ZN785_HUMAN
ID ZN785_HUMAN Reviewed; 405 AA.
AC A8K8V0; O75701; Q8IW91; Q8WV14; Q96MN0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Zinc finger protein 785;
GN Name=ZNF785;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Peripheral blood monocyte, and Testis;
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].
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] (ISOFORM 1).
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 VARIANTS GLY-316 AND ARG-337.
RX PubMed=26063658; DOI=10.1093/brain/awv155;
RA Verdura E., Herve D., Scharrer E., del Mar Amador M., Guyant-Marechal L.,
RA Philippi A., Corlobe A., Bergametti F., Gazal S., Prieto-Morin C.,
RA Beaufort N., Le Bail B., Viakhireva I., Dichgans M., Chabriat H.,
RA Haffner C., Tournier-Lasserve E.;
RT "Heterozygous HTRA1 mutations are associated with autosomal dominant
RT cerebral small vessel disease.";
RL Brain 138:2347-2358(2015).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- INTERACTION:
CC A8K8V0; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-3925400, EBI-357530;
CC A8K8V0; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-3925400, EBI-12011224;
CC A8K8V0; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-3925400, EBI-11524851;
CC A8K8V0; O95273: CCNDBP1; NbExp=3; IntAct=EBI-3925400, EBI-748961;
CC A8K8V0; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-3925400, EBI-739624;
CC A8K8V0; A2ABF9: EHMT2; NbExp=3; IntAct=EBI-3925400, EBI-10174566;
CC A8K8V0; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-3925400, EBI-5916454;
CC A8K8V0; Q9UJC3: HOOK1; NbExp=3; IntAct=EBI-3925400, EBI-746704;
CC A8K8V0; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-3925400, EBI-14069005;
CC A8K8V0; O76013-2: KRT36; NbExp=3; IntAct=EBI-3925400, EBI-11958506;
CC A8K8V0; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-3925400, EBI-10172150;
CC A8K8V0; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-3925400, EBI-10176379;
CC A8K8V0; Q99750: MDFI; NbExp=3; IntAct=EBI-3925400, EBI-724076;
CC A8K8V0; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-3925400, EBI-10172526;
CC A8K8V0; Q5JR59: MTUS2; NbExp=4; IntAct=EBI-3925400, EBI-742948;
CC A8K8V0; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-3925400, EBI-11522433;
CC A8K8V0; Q9UL42: PNMA2; NbExp=3; IntAct=EBI-3925400, EBI-302355;
CC A8K8V0; Q16623: STX1A; NbExp=3; IntAct=EBI-3925400, EBI-712466;
CC A8K8V0; P32856-2: STX2; NbExp=3; IntAct=EBI-3925400, EBI-11956649;
CC A8K8V0; P07951-2: TPM2; NbExp=3; IntAct=EBI-3925400, EBI-10977815;
CC A8K8V0; Q15654: TRIP6; NbExp=3; IntAct=EBI-3925400, EBI-742327;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A8K8V0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A8K8V0-2; Sequence=VSP_034965;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK056692; BAB71256.1; -; mRNA.
DR EMBL; AK292465; BAF85154.1; -; mRNA.
DR EMBL; CH471192; EAW52231.1; -; Genomic_DNA.
DR EMBL; BC040642; AAH40642.1; -; mRNA.
DR CCDS; CCDS10685.1; -. [A8K8V0-1]
DR RefSeq; NP_689671.2; NM_152458.6. [A8K8V0-1]
DR RefSeq; XP_016878456.1; XM_017022967.1. [A8K8V0-1]
DR AlphaFoldDB; A8K8V0; -.
DR SMR; A8K8V0; -.
DR BioGRID; 126995; 110.
DR IntAct; A8K8V0; 86.
DR STRING; 9606.ENSP00000378642; -.
DR iPTMnet; A8K8V0; -.
DR PhosphoSitePlus; A8K8V0; -.
DR BioMuta; ZNF785; -.
