ID ZNF3_HUMAN Reviewed; 446 AA. AC P17036; D6W5U0; P13683; Q9HBR4; Q9NNX8; Q9NXJ1; Q9UC15; Q9UC16; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2004, sequence version 3. DT 27-MAR-2024, entry version 230. DE RecName: Full=Zinc finger protein 3; DE AltName: Full=Zinc finger protein HF.12; DE AltName: Full=Zinc finger protein HZF3.1; DE AltName: Full=Zinc finger protein KOX25; GN Name=ZNF3; Synonyms=KOX25; 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] (ISOFORM 2). RA Gu J.R., Wan D.F., Zhao X.T., Zhou X.M., Jiang H.Q., Zhang P.P., Qin W.X., RA Huang Y., Qiu X.K., Qian L.F., He L.P., Li H.N., Yu Y., Yu J., Han L.H.; RT "Novel Human cDNA clones with function of inhibiting cancer cell growth."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-387 (ISOFORM 1). RC TISSUE=Colon mucosa; 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Ovary, and Skin; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-250 (ISOFORM 1). 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 340-395. RC TISSUE=Lymphoid tissue; RX PubMed=2288909; RA Thiesen H.-J.; RT "Multiple genes encoding zinc finger domains are expressed in human T RT cells."; RL New Biol. 2:363-374(1990). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 252-446. RC TISSUE=Placenta; RX PubMed=3380682; DOI=10.1093/nar/16.10.4227; RA Pannuti A., Lanfrancone L., Pascucci A., Pelicci P.-G., la Mantia G., RA Lania L.; RT "Isolation of cDNAs encoding finger proteins and measurement of the RT corresponding mRNA levels during myeloid terminal differentiation."; RL Nucleic Acids Res. 16:4227-4237(1988). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-419, 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 [10] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-151, 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 [11] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-125; LYS-151; LYS-163; LYS-173; RP LYS-422 AND LYS-431, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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: Involved in cell differentiation and/or proliferation. CC -!- INTERACTION: CC P17036; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1640965, EBI-618309; CC P17036; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-1640965, EBI-3044087; CC P17036; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-1640965, EBI-1216080; CC P17036; P23508: MCC; NbExp=3; IntAct=EBI-1640965, EBI-307531; CC P17036; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-1640965, EBI-742948; CC P17036; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-1640965, EBI-928842; CC P17036; Q15427: SF3B4; NbExp=3; IntAct=EBI-1640965, EBI-348469; CC P17036; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-1640965, EBI-2212028; CC P17036; Q9BUZ4: TRAF4; NbExp=8; IntAct=EBI-1640965, EBI-3650647; CC P17036; P13994: YJU2B; NbExp=5; IntAct=EBI-1640965, EBI-716093; CC P17036; Q9UDV6: ZNF212; NbExp=4; IntAct=EBI-1640965, EBI-1640204; CC P17036; P17036: ZNF3; NbExp=2; IntAct=EBI-1640965, EBI-1640965; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P17036-1; Sequence=Displayed; CC Name=2; CC IsoId=P17036-2; Sequence=VSP_041156; 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; AF217988; AAG17231.1; -; mRNA. DR EMBL; AF193057; AAG22485.1; -; mRNA. DR EMBL; AK000223; BAA91019.1; -; mRNA. DR EMBL; AK297625; BAH12633.1; -; mRNA. DR EMBL; CH471091; EAW76605.1; -; Genomic_DNA. DR EMBL; CH471091; EAW76606.1; -; Genomic_DNA. DR EMBL; CH471091; EAW76608.1; -; Genomic_DNA. DR EMBL; BC011887; AAH11887.2; -; mRNA. DR EMBL; BC013603; AAH13603.2; -; mRNA. DR EMBL; X60153; CAB94195.1; -; mRNA. DR EMBL; X52356; CAA36582.1; -; mRNA. DR EMBL; X07290; CAA30269.1; -; mRNA. DR CCDS; CCDS43618.1; -. [P17036-2] DR CCDS; CCDS43619.1; -. [P17036-1] DR PIR; S00754; S00754. DR RefSeq; NP_001265213.1; NM_001278284.1. [P17036-1] DR RefSeq; NP_001265216.1; NM_001278287.1. [P17036-1] DR RefSeq; NP_001265219.1; NM_001278290.1. [P17036-1] DR RefSeq; NP_001305064.1; NM_001318135.1. [P17036-1] DR RefSeq; NP_001305065.1; NM_001318136.1. DR RefSeq; NP_001305066.1; NM_001318137.1. DR RefSeq; NP_060185.2; NM_017715.3. [P17036-2] DR RefSeq; NP_116313.3; NM_032924.4. [P17036-1] DR AlphaFoldDB; P17036; -. DR SMR; P17036; -. DR BioGRID; 113383; 30. DR IntAct; P17036; 23. DR STRING; 9606.ENSP00000306372; -. DR iPTMnet; P17036; -. DR PhosphoSitePlus; P17036; -. DR BioMuta; ZNF3; -. DR DMDM; 46577682; -. DR EPD; P17036; -. DR jPOST; P17036; -. DR MassIVE; P17036; -. DR