HDGR2_HUMAN
ID HDGR2_HUMAN Reviewed; 671 AA.
AC Q7Z4V5; I3L080; K7EQZ6; Q96GI5; Q9BW08;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Hepatoma-derived growth factor-related protein 2;
DE Short=HDGF-related protein 2;
DE Short=HRP-2;
DE AltName: Full=Hepatoma-derived growth factor 2;
DE Short=HDGF-2;
GN Name=HDGFL2 {ECO:0000312|HGNC:HGNC:14680}; Synonyms=HDGF2, HDGFRP2, HRP2;
GN ORFNames=UNQ785/PRO1604;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Yu L.;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 103-671 (ISOFORM 1).
RC TISSUE=Kidney, and Muscle;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-366; SER-369;
RP SER-370 AND SER-625, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-232; SER-234;
RP SER-240 AND SER-664, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-490; SER-625;
RP SER-652 AND SER-664, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-240; SER-395;
RP SER-396; SER-397; SER-399; SER-454; SER-625; SER-633; SER-634; SER-652 AND
RP SER-664, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-232; SER-240;
RP SER-370; SER-454; SER-490; SER-625; SER-652 AND SER-664, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-137; SER-240;
RP SER-266; SER-305 AND SER-633, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH IWS1.
RX PubMed=25689719; DOI=10.1016/j.bbrc.2015.02.042;
RA Gao K., Xu C., Jin X., Wumaier R., Ma J., Peng J., Wang Y., Tang Y., Yu L.,
RA Zhang P.;
RT "HDGF-related protein-2 (HRP-2) acts as an oncogene to promote cell growth
RT in hepatocellular carcinoma.";
RL Biochem. Biophys. Res. Commun. 458:849-855(2015).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HISTONE H3K9ME3;
RP HISTONE H3K27ME2; H2AX; POGZ; RBBP8 AND CBX1.
RX PubMed=26721387; DOI=10.1093/nar/gkv1526;
RA Baude A., Aaes T.L., Zhai B., Al-Nakouzi N., Oo H.Z., Daugaard M.,
RA Rohde M., Jaeaettelae M.;
RT "Hepatoma-derived growth factor-related protein 2 promotes DNA repair by
RT homologous recombination.";
RL Nucleic Acids Res. 44:2214-2226(2016).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-554, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [18]
RP FUNCTION, INTERACTION WITH HISTONE H3K36ME2; DPF3; SMARCA4; SMARCC1 AND
RP SMARCD1, AND MUTAGENESIS OF TRP-21 AND 527-ARG--ARG-528.
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).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-93 IN COMPLEX WITH HISTONE H3
RP PEPTIDE, AND INTERACTION WITH HISTONE H3.
RX PubMed=21720545; DOI=10.1371/journal.pone.0018919;
RA Wu H., Zeng H., Lam R., Tempel W., Amaya M.F., Xu C., Dombrovski L.,
RA Qiu W., Wang Y., Min J.;
RT "Structural and histone binding ability characterizations of human PWWP
RT domains.";
RL PLoS ONE 6:E18919-E18919(2011).
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 (PubMed:26721387). Preferentially binds to chromatin
CC regions marked by H3K9me3, H3K27me3 and H3K36me2 (PubMed:26721387,
CC PubMed:32459350). Involved in cellular growth control, through the
CC regulation of cyclin D1 expression (PubMed:25689719).
CC {ECO:0000269|PubMed:25689719, ECO:0000269|PubMed:26721387,
CC ECO:0000269|PubMed:32459350}.
CC -!- SUBUNIT: Interacts with HDGF (By similarity). Interacts with
CC trimethylated 'Lys-36' of histone H3 (H3K36me3). Interacts with
CC trimethylated 'Lys-79' of histone H3 (H3K79me3), but has higher
CC affinity for H3K36me3. Interacts with IWS1 (PubMed:25689719). Interacts
CC with H2AX, POGZ, RBBP8 and CBX1 (PubMed:26721387). Interacts with
CC histones H3K9me3, H3K27me3 and H3K36me2 (PubMed:26721387,
CC PubMed:32459350). Interacts with DPF3a (isoform 2 of DPF3/BAF45C)
CC (PubMed:32459350). Interacts with SMARCA4/BRG1/BAF190A, SMARCC1/BAF155
CC and SMARCD1/BAF60A in a DPF3a-dependent manner (PubMed:32459350).
