ID PRDM2_HUMAN Reviewed; 1718 AA. AC Q13029; B1AJZ4; B5MC68; Q13149; Q14550; Q5THJ1; Q5VUL9; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 3. DT 27-MAR-2024, entry version 226. DE RecName: Full=PR domain zinc finger protein 2; DE EC=2.1.1.355; DE AltName: Full=GATA-3-binding protein G3B; DE AltName: Full=Lysine N-methyltransferase 8; DE AltName: Full=MTB-ZF; DE AltName: Full=MTE-binding protein; DE AltName: Full=PR domain-containing protein 2; DE AltName: Full=Retinoblastoma protein-interacting zinc finger protein; DE AltName: Full=Zinc finger protein RIZ; GN Name=PRDM2; Synonyms=KMT8, RIZ; 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), AND SUBCELLULAR LOCATION. RC TISSUE=Fetal brain, and Retinoblastoma; RX PubMed=7538672; DOI=10.1073/pnas.92.10.4467; RA Buyse I.M., Shao G., Huang S.; RT "The retinoblastoma protein binds to RIZ, a zinc-finger protein that shares RT an epitope with the adenovirus E1A protein."; RL Proc. Natl. Acad. Sci. U.S.A. 92:4467-4471(1995). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 3), ALTERNATIVE INITIATION, TISSUE RP SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=9006946; DOI=10.1074/jbc.272.5.2984; RA Liu L., Shao G., Steele-Perkins G., Huang S.; RT "The retinoblastoma interacting zinc finger gene RIZ produces a PR domain- RT lacking product through an internal promoter."; RL J. Biol. Chem. 272:2984-2991(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Retina; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). 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 NUCLEOTIDE SEQUENCE [MRNA] OF 159-550, AND INTERACTION WITH GATA3. RX PubMed=7590293; DOI=10.1016/0378-1119(95)00420-b; RA Shapiro V.S., Lee P., Winoto A.; RT "Identification and cloning of the G3B cDNA encoding a 3' segment of a RT protein binding to GATA-3."; RL Gene 163:329-330(1995). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 202-1718 (ISOFORM 2), AND TISSUE SPECIFICITY. RX PubMed=8654390; DOI=10.1111/j.1432-1033.1996.00471.x; RA Muraosa Y., Takahashi K., Yoshizawa M., Shibahara S.; RT "cDNA cloning of a novel protein containing two zinc-finger domains that RT may function as a transcription factor for the human heme-oxygenase-1 RT gene."; RL Eur. J. Biochem. 235:471-479(1996). RN [8] RP FUNCTION, MUTAGENESIS OF CYS-106; ALA-159 AND ILE-188, AND SUBCELLULAR RP LOCATION. RX PubMed=14633678; RA Kim K.-C., Geng L., Huang S.; RT "Inactivation of a histone methyltransferase by mutations in human RT cancers."; RL Cancer Res. 63:7619-7623(2003). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421; SER-643; SER-743 AND RP SER-796, AND IDENTIFICATION 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [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 [13] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-651 AND LYS-774, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-347; LYS-651; LYS-690; LYS-692; RP LYS-774; LYS-866; LYS-879; LYS-1147; LYS-1151; LYS-1257 AND LYS-1281, AND RP IDENTIFICATION BY MASS 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 [15] RP STRUCTURE BY NMR OF 1-161, AND INTERACTION WITH HISTONE H3. RX PubMed=18082620; DOI=10.1016/j.bbrc.2007.12.034; RA Briknarova K., Zhou X., Satterthwait A., Hoyt D.W., Ely K.R., Huang S.; RT "Structural studies of the SET domain from RIZ1 tumor suppressor."; RL Biochem. Biophys. Res. Commun. 366:807-813(2008). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 2-148. RX PubMed=20084102; DOI=10.1371/journal.pone.0008570; RA Wu H., Min J., Lunin V.V., Antoshenko T., Dombrovski L., Zeng H., RA Allali-Hassani A., Campagna-Slater V., Vedadi M., Arrowsmith C.H., RA Plotnikov A.N., Schapira M.; RT "Structural biology of human H3K9 methyltransferases."; RL PLoS ONE 5:E8570-E8570(2010). CC -!