NSD3_MOUSE
ID NSD3_MOUSE Reviewed; 1439 AA.
AC Q6P2L6; Q3TDS4; Q3U0L8; Q3V131; Q8BJT3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Histone-lysine N-methyltransferase NSD3;
DE EC=2.1.1.370 {ECO:0000250|UniProtKB:Q9BZ95};
DE EC=2.1.1.371 {ECO:0000250|UniProtKB:Q9BZ95};
DE AltName: Full=Nuclear SET domain-containing protein 3;
DE AltName: Full=Wolf-Hirschhorn syndrome candidate 1-like protein 1 homolog;
DE Short=WHSC1-like protein 1;
GN Name=Nsd3; Synonyms=Whsc1l1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, Spleen, Testis, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 899-914, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, 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 expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-790, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Histone methyltransferase. Preferentially dimethylates 'Lys-
CC 4' and 'Lys-27' of histone H3 forming H3K2me2 and H3K27me2. H3 'Lys-4'
CC methylation represents a specific tag for epigenetic transcriptional
CC activation, while 'Lys-27' is a mark for transcriptional repression.
CC {ECO:0000250|UniProtKB:Q9BZ95}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:64448, Rhea:RHEA-COMP:15540, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61976; EC=2.1.1.370;
CC Evidence={ECO:0000250|UniProtKB:Q9BZ95};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(27)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+)
CC + N(6),N(6)-dimethyl-L-lysyl(27)-[histone H3] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:64452, Rhea:RHEA-COMP:15539, Rhea:RHEA-
CC COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61976; EC=2.1.1.371;
CC Evidence={ECO:0000250|UniProtKB:Q9BZ95};
CC -!- SUBUNIT: Interacts with BRD4. {ECO:0000250|UniProtKB:Q9BZ95}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6P2L6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P2L6-2; Sequence=VSP_021432, VSP_021435, VSP_021436;
CC Name=3;
CC IsoId=Q6P2L6-3; Sequence=VSP_021431, VSP_021437, VSP_021438;
CC Name=4;
CC IsoId=Q6P2L6-4; Sequence=VSP_021432, VSP_021433, VSP_021434;
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AK079952; BAC37792.1; -; mRNA.
DR EMBL; AK132725; BAE21322.1; -; mRNA.
DR EMBL; AK156746; BAE33834.1; -; mRNA.
DR EMBL; AK170040; BAE41526.1; -; mRNA.
DR EMBL; AC156990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064447; AAH64447.1; -; mRNA.
DR CCDS; CCDS40305.1; -. [Q6P2L6-2]
DR CCDS; CCDS85518.1; -. [Q6P2L6-4]
DR RefSeq; NP_001001735.1; NM_001001735.2. [Q6P2L6-2]
DR RefSeq; NP_001295410.1; NM_001308481.1. [Q6P2L6-2]
DR RefSeq; NP_001295411.1; NM_001308482.1. [Q6P2L6-4]
DR AlphaFoldDB; Q6P2L6; -.
DR SMR; Q6P2L6; -.
DR BioGRID; 231497; 1.
DR STRING; 10090.ENSMUSP00000115470; -.
DR iPTMnet; Q6P2L6; -.
DR PhosphoSitePlus; Q6P2L6; -.
DR EPD; Q6P2L6; -.
DR jPOST; Q6P2L6; -.
DR MaxQB; Q6P2L6; -.
DR PaxDb; Q6P2L6; -.
DR PeptideAtlas; Q6P2L6; -.
DR PRIDE; Q6P2L6; -.
DR ProteomicsDB; 293980; -. [Q6P2L6-1]
DR ProteomicsDB; 293981; -. [Q6P2L6-2]
DR ProteomicsDB; 293982; -. [Q6P2L6-3]
DR ProteomicsDB; 293983; -. [Q6P2L6-4]
DR ABCD; Q6P2L6; 1 sequenced antibody.