CC {ECO:0000250|UniProtKB:Q3UMU9, ECO:0000269|PubMed:21720545,
CC ECO:0000269|PubMed:25689719, ECO:0000269|PubMed:26721387,
CC ECO:0000269|PubMed:32459350}.
CC -!- INTERACTION:
CC Q7Z4V5; Q15554: TERF2; NbExp=2; IntAct=EBI-1049136, EBI-706637;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26721387}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q925G1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q7Z4V5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z4V5-2; Sequence=VSP_031116;
CC Name=3;
CC IsoId=Q7Z4V5-3; Sequence=VSP_047329;
CC Name=4;
CC IsoId=Q7Z4V5-4; Sequence=VSP_047329, VSP_031116;
CC -!- TISSUE SPECIFICITY: Widely expressed. High expression is found in
CC heart, skeletal muscle, ovary and testis. Overexpression is frequently
CC observed in hepatocellular carcinoma samples.
CC {ECO:0000269|PubMed:25689719}.
CC -!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
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DR EMBL; AF294267; AAP97281.1; -; mRNA.
DR EMBL; AY358600; AAQ88963.1; -; mRNA.
DR EMBL; AC011498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471139; EAW69215.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69216.1; -; Genomic_DNA.
DR EMBL; BC000755; AAH00755.1; -; mRNA.
DR EMBL; BC009449; AAH09449.1; -; mRNA.
DR CCDS; CCDS42472.1; -. [Q7Z4V5-1]
DR CCDS; CCDS59336.1; -. [Q7Z4V5-2]
DR RefSeq; NP_001001520.1; NM_001001520.2. [Q7Z4V5-1]
DR RefSeq; NP_116020.1; NM_032631.3. [Q7Z4V5-2]
DR PDB; 3EAE; X-ray; 2.24 A; A/B=1-93.
DR PDB; 3QBY; X-ray; 1.95 A; A/B/C=1-93.
DR PDB; 3QJ6; X-ray; 2.30 A; A=1-93.
DR PDB; 6T3I; NMR; -; A=469-549.
DR PDBsum; 3EAE; -.
DR PDBsum; 3QBY; -.
DR PDBsum; 3QJ6; -.
DR PDBsum; 6T3I; -.
DR AlphaFoldDB; Q7Z4V5; -.
DR SMR; Q7Z4V5; -.
DR BioGRID; 124221; 198.
DR IntAct; Q7Z4V5; 52.
DR MINT; Q7Z4V5; -.
DR STRING; 9606.ENSP00000483345; -.
DR ChEMBL; CHEMBL4523364; -.
DR GlyGen; Q7Z4V5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z4V5; -.
DR PhosphoSitePlus; Q7Z4V5; -.
DR SwissPalm; Q7Z4V5; -.
DR BioMuta; HDGFL2; -.
DR DMDM; 74738715; -.
DR EPD; Q7Z4V5; -.
DR jPOST; Q7Z4V5; -.
DR MassIVE; Q7Z4V5; -.
DR MaxQB; Q7Z4V5; -.
DR PaxDb; Q7Z4V5; -.
DR PeptideAtlas; Q7Z4V5; -.
DR PRIDE; Q7Z4V5; -.
DR ProteomicsDB; 46298; -.
DR ProteomicsDB; 69248; -. [Q7Z4V5-1]
DR ProteomicsDB; 69249; -. [Q7Z4V5-2]
DR ABCD; Q7Z4V5; 1 sequenced antibody.
DR Antibodypedia; 42428; 151 antibodies from 28 providers.
DR DNASU; 84717; -.
DR Ensembl; ENST00000616600.5; ENSP00000483345.1; ENSG00000167674.15. [Q7Z4V5-1]
DR Ensembl; ENST00000621835.4; ENSP00000483702.1; ENSG00000167674.15. [Q7Z4V5-2]
DR GeneID; 84717; -.
DR KEGG; hsa:84717; -.
DR MANE-Select; ENST00000616600.5; ENSP00000483345.1; NM_001001520.3; NP_001001520.1.
DR UCSC; uc032hkd.2; human. [Q7Z4V5-1]
DR CTD; 84717; -.
DR DisGeNET; 84717; -.
DR GeneCards; HDGFL2; -.
DR HGNC; HGNC:14680; HDGFL2.
DR HPA; ENSG00000167674; Low tissue specificity.
DR MIM; 617884; gene.
DR neXtProt; NX_Q7Z4V5; -.
DR VEuPathDB; HostDB:ENSG00000167674; -.
DR eggNOG; KOG1904; Eukaryota.
DR GeneTree; ENSGT00940000153942; -.
