HDGR2_MOUSE
ID HDGR2_MOUSE Reviewed; 669 AA.
AC Q3UMU9; D6CHX5; O35540; Q3UIH6; Q99L92;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Hepatoma-derived growth factor-related protein 2;
DE Short=HRP-2;
GN Name=Hdgfl2; Synonyms=Hdgfrp2;
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).
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=9299445; DOI=10.1006/bbrc.1997.7233;
RA Izumoto Y., Kuroda T., Harada H., Kishimoto T., Nakamura H.;
RT "Hepatoma-derived growth factor belongs to a gene family in mice showing
RT significant homology in the amino terminus.";
RL Biochem. Biophys. Res. Commun. 238:26-32(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING, FUNCTION
RP (ISOFORMS 1; 3 AND 4), INTERACTION WITH HDGF (ISOFORMS 1; 3 AND 4),
RP SUBCELLULAR LOCATION (ISOFORMS 1; 3 AND 4), AND TISSUE SPECIFICITY (ISOFORM
RP 4).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=22212508; DOI=10.1111/j.1742-4658.2011.08464.x;
RA Thakar K., Votteler I., Kelkar D., Shidore T., Gupta S., Kelm S., Dietz F.;
RT "Interaction of HRP-2 isoforms with HDGF: chromatin binding of a specific
RT heteromer.";
RL FEBS J. 279:737-751(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Heart, Lung, and Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 AND SER-367, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 AND SER-367, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Teratocarcinoma;
RX PubMed=17622165; DOI=10.1021/pr070122r;
RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT cells.";
RL J. Proteome Res. 6:3174-3186(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366; SER-450 AND SER-635, AND
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 AND SER-367, AND
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 AND SER-367, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366; SER-450; SER-620;
RP SER-628; SER-629; SER-635; SER-640; SER-659; SER-661 AND SER-669,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567 (ISOFORM 4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [11]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH DPF3 AND SMARCA4, AND
RP MUTAGENESIS OF 523-ARG--ARG-524.
RX PubMed=32459350; DOI=10.1093/nar/gkaa441;
RA Zhu X., Lan B., Yi X., He C., Dang L., Zhou X., Lu Y., Sun Y., Liu Z.,
RA Bai X., Zhang K., Li B., Li M.J., Chen Y., Zhang L.;
RT "HRP2-DPF3a-BAF complex coordinates histone modification and chromatin
RT remodeling to regulate myogenic gene transcription.";
RL Nucleic Acids Res. 48:6563-6582(2020).
CC -!- FUNCTION: Acts as an epigenetic regulator of myogenesis in cooperation
CC with DPF3a (isoform 2 of DPF3/BAF45C) (PubMed:32459350). Associates
CC with the BAF complex via its interaction with DPF3a and HDGFL2-DPF3a
CC activate myogenic genes by increasing chromatin accessibility through
CC recruitment of SMARCA4/BRG1/BAF190A (ATPase subunit of the BAF complex)
CC to myogenic gene promoters (PubMed:32459350). Promotes the repair of
CC DNA double-strand breaks (DSBs) through the homologous recombination
CC pathway by facilitating the recruitment of the DNA endonuclease RBBP8
CC to the DSBs (By similarity). Preferentially binds to chromatin regions
CC marked by H3K9me3, H3K27me3 and H3K36me2 (By similarity). Involved in
CC cellular growth control, through the regulation of cyclin D1 expression
CC (By similarity). Associates with chromatin (PubMed:22212508).
CC {ECO:0000250|UniProtKB:Q7Z4V5, ECO:0000269|PubMed:22212508,
CC ECO:0000269|PubMed:32459350}.
CC -!- FUNCTION: [Isoform 1]: Binds to condensed chromatin in mitotic cells.
CC {ECO:0000269|PubMed:22212508}.
CC -!- FUNCTION: [Isoform 3]: Binds to condensed chromatin in mitotic cells.
CC {ECO:0000269|PubMed:22212508}.
CC -!- FUNCTION: [Isoform 4]: Binds to non-condensed chromatin in the presence
CC of HDGF. {ECO:0000269|PubMed:22212508}.
CC -!- SUBUNIT: Interacts with trimethylated 'Lys-36' of histone H3
CC (H3K36me3). Interacts with trimethylated 'Lys-79' of histone H3
CC (H3K79me3), but has higher affinity for H3K36me3 (By similarity).
