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Database: UniProt/SWISS-PROT
Entry: SETD2_MOUSE
LinkDB: SETD2_MOUSE
Original site: SETD2_MOUSE 
ID   SETD2_MOUSE             Reviewed;        2537 AA.
AC   E9Q5F9; Q69ZC0; Q6PCY9; Q8K0F3;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   12-SEP-2018, entry version 63.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD2 {ECO:0000305};
DE            EC=2.1.1.43 {ECO:0000269|PubMed:18157086};
DE   AltName: Full=Lysine N-methyltransferase 3A {ECO:0000250|UniProtKB:Q9BYW2};
DE   AltName: Full=Protein-lysine N-methyltransferase SETD2 {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000269|PubMed:27518565};
DE   AltName: Full=SET domain-containing protein 2 {ECO:0000303|PubMed:18157086};
GN   Name=Setd2 {ECO:0000303|PubMed:18157086, ECO:0000312|MGI:MGI:1918177};
GN   Synonyms=Kiaa1732 {ECO:0000303|PubMed:15368895},
GN   Kmt3a {ECO:0000250|UniProtKB:Q9BYW2};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2121-2537 AND 1800-2537
RP   (ISOFORM 2).
RC   TISSUE=Mammary tumor;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1834-2537 (ISOFORM 1).
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX   PubMed=18157086; DOI=10.1038/sj.emboj.7601967;
RA   Edmunds J.W., Mahadevan L.C., Clayton A.L.;
RT   "Dynamic histone H3 methylation during gene induction: HYPB/Setd2
RT   mediates all H3K36 trimethylation.";
RL   EMBO J. 27:406-420(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1387; SER-1389 AND
RP   SER-1391, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-242; SER-322;
RP   SER-324; SER-624; SER-633; SER-697; SER-1818; SER-1819; THR-1827;
RP   SER-1954; SER-1962 AND SER-1969, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20133625; DOI=10.1073/pnas.0915033107;
RA   Hu M., Sun X.J., Zhang Y.L., Kuang Y., Hu C.Q., Wu W.L., Shen S.H.,
RA   Du T.T., Li H., He F., Xiao H.S., Wang Z.G., Liu T.X., Lu H.,
RA   Huang Q.H., Chen S.J., Chen Z.;
RT   "Histone H3 lysine 36 methyltransferase Hypb/Setd2 is required for
RT   embryonic vascular remodeling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:2956-2961(2010).
RN   [8]
RP   FUNCTION.
RX   PubMed=25242323; DOI=10.1016/j.celrep.2014.08.031;
RA   Zhang Y., Xie S., Zhou Y., Xie Y., Liu P., Sun M., Xiao H., Jin Y.,
RA   Sun X., Chen Z., Huang Q., Chen S.;
RT   "H3K36 histone methyltransferase Setd2 is required for murine
RT   embryonic stem cell differentiation toward endoderm.";
RL   Cell Rep. 8:1989-2002(2014).
RN   [9]
RP   FUNCTION AS ALPHA-TUBULIN METHYLTRANSFERASE.
RX   PubMed=27518565; DOI=10.1016/j.cell.2016.07.005;
RA   Park I.Y., Powell R.T., Tripathi D.N., Dere R., Ho T.H., Blasius T.L.,
RA   Chiang Y.C., Davis I.J., Fahey C.C., Hacker K.E., Verhey K.J.,
RA   Bedford M.T., Jonasch E., Rathmell W.K., Walker C.L.;
RT   "Dual chromatin and cytoskeletal remodeling by SETD2.";
RL   Cell 166:950-962(2016).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated
CC       'Lys-36' (H3K36me2) as substrate (PubMed:18157086,
CC       PubMed:20133625). Represents the main enzyme generating H3K36me3,
CC       a specific tag for epigenetic transcriptional activation
CC       (PubMed:18157086, PubMed:20133625). Plays a role in chromatin
CC       structure modulation during elongation by coordinating recruitment
CC       of the FACT complex and by interacting with hyperphosphorylated
CC       POLR2A (By similarity). Acts as a key regulator of DNA mismatch
CC       repair in G1 and early S phase by generating H3K36me3, a mark
CC       required to recruit MSH6 subunit of the MutS alpha complex: early
CC       recruitment of the MutS alpha complex to chromatin to be
CC       replicated allows a quick identification of mismatch DNA to
CC       initiate the mismatch repair reaction (By similarity). Required
CC       for DNA double-strand break repair in response to DNA damage: acts
CC       by mediating formation of H3K36me3, promoting recruitment of RAD51
CC       and DNA repair via homologous recombination (HR) (By similarity).
