ZNF84_HUMAN
ID ZNF84_HUMAN Reviewed; 738 AA.
AC P51523; B2RAK5; D3DXJ1; Q3ZCV9; Q5D057; Q86XU8; Q9NNX7; Q9UC17; Q9UC18;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Zinc finger protein 84;
DE AltName: Full=Zinc finger protein HPF2;
GN Name=ZNF84;
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 [MRNA].
RC TISSUE=Placenta;
RX PubMed=2505992; DOI=10.1089/dna.1.1989.8.377;
RA Bellefroid E.J., Lecocq P.J., Benhida A., Poncelet D.A., Belayew A.,
RA Martial J.A.;
RT "The human genome contains hundreds of genes coding for finger proteins of
RT the Kruppel type.";
RL DNA 8:377-387(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Grimaldi G.;
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Testis, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-257.
RC TISSUE=Teratocarcinoma;
RX PubMed=1945843; DOI=10.1093/nar/19.20.5661;
RA Rosati M., Marino M., Franze A., Tramontano A., Grimaldi G.;
RT "Members of the zinc finger protein gene family sharing a conserved N-
RT terminal module.";
RL Nucleic Acids Res. 19:5661-5667(1991).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-112; LYS-125; LYS-191 AND
RP LYS-457, 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 P51523; O75031: HSF2BP; NbExp=3; IntAct=EBI-2849074, EBI-7116203;
CC P51523; P25800: LMO1; NbExp=3; IntAct=EBI-2849074, EBI-8639312;
CC P51523; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2849074, EBI-11742507;
CC P51523; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-2849074, EBI-12023934;
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; M27878; AAA79359.1; -; mRNA.
DR EMBL; X60156; CAB94232.2; -; mRNA.
DR EMBL; AK314232; BAG36902.1; -; mRNA.
DR EMBL; CH471218; EAW54799.1; -; Genomic_DNA.
DR EMBL; CH471218; EAW54801.1; -; Genomic_DNA.
DR EMBL; CH471218; EAW54802.1; -; Genomic_DNA.
DR EMBL; BC036656; AAH36656.1; -; mRNA.
DR EMBL; BC048350; AAH48350.2; -; mRNA.
DR EMBL; BC062552; AAH62552.1; -; mRNA.
DR CCDS; CCDS31940.1; -.
DR PIR; B32891; B32891.
DR RefSeq; NP_001120844.1; NM_001127372.2.
DR RefSeq; NP_001276900.1; NM_001289971.1.
DR RefSeq; NP_001276901.1; NM_001289972.1.
DR RefSeq; NP_003419.3; NM_003428.5.
DR RefSeq; XP_005266242.1; XM_005266185.1.
DR RefSeq; XP_005266243.1; XM_005266186.1.
DR RefSeq; XP_011533134.1; XM_011534832.1.
DR AlphaFoldDB; P51523; -.
DR SMR; P51523; -.
DR BioGRID; 113453; 8.
DR IntAct; P51523; 11.
DR MINT; P51523; -.
DR STRING; 9606.ENSP00000331465; -.
DR iPTMnet; P51523; -.
DR PhosphoSitePlus; P51523; -.
DR BioMuta; ZNF84; -.
DR DMDM; 94730445; -.
DR EPD; P51523; -.
DR jPOST; P51523; -.
DR MassIVE; P51523; -.
DR MaxQB; P51523; -.
DR PaxDb; P51523; -.
DR PeptideAtlas; P51523; -.
DR PRIDE; P51523; -.
DR ProteomicsDB; 56321; -.
DR Antibodypedia; 19535; 33 antibodies from 14 providers.
DR DNASU; 7637; -.
DR Ensembl; ENST00000327668.11; ENSP00000331465.7; ENSG00000198040.11.
DR Ensembl; ENST00000392319.6; ENSP00000376133.2; ENSG00000198040.11.
DR Ensembl; ENST00000539354.6; ENSP00000445549.1; ENSG00000198040.11.