- FUNCTION: S-adenosyl-L-methionine-dependent histone methyltransferase CC that specifically methylates 'Lys-9' of histone H3. May function as a CC DNA-binding transcription factor. Binds to the macrophage-specific TPA- CC responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and may CC act as a transcriptional activator of this gene. CC {ECO:0000269|PubMed:14633678}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA- CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355; CC -!- SUBUNIT: Binds to the retinoblastoma protein (RB). Interacts with CC GATA3. {ECO:0000269|PubMed:18082620, ECO:0000269|PubMed:7590293}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14633678, CC ECO:0000269|PubMed:7538672, ECO:0000269|PubMed:9006946}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=5; CC Name=1; Synonyms=RIZ1; CC IsoId=Q13029-1; Sequence=Displayed; CC Name=2; Synonyms=MTB-Zf; CC IsoId=Q13029-2; Sequence=VSP_006927, VSP_006928; CC Name=3; Synonyms=RIZ2; CC IsoId=Q13029-3; Sequence=VSP_018974; CC Name=4; CC IsoId=Q13029-4; Sequence=VSP_046421, VSP_046422; CC Name=5; CC IsoId=Q13029-5; Sequence=VSP_018974, VSP_006927, VSP_006928; CC -!- TISSUE SPECIFICITY: Highly expressed in retinoblastoma cell lines and CC in brain tumors. Also expressed in a number of other cell lines and in CC brain, heart, skeletal muscle, liver and spleen. Isoform 1 is expressed CC in testis at much higher level than isoform 3. CC {ECO:0000269|PubMed:8654390, ECO:0000269|PubMed:9006946}. CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation at Met- CC 202 of isoform 1. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA08110.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41834/PRDM2"; 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; U17838; AAC50820.2; -; mRNA. DR EMBL; BX647310; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AL031277; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL583942; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359771; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC014468; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; U23736; AAA87023.1; -; mRNA. DR EMBL; D45132; BAA08110.1; ALT_INIT; mRNA. DR CCDS; CCDS150.1; -. [Q13029-1] DR CCDS; CCDS30603.1; -. [Q13029-5] DR CCDS; CCDS44061.1; -. [Q13029-4] DR PIR; I38902; I38902. DR RefSeq; NP_001007258.1; NM_001007257.2. [Q13029-5] DR RefSeq; NP_001129082.1; NM_001135610.1. [Q13029-4] DR RefSeq; NP_036363.2; NM_012231.4. [Q13029-1] DR RefSeq; NP_056950.2; NM_015866.4. [Q13029-2] DR RefSeq; XP_016857744.1; XM_017002255.1. DR RefSeq; XP_016857745.1; XM_017002256.1. DR RefSeq; XP_016857746.1; XM_017002257.1. DR RefSeq; XP_016857748.1; XM_017002259.1. DR RefSeq; XP_016857749.1; XM_017002260.1. [Q13029-3] DR RefSeq; XP_016857750.1; XM_017002261.1. [Q13029-3] DR RefSeq; XP_016857751.1; XM_017002262.1. DR RefSeq; XP_016857752.1; XM_017002263.1. DR PDB; 2JV0; NMR; -; A=1-161. DR PDB; 2QPW; X-ray; 1.79 A; A=2-148. DR PDBsum; 2JV0; -. DR PDBsum; 2QPW; -. DR AlphaFoldDB; Q13029; -. DR SMR; Q13029; -. DR BioGRID; 113575; 35. DR DIP; DIP-428N; -. DR IntAct; Q13029; 9. DR STRING; 9606.ENSP00000235372; -. DR ChEMBL; CHEMBL5214862; -. DR GlyGen; Q13029; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q13029; -. DR PhosphoSitePlus; Q13029; -. DR SwissPalm; Q13029; -. DR BioMuta; PRDM2; -. DR DMDM; 56757653; -. DR EPD; Q13029; -. DR jPOST; Q13029; -. DR MassIVE; Q13029; -. DR MaxQB; Q13029; -. DR PaxDb; 9606-ENSP00000235372; -. DR PeptideAtlas; Q13029; -. DR ProteomicsDB; 3002; -. DR ProteomicsDB; 59110; -. [Q13029-1] DR ProteomicsDB; 59111; -. [Q13029-2] DR ProteomicsDB; 59112; -. [Q13029-3] DR ProteomicsDB; 65150; -. DR Pumba; Q13029; -. DR Antibodypedia; 1774; 288 antibodies from 25 providers. DR DNASU; 7799; -. DR Ensembl; ENST00000235372.11; ENSP00000235372.6; ENSG00000116731.23. [Q13029-1] DR Ensembl; ENST00000311066.10; ENSP00000312352.6; ENSG00000116731.23. [Q13029-1] DR Ensembl; ENST00000343137.8; ENSP00000341621.4; ENSG00000116731.23. [Q13029-5] DR Ensembl; ENST00000376048.9; ENSP00000365216.5; ENSG00000116731.23. [Q13029-4] DR