CC       Acts as a tumor suppressor (By similarity). H3K36me3 also plays an
CC       essential role in the maintenance of a heterochromatic state, by
CC       recruiting DNA methyltransferase DNMT3A (By similarity). H3K36me3
CC       is also enhanced in intron-containing genes, suggesting that SETD2
CC       recruitment is enhanced by splicing and that splicing is coupled
CC       to recruitment of elongating RNA polymerase (By similarity).
CC       Required during angiogenesis (PubMed:20133625). Required for
CC       endoderm development by promoting embryonic stem cell
CC       differentiation toward endoderm: acts by mediating formation of
CC       H3K36me3 in distal promoter regions of FGFR3, leading to regulate
CC       transcription initiation of FGFR3 (PubMed:25242323). In addition
CC       to histones, also mediates methylation of other proteins, such as
CC       tubulins and STAT1 (PubMed:27518565). Trimethylates 'Lys-40' of
CC       alpha-tubulins such as TUBA1B (alpha-TubK40me3); alpha-TubK40me3
CC       is required for normal mitosis and cytokinesis and may be a
CC       specific tag in cytoskeletal remodeling (PubMed:27518565).
CC       Involved in interferon-alpha-induced antiviral defense by
CC       mediating both monomethylation of STAT1 at 'Lys-525' and
CC       catalyzing H3K36me3 on promoters of some interferon-stimulated
CC       genes (ISGs) to activate gene transcription (By similarity).
CC       {ECO:0000250|UniProtKB:Q9BYW2, ECO:0000269|PubMed:18157086,
CC       ECO:0000269|PubMed:20133625, ECO:0000269|PubMed:25242323,
CC       ECO:0000269|PubMed:27518565}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000269|PubMed:18157086}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + [protein]-L-lysine =
CC       S-adenosyl-L-homocysteine + [protein]-N(6)-methyl-L-lysine.
CC       {ECO:0000250|UniProtKB:Q9BYW2}.
CC   -!- CATALYTIC ACTIVITY: 3 S-adenosyl-L-methionine + [protein]-L-lysine
CC       = 3 S-adenosyl-L-homocysteine + [protein]-N(6),N(6),N(6)-methyl-L-
CC       lysine. {ECO:0000269|PubMed:27518565}.
CC   -!- ACTIVITY REGULATION: Specifically inhibited by sinefungin
CC       derivatives. {ECO:0000250|UniProtKB:Q9BYW2}.
CC   -!- SUBUNIT: Specifically interacts with hyperphosphorylated C-
CC       terminal domain (CTD) of RNA polymerase II large subunit (POLR2A):
CC       binds to CTD heptad repeats doubly phosphorylated on 'Ser-2' and
CC       'Ser-5' of each heptad. Interacts with HTT. Interacts with IWS1.
CC       Interacts with p53/TP53; leading to regulate p53/TP53 target
CC       genes. Component of a complex with HNRNPL. Interacts with TUBA1A;
CC       the interaction is independent on alpha-tubulin acetylation on
CC       'Lys-40'. {ECO:0000250|UniProtKB:Q9BYW2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18157086}.
CC       Chromosome {ECO:0000269|PubMed:18157086}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=E9Q5F9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=E9Q5F9-2; Sequence=VSP_047946;
CC         Note=No experimental confirmation available.;
CC   -!- DOMAIN: The low charge region mediates the transcriptional
CC       activation activity. {ECO:0000250|UniProtKB:Q9BYW2}.
CC   -!- PTM: May be automethylated. {ECO:0000250|UniProtKB:Q9BYW2}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethality at E10.5-E11.5. Embryos
CC       show severe vascular defects in embryo, yolk sac and placenta.
