ID   EZH1_MOUSE              Reviewed;         747 AA.
AC   P70351; A2A4K5; Q3TPR1; Q3U3V5; Q3UU02; Q8BR85; Q922L1; Q9R089;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   04-NOV-2026, entry version 187.
DE   RecName: Full=Histone-lysine N-methyltransferase EZH1;
DE            EC=2.1.1.356 {ECO:0000269|PubMed:19026780};
DE   AltName: Full=ENX-2;
DE   AltName: Full=Enhancer of zeste homolog 1;
GN   Name=Ezh1; Synonyms=Enx2;
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 [MRNA] (ISOFORM 1).
RX   PubMed=9214638; DOI=10.1093/emboj/16.11.3219;
RA   Laible G., Wolf A., Dorn R., Reuter G., Nislow C., Lebersorger A.,
RA   Popkin D., Pillus L., Jenuwein T.;
RT   "Mammalian homologues of the Polycomb-group gene Enhancer of zeste mediate
RT   gene silencing in Drosophila heterochromatin and at S. cerevisiae
RT   telomeres.";
RL   EMBO J. 16:3219-3232(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=9473645; DOI=10.1016/s0167-4781(97)00156-5;
RA   Ogawa M., Hiraoka Y., Taniguchi K., Aiso S.;
RT   "Cloning and expression of a human/mouse Polycomb group gene, ENX-
RT   2/Enx-2.";
RL   Biochim. Biophys. Acta 1395:151-158(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=10051331; DOI=10.1007/s003359900993;
RA   Laible G., Haynes A.R., Lebersorger A., O'Carroll D., Mattei M.-G.,
RA   Denny P., Brown S.D.M., Jenuwein T.;
RT   "The murine polycomb-group genes ezh1 and ezh2 map close to hox gene
RT   clusters on mouse chromosomes 11 and 6.";
RL   Mamm. Genome 10:311-314(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=ILS, and ISS;
RX   PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants within
RT   alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Aorta, Cerebellum, Corpora quadrigemina, Hippocampus, 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   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; 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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
RX   PubMed=19026780; DOI=10.1016/j.molcel.2008.10.016;
RA   Shen X., Liu Y., Hsu Y.-J., Fujiwara Y., Kim J., Mao X., Yuan G.-C.,
RA   Orkin S.H.;
RT   "EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in
RT   maintaining stem cell identity and executing pluripotency.";
RL   Mol. Cell 32:491-502(2008).
RN   [10]
RP   IDENTIFICATION IN THE PRC2 COMPLEX.
RX   PubMed=20144788; DOI=10.1016/j.stem.2009.12.014;
RA   Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K., Torchia J.,
RA   Krogan N.J., Reiter J.F., Stanford W.L.;
RT   "Polycomb-like 2 associates with PRC2 and regulates transcriptional
RT   networks during mouse embryonic stem cell self-renewal and
RT   differentiation.";
RL   Cell Stem Cell 6:153-166(2010).
RN   [11]
RP   INTERACTION WITH EZHIP.
RX   PubMed=31451685; DOI=10.1038/s41467-019-11800-x;
RA   Ragazzini R., Perez-Palacios R., Baymaz I.H., Diop S., Ancelin K.,
RA   Zielinski D., Michaud A., Givelet M., Borsos M., Aflaki S., Legoix P.,
RA   Jansen P.W.T.C., Servant N., Torres-Padilla M.E., Bourc'his D., Fouchet P.,
RA   Vermeulen M., Margueron R.;
RT   "EZHIP constrains Polycomb Repressive Complex 2 activity in germ cells.";
RL   Nat. Commun. 10:3858-3858(2019).
CC   -!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the
CC       PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading
CC       to transcriptional repression of the affected target gene. Able to
CC       mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1,
CC       H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell
CC       derivation and self-renewal, suggesting that it is involved in
CC       safeguarding embryonic stem cell identity. Compared to EZH2-containing
CC       complexes, it is less abundant in embryonic stem cells, has weak
CC       methyltransferase activity and plays a less critical role in forming
CC       H3K27me3, which is required for embryonic stem cell identity and proper
CC       differentiation. {ECO:0000269|PubMed:19026780}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine =
CC         N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine + 3 H(+); Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535,
CC         Rhea:RHEA-COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
CC         EC=2.1.1.356; Evidence={ECO:0000269|PubMed:19026780};
CC   -!- SUBUNIT: Component of the PRC2/EED-EZH1 complex, which includes EED,
CC       EZH1, SUZ12, RBBP4 and AEBP2. The PRC2/EED-EZH1 is less abundant than
CC       the PRC2/EED-EZH2 complex, has weak methyltransferase activity and
CC       compacts chromatin in the absence of the methyltransferase cofactor S-
CC       adenosyl-L-methionine (SAM). Interacts with EZHIP; the interaction
CC       blocks EZH1 methyltransferase activity (PubMed:31451685).
