of a heterochromatic state, by
recruiting DNA methyltransferase DNMT3A (By similarity). H3K36me3
is also enhanced in intron-containing genes, suggesting that SETD2
recruitment is enhanced by splicing and that splicing is coupled
to recruitment of elongating RNA polymerase (By similarity).
Required during angiogenesis (PubMed:20133625). Required for
endoderm development by promoting embryonic stem cell
differentiation toward endoderm: acts by mediating formation of
H3K36me3 in distal promoter regions of FGFR3, leading to regulate
transcription initiation of FGFR3 (PubMed:25242323). In addition
to histones, also mediates methylation of other proteins, such as
tubulins and STAT1 (PubMed:27518565). Trimethylates 'Lys-40' of
alpha-tubulins such as TUBA1B (alpha-TubK40me3); alpha-TubK40me3
is required for normal mitosis and cytokinesis and may be a
specific tag in cytoskeletal remodeling (PubMed:27518565).
Involved in interferon-alpha-induced antiviral defense by
mediating both monomethylation of STAT1 at 'Lys-525' and
catalyzing H3K36me3 on promoters of some interferon-stimulated
genes (ISGs) to activate gene transcription (By similarity).
{ECO:0000250|UniProtKB:Q9BYW2, ECO:0000269|PubMed:18157086,
ECO:0000269|PubMed:20133625, ECO:0000269|PubMed:25242323,
ECO:0000269|PubMed:27518565}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:18157086}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + [protein]-L-lysine =
S-adenosyl-L-homocysteine + [protein]-N(6)-methyl-L-lysine.
{ECO:0000250|UniProtKB:Q9BYW2}.
-!- CATALYTIC ACTIVITY: 3 S-adenosyl-L-methionine + [protein]-L-lysine
= 3 S-adenosyl-L-homocysteine + [protein]-N(6),N(6),N(6)-methyl-L-
lysine. {ECO:0000269|PubMed:27518565}.
-!- ENZYME REGULATION: Specifically inhibited by sinefungin
derivatives. {ECO:0000250|UniProtKB:Q9BYW2}.
-!- SUBUNIT: Specifically interacts with hyperphosphorylated C-
terminal domain (CTD) of RNA polymerase II large subunit (POLR2A):
binds to CTD heptad repeats doubly phosphorylated on 'Ser-2' and
'Ser-5' of each heptad. Interacts with HTT. Interacts with IWS1.
Interacts with p53/TP53; leading to regulate p53/TP53 target
genes. Component of a complex with HNRNPL. Interacts with TUBA1A;
the interaction is independent on alpha-tubulin acetylation on
'Lys-40'. {ECO:0000250|UniProtKB:Q9BYW2}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18157086}.
Chromosome {ECO:0000269|PubMed:18157086}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=E9Q5F9-1; Sequence=Displayed;
Name=2;
IsoId=E9Q5F9-2; Sequence=VSP_047946;
Note=No experimental confirmation available.;
-!- DOMAIN: The low charge region mediates the transcriptional
activation activity. {ECO:0000250|UniProtKB:Q9BYW2}.
-!- PTM: May be automethylated. {ECO:0000250|UniProtKB:Q9BYW2}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality at E10.5-E11.5. Embryos
show severe vascular defects in embryo, yolk sac and placenta.
Capillaries are abnormally dilated in embryos and yolk sacs and
cannot be remodeled into large blood vessels or intricate
networks. The embryonic vessels fail to invade the labyrinthine
layer of placenta, which impair the embryonic-maternal vascular
connection. Defects are not caused by the extraembryonic tissues.
Impaired H3K36me3, but not H3K36me2 or H3K36me1.
{ECO:0000269|PubMed:20133625}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. SET2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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EMBL; AC132103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC031601; AAH31601.1; -; mRNA.
EMBL; BC059049; AAH59049.1; -; mRNA.
EMBL; AK173246; BAD32524.1; -; mRNA.
CCDS; CCDS40781.2; -. [E9Q5F9-1]
RefSeq; NP_001074809.2; NM_001081340.2. [E9Q5F9-1]
UniGene; Mm.288949; -.
ProteinModelPortal; E9Q5F9; -.
SMR; E9Q5F9; -.
BioGrid; 231695; 8.
IntAct; E9Q5F9; 8.
STRING; 10090.ENSMUSP00000116313; -.
iPTMnet; E9Q5F9; -.
PhosphoSitePlus; E9Q5F9; -.
MaxQB; E9Q5F9; -.
PaxDb; E9Q5F9; -.
PeptideAtlas; E9Q5F9; -.
PRIDE; E9Q5F9; -.
