ZN653_HUMAN
ID ZN653_HUMAN Reviewed; 615 AA.
AC Q96CK0; Q96AS7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Zinc finger protein 653;
DE AltName: Full=67 kDa zinc finger protein;
DE AltName: Full=Zinc finger protein Zip67;
GN Name=ZNF653; Synonyms=ZIP67;
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], FUNCTION, AND INTERACTION WITH NR5A1.
RC TISSUE=Testis;
RX PubMed=12920234; DOI=10.1210/me.2003-0158;
RA Borud B., Mellgren G., Lund J., Bakke M.;
RT "Cloning and characterization of a novel zinc finger protein that modulates
RT the transcriptional activity of nuclear receptors.";
RL Mol. Endocrinol. 17:2303-2319(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-54.
RC TISSUE=Brain, and Eye;
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).
CC -!- FUNCTION: Transcriptional repressor. May repress NR5A1, PPARG, NR1H3,
CC NR4A2, ESR1 and NR3C1 transcriptional activity.
CC {ECO:0000269|PubMed:12920234}.
CC -!- SUBUNIT: Interacts with NR5A1. {ECO:0000269|PubMed:12920234}.
CC -!- INTERACTION:
CC Q96CK0; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-12217757, EBI-742887;
CC Q96CK0; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-12217757, EBI-2341787;
CC Q96CK0; Q15691: MAPRE1; NbExp=3; IntAct=EBI-12217757, EBI-1004115;
CC Q96CK0; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-12217757, EBI-725997;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, cerebellum, temporal
CC lobe, hippocampus and the adrenal gland. Moderately expressed in
CC spleen, uterus, thymus, pancreas, kidney, stomach and rectum.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AY072704; AAL66763.1; -; mRNA.
DR EMBL; BC014187; AAH14187.1; -; mRNA.
DR EMBL; BC016816; AAH16816.1; -; mRNA.
DR CCDS; CCDS12261.1; -.
DR RefSeq; NP_620138.2; NM_138783.3.
DR AlphaFoldDB; Q96CK0; -.
DR SMR; Q96CK0; -.
DR BioGRID; 125464; 54.
DR IntAct; Q96CK0; 10.
DR STRING; 9606.ENSP00000293771; -.
DR iPTMnet; Q96CK0; -.
DR PhosphoSitePlus; Q96CK0; -.
DR BioMuta; ZNF653; -.
DR DMDM; 74760763; -.
DR EPD; Q96CK0; -.
DR jPOST; Q96CK0; -.
DR MassIVE; Q96CK0; -.
DR MaxQB; Q96CK0; -.
DR PaxDb; Q96CK0; -.
DR PeptideAtlas; Q96CK0; -.
DR PRIDE; Q96CK0; -.
DR ProteomicsDB; 76191; -.
DR Antibodypedia; 25888; 23 antibodies from 9 providers.
DR DNASU; 115950; -.
DR Ensembl; ENST00000293771.10; ENSP00000293771.3; ENSG00000161914.10.
DR GeneID; 115950; -.
DR KEGG; hsa:115950; -.
DR MANE-Select; ENST00000293771.10; ENSP00000293771.3; NM_138783.4; NP_620138.2.
DR UCSC; uc002mrz.2; human.
DR CTD; 115950; -.
DR DisGeNET; 115950; -.
DR GeneCards; ZNF653; -.
DR HGNC; HGNC:25196; ZNF653.
DR HPA; ENSG00000161914; Low tissue specificity.
DR MIM; 611371; gene.
DR neXtProt; NX_Q96CK0; -.
DR OpenTargets; ENSG00000161914; -.
DR PharmGKB; PA134989597; -.
DR VEuPathDB; HostDB:ENSG00000161914; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160257; -.
DR HOGENOM; CLU_037389_0_0_1; -.
DR InParanoid; Q96CK0; -.
DR OMA; GAPLCPN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q96CK0; -.
DR TreeFam; TF332664; -.
DR PathwayCommons; Q96CK0; -.
DR SignaLink; Q96CK0; -.
DR BioGRID-ORCS; 115950; 16 hits in 1098 CRISPR screens.
DR GenomeRNAi; 115950; -.
DR Pharos; Q96CK0; Tbio.
DR PRO; PR:Q96CK0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96CK0; protein.
DR Bgee; ENSG00000161914; Expressed in right hemisphere of cerebellum and 97 other tissues.
DR ExpressionAtlas; Q96CK0; baseline and differential.
DR Genevisible; Q96CK0; HS.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0050682; F:AF-2 domain binding; IMP:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:1900116; P:extracellular negative regulation of signal transduction; IDA:UniProtKB.
DR GO; GO:1903507; P:negative regulation of nucleic acid-templated transcription; IDA:UniProtKB.
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; 3.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..615
FT /note="Zinc finger protein 653"
FT /id="PRO_0000253344"
FT ZN_FING 467..492
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 498..522
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 528..550
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 556..578
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 586..609
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 107..118
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 445..451
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 27..48
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 VARIANT 54
FT /note="K -> R (in dbSNP:rs17851437)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028076"
FT VARIANT 329
FT /note="A -> T (in dbSNP:rs35556595)"
FT /id="VAR_057438"
SQ SEQUENCE 615 AA; 67235 MW; 7208224CD9CDA311 CRC64;
MAERALEPEA EAEAEAGAGG EAAAEEGAAG RKARGRPRLT ESDRARRRLE SRKKYDVRRV
YLGEAHGPWV DLRRRSGWSD AKLAAYLISL ERGQRSGRHG KPWEQVPKKP KRKKRRRRNV
NCLKNVVIWY EDHKHRCPYE PHLAELDPTF GLYTTAVWQC EAGHRYFQDL HSPLKPLSDS
DPDSDKVGNG LVAGSSDSSS SGSASDSEES PEGQPVKAAA AAAAATPTSP VGSSGLITQE
GVHIPFDVHH VESLAEQGTP LCSNPAGNGP EALETVVCVP VPVQVGAGPS ALFENVPQEA
LGEVVASCPM PGMVPGSQVI IIAGPGYDAL TAEGIHLNMA AGSGVPGSGL GEEVPCAMME
GVAAYTQTEP EGSQPSTMDA TAVAGIETKK EKEDLCLLKK EEKEEPVAPE LATTVPESAE
PEAEADGEEL DGSDMSAIIY EIPKEPEKRR RSKRSRVMDA DGLLEMFHCP YEGCSQVYVA
LSSFQNHVNL VHRKGKTKVC PHPGCGKKFY LSNHLRRHMI IHSGVREFTC ETCGKSFKRK
NHLEVHRRTH TGETPLQCEI CGYQCRQRAS LNWHMKKHTA EVQYNFTCDR CGKRFEKLDS
VKFHTLKSHP DHKPT