CC Interacts with IWS1 (By similarity). Interacts with H2AX, POGZ, RBBP8
CC and CBX1 (By similarity). Interacts with histones H3K9me3, H3K27me3 and
CC H3K36me2 (By similarity). Interacts with DPF3a (isoform 2 of
CC DPF3/BAF45C) (PubMed:32459350). Interacts with SMARCA4/BRG1/BAF190A, in
CC a DPF3a-dependent manner (PubMed:32459350). Interacts with
CC SMARCC1/BAF155 and SMARCD1/BAF60A in a DPF3a-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q7Z4V5,
CC ECO:0000269|PubMed:32459350}.
CC -!- SUBUNIT: [Isoform 1]: Interacts with HDGF.
CC {ECO:0000269|PubMed:22212508}.
CC -!- SUBUNIT: [Isoform 3]: Interacts with HDGF.
CC {ECO:0000269|PubMed:22212508}.
CC -!- SUBUNIT: [Isoform 4]: Selectively interacts with HDGF (N-terminally
CC processed form). {ECO:0000269|PubMed:22212508}.
CC -!- INTERACTION:
CC Q3UMU9; P51859: Hdgf; NbExp=4; IntAct=EBI-7627961, EBI-2943087;
CC Q3UMU9-1; P51859: Hdgf; NbExp=4; IntAct=EBI-7627862, EBI-2943087;
CC Q3UMU9-3; P51859: Hdgf; NbExp=4; IntAct=EBI-7627932, EBI-2943087;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q925G1}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:22212508}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus
CC {ECO:0000269|PubMed:22212508}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Nucleus
CC {ECO:0000269|PubMed:22212508}. Note=Displays a punctate pattern and
CC colocalizes with N-terminally processed HDFG.
CC {ECO:0000269|PubMed:22212508}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Isoform a;
CC IsoId=Q3UMU9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UMU9-2; Sequence=VSP_031118, VSP_031119;
CC Name=3; Synonyms=Isoform b;
CC IsoId=Q3UMU9-3; Sequence=VSP_031117;
CC Name=4; Synonyms=Isoform c;
CC IsoId=Q3UMU9-4; Sequence=VSP_047648, VSP_031119;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:22212508}.
CC -!- DISRUPTION PHENOTYPE: Mice show severely impaired post-injury muscle
CC regeneration. {ECO:0000269|PubMed:32459350}.
CC -!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
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DR EMBL; D63850; BAA22896.1; -; mRNA.
DR EMBL; FN687734; CBK52221.2; -; mRNA.
DR EMBL; AK143616; BAE25467.1; -; mRNA.
DR EMBL; AK144669; BAE25999.1; -; mRNA.
DR EMBL; AK146813; BAE27453.1; -; mRNA.
DR EMBL; AK146918; BAE27530.1; -; mRNA.
DR EMBL; BC003741; AAH03741.1; -; mRNA.
DR CCDS; CCDS28894.1; -. [Q3UMU9-1]
DR CCDS; CCDS89122.1; -. [Q3UMU9-3]
DR CCDS; CCDS89123.1; -. [Q3UMU9-2]
DR PIR; JC5662; JC5662.
DR RefSeq; NP_001291713.1; NM_001304784.2. [Q3UMU9-3]
DR RefSeq; NP_001291714.1; NM_001304785.2. [Q3UMU9-2]
DR RefSeq; NP_001317982.1; NM_001331053.1.
DR RefSeq; NP_032259.1; NM_008233.4. [Q3UMU9-1]
DR AlphaFoldDB; Q3UMU9; -.
DR SMR; Q3UMU9; -.
DR BioGRID; 200267; 9.
DR IntAct; Q3UMU9; 4.
DR MINT; Q3UMU9; -.
DR STRING; 10090.ENSMUSP00000002911; -.
DR iPTMnet; Q3UMU9; -.
DR PhosphoSitePlus; Q3UMU9; -.
DR EPD; Q3UMU9; -.
DR jPOST; Q3UMU9; -.
DR MaxQB; Q3UMU9; -.
DR PaxDb; Q3UMU9; -.
DR PeptideAtlas; Q3UMU9; -.
DR PRIDE; Q3UMU9; -.
DR ProteomicsDB; 269646; -. [Q3UMU9-1]
DR ProteomicsDB; 269647; -. [Q3UMU9-2]
DR ProteomicsDB; 269648; -. [Q3UMU9-3]
DR ProteomicsDB; 269649; -. [Q3UMU9-4]
DR Antibodypedia; 42428; 151 antibodies from 28 providers.
DR DNASU; 15193; -.
DR Ensembl; ENSMUST00000002911; ENSMUSP00000002911; ENSMUSG00000002833. [Q3UMU9-2]
DR Ensembl; ENSMUST00000225843; ENSMUSP00000153249; ENSMUSG00000002833. [Q3UMU9-3]
DR Ensembl; ENSMUST00000226053; ENSMUSP00000152948; ENSMUSG00000002833. [Q3UMU9-1]
DR GeneID; 15193; -.
