GenomeNet

Database: UniProt
Entry: Q13029
LinkDB: Q13029
Original site: Q13029 
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   13-FEB-2019, entry version 197.
DE   RecName: Full=PR domain zinc finger protein 2;
DE            EC=2.1.1.43;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   shares 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
RT   domain-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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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
RT   project: 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
RP   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
RT   that may function as a transcription factor for the human heme-
RT   oxygenase-1 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.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome 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
RP   AND SER-796, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver 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
RT   replication stress reveals novel small ubiquitin-like modified target
RT   proteins and 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;
RP   LYS-692; LYS-774; LYS-866; LYS-879; LYS-1147; LYS-1151; LYS-1257 AND
RP   LYS-1281, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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-
RT   modification 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.,
RA   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
CC       methyltransferase that specifically methylates 'Lys-9' of histone
CC       H3. May function as a DNA-binding transcription factor. Binds to
CC       the macrophage-specific TPA-responsive element (MTE) of the HMOX1
CC       (heme oxygenase 1) gene and may act as a transcriptional activator
CC       of this gene. {ECO:0000269|PubMed:14633678}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
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         Note=No experimental confirmation available.;
CC       Name=3; Synonyms=RIZ2;
CC         IsoId=Q13029-3; Sequence=VSP_018974;
CC         Note=Produced by alternative initiation at Met-202 of isoform
CC         1.;
CC       Name=4;
CC         IsoId=Q13029-4; Sequence=VSP_046421, VSP_046422;
CC         Note=No experimental confirmation available. Ref.5 (BC014468)
CC         sequence is in conflict in position: 198:Q->R. {ECO:0000305};
CC       Name=5;
CC         IsoId=Q13029-5; Sequence=VSP_018974, VSP_006927, VSP_006928;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Highly expressed in retinoblastoma cell lines
CC       and in brain tumors. Also expressed in a number of other cell
CC       lines and in brain, heart, skeletal muscle, liver and spleen.
CC       Isoform 1 is expressed in testis at much higher level than isoform
CC       3. {ECO:0000269|PubMed:8654390, ECO:0000269|PubMed:9006946}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA08110.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PRDM2ID41834ch1p36.html";
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   UniGene; Hs.371823; -.
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   ProteinModelPortal; Q13029; -.
DR   SMR; Q13029; -.
DR   BioGrid; 113575; 13.
DR   DIP; DIP-428N; -.
DR   IntAct; Q13029; 4.
DR   STRING; 9606.ENSP00000235372; -.
DR   iPTMnet; Q13029; -.
DR   PhosphoSitePlus; Q13029; -.
DR   BioMuta; PRDM2; -.
DR   DMDM; 56757653; -.
DR   EPD; Q13029; -.
DR   jPOST; Q13029; -.
DR   MaxQB; Q13029; -.
DR   PaxDb; Q13029; -.
DR   PeptideAtlas; Q13029; -.
DR   PRIDE; Q13029; -.
DR   ProteomicsDB; 59110; -.
DR   ProteomicsDB; 59111; -. [Q13029-2]
DR   ProteomicsDB; 59112; -. [Q13029-3]
DR   DNASU; 7799; -.
DR   Ensembl; ENST00000235372; ENSP00000235372; ENSG00000116731. [Q13029-1]
DR   Ensembl; ENST00000311066; ENSP00000312352; ENSG00000116731. [Q13029-2]
DR   Ensembl; ENST00000343137; ENSP00000341621; ENSG00000116731. [Q13029-5]
DR   Ensembl; ENST00000376048; ENSP00000365216; ENSG00000116731. [Q13029-4]
DR   Ensembl; ENST00000413440; ENSP00000411103; ENSG00000116731. [Q13029-5]
DR   GeneID; 7799; -.
DR   KEGG; hsa:7799; -.
DR   UCSC; uc001avg.4; human. [Q13029-1]
DR   CTD; 7799; -.
DR   DisGeNET; 7799; -.
