PRDM2_HUMAN
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 03-AUG-2022, entry version 217.
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="http://atlasgeneticsoncology.org/Genes/PRDM2ID41834ch1p36.html";
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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; CCDS151.1; -. [Q13029-2]
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. [Q13029-1]
DR RefSeq; XP_016857745.1; XM_017002256.1. [Q13029-1]
DR RefSeq; XP_016857746.1; XM_017002257.1. [Q13029-2]
DR RefSeq; XP_016857748.1; XM_017002259.1. [Q13029-3]
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. [Q13029-5]
DR RefSeq; XP_016857752.1; XM_017002263.1. [Q13029-3]
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; 27.
DR DIP; DIP-428N; -.
DR IntAct; Q13029; 10.
DR STRING; 9606.ENSP00000235372; -.
DR iPTMnet; Q13029; -.
DR PhosphoSitePlus; Q13029; -.
DR BioMuta; PRDM2; -.
DR DMDM; 56757653; -.
DR EPD; Q13029; -.
DR jPOST; Q13029; -.
DR MassIVE; Q13029; -.
DR MaxQB; Q13029; -.
DR PaxDb; Q13029; -.
DR PeptideAtlas; Q13029; -.
DR PRIDE; Q13029; -.
DR ProteomicsDB; 59110; -. [Q13029-1]
DR ProteomicsDB; 59111; -. [Q13029-2]
DR ProteomicsDB; 59112; -. [Q13029-3]
DR ProteomicsDB; 65150; -.
DR Antibodypedia; 1774; 275 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 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; GSPPCFD; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q13029; -.
DR TreeFam; TF332173; -.
DR BioCyc; MetaCyc:HS04042-MON; -.
DR PathwayCommons; Q13029; -.
DR SignaLink; Q13029; -.
DR SIGNOR; Q13029; -.
DR BioGRID-ORCS; 7799; 12 hits in 1110 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 201 other tissues.
DR ExpressionAtlas; Q13029; baseline and differential.
DR Genevisible; Q13029; HS.
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:0042054; F:histone methyltransferase activity; IEA:InterPro.
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: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:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR CDD; cd19188; PR-SET_PRDM2; 1.
DR DisProt; DP01757; -.
DR Gene3D; 2.170.270.10; -; 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 Pfam; PF00856; SET; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR PIRSF; PIRSF002395; RIZ_SET; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 2.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
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