CC       {ECO:0000269|PubMed:19026780, ECO:0000269|PubMed:20144788,
CC       ECO:0000269|PubMed:31451685}.
CC   -!- INTERACTION:
CC       P70351; Q62315: Jarid2; NbExp=4; IntAct=EBI-2531737, EBI-493592;
CC       P70351; Q02395: Mtf2; NbExp=3; IntAct=EBI-2531737, EBI-2531578;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with
CC       trimethylated 'Lys-27' of histone H3. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P70351-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P70351-2; Sequence=VSP_036388;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in kidney, adrenal gland,
CC       testis and brain. {ECO:0000269|PubMed:9473645}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. Histone-lysine methyltransferase family. EZ subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH07135.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAL90764.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAL90765.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA25018.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE23827.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE24446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE32680.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE37674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=EDL03899.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U60453; AAC53279.1; -; mRNA.
DR   EMBL; AB004817; BAA25018.1; ALT_INIT; mRNA.
DR   EMBL; AF104360; AAD54021.1; -; Genomic_DNA.
DR   EMBL; AF483490; AAL90764.1; ALT_INIT; mRNA.
DR   EMBL; AF483491; AAL90765.1; ALT_INIT; mRNA.
DR   EMBL; AK045374; BAC32334.1; -; mRNA.
DR   EMBL; AK138942; BAE23827.1; ALT_INIT; mRNA.
DR   EMBL; AK140694; BAE24446.1; ALT_INIT; mRNA.
DR   EMBL; AK154565; BAE32680.1; ALT_INIT; mRNA.
DR   EMBL; AK164192; BAE37674.1; ALT_INIT; mRNA.
DR   EMBL; AL590969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466677; EDL03899.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC007135; AAH07135.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001390738.1; NM_001403809.1. [P70351-1]
DR   RefSeq; NP_001390744.1; NM_001403815.1. [P70351-2]
DR   RefSeq; NP_031996.1; NM_007970.4.
DR   AlphaFoldDB; P70351; -.
DR   SMR; P70351; -.
DR   BioGRID; 199563; 19.
DR   DIP; DIP-56992N; -.
DR   FunCoup; P70351; 3044.
DR   IntAct; P70351; 8.
DR   STRING; 10090.ENSMUSP00000102906; -.
DR   ChEMBL; CHEMBL6066858; -.
DR   GlyGen; P70351; 1 site, 1 N-linked glycan (1 site).
DR   iPTMnet; P70351; -.
DR   PhosphoSitePlus; P70351; -.
DR   jPOST; P70351; -.
DR   PaxDb; 10090-ENSMUSP00000102906; -.
DR   PeptideAtlas; P70351; -.
DR   ProteomicsDB; 275809; -. [P70351-1]
DR   ProteomicsDB; 275810; -. [P70351-2]
DR   Antibodypedia; 1432; 446 antibodies from 40 providers.
DR   DNASU; 14055; -.
DR   Ensembl; ENSMPUT00000010229; ENSMPUP00000010067; ENSMPUG00000010144.
DR   Ensembl; ENSMUST00000100417.3; ENSMUSP00000097984.3; ENSMUSG00000006920.15. [P70351-2]
DR   Ensembl; ENSMUST00000107284.8; ENSMUSP00000102905.2; ENSMUSG00000006920.15. [P70351-1]
DR   GeneID; 14055; -.
DR   KEGG; mmu:14055; -.
DR   UCSC; uc007lnw.3; mouse. [P70351-2]
DR   UCSC; uc011yfk.2; mouse. [P70351-1]
DR   AGR; MGI:1097695; -.
DR   CTD; 2145; -.
DR   MGI; MGI:1097695; Ezh1.
DR   VEuPathDB; HostDB:ENSMUSG00000006920; -.
DR   eggNOG; KOG1079; Eukaryota.
DR   GeneTree; ENSGT00940000156604; -.
DR   HOGENOM; CLU_011342_0_0_1; -.
DR   InParanoid; P70351; -.
DR   OrthoDB; 6141102at2759; -.
DR   PhylomeDB; P70351; -.
DR   Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
DR   BioGRID-ORCS; 14055; 2 hits in 82 CRISPR screens.
DR   PRO; PR:P70351; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P70351; protein.
DR   Bgee; ENSMUSG00000006920; Expressed in ciliary body and 253 other cell types or tissues.
DR   ExpressionAtlas; P70351; baseline and differential.
DR   GO; GO:0000781; C:chromosome, telomeric region; IGI:ARUK-UCL.
DR   GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR   GO; GO:0000792; C:heterochromatin; IDA:ARUK-UCL.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; ISO:GO_Central.
DR   GO; GO:0046976; F:histone H3K27 methyltransferase activity; IDA:MGI.
DR   GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; ISO:GO_Central.
