ZFP14_HUMAN
ID ZFP14_HUMAN Reviewed; 533 AA.
AC Q9HCL3; A7MD23;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2002, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Zinc finger protein 14 homolog;
DE Short=Zfp-14;
DE AltName: Full=Zinc finger protein 531;
GN Name=ZFP14; Synonyms=KIAA1559, ZNF531;
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=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q9HCL3; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-6381556, EBI-746778;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13385.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB046779; BAB13385.1; ALT_INIT; mRNA.
DR EMBL; BC152446; AAI52447.1; -; mRNA.
DR CCDS; CCDS33002.1; -.
DR RefSeq; NP_065968.1; NM_020917.2.
DR RefSeq; XP_016882527.1; XM_017027038.1.
DR AlphaFoldDB; Q9HCL3; -.
DR SMR; Q9HCL3; -.
DR BioGRID; 121706; 5.
DR IntAct; Q9HCL3; 5.
DR MINT; Q9HCL3; -.
DR STRING; 9606.ENSP00000270001; -.
DR iPTMnet; Q9HCL3; -.
DR PhosphoSitePlus; Q9HCL3; -.
DR BioMuta; ZFP14; -.
DR DMDM; 20140808; -.
DR EPD; Q9HCL3; -.
DR jPOST; Q9HCL3; -.
DR MassIVE; Q9HCL3; -.
DR MaxQB; Q9HCL3; -.
DR PaxDb; Q9HCL3; -.
DR PeptideAtlas; Q9HCL3; -.
DR PRIDE; Q9HCL3; -.
DR ProteomicsDB; 81753; -.
DR Antibodypedia; 29750; 90 antibodies from 17 providers.
DR DNASU; 57677; -.
DR Ensembl; ENST00000270001.12; ENSP00000270001.6; ENSG00000142065.14.
DR GeneID; 57677; -.
DR KEGG; hsa:57677; -.
DR MANE-Select; ENST00000270001.12; ENSP00000270001.6; NM_020917.3; NP_065968.1.
DR UCSC; uc010eex.3; human.
DR CTD; 57677; -.
DR GeneCards; ZFP14; -.
DR HGNC; HGNC:29312; ZFP14.
DR HPA; ENSG00000142065; Low tissue specificity.
DR neXtProt; NX_Q9HCL3; -.
DR OpenTargets; ENSG00000142065; -.
DR PharmGKB; PA145147576; -.
DR VEuPathDB; HostDB:ENSG00000142065; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162016; -.
DR HOGENOM; CLU_002678_44_0_1; -.
DR InParanoid; Q9HCL3; -.
DR OMA; YECVECW; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9HCL3; -.
DR TreeFam; TF341817; -.
DR PathwayCommons; Q9HCL3; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9HCL3; -.
DR BioGRID-ORCS; 57677; 27 hits in 1092 CRISPR screens.
DR ChiTaRS; ZFP14; human.
DR GenomeRNAi; 57677; -.
DR Pharos; Q9HCL3; Tdark.
DR PRO; PR:Q9HCL3; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9HCL3; protein.
DR Bgee; ENSG00000142065; Expressed in cortical plate and 143 other tissues.
DR ExpressionAtlas; Q9HCL3; baseline and differential.
DR Genevisible; Q9HCL3; 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:0001835; P:blastocyst hatching; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..533
FT /note="Zinc finger protein 14 homolog"
FT /id="PRO_0000047285"
FT DOMAIN 6..78
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 172..194
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 200..222
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 228..250
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 256..278
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 284..306
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 312..334
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 340..362
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 368..390
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 396..418
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 424..446
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 452..474
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 480..502
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 508..530
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
SQ SEQUENCE 533 AA; 63463 MW; E40EF5EC22A99F10 CRC64;
MAHGSVTFRD VAIDFSQEEW EFLDPAQRDL YRDVMWENYS NFISLGPSIS KPDVITLLDE
ERKEPGMVVR EGTRRYCPDL ESRYRTNTLS PEKDIYEIYS FQWDIMERIK SYSLQGSIFR
NDWECKSKIE GEKEQQEGYF GQVKITSEKM TTYKRHNFLT EYQIVHNGEK VYECKECRKT
FIRRSTLSQH LRIHTGEKPY KCKECGQAFR QRAHLIRHHK LHTGEKPYEC KECGKAFTVL
QELTQHQRLH TGEKPYECKE CGKAFRVHQQ LARHQRIHTG EKPYECKDCG KTFRQCTHLT
RHQRLHTAEK LYECKECGKA FVCGPDLRVH QKIHFGEKPY ECKECGKAFR ICQQLTVHQS
IHTGEKPYEC KECGKTFRLR QQLVRHQRIH TREKPYECME CWKTFSSYSQ LISHQSIHIG
ERPYECEECG KAFRLLSQLT QHQSIHTGEK PYECKECRKP FRLLSQLTQH QSIHTGEKPY
ECKECGKAFR LYSFLTQHQR IHTGEKPYKC KECKKAFRQH SHLTQHQKIH NGI