DR GeneID; 7637; -.
DR KEGG; hsa:7637; -.
DR MANE-Select; ENST00000539354.6; ENSP00000445549.1; NM_001289971.2; NP_001276900.1.
DR UCSC; uc001ulm.5; human.
DR CTD; 7637; -.
DR DisGeNET; 7637; -.
DR GeneCards; ZNF84; -.
DR HGNC; HGNC:13159; ZNF84.
DR HPA; ENSG00000198040; Low tissue specificity.
DR MIM; 618554; gene.
DR neXtProt; NX_P51523; -.
DR OpenTargets; ENSG00000198040; -.
DR PharmGKB; PA37732; -.
DR VEuPathDB; HostDB:ENSG00000198040; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162931; -.
DR InParanoid; P51523; -.
DR OMA; YEVMKPG; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P51523; -.
DR TreeFam; TF337898; -.
DR PathwayCommons; P51523; -.
DR SignaLink; P51523; -.
DR BioGRID-ORCS; 7637; 40 hits in 1090 CRISPR screens.
DR ChiTaRS; ZNF84; human.
DR GenomeRNAi; 7637; -.
DR Pharos; P51523; Tdark.
DR PRO; PR:P51523; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P51523; protein.
DR Bgee; ENSG00000198040; Expressed in cortical plate and 196 other tissues.
DR ExpressionAtlas; P51523; baseline and differential.
DR Genevisible; P51523; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
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; 16.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 19.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 19.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 19.
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..738
FT /note="Zinc finger protein 84"
FT /id="PRO_0000047397"
FT DOMAIN 8..79
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 207..229
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 235..257
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 263..285
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 291..313
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 319..341
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 347..369
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 375..397
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 403..425
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 431..453
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 459..481
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 487..509
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 515..537
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 543..565
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 571..593
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 599..621
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 627..649
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 655..677
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 683..705
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 711..733
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 457
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 62
FT /note="Q -> E (in Ref. 1; AAA79359)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="T -> A (in Ref. 5; AAH36656)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 738 AA; 85457 MW; E682053680438D5F CRC64;
MTMLQESFSF DDLSVDFTQK EWQLLDPSQK NLYKDVMLEN YSSLVSLGYE VMKPDVIFKL
EQGEEPWVGD GEIPSSDSPE VWKVDGNMMW HQDNQDKLKI IKRGHECDAF GKNFNLNMNF
VPLRKSNSEG DLDGLILKHH LDLLIPKGDY GKAESDDFNV FDNFFLHSKP EDTDTWLKYY
DCDKYKESYK KSQIIIYHRN RLGEKLYECS ECRKRFSKKP SLIKHQSRHI RDIAFGCGNC
GKTFPQKSQF ITHHRTHTGE KPYNCSQCGK AFSQKSQLTS HQRTHTGEKP YECGECGKAF
SRKSHLISHW RTHTGEKPYG CNECGRAFSE KSNLINHQRI HTGEKPFECR ECGKAFSRKS
QLVTHHRTHT GTKPFGCSDC RKAFFEKSEL IRHQTIHTGE KPYECSECRK AFRERSSLIN
HQRTHTGEKP HGCIQCGKAF SQKSHLISHQ MTHTGEKPFI CSKCGKAFSR KSQLVRHQRT
HTGEKPYECS ECGKAFSEKL SLTNHQRIHT GEKPYVCSEC GKAFCQKSHL ISHQRTHTGE
KPYECSECGK AFGEKSSLAT HQRTHTGEKP YECRDCEKAF SQKSQLNTHQ RIHTGEKPYE
CSLCRKAFFE KSELIRHLRT HTGEKPYECN ECRKAFREKS SLINHQRIHT GEKPFECSEC
GKAFSRKSHL IPHQRTHTGE KPYGCSECRK AFSQKSQLVN HQRIHTGEKP YRCIECGKAF
SQKSQLINHQ RTHTVKKS
