ZN202_HUMAN
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 03-AUG-2022, entry version 201.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), AND VARIANT 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 11q23.3
RT 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 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 project:
RT 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., 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 [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., Skolnick M.,
RA 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 of ATP
RT binding cassette transporter A1 (ABCA1) and ABCG1 gene expression and a
RT 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 BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, AND IDENTIFICATION BY
RP 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; LYS-507 AND
RP LYS-521, AND 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).
CC -!- FUNCTION: Transcriptional repressor that binds to elements found
CC predominantly in genes that participate in lipid metabolism. Among its
CC 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 O95125; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-751960, EBI-3866279;
CC O95125; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-751960, EBI-739624;
CC O95125; Q96JC9: EAF1; NbExp=3; IntAct=EBI-751960, EBI-769261;
CC O95125; Q6A162: KRT40; NbExp=6; IntAct=EBI-751960, EBI-10171697;
CC O95125; P61968: LMO4; NbExp=4; IntAct=EBI-751960, EBI-2798728;
CC O95125; Q15013: MAD2L1BP; NbExp=3; IntAct=EBI-751960, EBI-712181;
CC O95125; P23508: MCC; NbExp=3; IntAct=EBI-751960, EBI-307531;
CC O95125; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-751960, EBI-16439278;
CC O95125; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-751960, EBI-3923617;
CC O95125; P41227: NAA10; NbExp=3; IntAct=EBI-751960, EBI-747693;
CC O95125; Q9BSU3: NAA11; NbExp=3; IntAct=EBI-751960, EBI-2585120;
CC O95125; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-751960, EBI-748391;
CC O95125; P49903: SEPHS1; NbExp=5; IntAct=EBI-751960, EBI-714091;
CC O95125; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-751960, EBI-2212028;
CC O95125; P15622-3: ZNF250; NbExp=3; IntAct=EBI-751960, EBI-10177272;
CC O95125; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-751960, EBI-11962468;
CC O95125; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-751960, EBI-5667516;
CC O95125; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-751960, EBI-11962574;
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 AlphaFoldDB; O95125; -.
DR SMR; O95125; -.
DR BioGRID; 113537; 31.
DR IntAct; O95125; 27.
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 Antibodypedia; 32833; 163 antibodies from 18 providers.
DR DNASU; 7753; -.
DR Ensembl; ENST00000336139.8; ENSP00000337724.4; ENSG00000166261.11. [O95125-1]
DR Ensembl; ENST00000529691.1; ENSP00000433881.1; ENSG00000166261.11. [O95125-1]
DR Ensembl; ENST00000530393.6; ENSP00000432504.1; ENSG00000166261.11. [O95125-1]
DR GeneID; 7753; -.
DR KEGG; hsa:7753; -.
DR MANE-Select; ENST00000530393.6; ENSP00000432504.1; NM_003455.4; NP_003446.2.
DR UCSC; uc001pzd.2; human. [O95125-1]
DR CTD; 7753; -.
DR DisGeNET; 7753; -.
DR GeneCards; ZNF202; -.
DR HGNC; HGNC:12994; ZNF202.
DR HPA; ENSG00000166261; Low tissue specificity.
DR MIM; 603430; gene.
DR neXtProt; NX_O95125; -.
DR OpenTargets; ENSG00000166261; -.
DR PharmGKB; PA37574; -.
DR VEuPathDB; HostDB:ENSG00000166261; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161189; -.
DR HOGENOM; CLU_002678_49_8_1; -.
DR InParanoid; O95125; -.
DR OMA; ELYLCNE; -.
DR PhylomeDB; O95125; -.
DR TreeFam; TF350829; -.
DR PathwayCommons; O95125; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; O95125; -.
DR SIGNOR; O95125; -.
DR BioGRID-ORCS; 7753; 24 hits in 1102 CRISPR screens.
DR ChiTaRS; ZNF202; human.
DR GeneWiki; ZNF202; -.
DR GenomeRNAi; 7753; -.
DR Pharos; O95125; Tbio.
DR PRO; PR:O95125; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O95125; protein.
DR Bgee; ENSG00000166261; Expressed in secondary oocyte and 134 other tissues.
DR ExpressionAtlas; O95125; baseline and differential.
DR Genevisible; O95125; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
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:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..648
FT /note="Zinc finger protein 202"
FT /id="PRO_0000047450"
FT DOMAIN 46..127
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 237..308
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 397..419
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 425..447
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 481..503
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 509..531
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 537..559
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 565..587
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 593..615
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 621..643
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 146..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 454
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 460
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 507
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 521
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..224
FT /note="Missing (in isoform Alpha)"
FT /evidence="ECO:0000303|PubMed:9790754"
FT /id="VSP_006902"
FT VARIANT 154
FT /note="V -> A (in dbSNP:rs1144507)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9790754, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.4"
FT /id="VAR_007818"
FT VARIANT 533
FT /note="G -> A (in dbSNP:rs34111365)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_023975"
FT CONFLICT 15
FT /note="E -> P (in Ref. 6; CAB82384)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="Missing (in Ref. 2; CAC21447)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="S -> AA (in Ref. 2)"
FT /evidence="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