CC       Capillaries are abnormally dilated in embryos and yolk sacs and
CC       cannot be remodeled into large blood vessels or intricate
CC       networks. The embryonic vessels fail to invade the labyrinthine
CC       layer of placenta, which impair the embryonic-maternal vascular
CC       connection. Defects are not caused by the extraembryonic tissues.
CC       Impaired H3K36me3, but not H3K36me2 or H3K36me1.
CC       {ECO:0000269|PubMed:20133625}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SET2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
DR   EMBL; AC132103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC031601; AAH31601.1; -; mRNA.
DR   EMBL; BC059049; AAH59049.1; -; mRNA.
DR   EMBL; AK173246; BAD32524.1; -; mRNA.
DR   CCDS; CCDS40781.2; -. [E9Q5F9-1]
DR   RefSeq; NP_001074809.2; NM_001081340.2. [E9Q5F9-1]
DR   UniGene; Mm.288949; -.
DR   ProteinModelPortal; E9Q5F9; -.
DR   SMR; E9Q5F9; -.
DR   BioGrid; 231695; 8.
DR   IntAct; E9Q5F9; 8.
DR   STRING; 10090.ENSMUSP00000116313; -.
DR   iPTMnet; E9Q5F9; -.
DR   PhosphoSitePlus; E9Q5F9; -.
DR   MaxQB; E9Q5F9; -.
DR   PaxDb; E9Q5F9; -.
DR   PeptideAtlas; E9Q5F9; -.
DR   PRIDE; E9Q5F9; -.
DR   Ensembl; ENSMUST00000153838; ENSMUSP00000116313; ENSMUSG00000044791. [E9Q5F9-1]
DR   GeneID; 235626; -.
DR   KEGG; mmu:235626; -.
DR   UCSC; uc009rug.2; mouse. [E9Q5F9-1]
DR   CTD; 29072; -.
DR   MGI; MGI:1918177; Setd2.
DR   eggNOG; KOG4442; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00780000121845; -.
DR   HOGENOM; HOG000081757; -.
DR   InParanoid; E9Q5F9; -.
DR   KO; K11423; -.
DR   OMA; FIGHDSH; -.
DR   OrthoDB; EOG091G040P; -.
DR   TreeFam; TF106477; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; Setd2; mouse.
DR   PRO; PR:E9Q5F9; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   Bgee; ENSMUSG00000044791; Expressed in 241 organ(s), highest expression level in mesenteric lymph node.
DR   ExpressionAtlas; E9Q5F9; baseline and differential.
DR   Genevisible; E9Q5F9; MM.
DR   GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IMP:UniProtKB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR   GO; GO:0035441; P:cell migration involved in vasculogenesis; IMP:MGI.
DR   GO; GO:0060977; P:coronary vasculature morphogenesis; IMP:MGI.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:MGI.
DR   GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR   GO; GO:0060669; P:embryonic placenta morphogenesis; IMP:MGI.
DR   GO; GO:0035987; P:endodermal cell differentiation; IMP:UniProtKB.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0097676; P:histone H3-K36 dimethylation; ISO:MGI.
DR   GO; GO:0010452; P:histone H3-K36 methylation; IMP:MGI.
DR   GO; GO:0097198; P:histone H3-K36 trimethylation; IMP:UniProtKB.
DR   GO; GO:0048332; P:mesoderm morphogenesis; IMP:MGI.
DR   GO; GO:1902850; P:microtubule cytoskeleton organization involved in mitosis; ISS:UniProtKB.
DR   GO; GO:0006298; P:mismatch repair; ISS:UniProtKB.
DR   GO; GO:0001763; P:morphogenesis of a branching structure; IMP:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0034728; P:nucleosome organization; ISS:UniProtKB.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; IMP:MGI.
DR   GO; GO:0060039; P:pericardium development; IMP:MGI.
DR   GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
DR   GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR   GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0010793; P:regulation of mRNA export from nucleus; ISO:MGI.
DR   GO; GO:1905634; P:regulation of protein localization to chromatin; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0034340; P:response to type I interferon; ISS:UniProtKB.
DR   GO; GO:0048864; P:stem cell development; IMP:MGI.
DR   GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 1.10.1740.100; -; 1.
DR   Gene3D; 1.20.930.10; -; 1.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR013257; SRI.
DR   InterPro; IPR038190; SRI_sf.