Ensembl; ENST00000413440.5; ENSP00000411103.1; ENSG00000116731.23. [Q13029-5] DR GeneID; 7799; -. DR KEGG; hsa:7799; -. DR MANE-Select; ENST00000311066.10; ENSP00000312352.6; NM_001393986.1; NP_001380915.1. DR UCSC; uc001avg.4; human. [Q13029-1] DR AGR; HGNC:9347; -. DR CTD; 7799; -. DR DisGeNET; 7799; -. DR GeneCards; PRDM2; -. DR HGNC; HGNC:9347; PRDM2. DR HPA; ENSG00000116731; Low tissue specificity. DR MIM; 601196; gene. DR neXtProt; NX_Q13029; -. DR OpenTargets; ENSG00000116731; -. DR PharmGKB; PA33715; -. DR VEuPathDB; HostDB:ENSG00000116731; -. DR eggNOG; KOG2461; Eukaryota. DR GeneTree; ENSGT00940000159410; -. DR HOGENOM; CLU_002916_1_0_1; -. DR InParanoid; Q13029; -. DR OMA; MASRCPS; -. DR OrthoDB; 5399106at2759; -. DR PhylomeDB; Q13029; -. DR TreeFam; TF332173; -. DR BioCyc; MetaCyc:HS04042-MONOMER; -. DR PathwayCommons; Q13029; -. DR SignaLink; Q13029; -. DR SIGNOR; Q13029; -. DR BioGRID-ORCS; 7799; 12 hits in 1189 CRISPR screens. DR ChiTaRS; PRDM2; human. DR EvolutionaryTrace; Q13029; -. DR GeneWiki; PRDM2; -. DR GenomeRNAi; 7799; -. DR Pharos; Q13029; Tbio. DR PRO; PR:Q13029; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q13029; Protein. DR Bgee; ENSG00000116731; Expressed in sural nerve and 203 other cell types or tissues. DR ExpressionAtlas; Q13029; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ARUK-UCL. DR GO; GO:0140949; F:histone H3K9 trimethyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:NTNU_SB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:ARUK-UCL. DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB. DR GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. 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; IDA:NTNU_SB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd19188; PR-SET_PRDM2; 1. DR DisProt; DP01757; -. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3. DR Gene3D; 2.170.270.10; SET domain; 1. DR IDEAL; IID00467; -. DR InterPro; IPR009170; PRDM2. DR InterPro; IPR044414; PRDM2_PR-SET. DR InterPro; IPR001214; SET_dom. DR InterPro; IPR046341; SET_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1. DR PANTHER; PTHR16515:SF37; PR DOMAIN ZINC FINGER PROTEIN 2; 1. DR Pfam; PF21549; PRDM2_PR; 1. DR Pfam; PF00096; zf-C2H2; 2. DR Pfam; PF13912; zf-C2H2_6; 2. DR PIRSF; PIRSF002395; RIZ_SET; 1. DR SMART; SM00317; SET; 1. DR SMART; SM00355; ZnF_C2H2; 8. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2. DR SUPFAM; SSF82199; SET domain; 1. DR PROSITE; PS50280; SET; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7. DR Genevisible; Q13029; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative initiation; Alternative splicing; KW DNA-binding; Isopeptide bond; Metal-binding; Methyltransferase; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; S-adenosyl-L-methionine; KW Transcription; Transcription regulation; Transferase; Ubl conjugation; KW Zinc; Zinc-finger. FT CHAIN 1..1718 FT /note="PR domain zinc finger protein 2" FT /id="PRO_0000041634" FT DOMAIN 28..141 FT /note="SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT ZN_FING 360..382 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 390..412 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 483..506 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1134..1156 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1162..1185 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1191..1214 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1333..1355 FT /note="C2H2-type 7; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1455..1478 FT /note="C2H2-type 8; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 155..335 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 294..316 FT /note="Retinoblastoma protein binding" FT REGION 405..457 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 513..550 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 622..660 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 