Ensembl; ENSMUST00000153838; ENSMUSP00000116313; ENSMUSG00000044791. [E9Q5F9-1]
GeneID; 235626; -.
KEGG; mmu:235626; -.
UCSC; uc009rug.2; mouse. [E9Q5F9-1]
CTD; 29072; -.
MGI; MGI:1918177; Setd2.
eggNOG; KOG4442; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00780000121845; -.
HOGENOM; HOG000081757; -.
InParanoid; E9Q5F9; -.
KO; K11423; -.
OMA; FIGHDSH; -.
OrthoDB; EOG091G040P; -.
TreeFam; TF106477; -.
Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
ChiTaRS; Setd2; mouse.
PRO; PR:E9Q5F9; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000044791; -.
ExpressionAtlas; E9Q5F9; baseline and differential.
Genevisible; E9Q5F9; MM.
GO; GO:0005694; C:chromosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IMP:UniProtKB.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0035441; P:cell migration involved in vasculogenesis; IMP:MGI.
GO; GO:0060977; P:coronary vasculature morphogenesis; IMP:MGI.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:MGI.
GO; GO:0048568; P:embryonic organ development; IMP:MGI.
GO; GO:0060669; P:embryonic placenta morphogenesis; IMP:MGI.
GO; GO:0035987; P:endodermal cell differentiation; IMP:UniProtKB.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0097676; P:histone H3-K36 dimethylation; ISO:MGI.
GO; GO:0010452; P:histone H3-K36 methylation; IMP:MGI.
GO; GO:0097198; P:histone H3-K36 trimethylation; IMP:UniProtKB.
GO; GO:0048332; P:mesoderm morphogenesis; IMP:MGI.
GO; GO:1902850; P:microtubule cytoskeleton organization involved in mitosis; ISS:UniProtKB.
GO; GO:0006298; P:mismatch repair; ISS:UniProtKB.
GO; GO:0001763; P:morphogenesis of a branching structure; IMP:MGI.
GO; GO:0001843; P:neural tube closure; IMP:MGI.
GO; GO:0034728; P:nucleosome organization; ISS:UniProtKB.
GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
GO; GO:0018023; P:peptidyl-lysine trimethylation; IMP:MGI.
GO; GO:0060039; P:pericardium development; IMP:MGI.
GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0010793; P:regulation of mRNA export from nucleus; ISO:MGI.
GO; GO:1905634; P:regulation of protein localization to chromatin; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0034340; P:response to type I interferon; ISS:UniProtKB.
GO; GO:0048864; P:stem cell development; IMP:MGI.
GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0001570; P:vasculogenesis; IMP:MGI.
CDD; cd00201; WW; 1.
InterPro; IPR006560; AWS_dom.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR001214; SET_dom.
InterPro; IPR013257; SRI.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
Pfam; PF00856; SET; 1.
Pfam; PF08236; SRI; 1.
Pfam; PF00397; WW; 1.
SMART; SM00570; AWS; 1.
SMART; SM00508; PostSET; 1.
SMART; SM00317; SET; 1.
SMART; SM00456; WW; 1.
SUPFAM; SSF51045; SSF51045; 1.
PROSITE; PS51215; AWS; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50280; SET; 1.
PROSITE; PS01159; WW_DOMAIN_1; 1.
PROSITE; PS50020; WW_DOMAIN_2; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Antiviral defense;
Chromatin regulator; Chromosome; Coiled coil; Complete proteome;
Developmental protein; Differentiation; DNA damage; DNA repair;
Immunity; Innate immunity; Isopeptide bond; Metal-binding;
Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Zinc.
CHAIN 1 2537 Histone-lysine N-methyltransferase SETD2.
/FTId=PRO_0000423553.
DOMAIN 1468 1522 AWS. {ECO:0000255|PROSITE-
ProRule:PRU00562}.
DOMAIN 1524 1641 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 1648 1664 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
DOMAIN 2362 2395 WW. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
REGION 1392 1688 Interaction with TUBA1A.
{ECO:0000250|UniProtKB:Q9BYW2}.
REGION 1534 1536 Inhibitor binding.
{ECO:0000250|UniProtKB:Q9BYW2}.
REGION 1534 1536 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9BYW2}.
REGION 1577 1579 Inhibitor binding.
{ECO:0000250|UniProtKB:Q9BYW2}.
REGION 1577 1579 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9BYW2}.
REGION 1602 1603 Inhibitor binding.
{ECO:0000250|UniProtKB:Q9BYW2}.
REGION 1602 1603 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9BYW2}.
REGION 2110 2339 Low charge region.
{ECO:0000250|UniProtKB:Q9BYW2}.