DR KEGG; mmu:15193; -.
DR UCSC; uc008dau.2; mouse. [Q3UMU9-1]
DR UCSC; uc008dav.3; mouse. [Q3UMU9-2]
DR UCSC; uc008daw.2; mouse. [Q3UMU9-3]
DR UCSC; uc012avq.2; mouse. [Q3UMU9-4]
DR CTD; 84717; -.
DR MGI; MGI:1194492; Hdgfl2.
DR VEuPathDB; HostDB:ENSMUSG00000002833; -.
DR eggNOG; KOG1904; Eukaryota.
DR GeneTree; ENSGT00940000153942; -.
DR HOGENOM; CLU_034054_0_0_1; -.
DR InParanoid; Q3UMU9; -.
DR OMA; DLEMGNA; -.
DR OrthoDB; 530959at2759; -.
DR PhylomeDB; Q3UMU9; -.
DR TreeFam; TF105385; -.
DR BioGRID-ORCS; 15193; 5 hits in 59 CRISPR screens.
DR ChiTaRS; Hdgfl2; mouse.
DR PRO; PR:Q3UMU9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3UMU9; protein.
DR Bgee; ENSMUSG00000002833; Expressed in retinal neural layer and 254 other tissues.
DR Genevisible; Q3UMU9; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0061628; F:H3K27me3 modified histone binding; ISS:UniProtKB.
DR GO; GO:0062072; F:H3K9me3 modified histone binding; ISS:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0042692; P:muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:UniProtKB.
DR CDD; cd05834; HDGF_related; 1.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR035496; HDGF-rel_PWWP.
DR InterPro; IPR036218; HIVI-bd_sf.
DR InterPro; IPR021567; LEDGF_IBD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR Pfam; PF11467; LEDGF; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF140576; SSF140576; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; Isopeptide bond; Myogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..669
FT /note="Hepatoma-derived growth factor-related protein 2"
FT /id="PRO_0000317644"
FT DOMAIN 7..64
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 87..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..548
FT /note="Interaction with DPF3/BAF45C isoform 2"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT REGION 558..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 550..575
FT /evidence="ECO:0000255"
FT COMPBIAS 111..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:17622165,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q925G1"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 550
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4V5"
FT VAR_SEQ 66..118
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:22212508"
FT /id="VSP_047648"
FT VAR_SEQ 224..225
FT /note="KK -> KKHPTGYACPQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031117"
FT VAR_SEQ 226
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031118"
FT VAR_SEQ 635
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:22212508"
FT /id="VSP_031119"
FT MUTAGEN 523..524
FT /note="RR->AA: Loss of interaction with SMARCA4."
FT /evidence="ECO:0000269|PubMed:32459350"
FT MOD_RES Q3UMU9-2:619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q3UMU9-4:567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 669 AA; 74291 MW; 01228985D4616848 CRC64;
MPHAFKPGDL VFAKMKGYPH WPARIDDIAD GAVKPPPNKY PIFFFGTHET AFLGPKDLFP
YDKCKDKYGK PNKRKGFNEG LWEIQNNPHA SYSAPPPVSS SDSEAPEADL GCGSDVDKDK
ESRRVMTVTA VTTTATSDRM ESDSDSDKSS DHSGLKRKTP VLKVSVSKRA RRASSDLDQA
SVSPSEEDSE SPSESEKTSD QDFTPEKKTA ARPPRRGPLG GRKKKKVPSA SDSDSKADSD
GAKEEPVVTA QPSPSSSSSS SSSSSSDSDV SVKKPPRGRK PAEKPPPKPR GRRPKPERPP
STSSSDSDSD SGEVDRISEW KRRDEERRRE LEARRRREQE EELRRLREQE REEKERRKER
AERGGSSGEE LEDEEPVKKR SRKARGRGTP SSSDSEPEGE LGKEGKKLAK KSQLPGSESA
RKPGQKEKRG RPDEKPRARP VKVERTRKRS EGLSLERKGE KKKEPSVEER LQKLHSEIKF
ALKVDNPDVR KCLSALEELG TLQVTSQILQ KNTDVVATLK KIRRYKANKD VMAKAAEVYT
RLKSRVLGPK VEALQKVNKA GAEKERADNE KLEEQPGEQA PRELAEDEPS TDRSAPVNGE
ATSQKGENME DRAQEDGQDS EDGPRGGSSE ELHDSPRDNS DPAKPGNERQ DHERTRLASE
SANDDNEDS