729..797 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 903..1083 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1244..1265 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1478..1576 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1589..1612 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1625..1652 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 970..979 FT /note="SH3-binding" FT /evidence="ECO:0000255" FT MOTIF 985..998 FT /note="SH3-binding" FT /evidence="ECO:0000255" FT MOTIF 1028..1052 FT /note="SH3-binding" FT /evidence="ECO:0000255" FT COMPBIAS 163..177 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 182..200 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 263..298 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 299..331 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 729..746 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 941..965 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 966..1005 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1006..1023 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1024..1043 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1046..1083 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1522..1576 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 421 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 643 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 743 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 781 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63755" FT MOD_RES 785 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63755" FT MOD_RES 796 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 347 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 651 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 690 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 692 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 774 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 866 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 879 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1147 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1151 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1257 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1281 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..201 FT /note="Missing (in isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_018974" FT VAR_SEQ 171..226 FT /note="GKKKSQENKNKGNKIQDIQLKTSEPDFTSANMRDSAEGPKEDEEKPSASALE FT QPAT -> ATASAWRPDALHQRPRTSPGSIGRSKLQLQPSSRDHSSKSRHSGCSLTAPE FT VTWNQ (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_046421" FT VAR_SEQ 227..1718 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_046422" FT VAR_SEQ 1679..1682 FT /note="SYSL -> RNFL (in isoform 2 and isoform 5)" FT /evidence="ECO:0000303|PubMed:17974005, FT ECO:0000303|PubMed:8654390" FT /id="VSP_006927" FT VAR_SEQ 1683..1718 FT /note="Missing (in isoform 2 and isoform 5)" FT /evidence="ECO:0000303|PubMed:17974005, FT ECO:0000303|PubMed:8654390" FT /id="VSP_006928" FT VARIANT 283 FT /note="D -> E (in dbSNP:rs2076324)" FT /id="VAR_052929" FT VARIANT 450 FT /note="S -> N (in dbSNP:rs17350795)" FT /id="VAR_052930" FT MUTAGEN 106 FT /note="C->Y: Reduced histone methyltransferase activity." FT /evidence="ECO:0000269|PubMed:14633678" FT MUTAGEN 159 FT /note="A->V: Reduced histone methyltransferase activity." FT /evidence="ECO:0000269|PubMed:14633678" FT MUTAGEN 188 FT /note="I->V: Loss of histone methyltransferase activity." FT /evidence="ECO:0000269|PubMed:14633678" FT CONFLICT 164 FT /note="S -> T (in Ref. 6; AAA87023)" FT /evidence="ECO:0000305" FT CONFLICT 196 FT /note="D -> S (in Ref. 6; AAA87023)" FT /evidence="ECO:0000305" FT CONFLICT 200 FT /note="A -> G (in Ref. 6; AAA87023)" FT /evidence="ECO:0000305" FT CONFLICT 276..293 FT /note="EDEEEEEDDDDDELEDEG -> VGGGGGVVVVVSWKARGE (in Ref. 6; FT AAA87023)" FT /evidence="ECO:0000305" FT CONFLICT 307..318 FT /note="EPEIRCDEKPED -> SQKYGVMRSQKI (in Ref. 6; AAA87023)" FT /evidence="ECO:0000305" FT CONFLICT 336..337 FT /note="EV -> DL (in Ref. 6; AAA87023)" FT /evidence="ECO:0000305" FT CONFLICT 371 FT /note="T -> I (in Ref. 6; AAA87023)" FT /evidence="ECO:0000305" FT CONFLICT 466..467 FT /note="DT -> VS (in Ref. 6; AAA87023)" FT /evidence="ECO:0000305" FT CONFLICT 530 FT /note="Q -> L (in Ref. 3; BX647310)" FT /evidence="ECO:0000305" FT CONFLICT 534..550 FT /note="TQNVYVPSTEPEEEGEA -> PRTCMYQAQSRRGRGSR (in Ref. 6; FT AAA87023)" FT /evidence="ECO:0000305" FT CONFLICT 703 FT /note="P -> PP (in Ref. 1 and 7)" FT /evidence="ECO:0000305" FT CONFLICT 856 FT /note="H -> R (in Ref. 3; BX647310)" FT /evidence="ECO:0000305" FT CONFLICT 1456 FT /note="I -> T (in Ref. 3; BX647310)" FT /evidence="ECO:0000305" FT STRAND 5..7 FT /evidence="ECO:0007829|PDB:2QPW" FT HELIX 15..17 FT /evidence="ECO:0007829|PDB:2QPW" FT HELIX 20..24 FT /evidence="ECO:0007829|PDB:2QPW" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:2JV0" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:2QPW" FT TURN 36..39 FT /evidence="ECO:0007829|PDB:2JV0" FT STRAND 41..48 FT /evidence="ECO:0007829|PDB:2QPW" FT STRAND 54..59 FT /evidence="ECO:0007829|PDB:2JV0" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:2QPW" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:2QPW" FT STRAND 72..80 FT /evidence="ECO:0007829|PDB:2QPW" FT TURN 81..83 FT /evidence="ECO:0007829|PDB:2QPW" FT STRAND 84..89 FT /evidence="ECO:0007829|PDB:2QPW" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:2QPW" FT HELIX 98..101 FT /evidence="ECO:0007829|PDB:2QPW" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:2JV0" FT STRAND 113..118 FT /evidence="ECO:0007829|PDB:2QPW" FT STRAND 121..128 FT /evidence="ECO:0007829|PDB:2QPW" FT HELIX 146..158 FT /evidence="ECO:0007829|PDB:2JV0" FT CONFLICT Q13029-4:198 FT /note="Q -> R (in Ref. 5; BC014468)" FT /evidence="ECO:0000305" SQ SEQUENCE 1718 AA; 188915 MW; 536BD68667AFE433 CRC64; MNQNTTEPVA ATETLAEVPE HVLRGLPEEV RLFPSAVDKT RIGVWATKPI LKGKKFGPFV GDKKKRSQVK NNVYMWEVYY PNLGWMCIDA TDPEKGNWLR YVNWACSGEE QNLFPLEINR AIYYKTLKPI APGEELLVWY NGEDNPEIAA AIEEERASAR SKRSSPKSRK GKKKSQENKN KGNKIQDIQL KTSEPDFTSA NMRDSAEGPK EDEEKPSASA LEQPATLQEV ASQEVPPELA TPAPAWEPQP EPDERLEAAA CEVNDLGEEE EEEEEEDEEE EEDDDDDELE DEGEEEASMP NENSVKEPEI RCDEKPEDLL EEPKTTSEET LEDCSEVTPA MQIPRTKEEA NGDVFETFMF PCQHCERKFT TKQGLERHMH IHISTVNHAF KCKYCGKAFG TQINRRRHER RHEAGLKRKP SQTLQPSEDL ADGKASGENV ASKDDSSPPS LGPDCLIMNS EKASQDTINS SVVEENGEVK ELHPCKYCKK VFGTHTNMRR HQRRVHERHL IPKGVRRKGG LEEPQPPAEQ AQATQNVYVP STEPEEEGEA DDVYIMDISS NISENLNYYI DGKIQTNNNT SNCDVIEMES ASADLYGINC LLTPVTVEIT QNIKTTQVPV TEDLPKEPLG STNSEAKKRR TASPPALPKI KAETDSDPMV PSCSLSLPLS ISTTEAVSFH KEKSVYLSSK LKQLLQTQDK LTPAGISATE IAKLGPVCVS APASMLPVTS SRFKRRTSSP PSSPQHSPAL RDFGKPSDGK AAWTDAGLTS KKSKLESHSD SPAWSLSGRD ERETVSPPCF DEYKMSKEWT ASSAFSSVCN QQPLDLSSGV KQKAEGTGKT PVQWESVLDL SVHKKHCSDS EGKEFKESHS VQPTCSAVKK RKPTTCMLQK VLLNEYNGID LPVENPADGT RSPSPCKSLE AQPDPDLGPG SGFPAPTVES TPDVCPSSPA LQTPSLSSGQ LPPLLIPTDP SSPPPCPPVL TVATPPPPLL PTVPLPAPSS SASPHPCPSP LSNATAQSPL PILSPTVSPS PSPIPPVEPL MSAASPGPPT LSSSSSSSSS SSSFSSSSSS SSPSPPPLSA ISSVVSSGDN LEASLPMISF KQEELENEGL KPREEPQSAA EQDVVVQETF NKNFVCNVCE SPFLSIKDLT KHLSIHAEEW PFKCEFCVQL FKDKTDLSEH RFLLHGVGNI FVCSVCKKEF AFLCNLQQHQ RDLHPDKVCT HHEFESGTLR PQNFTDPSKA HVEHMQSLPE DPLETSKEEE ELNDSSEELY TTIKIMASGI KTKDPDVRLG LNQHYPSFKP PPFQYHHRNP MGIGVTATNF TTHNIPQTFT TAIRCTKCGK GVDNMPELHK HILACASASD KKRYTPKKNP VPLKQTVQPK NGVVVLDNSG KNAFRRMGQP KRLNFSVELS KMSSNKLKLN ALKKKNQLVQ KAILQKNKSA KQKADLKNAC ESSSHICPYC NREFTYIGSL NKHAAFSCPK KPLSPPKKKV SHSSKKGGHS SPASSDKNSN SNHRRRTADA EIKMQSMQTP LGKTRARSSG PTQVPLPSSS FRSKQNVKFA ASVKSKKPSS SSLRNSSPIR MAKITHVEGK KPKAVAKNHS AQLSSKTSRS LHVRVQKSKA VLQSKSTLAS KKRTDRFNIK SRERSGGPVT RSLQLAAAAD LSENKREDGS AKQELKDFSY SLRLASRCSP PAAPYITRQY RKVKAPAAAQ FQGPFFKE //