DR   EuPathDB; HostDB:ENSG00000116731.22; -.
DR   GeneCards; PRDM2; -.
DR   HGNC; HGNC:9347; PRDM2.
DR   HPA; HPA005809; -.
DR   MIM; 601196; gene.
DR   neXtProt; NX_Q13029; -.
DR   OpenTargets; ENSG00000116731; -.
DR   PharmGKB; PA33715; -.
DR   eggNOG; KOG2461; Eukaryota.
DR   eggNOG; ENOG410ZFVU; LUCA.
DR   GeneTree; ENSGT00940000159410; -.
DR   HOGENOM; HOG000231078; -.
DR   HOVERGEN; HBG053671; -.
DR   InParanoid; Q13029; -.
DR   KO; K11432; -.
DR   OMA; KPKLESH; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q13029; -.
DR   TreeFam; TF332173; -.
DR   SIGNOR; Q13029; -.
DR   ChiTaRS; PRDM2; human.
DR   EvolutionaryTrace; Q13029; -.
DR   GeneWiki; PRDM2; -.
DR   GenomeRNAi; 7799; -.
DR   PRO; PR:Q13029; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000116731; Expressed in 229 organ(s), highest expression level in middle temporal gyrus.
DR   ExpressionAtlas; Q13029; baseline and differential.
DR   Genevisible; Q13029; HS.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR   GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR   InterPro; IPR009170; RIZ_retinblastoma-bd_prot.
DR   InterPro; IPR001214; SET_dom.
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   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   Complete proteome; DNA-binding; Isopeptide bond; Metal-binding;
KW   Methyltransferase; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1718       PR domain zinc finger protein 2.
FT                                /FTId=PRO_0000041634.
FT   DOMAIN       28    141       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     360    382       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     390    412       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     483    506       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1134   1156       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1162   1185       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1191   1214       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING    1333   1355       C2H2-type 7; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING    1455   1478       C2H2-type 8; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   REGION      294    316       Retinoblastoma protein binding.
FT   MOTIF       970    979       SH3-binding. {ECO:0000255}.
FT   MOTIF       985    998       SH3-binding. {ECO:0000255}.
FT   MOTIF      1028   1052       SH3-binding. {ECO:0000255}.
FT   COMPBIAS    268    296       Asp/Glu-rich (acidic).
FT   COMPBIAS    933   1049       Pro-rich.
FT   COMPBIAS   1052   1074       Poly-Ser.
FT   COMPBIAS   1361   1447       Arg/Lys-rich (basic).
FT   MOD_RES     421    421       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     643    643       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     743    743       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     781    781       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q63755}.
FT   MOD_RES     785    785       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q63755}.
FT   MOD_RES     796    796       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   CROSSLNK    347    347       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    651    651       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    690    690       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    692    692       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    774    774       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25755297,
FT                                ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    866    866       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    879    879       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1147   1147       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1151   1151       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1257   1257       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK   1281   1281       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ       1    201       Missing (in isoform 3 and isoform 5).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_018974.
FT   VAR_SEQ     171    226       GKKKSQENKNKGNKIQDIQLKTSEPDFTSANMRDSAEGPKE
FT                                DEEKPSASALEQPAT -> ATASAWRPDALHQRPRTSPGSI
FT                                GRSKLQLQPSSRDHSSKSRHSGCSLTAPEVTWNQ (in
FT                                isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_046421.
FT   VAR_SEQ     227   1718       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_046422.
FT   VAR_SEQ    1679   1682       SYSL -> RNFL (in isoform 2 and isoform
FT                                5). {ECO:0000303|PubMed:17974005,
FT                                ECO:0000303|PubMed:8654390}.
FT                                /FTId=VSP_006927.
FT   VAR_SEQ    1683   1718       Missing (in isoform 2 and isoform 5).
FT                                {ECO:0000303|PubMed:17974005,
FT                                ECO:0000303|PubMed:8654390}.
FT                                /FTId=VSP_006928.
FT   VARIANT     283    283       D -> E (in dbSNP:rs2076324).
