ID   ZN202_HUMAN             Reviewed;         648 AA.
AC   O95125; B0LPH9; Q4JG21; Q9H1B9; Q9NSM4;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 4.
DT   16-OCT-2019, entry version 186.
DE   RecName: Full=Zinc finger protein 202;
DE   AltName: Full=Zinc finger protein with KRAB and SCAN domains 10;
GN   Name=ZNF202; Synonyms=ZKSCAN10;
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] (ISOFORMS ALPHA AND BETA), AND VARIANT
RP   ALA-154.
RC   TISSUE=Testis;
RX   PubMed=9790754; DOI=10.1006/geno.1998.5419;
RA   Monaco C., Helmer Citterich M., Caprini E., Vorechovsky I., Russo G.,
RA   Croce C.M., Barbanti-Brodano G., Negrini M.;
RT   "Molecular cloning and characterization of ZNF202: a new gene at
RT   11q23.3 encoding testis-specific zinc finger proteins.";
RL   Genomics 52:358-362(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-154.
RA   Langmann T., Porsch-Oezcueruemez M., Heimerl S., Andrikovics H.,
RA   Schmitz G.;
RT   "Genomic sequence analysis of the ZNF202 gene: relevance for lipid
RT   parameters.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-154 AND ALA-533.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-154.
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA), AND VARIANT
RP   ALA-154.
RC   TISSUE=Brain;
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 [LARGE SCALE MRNA] OF 15-648 (ISOFORM BETA).
RC   TISSUE=Mammary cancer;
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   [7]
RP   CHARACTERIZATION.
RX   PubMed=10748193; DOI=10.1074/jbc.m910152199;
RA   Wagner S., Hess M.A., Ormonde-Hanson P., Malandro J., Hu H., Chen M.,
RA   Kehrer R., Frodsham M., Schumacher C., Beluch M., Honer C.,
RA   Skolnick M., Ballinger D., Bowen B.R.;
RT   "A broad role for the zinc finger protein ZNF202 in human lipid
RT   metabolism.";
RL   J. Biol. Chem. 275:15685-15690(2000).
RN   [8]
RP   POSSIBLE FUNCTION.
RX   PubMed=11279031; DOI=10.1074/jbc.m100218200;
RA   Porsch-Oezcueruemez M., Langmann T., Heimerl S., Borsukova H.,
RA   Kaminski W.E., Drobnik W., Honer C., Schumacher C., Schmitz G.;
RT   "The zinc finger protein 202 (ZNF202) is a transcriptional repressor
RT   of ATP binding cassette transporter A1 (ABCA1) and ABCG1 gene
RT   expression and a modulator of cellular lipid efflux.";
RL   J. Biol. Chem. 276:12427-12433(2001).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, AND IDENTIFICATION
RP   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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, 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   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-454; LYS-460;
RP   LYS-507 AND LYS-521, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   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-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: Transcriptional repressor that binds to elements found
CC       predominantly in genes that participate in lipid metabolism. Among
CC       its targets are structural components of lipoprotein particles
CC       (apolipoproteins AIV, CIII, and E), enzymes involved in lipid
CC       processing (lipoprotein lipase, lecithin cholesteryl ester
CC       transferase), transporters involved in lipid homeostasis (ABCA1,
CC       ABCG1), and several genes involved in processes related to energy
CC       metabolism and vascular disease.
CC   -!- SUBUNIT: Interacts with SDP1.
CC   -!- INTERACTION:
CC       Q6A162:KRT40; NbExp=5; IntAct=EBI-751960, EBI-10171697;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Beta; Synonyms=2;
CC         IsoId=O95125-1; Sequence=Displayed;
CC       Name=Alpha; Synonyms=1;
CC         IsoId=O95125-2; Sequence=VSP_006902;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in
CC       breast carcinoma cell lines.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/znf202/";
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DR   EMBL; AF027219; AAC79941.1; -; mRNA.