REGION 2430 2537 Interaction with POLR2A.
{ECO:0000250|UniProtKB:Q9BYW2}.
COILED 2090 2119 {ECO:0000255}.
COMPBIAS 167 231 Pro-rich.
COMPBIAS 294 439 Ser-rich.
COMPBIAS 369 457 Arg-rich.
COMPBIAS 2233 2338 Gln-rich.
METAL 1473 1473 Zinc 1. {ECO:0000250|UniProtKB:Q9BYW2}.
METAL 1475 1475 Zinc 1. {ECO:0000250|UniProtKB:Q9BYW2}.
METAL 1490 1490 Zinc 1. {ECO:0000250|UniProtKB:Q9BYW2}.
METAL 1490 1490 Zinc 2. {ECO:0000250|UniProtKB:Q9BYW2}.
METAL 1494 1494 Zinc 1. {ECO:0000250|UniProtKB:Q9BYW2}.
METAL 1503 1503 Zinc 2. {ECO:0000250|UniProtKB:Q9BYW2}.
METAL 1507 1507 Zinc 2. {ECO:0000250|UniProtKB:Q9BYW2}.
METAL 1513 1513 Zinc 2. {ECO:0000250|UniProtKB:Q9BYW2}.
METAL 1605 1605 Zinc 3. {ECO:0000250|UniProtKB:Q9BYW2}.
METAL 1652 1652 Zinc 3. {ECO:0000250|UniProtKB:Q9BYW2}.
METAL 1654 1654 Zinc 3. {ECO:0000250|UniProtKB:Q9BYW2}.
METAL 1659 1659 Zinc 3. {ECO:0000250|UniProtKB:Q9BYW2}.
BINDING 1599 1599 Inhibitor.
{ECO:0000250|UniProtKB:Q9BYW2}.
BINDING 1650 1650 Inhibitor; alternate.
{ECO:0000250|UniProtKB:Q9BYW2}.
BINDING 1650 1650 S-adenosyl-L-methionine; alternate.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 1653 1653 Inhibitor; via amide nitrogen; alternate.
{ECO:0000250|UniProtKB:Q9BYW2}.
BINDING 1653 1653 S-adenosyl-L-methionine; via amide
nitrogen; alternate.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 322 322 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 324 324 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 532 532 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 614 614 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 624 624 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 626 626 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 633 633 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 697 697 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 707 707 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 743 743 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 753 753 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 1077 1077 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 1201 1201 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 1387 1387 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 1389 1389 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 1391 1391 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 1670 1670 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 1818 1818 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1819 1819 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1827 1827 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1846 1846 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 1862 1862 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 1926 1926 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 1954 1954 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1962 1962 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1969 1969 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2053 2053 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYW2}.
MOD_RES 2055 2055 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BYW2}.
CROSSLNK 360 360 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9BYW2}.
