ZNF85_HUMAN
ID ZNF85_HUMAN Reviewed; 595 AA.
AC Q03923; B9ZVP4; Q6NVI0;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Zinc finger protein 85;
DE AltName: Full=Zinc finger protein HPF4;
DE AltName: Full=Zinc finger protein HTF1;
GN Name=ZNF85;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND VARIANTS ARG-84 AND ALA-266.
RC TISSUE=Placenta;
RX PubMed=9839802; DOI=10.1089/dna.1998.17.931;
RA Poncelet D.A., Bellefroid E.J., Bastiaens P.V., Demoitie M.A., Marine J.C.,
RA Pendeville H., Alami Y., Devos N., Lecocq P.J., Ogawa T., Muller M.,
RA Martial J.A.;
RT "Functional analysis of ZNF85 KRAB zinc finger protein, a member of the
RT highly homologous ZNF91 family.";
RL DNA Cell Biol. 17:931-943(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-196 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 12-196 (ISOFORM 2), VARIANTS ARG-84; ILE-115; ARG-177 AND ARG-184, AND
RP TISSUE SPECIFICITY.
RX PubMed=2023909; DOI=10.1073/pnas.88.9.3608;
RA Bellefroid E.J., Poncelet D.A., Lecocq P.J., Revelant O., Martial J.A.;
RT "The evolutionarily conserved Kruppel-associated box domain defines a
RT subfamily of eukaryotic multifingered proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3608-3612(1991).
CC -!- FUNCTION: May be a transcriptional repressor.
CC {ECO:0000269|PubMed:9839802}.
CC -!- INTERACTION:
CC Q03923-3; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-10223330, EBI-742887;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9839802}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q03923-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03923-2; Sequence=VSP_035771;
CC Name=3;
CC IsoId=Q03923-3; Sequence=VSP_042154, VSP_042155;
CC -!- TISSUE SPECIFICITY: Widely expressed, including in testis.
CC {ECO:0000269|PubMed:2023909, ECO:0000269|PubMed:9839802}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U35376; AAA79179.1; -; mRNA.
DR EMBL; AC008739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC068066; AAH68066.1; -; mRNA.
DR EMBL; M61866; AAA52689.1; -; mRNA.
DR EMBL; M61868; AAA58671.1; -; mRNA.
DR CCDS; CCDS32977.1; -. [Q03923-1]
DR CCDS; CCDS58657.1; -. [Q03923-3]
DR PIR; A39384; A39384.
DR PIR; C39384; C39384.
DR PIR; G02075; G02075.
DR RefSeq; NP_001243101.1; NM_001256172.1. [Q03923-3]
DR RefSeq; NP_003420.2; NM_003429.4. [Q03923-1]
DR AlphaFoldDB; Q03923; -.
DR SMR; Q03923; -.
DR BioGRID; 113455; 8.
DR IntAct; Q03923; 2.
DR STRING; 9606.ENSP00000329793; -.
DR iPTMnet; Q03923; -.
DR PhosphoSitePlus; Q03923; -.
DR BioMuta; ZNF85; -.
DR DMDM; 215274175; -.
DR jPOST; Q03923; -.
DR MassIVE; Q03923; -.
DR MaxQB; Q03923; -.
DR PaxDb; Q03923; -.
DR PeptideAtlas; Q03923; -.
DR PRIDE; Q03923; -.
DR Antibodypedia; 28656; 108 antibodies from 13 providers.
DR DNASU; 7639; -.
DR Ensembl; ENST00000300540.7; ENSP00000300540.2; ENSG00000105750.15. [Q03923-3]
DR Ensembl; ENST00000328178.13; ENSP00000329793.7; ENSG00000105750.15. [Q03923-1]
DR Ensembl; ENST00000345030.6; ENSP00000342340.5; ENSG00000105750.15. [Q03923-2]
DR Ensembl; ENST00000613159.2; ENSP00000479316.2; ENSG00000278091.4. [Q03923-2]
DR Ensembl; ENST00000615320.4; ENSP00000483118.1; ENSG00000278091.4. [Q03923-1]
DR Ensembl; ENST00000615882.4; ENSP00000479120.1; ENSG00000278091.4. [Q03923-3]
DR GeneID; 7639; -.
DR KEGG; hsa:7639; -.
DR MANE-Select; ENST00000328178.13; ENSP00000329793.7; NM_003429.5; NP_003420.2.
DR UCSC; uc002npf.5; human. [Q03923-1]
DR CTD; 7639; -.
DR DisGeNET; 7639; -.
DR GeneCards; ZNF85; -.
DR HGNC; HGNC:13160; ZNF85.
