ZN765_HUMAN
ID ZN765_HUMAN Reviewed; 523 AA.
AC Q7L2R6; A8MYG0; B4DF18; B7ZAI5; B9EIL1; Q9BV49;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Zinc finger protein 765;
GN Name=ZNF765;
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] (ISOFORM 1), AND VARIANT GLY-389.
RC TISSUE=Cerebellum, and Placenta;
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 [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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLY-389.
RC TISSUE=Lymph;
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 [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-205, AND IDENTIFICATION BY MASS
RP 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 Q7L2R6; Q86Y13: DZIP3; NbExp=3; IntAct=EBI-9676069, EBI-948630;
CC Q7L2R6; Q04864: REL; NbExp=3; IntAct=EBI-9676069, EBI-307352;
CC Q7L2R6; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-9676069, EBI-739895;
CC Q7L2R6-2; Q03989: ARID5A; NbExp=3; IntAct=EBI-12834294, EBI-948603;
CC Q7L2R6-2; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-12834294, EBI-953896;
CC Q7L2R6-2; Q6IPU0: CENPP; NbExp=3; IntAct=EBI-12834294, EBI-10250303;
CC Q7L2R6-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-12834294, EBI-742054;
CC Q7L2R6-2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-12834294, EBI-6509505;
CC Q7L2R6-2; P59942: MCCD1; NbExp=3; IntAct=EBI-12834294, EBI-11987923;
CC Q7L2R6-2; P32243-2: OTX2; NbExp=3; IntAct=EBI-12834294, EBI-9087860;
CC Q7L2R6-2; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-12834294, EBI-6257312;
CC Q7L2R6-2; Q86WV8: TSC1; NbExp=3; IntAct=EBI-12834294, EBI-12806590;
CC Q7L2R6-2; Q9BRT2: UQCC2; NbExp=3; IntAct=EBI-12834294, EBI-1054584;
CC Q7L2R6-2; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-12834294, EBI-745520;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7L2R6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7L2R6-2; Sequence=VSP_034746, VSP_034747;
CC Name=3;
CC IsoId=Q7L2R6-3; Sequence=VSP_055629, VSP_055630;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK293890; BAG57279.1; -; mRNA.
DR EMBL; AK316300; BAH14671.1; -; mRNA.
DR EMBL; AC022137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72134.1; -; Genomic_DNA.
DR EMBL; BC001610; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC017357; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC140724; AAI40725.1; -; mRNA.
DR CCDS; CCDS46171.1; -. [Q7L2R6-1]
DR RefSeq; NP_001035275.1; NM_001040185.1. [Q7L2R6-1]
DR AlphaFoldDB; Q7L2R6; -.
DR SMR; Q7L2R6; -.
DR BioGRID; 124860; 25.
DR IntAct; Q7L2R6; 16.
DR MINT; Q7L2R6; -.
DR STRING; 9606.ENSP00000379689; -.
DR iPTMnet; Q7L2R6; -.
DR PhosphoSitePlus; Q7L2R6; -.
DR BioMuta; ZNF765; -.
DR DMDM; 205639967; -.
DR EPD; Q7L2R6; -.
DR jPOST; Q7L2R6; -.
DR MassIVE; Q7L2R6; -.
DR MaxQB; Q7L2R6; -.
DR PaxDb; Q7L2R6; -.
DR PeptideAtlas; Q7L2R6; -.
DR PRIDE; Q7L2R6; -.
DR ProteomicsDB; 68766; -. [Q7L2R6-1]
DR ProteomicsDB; 68767; -. [Q7L2R6-2]
DR TopDownProteomics; Q7L2R6-2; -. [Q7L2R6-2]
DR Antibodypedia; 32701; 73 antibodies from 13 providers.
DR DNASU; 91661; -.
DR Ensembl; ENST00000396408.8; ENSP00000379689.3; ENSG00000196417.13. [Q7L2R6-1]
DR Ensembl; ENST00000504235.5; ENSP00000424395.1; ENSG00000196417.13. [Q7L2R6-2]
DR Ensembl; ENST00000594030.2; ENSP00000470468.1; ENSG00000196417.13. [Q7L2R6-2]
DR GeneID; 91661; -.
DR KEGG; hsa:91661; -.
DR MANE-Select; ENST00000396408.8; ENSP00000379689.3; NM_001040185.3; NP_001035275.1.
