ZN766_HUMAN
ID ZN766_HUMAN Reviewed; 468 AA.
AC Q5HY98; B2RNE0; Q7Z326;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Zinc finger protein 766;
GN Name=ZNF766;
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=Esophageal carcinoma, and Salivary gland;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75; LYS-157; LYS-179 AND LYS-367,
RP 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: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q5HY98; Q5TD97: FHL5; NbExp=3; IntAct=EBI-2686489, EBI-750641;
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=CAD98055.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX538183; CAD98055.1; ALT_INIT; mRNA.
DR EMBL; BX648899; CAI45991.1; -; mRNA.
DR EMBL; CH471135; EAW72068.1; -; Genomic_DNA.
DR EMBL; BC136833; AAI36834.1; -; mRNA.
DR EMBL; BC136834; AAI36835.1; -; mRNA.
DR CCDS; CCDS46163.1; -.
DR RefSeq; NP_001010851.1; NM_001010851.2.
DR AlphaFoldDB; Q5HY98; -.
DR SMR; Q5HY98; -.
DR BioGRID; 124692; 8.
DR IntAct; Q5HY98; 4.
DR STRING; 9606.ENSP00000409652; -.
DR iPTMnet; Q5HY98; -.
DR PhosphoSitePlus; Q5HY98; -.
DR BioMuta; ZNF766; -.
DR DMDM; 74755487; -.
DR EPD; Q5HY98; -.
DR jPOST; Q5HY98; -.
DR MassIVE; Q5HY98; -.
DR MaxQB; Q5HY98; -.
DR PaxDb; Q5HY98; -.
DR PeptideAtlas; Q5HY98; -.
DR PRIDE; Q5HY98; -.
DR ProteomicsDB; 62926; -.
DR Antibodypedia; 32582; 62 antibodies from 14 providers.
DR DNASU; 90321; -.
DR Ensembl; ENST00000439461.6; ENSP00000409652.1; ENSG00000196214.11.
DR GeneID; 90321; -.
DR KEGG; hsa:90321; -.
DR MANE-Select; ENST00000439461.6; ENSP00000409652.1; NM_001010851.3; NP_001010851.1.
DR UCSC; uc002pyr.2; human.
DR CTD; 90321; -.
DR GeneCards; ZNF766; -.
DR HGNC; HGNC:28063; ZNF766.
DR HPA; ENSG00000196214; Low tissue specificity.
DR neXtProt; NX_Q5HY98; -.
DR OpenTargets; ENSG00000196214; -.
DR PharmGKB; PA162410313; -.
DR VEuPathDB; HostDB:ENSG00000196214; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000165090; -.
DR HOGENOM; CLU_002678_0_9_1; -.
DR InParanoid; Q5HY98; -.
DR OMA; FREIREH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5HY98; -.
DR TreeFam; TF341892; -.
DR PathwayCommons; Q5HY98; -.
DR SignaLink; Q5HY98; -.
DR BioGRID-ORCS; 90321; 15 hits in 1096 CRISPR screens.
DR ChiTaRS; ZNF766; human.
DR GenomeRNAi; 90321; -.
DR Pharos; Q5HY98; Tdark.
DR PRO; PR:Q5HY98; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q5HY98; protein.
DR Bgee; ENSG00000196214; Expressed in sperm and 187 other tissues.
DR ExpressionAtlas; Q5HY98; baseline and differential.
DR Genevisible; Q5HY98; HS.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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; 9.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
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..468
FT /note="Zinc finger protein 766"
FT /id="PRO_0000280435"
FT DOMAIN 9..80
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 187..209
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 215..237
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 243..265
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 271..293
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 299..321
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 327..349
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..377
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 383..405
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 411..433
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 439..462
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 75
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 367
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 95
FT /note="C -> Y (in dbSNP:rs12462608)"
FT /id="VAR_052899"
FT CONFLICT 9
FT /note="L -> S (in Ref. 1; CAD98055)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 54507 MW; 7B44DD720845E9BA CRC64;
MAQLRRGHLT FRDVAIEFSQ EEWKCLDPVQ KALYRDVMLE NYRNLVSLGI CLPDLSIISM
MKQRTEPWTV ENEMKVAKNP DRWEGIKDIN TGRSCAVRSK AGNKPITNQL GLTFQLPLPE
LEIFQGEGKI YECNQVQKFI SHSSSVSPLQ RIYSGVKTHI FNKHRNDFVD FPLLSQEQKA
HIRRKPYECN EQGKVFRVSS SLPNHQVIHT ADKPNRCHEC GKTVRDKSGL AEHWRIRTGE
KPYKCKECGK LFNRIAYLAR HEKVHTGESP YKCNECGKVF SRITYLVRHQ KIHTREKPHK
CNKCGKVYSS SSYLAQHWRI HTGEKLYKCN KCGKEFSGHS SLTTHLLIHT GEKPYKCKEC
DKAFRHKFSL TVHQRNHNGE KPYKCHECGK VFTQVSHLAR HQKIHTGEKP YKCNECGKVF
TQNSHLANHQ RIHTGEKPYK CHVCGKVFRH SSWFVQHQRS VHERVLTN