DR Antibodypedia; 984; 367 antibodies from 35 providers.
DR DNASU; 234135; -.
DR Ensembl; ENSMUST00000136107; ENSMUSP00000147840; ENSMUSG00000054823. [Q6P2L6-4]
DR Ensembl; ENSMUST00000146919; ENSMUSP00000115470; ENSMUSG00000054823. [Q6P2L6-2]
DR Ensembl; ENSMUST00000153597; ENSMUSP00000123028; ENSMUSG00000054823. [Q6P2L6-3]
DR Ensembl; ENSMUST00000155861; ENSMUSP00000117596; ENSMUSG00000054823. [Q6P2L6-2]
DR GeneID; 234135; -.
DR KEGG; mmu:234135; -.
DR UCSC; uc009lgk.1; mouse. [Q6P2L6-4]
DR UCSC; uc009lgm.1; mouse. [Q6P2L6-2]
DR UCSC; uc009lgp.1; mouse. [Q6P2L6-3]
DR CTD; 54904; -.
DR MGI; MGI:2142581; Nsd3.
DR VEuPathDB; HostDB:ENSMUSG00000054823; -.
DR eggNOG; KOG1081; Eukaryota.
DR GeneTree; ENSGT00940000155355; -.
DR HOGENOM; CLU_488831_0_0_1; -.
DR InParanoid; Q6P2L6; -.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR BioGRID-ORCS; 234135; 11 hits in 78 CRISPR screens.
DR ChiTaRS; Whsc1l1; mouse.
DR PRO; PR:Q6P2L6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6P2L6; protein.
DR Bgee; ENSMUSG00000054823; Expressed in manus and 222 other tissues.
DR ExpressionAtlas; Q6P2L6; baseline and differential.
DR Genevisible; Q6P2L6; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IDA:MGI.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IBA:GO_Central.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:MGI.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140537; F:transcription regulator activator activity; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016571; P:histone methylation; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:2001255; P:positive regulation of histone H3-K36 trimethylation; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 4.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR041306; C5HCH.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF17982; C5HCH; 1.
DR Pfam; PF00855; PWWP; 2.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00249; PHD; 5.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00293; PWWP; 2.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; SSF57903; 3.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50812; PWWP; 2.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromatin regulator; Chromosome;
KW Coiled coil; Direct protein sequencing; Isopeptide bond; Metal-binding;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1439
FT /note="Histone-lysine N-methyltransferase NSD3"
FT /id="PRO_0000259522"
FT DOMAIN 270..333
FT /note="PWWP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT DOMAIN 960..1025
FT /note="PWWP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT DOMAIN 1096..1146
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 1148..1265
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1272..1288
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT ZN_FING 701..748
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 749..805
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 862..955
FT /note="PHD-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1323..1370
FT /note="PHD-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 121..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1036..1065
FT /evidence="ECO:0000255"
FT COMPBIAS 124..142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ95"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ95"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ95"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ95"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ95"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ95"
