ZFP3_HUMAN
ID ZFP3_HUMAN Reviewed; 502 AA.
AC Q96NJ6; A5PLL4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Zinc finger protein 3 homolog;
DE Short=Zfp-3;
DE AltName: Full=Zinc finger protein 752;
GN Name=ZFP3; Synonyms=ZNF752;
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=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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-11, AND IDENTIFICATION
RP 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 Q96NJ6; P13994: YJU2B; NbExp=5; IntAct=EBI-12302147, EBI-716093;
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; AK055288; BAB70898.1; -; mRNA.
DR EMBL; CH471108; EAW90362.1; -; Genomic_DNA.
DR EMBL; BC142962; AAI42963.1; -; mRNA.
DR CCDS; CCDS11067.1; -.
DR RefSeq; NP_694563.1; NM_153018.2.
DR AlphaFoldDB; Q96NJ6; -.
DR SMR; Q96NJ6; -.
DR BioGRID; 125904; 1.
DR IntAct; Q96NJ6; 1.
DR STRING; 9606.ENSP00000320347; -.
DR iPTMnet; Q96NJ6; -.
DR PhosphoSitePlus; Q96NJ6; -.
DR BioMuta; ZFP3; -.
DR DMDM; 74761006; -.
DR EPD; Q96NJ6; -.
DR jPOST; Q96NJ6; -.
DR MassIVE; Q96NJ6; -.
DR MaxQB; Q96NJ6; -.
DR PaxDb; Q96NJ6; -.
DR PeptideAtlas; Q96NJ6; -.
DR PRIDE; Q96NJ6; -.
DR ProteomicsDB; 77523; -.
DR Antibodypedia; 23592; 44 antibodies from 14 providers.
DR DNASU; 124961; -.
DR Ensembl; ENST00000318833.4; ENSP00000320347.3; ENSG00000180787.6.
DR GeneID; 124961; -.
DR KEGG; hsa:124961; -.
DR MANE-Select; ENST00000318833.4; ENSP00000320347.3; NM_153018.3; NP_694563.1.
DR UCSC; uc002gaq.4; human.
DR CTD; 124961; -.
DR DisGeNET; 124961; -.
DR GeneCards; ZFP3; -.
DR HGNC; HGNC:12861; ZFP3.
DR HPA; ENSG00000180787; Low tissue specificity.
DR MIM; 194480; gene.
DR neXtProt; NX_Q96NJ6; -.
DR OpenTargets; ENSG00000180787; -.
DR PharmGKB; PA37450; -.
DR VEuPathDB; HostDB:ENSG00000180787; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162652; -.
DR HOGENOM; CLU_002678_52_2_1; -.
DR InParanoid; Q96NJ6; -.
DR OMA; YHECSEC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q96NJ6; -.
DR TreeFam; TF337005; -.
DR PathwayCommons; Q96NJ6; -.
DR SignaLink; Q96NJ6; -.
DR BioGRID-ORCS; 124961; 7 hits in 1090 CRISPR screens.
DR ChiTaRS; ZFP3; human.
DR GenomeRNAi; 124961; -.
DR Pharos; Q96NJ6; Tdark.
DR PRO; PR:Q96NJ6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96NJ6; protein.
DR Bgee; ENSG00000180787; Expressed in cardiac muscle of right atrium and 160 other tissues.
DR Genevisible; Q96NJ6; 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: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: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; 12.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
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..502
FT /note="Zinc finger protein 3 homolog"
FT /id="PRO_0000233713"
FT ZN_FING 141..163
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 169..191
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 197..219
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 225..247
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 253..275
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 281..303
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 309..331
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 337..359
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 365..387
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 393..415
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 421..443
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 449..471
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 477..499
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 502 AA; 57662 MW; FFA5DF474A5059A4 CRC64;
MGTENKEVIP KEEISEESEP HGSLLEKFPK VVYQGHEFGA GCEEDMLEGH SRESMEEVIE
QMSPQERDFP SGLMIFKKSP SSEKDRENNE SERGCSPSPN LVTHQGDTTE GVSAFATSGQ
NFLEILESNK TQRSSVGEKP HTCKECGKAF NQNSHLIQHM RVHSGEKPFE CKECGKTFGT
NSSLRRHLRI HAGEKPFACN ECGKAFIQSS HLIHHHRIHT GERPYKCEEC GKAFSQNSAL
ILHQRIHTGE KPYECNECGK TFRVSSQLIQ HQRIHTEERY HECNECGKAF KHSSGLIRHQ
KIHTGEKPYL CNECGKGFGQ SSELIRHQRI HTGDKPYECN ECGKTFGQNS EIIRHIRIHT
GEKPYVCKEC GKAFRGNSEL LRHERIHTGE KPYECFECGK AFRRTSHLIV HQRIHTGEKP
HQCNECARTF WDNSELLLHQ KIHIGEKPYE CSECEKTFSQ HSQLIIHQRI HTGEKPYECQ
ECQKTFSRSS HLLRHQSVHC ME