DR UCSC; uc002qbm.4; human. [Q7L2R6-1]
DR CTD; 91661; -.
DR DisGeNET; 91661; -.
DR GeneCards; ZNF765; -.
DR HGNC; HGNC:25092; ZNF765.
DR HPA; ENSG00000196417; Low tissue specificity.
DR neXtProt; NX_Q7L2R6; -.
DR OpenTargets; ENSG00000196417; -.
DR OpenTargets; ENSG00000204604; -.
DR PharmGKB; PA162410312; -.
DR VEuPathDB; HostDB:ENSG00000196417; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154397; -.
DR HOGENOM; CLU_002678_69_15_1; -.
DR InParanoid; Q7L2R6; -.
DR OMA; FTCHHRV; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q7L2R6; -.
DR TreeFam; TF341892; -.
DR PathwayCommons; Q7L2R6; -.
DR SignaLink; Q7L2R6; -.
DR BioGRID-ORCS; 91661; 11 hits in 1028 CRISPR screens.
DR GenomeRNAi; 91661; -.
DR Pharos; Q7L2R6; Tdark.
DR PRO; PR:Q7L2R6; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q7L2R6; protein.
DR Bgee; ENSG00000196417; Expressed in oocyte and 183 other tissues.
DR ExpressionAtlas; Q7L2R6; baseline and differential.
DR Genevisible; Q7L2R6; 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; 11.
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; 11.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..523
FT /note="Zinc finger protein 765"
FT /id="PRO_0000344217"
FT DOMAIN 8..81
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 215..237
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 243..265
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 271..293
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 299..321
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 327..349
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..377
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 383..405
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 411..432
FT /note="C2H2-type 8; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 438..460
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 466..488
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 494..516
FT /note="C2H2-type 11; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 48..127
FT /note="DISSKCMMKEFSSTAQGNREVFHAGTSQRHESHHNGDFCFQDIDKDIHDIEF
FT QWQEDERNGHEALMTKIKKLTGSTERYD -> EFWSVIPAKVQWCHLRSLQPPLPRFKQ
FT FSCLSLPSTWDYRYLFQMHVEDVVVNRARQYRSDPHRDIAQTSKSSHWRILFP (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_055629"
FT VAR_SEQ 48..60
FT /note="DISSKCMMKEFSS -> ELSGECPLAAPAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034746"
FT VAR_SEQ 61..523
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034747"
FT VAR_SEQ 128..523
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_055630"
FT VARIANT 389
FT /note="S -> G (in dbSNP:rs10425136)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_045598"
FT CONFLICT 61
FT /note="T -> A (in Ref. 1; BAG57279)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="Q -> R (in Ref. 1; BAG57279)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="K -> N (in Ref. 1; BAG57279)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="K -> E (in Ref. 1; BAG57279)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="P -> L (in Ref. 1; BAG57279)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="Y -> N (in Ref. 1; BAH14671)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 61633 MW; AF353F9210751258 CRC64;
MALPQGLLTF RDVAIEFSQE EWKCLDPAQR TLYRDVMLEN YRNLVSLDIS SKCMMKEFSS
TAQGNREVFH AGTSQRHESH HNGDFCFQDI DKDIHDIEFQ WQEDERNGHE ALMTKIKKLT
GSTERYDQNY AGNKPVKYQL GFSFHSHLPE LHIFHTEEKI DNQVVKSIHD ASLVSTAQRI
SCRPETHISN DYGNNFLNSS LFTQKQEVHM REKSFQCNDS GKAYNCSSLL RKHQLIHLGE
KQYKCDICGK VFNSKRYVAR HRRCHTGEKP YKCNECGKTF SQTYYLTCHR RLHTGEKPYK
CEECDKAFHF KSKLQIHRRI HTGEKPYKCN ECGKTFSQKS YLTCHRRLHT GEKPYKCNEC
GKTFSRKSHF TCHHRVHTGE KPYKCNECSK TFSHKSSLTY HRRLHTEEKP YKCNECGKTF
NQQLTLNICR LHSGEKPYKC EECDKAYSFK SNLEIHQKIH TEENPYKCNE CGKTFSRTSS
LTYHHRLHTG QKPYKCEDCD EAFSFKSNLE RHRRIYTGEK LHV
