ZN652_HUMAN
ID ZN652_HUMAN Reviewed; 606 AA.
AC Q9Y2D9; A4QPD9; Q5H9Q0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Zinc finger protein 652;
GN Name=ZNF652; Synonyms=KIAA0924;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 FUNCTION, INTERACTION WITH CBFA2T3, AND TISSUE SPECIFICITY.
RX PubMed=16966434; DOI=10.1158/1541-7786.mcr-05-0249;
RA Kumar R., Manning J., Spendlove H.E., Kremmidiotis G., McKirdy R., Lee J.,
RA Millband D.N., Cheney K.M., Stampfer M.R., Dwivedi P.P., Morris H.A.,
RA Callen D.F.;
RT "ZNF652, a novel zinc finger protein, interacts with the putative breast
RT tumor suppressor CBFA2T3 to repress transcription.";
RL Mol. Cancer Res. 4:655-665(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-204, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-197 AND SER-204, AND
RP 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 [11]
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).
CC -!- FUNCTION: Functions as a transcriptional repressor.
CC {ECO:0000269|PubMed:16966434}.
CC -!- SUBUNIT: Interacts with CBFA2T3. {ECO:0000269|PubMed:16966434}.
CC -!- INTERACTION:
CC Q9Y2D9; O75081: CBFA2T3; NbExp=2; IntAct=EBI-1190229, EBI-1190217;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in breast,
CC prostate, vulva and pancreas. {ECO:0000269|PubMed:16966434}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76768.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB023141; BAA76768.2; ALT_INIT; mRNA.
DR EMBL; CR933680; CAI45974.1; -; mRNA.
DR EMBL; CH471109; EAW94682.1; -; Genomic_DNA.
DR EMBL; BC139779; AAI39780.1; -; mRNA.
DR EMBL; BC152440; AAI52441.1; -; mRNA.
DR CCDS; CCDS32677.1; -.
DR RefSeq; NP_001138837.1; NM_001145365.1.
DR RefSeq; NP_055712.1; NM_014897.2.
DR AlphaFoldDB; Q9Y2D9; -.
DR SMR; Q9Y2D9; -.
DR BioGRID; 116508; 5.
DR IntAct; Q9Y2D9; 6.
DR STRING; 9606.ENSP00000354686; -.
DR iPTMnet; Q9Y2D9; -.
DR PhosphoSitePlus; Q9Y2D9; -.
DR BioMuta; ZNF652; -.
DR DMDM; 134035373; -.
DR EPD; Q9Y2D9; -.
DR jPOST; Q9Y2D9; -.
DR MassIVE; Q9Y2D9; -.
DR MaxQB; Q9Y2D9; -.
DR PaxDb; Q9Y2D9; -.
DR PeptideAtlas; Q9Y2D9; -.
DR PRIDE; Q9Y2D9; -.
DR ProteomicsDB; 85745; -.
DR Antibodypedia; 30374; 71 antibodies from 21 providers.
DR DNASU; 22834; -.
DR Ensembl; ENST00000362063.6; ENSP00000354686.2; ENSG00000198740.9.
DR Ensembl; ENST00000430262.3; ENSP00000416305.2; ENSG00000198740.9.
DR GeneID; 22834; -.
DR KEGG; hsa:22834; -.
DR MANE-Select; ENST00000430262.3; ENSP00000416305.2; NM_001145365.3; NP_001138837.1.
DR UCSC; uc002iov.5; human.
DR CTD; 22834; -.
DR DisGeNET; 22834; -.
DR GeneCards; ZNF652; -.
DR HGNC; HGNC:29147; ZNF652.
DR HPA; ENSG00000198740; Tissue enhanced (brain).
DR MIM; 613907; gene.
DR neXtProt; NX_Q9Y2D9; -.
DR OpenTargets; ENSG00000198740; -.
DR PharmGKB; PA134896615; -.
DR VEuPathDB; HostDB:ENSG00000198740; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157416; -.
DR HOGENOM; CLU_002678_74_2_1; -.
DR InParanoid; Q9Y2D9; -.
DR OMA; VENCAAH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9Y2D9; -.
DR TreeFam; TF332655; -.
DR PathwayCommons; Q9Y2D9; -.
DR SignaLink; Q9Y2D9; -.
DR SIGNOR; Q9Y2D9; -.
DR BioGRID-ORCS; 22834; 19 hits in 1111 CRISPR screens.
DR ChiTaRS; ZNF652; human.
DR GenomeRNAi; 22834; -.
DR Pharos; Q9Y2D9; Tbio.
DR PRO; PR:Q9Y2D9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y2D9; protein.
DR Bgee; ENSG00000198740; Expressed in medial globus pallidus and 195 other tissues.
DR ExpressionAtlas; Q9Y2D9; baseline and differential.
DR Genevisible; Q9Y2D9; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..606
FT /note="Zinc finger protein 652"
FT /id="PRO_0000280428"
FT ZN_FING 245..268
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 272..294
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 299..322
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 329..351
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 357..379
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 385..407
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 413..435
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 441..463
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 469..492
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 71..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..606
FT /note="Mediates interaction with CBFA2T3"
FT /evidence="ECO:0000269|PubMed:16966434"
FT COMPBIAS 71..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..167
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1L1J6"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A1L1J6"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
SQ SEQUENCE 606 AA; 69744 MW; C066D10E179985CC CRC64;
MSHTASSCQE LVENCAVHVA GMAQEDSRRG QVPSSFYHGA NQELDLSTKV YKRESGSPYS
VLVDTKMSKP HLHETEEQPY FRETRAVSDV HAVKEDRENS DDTEEEEEEV SYKREQIIVE
VNLNNQTLNV SKGEKGVSSQ SKETPVLKTS SEEEEEESEE EATDDSNDYG ENEKQKKKEK
IVEKVSVTQR RTRRAASVAA ATTSPTPRTT RGRRKSVEPP KRKKRATKEP KAPVQKAKCE
EKETLTCEKC PRVFNTRWYL EKHMNVTHRR MQICDKCGKK FVLESELSLH QQTDCEKNIQ
CVSCNKSFKK LWSLHEHIKI VHGYAEKKFS CEICEKKFYT MAHVRKHMVA HTKDMPFTCE
TCGKSFKRSM SLKVHSLQHS GEKPFRCENC DERFQYKYQL RSHMSIHIGH KQFMCQWCGK
DFNMKQYFDE HMKTHTGEKP FICEICGKSF TSRPNMKRHR RTHTGEKPYP CDVCGQRFRF
SNMLKAHKEK CFRVTSPVNV PPAVQIPLTT SPATPVPSVV NTATTPTPPI NMNPVSTLPP
RPIPHPFSHL HIHPHPHHPH HLPIPPVPHL PPPPALFKSE PLNHRGQSED NFLRHLAEKN
SSAQHH
