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   27-MAR-2024, entry version 156.
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 (By similarity). Interacts (via KIKL
CC       motif) with BRD3 (via NET domain) (By similarity).
CC       {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   -!- DOMAIN: The KIKL motif recognizes and binds the NET domain of BRD3.
CC       {ECO:0000250|UniProtKB:Q9BZ95}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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.ENSMUSP00000117778; -.
DR   iPTMnet; Q6P2L6; -.
DR   PhosphoSitePlus; Q6P2L6; -.
DR   EPD; Q6P2L6; -.
DR   jPOST; Q6P2L6; -.
DR   MaxQB; Q6P2L6; -.
DR   PaxDb; 10090-ENSMUSP00000115470; -.
DR   PeptideAtlas; Q6P2L6; -.
DR   ProteomicsDB; 293980; -. [Q6P2L6-1]
DR   ProteomicsDB; 293981; -. [Q6P2L6-2]
DR   ProteomicsDB; 293982; -. [Q6P2L6-3]
DR   ProteomicsDB; 293983; -. [Q6P2L6-4]
DR   Pumba; Q6P2L6; -.
DR   ABCD; Q6P2L6; 1 sequenced antibody.
DR   Antibodypedia; 984; 419 antibodies from 35 providers.
DR   DNASU; 234135; -.
DR   Ensembl; ENSMUST00000136107.9; ENSMUSP00000147840.2; ENSMUSG00000054823.18. [Q6P2L6-4]
DR   Ensembl; ENSMUST00000146919.8; ENSMUSP00000115470.2; ENSMUSG00000054823.18. [Q6P2L6-2]
DR   Ensembl; ENSMUST00000153597.3; ENSMUSP00000123028.3; ENSMUSG00000054823.18. [Q6P2L6-3]
DR   Ensembl; ENSMUST00000155861.8; ENSMUSP00000117596.2; ENSMUSG00000054823.18. [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   AGR; MGI:2142581; -.
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; 13 hits in 84 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 225 other cell types or tissues.
DR   ExpressionAtlas; Q6P2L6; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0140952; F:histone H3K27 dimethyltransferase activity; ISO:MGI.
DR   GO; GO:0046976; F:histone H3K27 methyltransferase activity; IDA:MGI.
DR   GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; ISO:MGI.
DR   GO; GO:0046975; F:histone H3K36 methyltransferase activity; ISO:MGI.
DR   GO; GO:0140946; F:histone H3K4 dimethyltransferase activity; ISO:MGI.
DR   GO; GO:0042800; F:histone H3K4 methyltransferase activity; IDA: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:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd15652; PHD2_NSD3; 1.
DR   CDD; cd15658; PHD4_NSD3; 1.
DR   CDD; cd15661; PHD5_NSD3; 1.
DR   CDD; cd20163; PWWP_NSD3_rpt1; 1.
DR   CDD; cd20166; PWWP_NSD3_rpt2; 1.
DR   CDD; cd19212; SET_NSD3; 1.
DR   Gene3D; 2.30.30.140; -; 2.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 4.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR041306; C5HCH.
DR   InterPro; IPR047456; PHD2_NSD3.
DR   InterPro; IPR047458; PHD4_NSD3.
DR   InterPro; IPR047527; PHD5_NSD3.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR000313; PWWP_dom.
DR   InterPro; IPR047451; PWWP_NSD3_rpt1.
DR   InterPro; IPR047453; PWWP_NSD3_rpt2.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR047461; SET_NSD3.
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   PANTHER; PTHR22884:SF473; HISTONE-LYSINE N-METHYLTRANSFERASE NSD3; 1.
DR   PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
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; FYVE/PHD zinc finger; 3.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
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.
DR   Genevisible; Q6P2L6; MM.
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   MOTIF           154..157
FT                   /note="KIKL"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZ95"
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
//