DR   InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF08236; SRI; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF51045; SSF51045; 1.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Antiviral defense;
KW   Chromatin regulator; Chromosome; Coiled coil; Complete proteome;
KW   Developmental protein; Differentiation; DNA damage; DNA repair;
KW   Immunity; Innate immunity; Isopeptide bond; Metal-binding;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation; Zinc.
FT   CHAIN         1   2537       Histone-lysine N-methyltransferase SETD2.
FT                                /FTId=PRO_0000423553.
FT   DOMAIN     1468   1522       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN     1524   1641       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1648   1664       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   DOMAIN     2362   2395       WW. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00224}.
FT   REGION     1392   1688       Interaction with TUBA1A.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   REGION     1534   1536       Inhibitor binding.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   REGION     1534   1536       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   REGION     1577   1579       Inhibitor binding.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   REGION     1577   1579       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   REGION     1602   1603       Inhibitor binding.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   REGION     1602   1603       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   REGION     2110   2339       Low charge region.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   REGION     2430   2537       Interaction with POLR2A.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   COILED     2090   2119       {ECO:0000255}.
FT   COMPBIAS    167    231       Pro-rich.
FT   COMPBIAS    294    439       Ser-rich.
FT   COMPBIAS    369    457       Arg-rich.
FT   COMPBIAS   2233   2338       Gln-rich.
FT   METAL      1473   1473       Zinc 1. {ECO:0000250|UniProtKB:Q9BYW2}.
FT   METAL      1475   1475       Zinc 1. {ECO:0000250|UniProtKB:Q9BYW2}.
FT   METAL      1490   1490       Zinc 1. {ECO:0000250|UniProtKB:Q9BYW2}.
FT   METAL      1490   1490       Zinc 2. {ECO:0000250|UniProtKB:Q9BYW2}.
FT   METAL      1494   1494       Zinc 1. {ECO:0000250|UniProtKB:Q9BYW2}.
FT   METAL      1503   1503       Zinc 2. {ECO:0000250|UniProtKB:Q9BYW2}.
FT   METAL      1507   1507       Zinc 2. {ECO:0000250|UniProtKB:Q9BYW2}.
FT   METAL      1513   1513       Zinc 2. {ECO:0000250|UniProtKB:Q9BYW2}.
FT   METAL      1605   1605       Zinc 3. {ECO:0000250|UniProtKB:Q9BYW2}.
FT   METAL      1652   1652       Zinc 3. {ECO:0000250|UniProtKB:Q9BYW2}.
FT   METAL      1654   1654       Zinc 3. {ECO:0000250|UniProtKB:Q9BYW2}.
FT   METAL      1659   1659       Zinc 3. {ECO:0000250|UniProtKB:Q9BYW2}.
FT   BINDING    1599   1599       Inhibitor.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   BINDING    1650   1650       Inhibitor; alternate.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   BINDING    1650   1650       S-adenosyl-L-methionine; alternate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING    1653   1653       Inhibitor; via amide nitrogen; alternate.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   BINDING    1653   1653       S-adenosyl-L-methionine; via amide
FT                                nitrogen; alternate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   MOD_RES     132    132       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     242    242       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     322    322       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     324    324       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     345    345       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES     423    423       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES     532    532       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES     614    614       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES     624    624       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     626    626       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES     633    633       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     697    697       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     707    707       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES     743    743       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES     753    753       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES    1077   1077       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES    1201   1201       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES    1387   1387       Phosphoserine.
FT                                {ECO:0000244|PubMed:19144319}.
FT   MOD_RES    1389   1389       Phosphoserine.
FT                                {ECO:0000244|PubMed:19144319}.
FT   MOD_RES    1391   1391       Phosphoserine.
FT                                {ECO:0000244|PubMed:19144319}.
FT   MOD_RES    1670   1670       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES    1818   1818       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1819   1819       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1827   1827       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1846   1846       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES    1862   1862       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES    1926   1926       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES    1954   1954       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1962   1962       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1969   1969       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2053   2053       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   MOD_RES    2055   2055       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   CROSSLNK    360    360       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   CROSSLNK    637    637       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   CROSSLNK    775    775       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9BYW2}.
FT   VAR_SEQ    2011   2011       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_047946.
SQ   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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