FT                                /FTId=VAR_052929.
FT   VARIANT     450    450       S -> N (in dbSNP:rs17350795).
FT                                /FTId=VAR_052930.
FT   MUTAGEN     106    106       C->Y: Reduced histone methyltransferase
FT                                activity. {ECO:0000269|PubMed:14633678}.
FT   MUTAGEN     159    159       A->V: Reduced histone methyltransferase
FT                                activity. {ECO:0000269|PubMed:14633678}.
FT   MUTAGEN     188    188       I->V: Loss of histone methyltransferase
FT                                activity. {ECO:0000269|PubMed:14633678}.
FT   CONFLICT    164    164       S -> T (in Ref. 6; AAA87023).
FT                                {ECO:0000305}.
FT   CONFLICT    196    196       D -> S (in Ref. 6; AAA87023).
FT                                {ECO:0000305}.
FT   CONFLICT    200    200       A -> G (in Ref. 6; AAA87023).
FT                                {ECO:0000305}.
FT   CONFLICT    276    293       EDEEEEEDDDDDELEDEG -> VGGGGGVVVVVSWKARGE
FT                                (in Ref. 6; AAA87023). {ECO:0000305}.
FT   CONFLICT    307    318       EPEIRCDEKPED -> SQKYGVMRSQKI (in Ref. 6;
FT                                AAA87023). {ECO:0000305}.
FT   CONFLICT    336    337       EV -> DL (in Ref. 6; AAA87023).
FT                                {ECO:0000305}.
FT   CONFLICT    371    371       T -> I (in Ref. 6; AAA87023).
FT                                {ECO:0000305}.
FT   CONFLICT    466    467       DT -> VS (in Ref. 6; AAA87023).
FT                                {ECO:0000305}.
FT   CONFLICT    530    530       Q -> L (in Ref. 3; BX647310).
FT                                {ECO:0000305}.
FT   CONFLICT    534    550       TQNVYVPSTEPEEEGEA -> PRTCMYQAQSRRGRGSR
FT                                (in Ref. 6; AAA87023). {ECO:0000305}.
FT   CONFLICT    703    703       P -> PP (in Ref. 1 and 7). {ECO:0000305}.
FT   CONFLICT    856    856       H -> R (in Ref. 3; BX647310).
FT                                {ECO:0000305}.
FT   CONFLICT   1456   1456       I -> T (in Ref. 3; BX647310).
FT                                {ECO:0000305}.
FT   STRAND        5      7       {ECO:0000244|PDB:2QPW}.
FT   HELIX        15     17       {ECO:0000244|PDB:2QPW}.
FT   HELIX        20     24       {ECO:0000244|PDB:2QPW}.
FT   STRAND       27     29       {ECO:0000244|PDB:2JV0}.
FT   STRAND       30     34       {ECO:0000244|PDB:2QPW}.
FT   TURN         36     39       {ECO:0000244|PDB:2JV0}.
FT   STRAND       41     48       {ECO:0000244|PDB:2QPW}.
FT   STRAND       54     59       {ECO:0000244|PDB:2JV0}.
FT   STRAND       62     64       {ECO:0000244|PDB:2QPW}.
FT   HELIX        66     68       {ECO:0000244|PDB:2QPW}.
FT   STRAND       72     80       {ECO:0000244|PDB:2QPW}.
FT   TURN         81     83       {ECO:0000244|PDB:2QPW}.
FT   STRAND       84     89       {ECO:0000244|PDB:2QPW}.
FT   HELIX        93     95       {ECO:0000244|PDB:2QPW}.
FT   HELIX        98    101       {ECO:0000244|PDB:2QPW}.
FT   STRAND      106    110       {ECO:0000244|PDB:2JV0}.
FT   STRAND      113    118       {ECO:0000244|PDB:2QPW}.
FT   STRAND      121    128       {ECO:0000244|PDB:2QPW}.
FT   HELIX       146    158       {ECO:0000244|PDB:2JV0}.
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
//
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