ZN784_HUMAN
ID ZN784_HUMAN Reviewed; 323 AA.
AC Q8NCA9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Zinc finger protein 784;
GN Name=ZNF784;
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=Teratocarcinoma;
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 MRNA].
RC TISSUE=PNS;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [4]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-318, 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-318, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-318, 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.
CC -!- INTERACTION:
CC Q8NCA9; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-7138303, EBI-2556193;
CC Q8NCA9; Q99750: MDFI; NbExp=3; IntAct=EBI-7138303, EBI-724076;
CC Q8NCA9; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-7138303, EBI-10172526;
CC Q8NCA9; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-7138303, EBI-10226430;
CC Q8NCA9; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-7138303, EBI-3650647;
CC Q8NCA9; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-7138303, EBI-725997;
CC Q8NCA9; Q6PF05: TTC23L; NbExp=3; IntAct=EBI-7138303, EBI-8656864;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK074859; BAC11251.1; -; mRNA.
DR EMBL; BC065822; AAH65822.1; -; mRNA.
DR CCDS; CCDS12930.1; -.
DR RefSeq; NP_976308.1; NM_203374.1.
DR AlphaFoldDB; Q8NCA9; -.
DR SMR; Q8NCA9; -.
DR BioGRID; 127091; 32.
DR IntAct; Q8NCA9; 11.
DR MINT; Q8NCA9; -.
DR STRING; 9606.ENSP00000320096; -.
DR iPTMnet; Q8NCA9; -.
DR PhosphoSitePlus; Q8NCA9; -.
DR BioMuta; ZNF784; -.
DR DMDM; 74760138; -.
DR EPD; Q8NCA9; -.
DR MassIVE; Q8NCA9; -.
DR MaxQB; Q8NCA9; -.
DR PaxDb; Q8NCA9; -.
DR PeptideAtlas; Q8NCA9; -.
DR PRIDE; Q8NCA9; -.
DR ProteomicsDB; 72867; -.
DR Antibodypedia; 46462; 29 antibodies from 12 providers.
DR DNASU; 147808; -.
DR Ensembl; ENST00000325351.5; ENSP00000320096.2; ENSG00000179922.6.
DR GeneID; 147808; -.
DR KEGG; hsa:147808; -.
DR MANE-Select; ENST00000325351.5; ENSP00000320096.2; NM_203374.2; NP_976308.1.
DR UCSC; uc002qll.2; human.
DR CTD; 147808; -.
DR GeneCards; ZNF784; -.
DR HGNC; HGNC:33111; ZNF784.
DR HPA; ENSG00000179922; Tissue enhanced (skeletal).
DR neXtProt; NX_Q8NCA9; -.
DR OpenTargets; ENSG00000179922; -.
DR PharmGKB; PA162410458; -.
DR VEuPathDB; HostDB:ENSG00000179922; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162820; -.
DR HOGENOM; CLU_055458_0_0_1; -.
DR InParanoid; Q8NCA9; -.
DR OMA; DLLFHEH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8NCA9; -.
DR TreeFam; TF337573; -.
DR PathwayCommons; Q8NCA9; -.
DR SignaLink; Q8NCA9; -.
DR BioGRID-ORCS; 147808; 15 hits in 1096 CRISPR screens.
DR ChiTaRS; ZNF784; human.
DR GenomeRNAi; 147808; -.
DR Pharos; Q8NCA9; Tdark.
DR PRO; PR:Q8NCA9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8NCA9; protein.
DR Bgee; ENSG00000179922; Expressed in hindlimb stylopod muscle and 98 other tissues.
DR ExpressionAtlas; Q8NCA9; baseline and differential.
DR Genevisible; Q8NCA9; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator 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:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..323
FT /note="Zinc finger protein 784"
FT /id="PRO_0000270996"
FT ZN_FING 65..87
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 101..123
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 129..151
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 196..218
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 224..246
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 252..274
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 318
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
SQ SEQUENCE 323 AA; 34237 MW; FB7FD1019F8B86D6 CRC64;
MAAARPEAQS RSSPTPESRS QEPLDLVLVP DDCRPGTPPS DLIEIQVVKV TDTTLVPEPP
EPGSFHCALC PAAFRLVSEL LFHEHGHLAG AEGGGQGGDP SRCHVCGHSC PGPASLRAHY
SLHTGERPYR CALCPRAFKA LAPLLRHQHR HGVEPGTSRR PPDTAAVAEQ RPGVAPERAE
VVMAAAAAGA AVGKPFACRF CAKPFRRSSD MRDHERVHTG ERPYHCGICG KGFTQSSVLS
GHARIHTGER PFRCTLCDRT FNNSSNFRKH QRTHFHGPGP GLGDSGGQLG SSAAEGSGSG
CGVGDPAEEG RGETAKVKVE ADQ