DR InParanoid; Q7Z4V5; -.
DR OMA; DLEMGNA; -.
DR OrthoDB; 530959at2759; -.
DR PhylomeDB; Q7Z4V5; -.
DR TreeFam; TF105385; -.
DR PathwayCommons; Q7Z4V5; -.
DR SignaLink; Q7Z4V5; -.
DR BioGRID-ORCS; 84717; 33 hits in 1040 CRISPR screens.
DR ChiTaRS; HDGFRP2; human.
DR EvolutionaryTrace; Q7Z4V5; -.
DR GenomeRNAi; 84717; -.
DR Pharos; Q7Z4V5; Tbio.
DR PRO; PR:Q7Z4V5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q7Z4V5; protein.
DR Bgee; ENSG00000167674; Expressed in ventricular zone and 172 other tissues.
DR ExpressionAtlas; Q7Z4V5; baseline and differential.
DR Genevisible; Q7Z4V5; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0061628; F:H3K27me3 modified histone binding; IDA:UniProtKB.
DR GO; GO:0062072; F:H3K9me3 modified histone binding; IDA:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IMP: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; IMP:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IMP: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; ISS: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 3D-structure; 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..671
FT /note="Hepatoma-derived growth factor-related protein 2"
FT /id="PRO_0000317643"
FT DOMAIN 7..64
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 86..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..552
FT /note="Interaction with DPF3/BAF45C isoform 2"
FT /evidence="ECO:0000269|PubMed:32459350"
FT REGION 562..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 521..581
FT /evidence="ECO:0000255"
FT COMPBIAS 86..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q925G1"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UMU9"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 574
FT /note="K -> KLAGEE (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047329"
FT VAR_SEQ 640
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031116"
FT MUTAGEN 21
FT /note="W->A: Loss of interaction with histone H3K36me2."
FT /evidence="ECO:0000269|PubMed:32459350"
FT MUTAGEN 527..528
FT /note="RR->AA,DD: Loss of interaction with SMARCA4,
FT SMARCC1, SMARCD1 and DPF3/BAF45C isoform 2."
FT /evidence="ECO:0000269|PubMed:32459350"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:3QBY"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:3QBY"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:3EAE"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:3QBY"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3QBY"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3QBY"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3QBY"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3QBY"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:3QBY"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:3QBY"
FT HELIX 471..485
FT /evidence="ECO:0007829|PDB:6T3I"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:6T3I"
FT HELIX 493..503
FT /evidence="ECO:0007829|PDB:6T3I"
FT HELIX 510..513
FT /evidence="ECO:0007829|PDB:6T3I"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:6T3I"
FT HELIX 517..526
FT /evidence="ECO:0007829|PDB:6T3I"
FT HELIX 533..547
FT /evidence="ECO:0007829|PDB:6T3I"
SQ SEQUENCE 671 AA; 74317 MW; 66CA046E0E802741 CRC64;
MPHAFKPGDL VFAKMKGYPH WPARIDDIAD GAVKPPPNKY PIFFFGTHET AFLGPKDLFP
YDKCKDKYGK PNKRKGFNEG LWEIQNNPHA SYSAPPPVSS SDSEAPEANP ADGSDADEDD
EDRGVMAVTA VTATAASDRM ESDSDSDKSS DNSGLKRKTP ALKMSVSKRA RKASSDLDQA
SVSPSEEENS ESSSESEKTS DQDFTPEKKA AVRAPRRGPL GGRKKKKAPS ASDSDSKADS
DGAKPEPVAM ARSASSSSSS SSSSDSDVSV KKPPRGRKPA EKPLPKPRGR KPKPERPPSS
SSSDSDSDEV DRISEWKRRD EARRRELEAR RRREQEEELR RLREQEKEEK ERRRERADRG
EAERGSGGSS GDELREDDEP VKKRGRKGRG RGPPSSSDSE PEAELEREAK KSAKKPQSSS
TEPARKPGQK EKRVRPEEKQ QAKPVKVERT RKRSEGFSMD RKVEKKKEPS VEEKLQKLHS
EIKFALKVDS PDVKRCLNAL EELGTLQVTS QILQKNTDVV ATLKKIRRYK ANKDVMEKAA
EVYTRLKSRV LGPKIEAVQK VNKAGMEKEK AEEKLAGEEL AGEEAPQEKA EDKPSTDLSA
PVNGEATSQK GESAEDKEHE EGRDSEEGPR CGSSEDLHDS VREGPDLDRP GSDRQERERA
RGDSEALDEE S
