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 27-MAR-2024, entry version 165. 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}; GN Synonyms=HDGF2 {ECO:0000312|EMBL:AAP97281.1}, 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}. 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; 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; 220. DR IntAct; Q7Z4V5; 51. DR MINT; Q7Z4V5; -. DR STRING; 9606.ENSP00000483345; -. DR ChEMBL; CHEMBL4523364; -. DR GlyCosmos; Q7Z4V5; 1 site, 1 glycan. 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; 9606-ENSP00000483345; -. DR PeptideAtlas; Q7Z4V5; -. DR ProteomicsDB; 46298; -. DR ProteomicsDB; 69248; -. [Q7Z4V5-1] DR ProteomicsDB; 69249; -. [Q7Z4V5-2] DR Pumba; Q7Z4V5; -. DR ABCD; Q7Z4V5; 1 sequenced antibody. DR Antibodypedia; 42428; 166 antibodies from 29 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 AGR; HGNC:14680; -. 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; AEETHNN; -. DR OrthoDB; 4271850at2759; -. DR PhylomeDB; Q7Z4V5; -. DR TreeFam; TF105385; -. DR PathwayCommons; Q7Z4V5; -. DR SignaLink; Q7Z4V5; -. DR BioGRID-ORCS; 84717; 36 hits in 1122 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 174 other cell types or tissues. DR ExpressionAtlas; Q7Z4V5; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. 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:0140566; F:histone reader activity; IDA:GO_Central. DR GO; GO:0035064; F:methylated histone binding; IMP:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; 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:0140861; P:DNA repair-dependent chromatin remodeling; IMP:GO_Central. 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:0043403; P:skeletal muscle tissue regeneration; ISS:UniProtKB. DR CDD; cd20149; PWWP_HDGFL2; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1. DR InterPro; IPR036218; HIVI-bd_sf. DR InterPro; IPR021567; LEDGF_IBD. DR InterPro; IPR000313; PWWP_dom. DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf. DR PANTHER; PTHR12550; HEPATOMA-DERIVED GROWTH FACTOR-RELATED; 1. DR PANTHER; PTHR12550:SF18; HEPATOMA-DERIVED GROWTH FACTOR-RELATED PROTEIN 2; 1. DR Pfam; PF11467; LEDGF; 1. DR Pfam; PF00855; PWWP; 1. DR SMART; SM00293; PWWP; 1. DR SUPFAM; SSF140576; HIV integrase-binding domain; 1. DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1. DR PROSITE; PS50812; PWWP; 1. DR Genevisible; Q7Z4V5; HS. 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 //