DR HPA; ENSG00000105750; Low tissue specificity.
DR MIM; 603899; gene.
DR neXtProt; NX_Q03923; -.
DR OpenTargets; ENSG00000105750; -.
DR PharmGKB; PA37733; -.
DR VEuPathDB; HostDB:ENSG00000105750; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154251; -.
DR HOGENOM; CLU_002678_69_11_1; -.
DR InParanoid; Q03923; -.
DR OMA; QAFICSS; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q03923; -.
DR TreeFam; TF342117; -.
DR PathwayCommons; Q03923; -.
DR SignaLink; Q03923; -.
DR BioGRID-ORCS; 7639; 91 hits in 1063 CRISPR screens.
DR ChiTaRS; ZNF85; human.
DR GenomeRNAi; 7639; -.
DR Pharos; Q03923; Tbio.
DR PRO; PR:Q03923; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q03923; protein.
DR Bgee; ENSG00000105750; Expressed in ganglionic eminence and 104 other tissues.
DR ExpressionAtlas; Q03923; baseline and differential.
DR Genevisible; Q03923; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA: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; IDA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; 13.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
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..595
FT /note="Zinc finger protein 85"
FT /id="PRO_0000047398"
FT DOMAIN 4..75
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 146..168
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 174..196
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 202..224
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 230..252
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 258..280
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 286..308
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 314..336
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 342..364
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 370..392
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 398..420
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 426..448
FT /note="C2H2-type 11; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 454..476
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 482..504
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 510..532
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 538..560
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 566..588
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT VAR_SEQ 44..76
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2023909"
FT /id="VSP_035771"
FT VAR_SEQ 77..87
FT /note="VMCSHFAQDLW -> ESYSVTQSGMQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042154"
FT VAR_SEQ 88..595
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042155"
FT VARIANT 60
FT /note="K -> T (in dbSNP:rs7254311)"
FT /id="VAR_033552"
FT VARIANT 84
FT /note="Q -> R (in dbSNP:rs56321708)"
FT /evidence="ECO:0000269|PubMed:2023909,
FT ECO:0000269|PubMed:9839802"
FT /id="VAR_061932"
FT VARIANT 115
FT /note="R -> I (in dbSNP:rs56231962)"
FT /evidence="ECO:0000269|PubMed:2023909"
FT /id="VAR_061933"
FT VARIANT 177
FT /note="T -> R (in dbSNP:rs56393308)"
FT /evidence="ECO:0000269|PubMed:2023909"
FT /id="VAR_061934"
FT VARIANT 184
FT /note="G -> R (in dbSNP:rs11665978)"
FT /evidence="ECO:0000269|PubMed:2023909"
FT /id="VAR_033553"
FT VARIANT 266
FT /note="T -> A (in dbSNP:rs1063156)"
FT /evidence="ECO:0000269|PubMed:9839802"
FT /id="VAR_047515"
FT VARIANT 270
FT /note="F -> S (in dbSNP:rs11670246)"
FT /id="VAR_033554"
FT CONFLICT 428
FT /note="C -> S (in Ref. 1; AAA79179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 68736 MW; F21FA8927C28DE90 CRC64;
MGPLTFRDVA IEFSLKEWQC LDTAQRNLYR NVMLENYRNL VFLGITVSKP DLITCLEQGK
EAWSMKRHEI MVAKPTVMCS HFAQDLWPEQ NIKDSFQKVT LKRYGKCRHE NLPLRKGCES
MDECKMHKGG CNGLNQCLTA TQSKIFQCDK YVKVAHKFSN SNRHEIRHTK KKPFKCTKCG
KSFGMISCLT EHSRIHTRVN FYKCEECGKA FNWSSTLTKH KRIHTGEKPY KCEECGKAFN
QSSNLIKHKK IHTGEKPYKC EECGKTFNRF STLTTHKIIH TGEKPYKCKE CGKAFNRSST
LTTHRKIHTG EKPYKCEECG KAFKQSSNLT THKIIHTGEK PYKCKKCGKA FNQSAHLTTH
EVIHTGEKPY KCEKCGKAFN HFSHLTTHKI IHTGEKPYKC KECGKAFKHS STLTKHKIIH
TGEKPYKCKE CEKAFNQSSK LTEHKKIHTG EKPYECEKCG KAFNQSSNLT RHKKSHTEEK
PYKCEECGKG FKWPSTLTIH KIIHTGEKPY KCEECGKAFN QSSKLTKHKK IHTGEKPYTC
EECGKAFNQS SNLTKHKRIH TGEKPYKCEE CDKAFKWSSV LTKHKIIHTG EKLQI