FT MOD_RES 790
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 218
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ95"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ95"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ95"
FT CROSSLNK 502
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ95"
FT CROSSLNK 532
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ95"
FT CROSSLNK 628
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ95"
FT CROSSLNK 1154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ95"
FT VAR_SEQ 1..941
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021431"
FT VAR_SEQ 135
FT /note="P -> PLPPPPPPPPP (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021432"
FT VAR_SEQ 603..611
FT /note="QVETAPQAS -> QVGFLHVES (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021433"
FT VAR_SEQ 612..1439
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021434"
FT VAR_SEQ 620..645
FT /note="ASEISDSCKPLKKRSRASTDVETASC -> SADRGAQGSVRFSDSSVSAAKE
FT ETVD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021435"
FT VAR_SEQ 646..1439
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021436"
FT VAR_SEQ 973..975
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021437"
FT VAR_SEQ 1199..1209
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021438"
FT CONFLICT 122
FT /note="H -> R (in Ref. 1; BAE33834)"
FT /evidence="ECO:0000305"
FT CONFLICT 950
FT /note="N -> K (in Ref. 1; BAE21322)"
FT /evidence="ECO:0000305"
FT CONFLICT 1149
FT /note="D -> N (in Ref. 1; BAE21322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1439 AA; 161002 MW; 917C7ADCD1248525 CRC64;
MDFSFSFMQG IMGNTIQQPP QLIDSANIRQ EDAFDNHSDI VEDGGPTPFE ATLQQGFQYP
PTTEDLPPLT NGYPPSISLY ETQTKYPPYN QYPNGSANGF GAVRNFSPTD YYHSEIPNTR
PHEILEKPSP PQPPPPPSVP QTVIPKKTGS PEIKLKITKT IQNGRELFES SLCGDLLNEV
QASEHTKSKH ESRKEKRKKS NRHESSRSEE RRSHKIPKLE PEGQNRPNER VDTAPEKPRE
EPVLKEAIPV QPILSSVPTT ETSTGVKFQV GDLVWSKVGT YPWWPCMVSS DPQLEVHSKI
NTRGAREYHV QFFSNQPERA WVHEKRVREY KGHEQYEELL AEAAKQASNH SEKQKIRKPR
PQRERAQWDI GIAHAEKALK MTREERVEQY TFIYIDKQPE EASSQAKKNV TSKTEVKKPR
RPRSVLNSQP EQTNAGEVAS SQSSTDLRRQ SQRRHTSLEE EEPPPVKIAW KTAAARKSLP
ASITMHKGSL DLQKCNMSPV VKIEQVFALQ NATGDGKFID QFVYSTKGIG NKTEISVRGQ
DRLIISSPSQ RSEKPAQSAS SPEATSGSAG PVEKKQQRRS IRTRSESEKS AEVVPKKKIK
KEQVETAPQA SLKTGLQKGA SEISDSCKPL KKRSRASTDV ETASCTYRDT SDSDSRGLSD
GQVGFGKQVD SPSATADADA SDAQSVDSSL SRRGVGTSKK DTVCQVCEKA GDCLVACEGE
CCRHFHVECL GLTAVPEGHF TCEECETGQH PCFSCKVSGK DVKRCSVSVC GKFYHEACVR
KFPTAIFESK GFRCPQHCCS SCSMEKDIHK ASKGRMMRCL RCPVAYHVGD ACVAAGSVSV
SSHILICSNH SKRSSQSAAI NVGFCFVCAR GLIVQDHSDP MFSSYAYKSH YLLSESNRAE
LMKLPMIPSS SASKKRCEKG GRLLCCESCP ASFHPECLSI DMPEGCWNCN DCKAGKKLHY
KQIVWVKLGN YRQVLWWPAE ICSPRSVPLN IQGLKHDLGD FPVFFFGSHD YYWVHQGRVF
PYVEGDKHFA EGQTSINKTF KKALEEAAKR FQELKAQRES KEALEMERTS RKPPPYKHIK
ANKVIGKVQV QVADLSEIPR CNCKPGDENP CGLESQCLNR MSQYECHPQV CPAGDRCQNQ
CFTKRLYPDA EVIKTERRGW GLRTKRSIKK GEFVNEYVGE LIDEEECRLR IKRAHENSVT
NFYMLTVTKD RIIDAGPKGN YSRFMNHSCN PNCETQKWTV NGDVRVGLFA LCDIPAGMEL
TFNYNLDCLG NGRTVCHCGA DNCSGFLGVR PKSACTSAVD EKTKNAKLKK RRKVKAEAKP
IHEDYCFQCG DGGELVMCDK KDCPKAYHLL CLNLTQPPHG KWECPWHRCD ECGSVAVSFC
EFCPHSFCKA HGKGALVPSA LEGRLCCSSH DPASPVSPEY WSKIRCKWES QDSGEEVKE
