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 27-MAR-2024, entry version 167. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 3. DR IntAct; Q96NJ6; 2. DR STRING; 9606.ENSP00000320347; -. DR GlyGen; Q96NJ6; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000320347; -. DR PeptideAtlas; Q96NJ6; -. DR ProteomicsDB; 77523; -. DR Antibodypedia; 23592; 55 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 AGR; HGNC:12861; -. 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; 3884582at2759; -. DR PhylomeDB; Q96NJ6; -. DR TreeFam; TF337005; -. DR PathwayCommons; Q96NJ6; -. DR SignaLink; Q96NJ6; -. DR BioGRID-ORCS; 124961; 8 hits in 1177 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 162 other cell types or tissues. 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 Gene3D; 3.30.160.60; Classic Zinc Finger; 13. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23226; ZINC FINGER AND SCAN DOMAIN-CONTAINING; 1. DR PANTHER; PTHR23226:SF416; ZINC FINGER PROTEIN 46; 1. DR Pfam; PF00096; zf-C2H2; 12. DR SMART; SM00355; ZnF_C2H2; 13. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 13. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13. DR Genevisible; Q96NJ6; HS. 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 //