DR MassIVE; A8K8V0; -.
DR PaxDb; A8K8V0; -.
DR PeptideAtlas; A8K8V0; -.
DR PRIDE; A8K8V0; -.
DR ProteomicsDB; 1888; -. [A8K8V0-1]
DR ProteomicsDB; 1889; -. [A8K8V0-2]
DR Antibodypedia; 27353; 188 antibodies from 25 providers.
DR DNASU; 146540; -.
DR Ensembl; ENST00000395216.3; ENSP00000378642.2; ENSG00000197162.10. [A8K8V0-1]
DR Ensembl; ENST00000470110.2; ENSP00000420340.1; ENSG00000197162.10. [A8K8V0-2]
DR GeneID; 146540; -.
DR KEGG; hsa:146540; -.
DR MANE-Select; ENST00000395216.3; ENSP00000378642.2; NM_152458.7; NP_689671.2.
DR UCSC; uc002dyv.3; human. [A8K8V0-1]
DR CTD; 146540; -.
DR DisGeNET; 146540; -.
DR GeneCards; ZNF785; -.
DR HGNC; HGNC:26496; ZNF785.
DR HPA; ENSG00000197162; Low tissue specificity.
DR neXtProt; NX_A8K8V0; -.
DR OpenTargets; ENSG00000197162; -.
DR PharmGKB; PA162410467; -.
DR VEuPathDB; HostDB:ENSG00000197162; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164477; -.
DR HOGENOM; CLU_002678_13_0_1; -.
DR InParanoid; A8K8V0; -.
DR OMA; GHLGALX; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; A8K8V0; -.
DR TreeFam; TF337922; -.
DR PathwayCommons; A8K8V0; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; A8K8V0; -.
DR BioGRID-ORCS; 146540; 13 hits in 1099 CRISPR screens.
DR ChiTaRS; ZNF785; human.
DR GenomeRNAi; 146540; -.
DR Pharos; A8K8V0; Tdark.
DR PRO; PR:A8K8V0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; A8K8V0; protein.
DR Bgee; ENSG00000197162; Expressed in buccal mucosa cell and 174 other tissues.
DR ExpressionAtlas; A8K8V0; baseline and differential.
DR Genevisible; A8K8V0; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
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; 6.
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 Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..405
FT /note="Zinc finger protein 785"
FT /id="PRO_0000345630"
FT DOMAIN 29..100
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 172..194
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 200..222
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 228..250
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 256..278
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 284..306
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 312..334
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 340..362
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 98..112
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034965"
FT VARIANT 316
FT /note="D -> G (in dbSNP:rs1391888354)"
FT /evidence="ECO:0000269|PubMed:26063658"
FT /id="VAR_076389"
FT VARIANT 337
FT /note="S -> R (in dbSNP:rs201574418)"
FT /evidence="ECO:0000269|PubMed:26063658"
FT /id="VAR_076390"
SQ SEQUENCE 405 AA; 46168 MW; 521391E814B117F0 CRC64;
MGPPLAPRPA HVPGEAGPRR TRESRPGAVS FADVAVYFSP EEWECLRPAQ RALYRDVMRE
TFGHLGALGF SVPKPAFISW VEGEVEAWSP EAQDPDGESS AAFSRGQGQE AGSRDGNEEK
ERLKKCPKQK EVAHEVAVKE WWPSVACPEF CNPRQSPMNP WLKDTLTRRL PHSCPDCGRN
FSYPSLLASH QRVHSGERPF SCGQCQARFS QRRYLLQHQF IHTGEKPYPC PDCGRRFRQR
GSLAIHRRAH TGEKPYACSD CKSRFTYPYL LAIHQRKHTG EKPYSCPDCS LRFAYTSLLA
IHRRIHTGEK PYPCPDCGRR FTYSSLLLSH RRIHSDSRPF PCVECGKGFK RKTALEAHRW
IHRSCSERRA WQQAVVGRSE PIPVLGGKDP PVHFRHFPDI FQECG