CROSSLNK 637 637 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9BYW2}.
CROSSLNK 775 775 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9BYW2}.
VAR_SEQ 2011 2011 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_047946.
SEQUENCE 2537 AA; 285663 MW; 4ED47D778291DA9D CRC64;
MKPLPSQQPP PKMGDFYDPE HPTPEEEENE AKIENVQKTG FIKGPVFKGV ASSRFLPKGT
KTKVNLEEQG RQKVSFSFSF TKKTLQNRFL TALSNEKQSD SPNSPAPPLQ VDSNPKVKMD
AGDTFPATEE SSPPKSRVEL GRIHFKKHLL HVTSRPQLAA STTAASPLPP TTQLPAVLAE
SMIDSPPSSP PPPPPPPQAS SPSPPAQISE PVALPQPPAT ALMTSPPGPL PGDVAVRAQK
ESPVKSGPEV LEVDTKQDIV SNSLEEHTVQ TLKEQADHLL QKEDSHIGKE EEVSDGSKIS
LSSKKASSKK KSSQFEGTFL GSESDEDSVR TSSSQRSHDL KSSTSIDKER DFKKSSAPSK
SEDLGKSSRS KTERDDRYCS YSKLERDTRY VSSRCRSERD RRRSRSRSRS DRASRTSLSY
SRSERSHYYD SERRYHRSSP YRERTRYSRP YTDNRARESS DSEDEYKKTY PRRTSAHSYR
DLRTSSSYSK FDRDCKTETS YLEMERRGKY TSKLERESKR TSEHETIKRC CSPPNELGFR
RGSSYSKHDN STSRYKSALS KSISKNDKFK NSFCCTELNE ENKQSHSFSL QTPCSKGSEL
RTINKISERE KTGSPTPSNQ LNDSPTFKKL DESPVLKPEF IGHDGRESIK ELELSKVKND
QLRNFCSIEL NVNGSPETEA DVATFCTSKT DAISMTSDDS VTGSEVSPLI KACMLSSNGF
QNVGRCRERD SDDTCRQHNT SKSPFREMEP LLSPHHDKLM SLPVKTIDYP KTLIKEPVDK
RHSCCKTKDS DIYCSPNENP EAENAEPSAM TISSHSFVNV HLESKTVICD NREPTDRHSE
NTCDEYKQSI GSTSSASHNH FDGLYEPIGS SGISSLQSPP SGIRCEENTS PTLDAVESKK
GIDFLKYARK ETDVGSALPD SGKGFSWENR HNNVLSGQSL QEAQEEGNSI LHERRGRPEI
PLDEEQRGHT HISDDSEVVF PYDLNLTMED SDGITYTLKC DSSGNAPEIV STVHEDYSGS
SASSSDESDS EDTESDDSSI PRNRLQSVVV VPKNSTLPME ETSPCSSRSS QSYKHYSDRW
EDGLETRRHA YEEEYESKGC SQTEKYFLHK GTERSAESCY SQFGRKADNH LPDIAHAQSD
GVDSTSQTDS RSDHLGHLNP EDTLRAKTSR PQELPVYSDD FEDLPNKSRQ QMIFSNRPDS
SRLGKTELSF SSSCDISRMD GLHSSEELRN LGWDFSQQER PTTTYQQPDS SYGTCGTHKY
QQSTEHYGGT HNYWQGNGYW DPRSAGRPPG TGLAYDRIQG QVPDSLTDDR EEEEHWDQRS
GSHFSSPSNK FFFHQKDKGS VQAPEISSNS IKDALVMNER KDFSKNFEKN DIKERGPPKK
RRQELESDSE SDGELQARKK VRVEMEQGES SVPQHSELMG PSCAMDDFRD PQRWKEFAKL
GKMPCYFDLI EENVYLTERK KNKSHRDIKR MQCECTPLSK DERAQGEVAC GEDCLNRLLM
IECSSRCPNG DYCSNRRFQR KQHADVEVIL TEKKGWGLRA AKDLPSNTFV LEYCGEVLDH
KEFKARVKEY ARNKNIHYYF MALKNDEIID ATQKGNCSRF MNHSCEPNCE TQKWTVNGQL
RVGFFTTKLV PSGSELTFDY QFQRYGKEAQ KCFCGSANCR GYLGGENRVS IRAAGGKMKK
ERSRKKDSVD GELEALMENG EGLSDKNQVL SLSRLMVRIE TLEQKLTCLK LIQNTHSQSC
LKSFLERHGL SLLWIWMAEL GDGRESNQKL QEEIIKTLEH LPIPTKNMLE ESKVLPIIQR
WSQTKTAVPQ LSEGDGYSSE NTSRAHTPLN TPDPSAKPST EMDTDTPKKL IFRRLKIISE
NSMDSAVSDV TSELECKDGK EDLDQLETVT VEEDEELQSQ QLLPQQLCES KVESEATIEV
SKLPTSEPEA DTETEPKDSN GTKLEETIAE ETPSQDEEEG VSDVESERSQ EPPDKTVDIS
DLATKLLDSW KDLKEVYRIP KKSQTEKEST VAERGRDAAA FRDQTAPKTP NRSRERDPDK
QSQNKEKRKR RGSLSPPSSA YERGTKRPDD RYDTPTSKKK VRIKDRNKLS TEERRKLFEQ
EVAQREAQKQ QQQMQNLGMT SPLPFDSLGY NASHHPFAGY PPGYPMQAYV DPSNPNAGKV
LLPTPSMDPV CSPAPYDHAQ PLVGHSTESL AAPPSVPVVP HVAASVEVSS SQYVAQNESV
VHQDSNVPVM PVQAPGPVQG QNYNVWESNQ QSVSVQQQYS PAQSQTTIYY QGQTCSTVYS
VTSPYSQTTP PIVQSYAQPS LQYIQGQQIF TAHPQGVVVQ PTAAVTSIVA PGQPQSLQPP
EMVVTNNLLD LPPPSPPKPK TIVLPPNWKT ARDPEGKIYY YHVITRQTQW DPPTWESPGD
DASLEHEAEM DLGTPTYDEN PMKTSKKPKT AEADTSSELA KKSKEVFRKE MSQFIVQCLN
PYRKPDCKVG RITTTEDFKH LARKLTHGVM NKELKYCKNP EDLECNENVK HKTKEYIKKY
MQKFGAVYKP KEDTELE


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