ZN776_HUMAN
ID ZN776_HUMAN Reviewed; 518 AA.
AC Q68DI1; Q6ZS36; Q8N968;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Zinc finger protein 776;
GN Name=ZNF776;
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=Prostate;
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].
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] OF 32-518.
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-196, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-171; LYS-196; LYS-220 AND
RP LYS-247, 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. {ECO:0000250}.
CC -!- INTERACTION:
CC Q68DI1; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-12878746, EBI-12012928;
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=BAC04588.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=BAC87119.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR749390; CAH18239.1; -; mRNA.
DR EMBL; AC003006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK127764; BAC87119.1; ALT_INIT; mRNA.
DR EMBL; AK095607; BAC04588.1; ALT_SEQ; mRNA.
DR CCDS; CCDS12962.2; -.
DR RefSeq; NP_001334936.1; NM_001348007.1.
DR RefSeq; NP_775903.3; NM_173632.3.
DR AlphaFoldDB; Q68DI1; -.
DR SMR; Q68DI1; -.
DR BioGRID; 129824; 15.
DR IntAct; Q68DI1; 1.
DR STRING; 9606.ENSP00000321812; -.
DR iPTMnet; Q68DI1; -.
DR PhosphoSitePlus; Q68DI1; -.
DR BioMuta; ZNF776; -.
DR DMDM; 296453057; -.
DR MassIVE; Q68DI1; -.
DR MaxQB; Q68DI1; -.
DR PaxDb; Q68DI1; -.
DR PeptideAtlas; Q68DI1; -.
DR PRIDE; Q68DI1; -.
DR ProteomicsDB; 66081; -.
DR Antibodypedia; 33289; 81 antibodies from 14 providers.
DR DNASU; 284309; -.
DR Ensembl; ENST00000317178.10; ENSP00000321812.5; ENSG00000152443.13.
DR GeneID; 284309; -.
DR KEGG; hsa:284309; -.
DR MANE-Select; ENST00000317178.10; ENSP00000321812.5; NM_173632.4; NP_775903.3.
DR UCSC; uc002qqa.3; human.
DR CTD; 284309; -.
DR GeneCards; ZNF776; -.
DR HGNC; HGNC:26765; ZNF776.
DR HPA; ENSG00000152443; Low tissue specificity.
DR neXtProt; NX_Q68DI1; -.
DR OpenTargets; ENSG00000152443; -.
DR PharmGKB; PA162410382; -.
DR VEuPathDB; HostDB:ENSG00000152443; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164345; -.
DR HOGENOM; CLU_002678_0_2_1; -.
DR InParanoid; Q68DI1; -.
DR OMA; MSHEPFI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q68DI1; -.
DR TreeFam; TF342033; -.
DR PathwayCommons; Q68DI1; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q68DI1; -.
DR BioGRID-ORCS; 284309; 9 hits in 1084 CRISPR screens.
DR ChiTaRS; ZNF776; human.
DR GenomeRNAi; 284309; -.
DR Pharos; Q68DI1; Tdark.
DR PRO; PR:Q68DI1; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q68DI1; protein.
DR Bgee; ENSG00000152443; Expressed in endothelial cell and 186 other tissues.
DR ExpressionAtlas; Q68DI1; baseline and differential.
DR Genevisible; Q68DI1; 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; 9.
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; 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..518
FT /note="Zinc finger protein 776"
FT /id="PRO_0000305140"
FT DOMAIN 14..89
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 208..230
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 236..258
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 264..286
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 292..314
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 320..342
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 348..370
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 376..398
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 404..426
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 432..454
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 460..482
FT /note="C2H2-type 10; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 488..510
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 196
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 247
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 183
FT /note="E -> V (in Ref. 1; CAH18239)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="C -> R (in Ref. 1; CAH18239)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="H -> R (in Ref. 3; BAC04588)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 59613 MW; 53CD86B2636EE04B CRC64;
MAAAALRPPA QGTVTFEDVA VNFSQEEWSL LSEAQRCLYH DVMLENLTLI SSLGCWYGAK
DETPSKQTLS IQQESPLRTH WTGVCTKKVH LWGMCGPLLG DILHQGTQHN QKLNGFGAYE
KKLDDDANHH QDQKQHIGEK SYRSNAKGTS FVKNCKFHMS HEPFIFHEVG KDFLSSLRLL
QQEDIHTSGK SNFETKHGIP LQGGKTHYIC GESTIPFSNK HSLVLHQRLL PREGPYVCSD
SGKFTSKSNS FNNHQGVRTG KRPYQCGQCD ESFWYKAHLT EHQRVHTGER PYECGECDKS
FSHKHSLVDH QRVHTGERPY ECDECGKSFS HKRSLVHHQR VHTGERPYQC GECGKSFNHK
CNLIQHQRVH TGERPFECTA CGKLFRSNSH LKEHQRVHTG ERPYECKECR KSFRYKSHLT
EHQRVHTGER PYECRECGKC FHQKGSLIQH QQIHSGERPH ECGECGKCFH QKGSLIRHQQ
IHSGERPHEC GECGKCFRQK GNLIKHQRVH TGERHHEC