ZIK1_HUMAN
ID ZIK1_HUMAN Reviewed; 487 AA.
AC Q3SY52; O43339; Q3SY51; Q3SY53;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Zinc finger protein interacting with ribonucleoprotein K;
DE AltName: Full=Zinc finger protein 762;
GN Name=ZIK1; Synonyms=ZNF762;
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=17071588; DOI=10.2353/ajpath.2006.060552;
RA Mihara M., Yoshida Y., Tsukamoto T., Inada K., Nakanishi Y., Yagi Y.,
RA Imai K., Sugimura T., Tatematsu M., Ushijima T.;
RT "Methylation of multiple genes in gastric glands with intestinal
RT metaplasia: a disorder with polyclonal origins.";
RL Am. J. Pathol. 169:1643-1651(2006).
CC -!- FUNCTION: May be a transcriptional repressor. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HNRPK. {ECO:0000250}.
CC -!- INTERACTION:
CC Q3SY52; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-20857691, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3SY52-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3SY52-2; Sequence=VSP_025147;
CC Name=3;
CC IsoId=Q3SY52-3; Sequence=VSP_025148;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in gastric glands, and at
CC low levels in colon and small intestine. Silenced through promoter
CC methylation in gastric glands with intestinal metaplasia.
CC {ECO:0000269|PubMed:17071588}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC003682; AAC24608.1; -; Genomic_DNA.
DR EMBL; BC103957; AAI03958.1; -; mRNA.
DR EMBL; BC103958; AAI03959.1; -; mRNA.
DR EMBL; BC103959; AAI03960.1; -; mRNA.
DR CCDS; CCDS33135.1; -. [Q3SY52-1]
DR CCDS; CCDS82408.1; -. [Q3SY52-2]
DR RefSeq; NP_001010879.2; NM_001010879.3. [Q3SY52-1]
DR RefSeq; NP_001308074.1; NM_001321145.1.
DR RefSeq; NP_001308075.1; NM_001321146.1. [Q3SY52-2]
DR RefSeq; NP_001308076.1; NM_001321147.1. [Q3SY52-3]
DR RefSeq; XP_011525068.1; XM_011526766.2. [Q3SY52-2]
DR RefSeq; XP_011525069.1; XM_011526767.2. [Q3SY52-3]
DR AlphaFoldDB; Q3SY52; -.
DR SMR; Q3SY52; -.
DR BioGRID; 129823; 6.
DR IntAct; Q3SY52; 4.
DR STRING; 9606.ENSP00000472867; -.
DR iPTMnet; Q3SY52; -.
DR PhosphoSitePlus; Q3SY52; -.
DR BioMuta; ZIK1; -.
DR DMDM; 121942960; -.
DR MassIVE; Q3SY52; -.
DR MaxQB; Q3SY52; -.
DR PaxDb; Q3SY52; -.
DR PeptideAtlas; Q3SY52; -.
DR PRIDE; Q3SY52; -.
DR Antibodypedia; 33273; 102 antibodies from 19 providers.
DR DNASU; 284307; -.
DR Ensembl; ENST00000597850.2; ENSP00000472867.1; ENSG00000171649.12. [Q3SY52-1]
DR Ensembl; ENST00000599456.1; ENSP00000468937.1; ENSG00000171649.12. [Q3SY52-2]
DR GeneID; 284307; -.
DR KEGG; hsa:284307; -.
DR MANE-Select; ENST00000597850.2; ENSP00000472867.1; NM_001010879.4; NP_001010879.2.
DR UCSC; uc002qpg.4; human. [Q3SY52-1]
DR CTD; 284307; -.
DR DisGeNET; 284307; -.
DR GeneCards; ZIK1; -.
DR HGNC; HGNC:33104; ZIK1.
DR HPA; ENSG00000171649; Low tissue specificity.
DR neXtProt; NX_Q3SY52; -.
DR OpenTargets; ENSG00000171649; -.
DR PharmGKB; PA162409747; -.
DR VEuPathDB; HostDB:ENSG00000171649; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162907; -.
DR HOGENOM; CLU_002678_55_4_1; -.
DR InParanoid; Q3SY52; -.
DR OMA; WDVEKDL; -.
DR PhylomeDB; Q3SY52; -.
DR TreeFam; TF342033; -.
DR PathwayCommons; Q3SY52; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q3SY52; -.
DR BioGRID-ORCS; 284307; 9 hits in 1088 CRISPR screens.
DR GenomeRNAi; 284307; -.
DR Pharos; Q3SY52; Tdark.
DR PRO; PR:Q3SY52; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q3SY52; protein.
DR Bgee; ENSG00000171649; Expressed in ganglionic eminence and 110 other tissues.
DR ExpressionAtlas; Q3SY52; baseline and differential.
DR Genevisible; Q3SY52; 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 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; 8.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..487
FT /note="Zinc finger protein interacting with
FT ribonucleoprotein K"
FT /id="PRO_0000286793"
FT DOMAIN 27..136
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 239..261
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 267..289
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 295..317
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 323..345
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 351..373
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 379..401
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 407..429
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 435..457
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 463..485
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 71..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025148"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025147"
FT CONFLICT 207
FT /note="Q -> K (in Ref. 2; AAI03960)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 54786 MW; 3D03318613E832E4 CRC64;
MAAAALRAPT QVTVSPETHM DLTKGCVTFE DIAIYFSQDE WGLLDEAQRL LYLEVMLENF
ALVASLGCGH GTEDEETPSD QNVSVGVSQS KAGSSTQKTQ SCEMCVPVLK DILHLADLPG
QKPYLVGECT NHHQHQKHHS AKKSLKRDMD RASYVKCCLF CMSLKPFRKW EVGKDLPAML
RLLRSLVFPG GKKPGTITEC GEDIRSQKSH YKSGECGKAS RHKHTPVYHP RVYTGKKLYE
CSKCGKAFRG KYSLVQHQRV HTGERPWECN ECGKFFSQTS HLNDHRRIHT GERPYECSEC
GKLFRQNSSL VDHQKIHTGA RPYECSQCGK SFSQKATLVK HQRVHTGERP YKCGECGNSF
SQSAILNQHR RIHTGAKPYE CGQCGKSFSQ KATLIKHQRV HTGERPYKCG DCGKSFSQSS
ILIQHRRIHT GARPYECGQC GKSFSQKSGL IQHQVVHTGE RPYECNKCGN SFSQCSSLIH
HQKCHNT