DR   GO; GO:0140693; F:molecular condensate scaffold activity; ISO:GO_Central.
DR   GO; GO:0031491; F:nucleosome binding; ISO:GO_Central.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISO:GO_Central.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:ARUK-UCL.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:ARUK-UCL.
DR   GO; GO:0140718; P:facultative heterochromatin formation; IDA:GO_Central.
DR   GO; GO:0036333; P:hepatocyte homeostasis; IGI:MGI.
DR   GO; GO:0031507; P:heterochromatin formation; IDA:ARUK-UCL.
DR   GO; GO:0097421; P:liver regeneration; IGI:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:GO_Central.
DR   GO; GO:1904772; P:response to tetrachloromethane; IGI:MGI.
DR   GO; GO:0031509; P:subtelomeric heterochromatin formation; IGI:ARUK-UCL.
DR   CDD; cd00167; SANT; 1.
DR   CDD; cd19217; SET_EZH1; 1.
DR   FunFam; 2.170.270.10:FF:000001; Putative histone-lysine N-methyltransferase EZH2; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR026489; CXC_dom.
DR   InterPro; IPR045318; EZH1/2-like.
DR   InterPro; IPR048358; EZH1/2_MCSS.
DR   InterPro; IPR021654; EZH1/EZH2_N.
DR   InterPro; IPR044438; EZH1_SET.
DR   InterPro; IPR041343; PRC2_HTH_1.
DR   InterPro; IPR041355; Pre-SET_CXC.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR   PANTHER; PTHR45747; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1.
DR   PANTHER; PTHR45747:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE EZH1; 1.
DR   Pfam; PF21358; Ezh2_MCSS; 1.
DR   Pfam; PF11616; EZH2_WD-Binding; 1.
DR   Pfam; PF18118; PRC2_HTH_1; 1.
DR   Pfam; PF18264; preSET_CXC; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM01114; CXC; 1.
DR   SMART; SM00717; SANT; 2.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51633; CXC; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Isopeptide bond;
KW   Methyltransferase; Nucleus; Reference proteome; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation.
FT   CHAIN           1..747
FT                   /note="Histone-lysine N-methyltransferase EZH1"
FT                   /id="PRO_0000213991"
FT   DOMAIN          504..606
FT                   /note="CXC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00970"
FT   DOMAIN          613..728
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   REGION          188..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           491..496
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        194..211
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..381
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        327
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q92800"
FT   VAR_SEQ         555..747
FT                   /note="QNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVVSCKNCS
FT                   IQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSS
FT                   FLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQAGEELF
FT                   FDYRYSQADALKYVGIERETDVF -> KSTLLSPSSTQVVGLGVPRLFSPAP (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_036388"
FT   CONFLICT        84
FT                   /note="T -> A (in Ref. 5; BAE32680)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        446
FT                   /note="H -> Y (in Ref. 2; AAD54021)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        452
FT                   /note="N -> Y (in Ref. 2; AAD54021)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   747 AA;  85188 MW;  43CECFBDF3E49192 CRC64;
     MDIASPPTSK CITYWKRKVK SEYMRLRQLK RLQANMGAKA LYVANFAKVQ EKTQILNEEW
     KKLRVQPVQP MKPVSGHPFL KKCTIESIFP GFDSQDMLMR SLNTVALVPI MYSWSPLQQN
     FMVEDETVLC NIPYMGDEVK EEDETFIEEL INNYDGKVHG EEEMIPGSVL ISDAVFLELV
     DALNQYSDEE EDGHNDPSDG KQDDSKEDLP VTRKRKRHAI EGNKKSSKKQ FPNDMIFSAI
     ASMFPENGVP DDMKERYREL TEMSDPNALP PQCTPNIDGP NAKSVQREQS LHSFHTLFCR
     RCFKYDCFLH PFHATPNVYK RKNKEIKIEP EPCGTDCFLL LEGAKEYAML HNPRSKCSGR
     RRRRHPVVSA SCSNASASAM AETKEGDSDR DTGNDWASSS SEANSRCQTP TKQKASPAPA
     QLCVVEAPSE PVEWTGAEES LFRVFHGTYF NNFCSIARLL GTKTCKQVFQ FAVKESLILK
     LPTDELMNPA QKKKRKHRLW AAHCRKIQLK KDNNSTQVYN YQPCDHPDRP CDSTCPCIMT
     QNFCEKFCQC SPDCQNRFPG CRCKTQCNTK QCPCYLAVRE CDPDLCLTCG ASEHWDCKVV
     SCKNCSIQRG LKKHLLLAPS DVAGWGTFIK ESVQKNEFIS EYCGELISQD EADRRGKVYD
     KYMSSFLFNL NNDFVVDATR KGNKIRFANH SVNPNCYAKV VMVNGDHRIG IFAKRAIQAG
     EELFFDYRYS QADALKYVGI ERETDVF
//