DR   EMBL; AF027218; AAC79940.1; -; mRNA.
DR   EMBL; AJ276177; CAC21447.1; -; Genomic_DNA.
DR   EMBL; AJ276178; CAC21447.1; JOINED; Genomic_DNA.
DR   EMBL; AJ276179; CAC21447.1; JOINED; Genomic_DNA.
DR   EMBL; AJ276180; CAC21447.1; JOINED; Genomic_DNA.
DR   EMBL; AJ276181; CAC21447.1; JOINED; Genomic_DNA.
DR   EMBL; AJ276182; CAC21447.1; JOINED; Genomic_DNA.
DR   EMBL; DQ093962; AAY88738.1; -; Genomic_DNA.
DR   EMBL; EU332869; ABY87558.1; -; Genomic_DNA.
DR   EMBL; BC013382; AAH13382.1; -; mRNA.
DR   EMBL; AL162031; CAB82384.1; -; mRNA.
DR   CCDS; CCDS8443.1; -. [O95125-1]
DR   PIR; T47156; T47156.
DR   RefSeq; NP_001288708.1; NM_001301779.1. [O95125-1]
DR   RefSeq; NP_001288709.1; NM_001301780.1. [O95125-1]
DR   RefSeq; NP_001288748.1; NM_001301819.1. [O95125-2]
DR   RefSeq; NP_003446.2; NM_003455.3. [O95125-1]
DR   RefSeq; XP_005271716.1; XM_005271659.1. [O95125-1]
DR   RefSeq; XP_005271717.1; XM_005271660.1. [O95125-1]
DR   RefSeq; XP_005271718.1; XM_005271661.1. [O95125-1]
DR   RefSeq; XP_005271721.1; XM_005271664.1. [O95125-2]
DR   RefSeq; XP_006718964.1; XM_006718901.2. [O95125-1]
DR   RefSeq; XP_011541274.1; XM_011542972.1. [O95125-1]
DR   RefSeq; XP_011541275.1; XM_011542973.1. [O95125-1]
DR   RefSeq; XP_011541277.1; XM_011542975.1. [O95125-1]
DR   RefSeq; XP_011541278.1; XM_011542976.1.
DR   RefSeq; XP_016873757.1; XM_017018268.1. [O95125-1]
DR   SMR; O95125; -.
DR   BioGrid; 113537; 13.
DR   IntAct; O95125; 25.
DR   STRING; 9606.ENSP00000337724; -.
DR   iPTMnet; O95125; -.
DR   PhosphoSitePlus; O95125; -.
DR   BioMuta; ZNF202; -.
DR   EPD; O95125; -.
DR   jPOST; O95125; -.
DR   MassIVE; O95125; -.
DR   MaxQB; O95125; -.
DR   PaxDb; O95125; -.
DR   PeptideAtlas; O95125; -.
DR   PRIDE; O95125; -.
DR   ProteomicsDB; 50655; -. [O95125-1]
DR   ProteomicsDB; 50656; -. [O95125-2]
DR   DNASU; 7753; -.
DR   Ensembl; ENST00000336139; ENSP00000337724; ENSG00000166261. [O95125-1]
DR   Ensembl; ENST00000529691; ENSP00000433881; ENSG00000166261. [O95125-1]
DR   Ensembl; ENST00000530393; ENSP00000432504; ENSG00000166261. [O95125-1]
DR   GeneID; 7753; -.
DR   KEGG; hsa:7753; -.
DR   UCSC; uc001pzd.2; human. [O95125-1]
DR   CTD; 7753; -.
DR   DisGeNET; 7753; -.
DR   GeneCards; ZNF202; -.
DR   HGNC; HGNC:12994; ZNF202.
DR   MIM; 603430; gene.
DR   neXtProt; NX_O95125; -.
DR   OpenTargets; ENSG00000166261; -.
DR   PharmGKB; PA37574; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00940000161189; -.
