ZNF8_HUMAN
ID ZNF8_HUMAN Reviewed; 575 AA.
AC P17098; Q6PI99;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Zinc finger protein 8;
DE AltName: Full=Zinc finger protein HF.18;
GN Name=ZNF8;
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=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-575, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=2106481; DOI=10.1016/0888-7543(90)90574-e;
RA Lania L., Donti E., Pannuti A., Pascucci A., Pengue G., Feliciello I.,
RA la Mantia G., Lanfrancone L., Pelicci P.-G.;
RT "cDNA isolation, expression analysis, and chromosomal localization of two
RT human zinc finger genes.";
RL Genomics 6:333-340(1990).
RN [3]
RP INTERACTION WITH SMAD3; SMAD4 AND SMAD5.
RX PubMed=12370310; DOI=10.1128/mcb.22.21.7633-7644.2002;
RA Jiao K., Zhou Y., Hogan B.L.M.;
RT "Identification of mZnf8, a mouse Kruppel-like transcriptional repressor,
RT as a novel nuclear interaction partner of Smad1.";
RL Mol. Cell. Biol. 22:7633-7644(2002).
RN [4]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-174; LYS-249; LYS-441 AND
RP LYS-545, 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. May modulate BMP and TGF-beta
CC signal transduction, through its interaction with SMAD proteins.
CC {ECO:0000250|UniProtKB:Q8BGV5}.
CC -!- SUBUNIT: Interacts with SMAD1 (via MH1 and MH2 domains) (By
CC similarity). Interacts with SMAD5 (PubMed:12370310). Interacts weakly
CC with SMAD2 (By similarity). Interacts weakly with SMAD3 and SMAD4
CC (PubMed:12370310). {ECO:0000250|UniProtKB:Q8BGV5,
CC ECO:0000269|PubMed:12370310}.
CC -!- INTERACTION:
CC P17098; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-2555757, EBI-541426;
CC P17098; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-2555757, EBI-348259;
CC P17098; Q8NC26: ZNF114; NbExp=3; IntAct=EBI-2555757, EBI-10265237;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously present in many human cell lines of
CC different embryological derivation. {ECO:0000269|PubMed:2106481}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BC039323; AAH39323.1; -; mRNA.
DR EMBL; M29581; AAA61314.1; -; mRNA.
DR CCDS; CCDS12974.1; -.
DR PIR; B34612; B34612.
DR RefSeq; NP_066575.2; NM_021089.2.
DR AlphaFoldDB; P17098; -.
DR SMR; P17098; -.
DR BioGRID; 113386; 42.
DR IntAct; P17098; 8.
DR MINT; P17098; -.
DR STRING; 9606.ENSP00000477716; -.
DR iPTMnet; P17098; -.
DR PhosphoSitePlus; P17098; -.
DR BioMuta; ZNF8; -.
DR DMDM; 55977777; -.
DR EPD; P17098; -.
DR jPOST; P17098; -.
DR MassIVE; P17098; -.
DR MaxQB; P17098; -.
DR PaxDb; P17098; -.
DR PeptideAtlas; P17098; -.
DR PRIDE; P17098; -.
DR ProteomicsDB; 53457; -.
DR Antibodypedia; 74823; 92 antibodies from 15 providers.
DR DNASU; 7554; -.
DR Ensembl; ENST00000621650.2; ENSP00000477716.1; ENSG00000278129.2.
DR GeneID; 7554; -.
DR KEGG; hsa:7554; -.
DR MANE-Select; ENST00000621650.2; ENSP00000477716.1; NM_021089.3; NP_066575.2.
DR UCSC; uc002qry.2; human.
DR CTD; 7554; -.
DR GeneCards; ZNF8; -.
DR HGNC; HGNC:13154; ZNF8.
DR HPA; ENSG00000278129; Low tissue specificity.
DR MIM; 194532; gene.
DR neXtProt; NX_P17098; -.
DR OpenTargets; ENSG00000278129; -.
DR PharmGKB; PA37728; -.
DR VEuPathDB; HostDB:ENSG00000278129; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162352; -.
DR HOGENOM; CLU_002678_57_1_1; -.
DR InParanoid; P17098; -.
DR OMA; ECQSQGL; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P17098; -.
DR TreeFam; TF337055; -.
DR PathwayCommons; P17098; -.
DR SignaLink; P17098; -.
DR BioGRID-ORCS; 7554; 14 hits in 1096 CRISPR screens.
DR GeneWiki; ZNF8; -.
DR GenomeRNAi; 7554; -.
DR Pharos; P17098; Tdark.
DR PRO; PR:P17098; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P17098; protein.
DR Bgee; ENSG00000278129; Expressed in cortical plate and 167 other tissues.
DR Genevisible; P17098; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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; 7.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..575
FT /note="Zinc finger protein 8"
FT /id="PRO_0000047331"
FT DOMAIN 25..96
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 257..279
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 285..307
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 313..335
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 341..363
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 369..391
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 397..419
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 467..489
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 92..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 441
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 545
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 60
FT /note="H -> Y (in Ref. 2; AAA61314)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="G -> A (in Ref. 2; AAA61314)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="A -> R (in Ref. 2; AAA61314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 64970 MW; E8F5B9C2FBED92C6 CRC64;
MDPEDEGVAG VMSVGPPAAR LQEPVTFRDV AVDFTQEEWG QLDPTQRILY RDVMLETFGH
LLSIGPELPK PEVISQLEQG TELWVAERGT TQGCHPAWEP RSESQASRKE EGLPEEEPSH
VTGREGFPTD APYPTTLGKD RECQSQSLAL KEQNNLKQLE FGLKEAPVQD QGYKTLRLRE
NCVLSSSPNP FPEISRGEYL YTYDSQITDS EHNSSLVSQQ TGSPGKQPGE NSDCHRDSSQ
AIPITELTKS QVQDKPYKCT DCGKSFNHNA HLTVHKRIHT GERPYMCKEC GKAFSQNSSL
VQHERIHTGD KPYKCAECGK SFCHSTHLTV HRRIHTGEKP YECQDCGRAF NQNSSLGRHK
RTHTGEKPYT CSVCGKSFSR TTCLFLHLRT HTEERPYECN HCGKGFRHSS SLAQHQRKHA
GEKPFECRQR LIFEQTPALT KHEWTEALGC DPPLSQDERT HRSDRPFKCN QCGKCFIQSS
HLIRHQITHT REEQPHGRSR RREQSSSRNS HLVQHQHPNS RKSSAGGAKA GQPESRALAL
FDIQKIMQEK NPVHVIGVEE PSVGASMLFD IREST