DR   HOGENOM; HOG000234619; -.
DR   InParanoid; O95125; -.
DR   KO; K09229; -.
DR   OMA; QKVHKMG; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; O95125; -.
DR   TreeFam; TF350829; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; O95125; -.
DR   SIGNOR; O95125; -.
DR   ChiTaRS; ZNF202; human.
DR   GeneWiki; ZNF202; -.
DR   GenomeRNAi; 7753; -.
DR   Pharos; O95125; -.
DR   PRO; PR:O95125; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000166261; Expressed in 167 organ(s), highest expression level in amniotic fluid.
DR   ExpressionAtlas; O95125; baseline and differential.
DR   Genevisible; O95125; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; NAS:NTNU_SB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   CDD; cd07936; SCAN; 1.
DR   Gene3D; 1.10.4020.10; -; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 7.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 4.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; DNA-binding; Isopeptide bond;
KW   Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1    648       Zinc finger protein 202.
FT                                /FTId=PRO_0000047450.
FT   DOMAIN       46    127       SCAN box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00187}.
FT   DOMAIN      237    308       KRAB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00119}.
FT   ZN_FING     397    419       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     425    447       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     481    503       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     509    531       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     537    559       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     565    587       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     593    615       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     621    643       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   MOD_RES     466    466       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   CROSSLNK     22     22       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    454    454       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    460    460       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    507    507       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    521    521       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ       1    224       Missing (in isoform Alpha).
FT                                {ECO:0000303|PubMed:9790754}.
FT                                /FTId=VSP_006902.
FT   VARIANT     154    154       V -> A (in dbSNP:rs1144507).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:9790754,
FT                                ECO:0000269|Ref.2, ECO:0000269|Ref.3,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_007818.
FT   VARIANT     533    533       G -> A (in dbSNP:rs34111365).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_023975.
FT   CONFLICT     15     15       E -> P (in Ref. 6; CAB82384).
FT                                {ECO:0000305}.
FT   CONFLICT    205    205       Missing (in Ref. 2; CAC21447).
FT                                {ECO:0000305}.
FT   CONFLICT    278    278       S -> AA (in Ref. 2). {ECO:0000305}.
SQ   SEQUENCE   648 AA;  74720 MW;  E738506D71DAFAE9 CRC64;
     MATAVEPEDQ DLWEEEGILM VKLEDDFTCR PESVLQRDDP VLETSHQNFR RFRYQEAASP
     REALIRLREL CHQWLRPERR TKEQILELLV LEQFLTVLPG ELQSWVRGQR PESGEEAVTL
     VEGLQKQPRR PRRWVTVHVH GQEVLSEETV HLGVEPESPN ELQDPVQSST PEQSPEETTQ
     SPDLGAPAEQ RPHQEEELQT LQESEVPVPE DPDLPAERSS GDSEMVALLT ALSQGLVTFK
     DVAVCFSQDQ WSDLDPTQKE FYGEYVLEED CGIVVSLSFP IPRPDEISQV REEEPWVPDI
     QEPQETQEPE ILSFTYTGDR SKDEEECLEQ EDLSLEDIHR PVLGEPEIHQ TPDWEIVFED
     NPGRLNERRF GTNISQVNSF VNLRETTPVH PLLGRHHDCS VCGKSFTCNS HLVRHLRTHT
     GEKPYKCMEC GKSYTRSSHL ARHQKVHKMN APYKYPLNRK NLEETSPVTQ AERTPSVEKP
     YRCDDCGKHF RWTSDLVRHQ RTHTGEKPFF CTICGKSFSQ KSVLTTHQRI HLGGKPYLCG
     ECGEDFSEHR RYLAHRKTHA AEELYLCSEC GRCFTHSAAF AKHLRGHASV RPCRCNECGK
     SFSRRDHLVR HQRTHTGEKP FTCPTCGKSF SRGYHLIRHQ RTHSEKTS
//