MaxQB; P17036; -. DR PaxDb; 9606-ENSP00000306372; -. DR PeptideAtlas; P17036; -. DR ProteomicsDB; 53438; -. [P17036-1] DR ProteomicsDB; 53439; -. [P17036-2] DR Pumba; P17036; -. DR Antibodypedia; 832; 140 antibodies from 22 providers. DR DNASU; 7551; -. DR Ensembl; ENST00000299667.9; ENSP00000299667.4; ENSG00000166526.19. [P17036-1] DR Ensembl; ENST00000413658.6; ENSP00000399951.2; ENSG00000166526.19. [P17036-2] DR Ensembl; ENST00000424697.5; ENSP00000415358.1; ENSG00000166526.19. [P17036-1] DR GeneID; 7551; -. DR KEGG; hsa:7551; -. DR MANE-Select; ENST00000299667.9; ENSP00000299667.4; NM_032924.5; NP_116313.3. DR UCSC; uc003usp.5; human. [P17036-1] DR AGR; HGNC:13089; -. DR CTD; 7551; -. DR DisGeNET; 7551; -. DR GeneCards; ZNF3; -. DR HGNC; HGNC:13089; ZNF3. DR HPA; ENSG00000166526; Low tissue specificity. DR MIM; 194510; gene. DR MIM; 601261; gene. DR neXtProt; NX_P17036; -. DR OpenTargets; ENSG00000166526; -. DR PharmGKB; PA37664; -. DR VEuPathDB; HostDB:ENSG00000166526; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000153104; -. DR HOGENOM; CLU_1980905_0_0_1; -. DR InParanoid; P17036; -. DR OMA; MGDRPHK; -. DR OrthoDB; 4624799at2759; -. DR PhylomeDB; P17036; -. DR TreeFam; TF337732; -. DR PathwayCommons; P17036; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; P17036; -. DR BioGRID-ORCS; 7551; 11 hits in 1180 CRISPR screens. DR ChiTaRS; ZNF3; human. DR GeneWiki; ZNF3; -. DR GenomeRNAi; 7551; -. DR Pharos; P17036; Tbio. DR PRO; PR:P17036; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P17036; Protein. DR Bgee; ENSG00000166526; Expressed in right uterine tube and 172 other cell types or tissues. DR ExpressionAtlas; P17036; baseline and differential. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0045321; P:leukocyte activation; NAS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd07765; KRAB_A-box; 1. DR Gene3D; 6.10.140.140; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 8. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. 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; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 8. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 8. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8. DR Genevisible; P17036; HS. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Developmental protein; Differentiation; 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..446 FT /note="Zinc finger protein 3" FT /id="PRO_0000047368" FT DOMAIN 51..123 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 200..222 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 228..250 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 256..278 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 284..306 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 312..334 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 340..362 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 368..390 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 396..418 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT MOD_RES 143 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 419 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" 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 151 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 163 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 173 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 422 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 431 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 92..446 FT /note="RETRTENDQEISEDTRSHGVLLGRFQKDISQGLKFKEAYEREVSLKRPLGNS FT PGERLNRKMPDFGQVTVEEKLTPRGERSEKYNDFGNSFTVNSNLISHQRLPVGDRPHKC FT DECSKSFNRTSDLIQHQRIHTGEKPYECNECGKAFSQSSHLIQHQRIHTGEKPYECSDC FT GKTFSCSSALILHRRIHTGEKPYECNECGKTFSWSSTLTHHQRIHTGEKPYACNECGKA FT FSRSSTLIHHQRIHTGEKPYECNECGKAFSQSSHLYQHQRIHTGEKPYECMECGGKFTY FT SSGLIQHQRIHTGENPYECSECGKAFRYSSALVRHQRIHTGEKPLNGIGMSKSSLRVTT FT ELNIREST -> WIHVCLTTQKVMLAWLTGTLSVAKGLCSSELASVEPPDTF (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1" FT /id="VSP_041156" FT VARIANT 102 FT /note="I -> T (in dbSNP:rs11550034)" FT /id="VAR_052743" FT CONFLICT 21 FT /note="P -> L (in Ref. 2; BAA91019)" FT /evidence="ECO:0000305" FT CONFLICT 252..256 FT /note="GEKPY -> IRDSG (in Ref. 7; CAA30269)" FT /evidence="ECO:0000305" FT CONFLICT 336..387 FT /note="GEKPYECNECGKAFSQSSHLYQHQRIHTGEKPYECMECGGKFTYSSGLIQHQ FT -> EALPTFVTLIRLLPSVDPIVTNEAAFPAESLATIFALIWRLFCVHSLMFKKV (in FT Ref. 2; BAA91019)" FT /evidence="ECO:0000305" SQ SEQUENCE 446 AA; 50916 MW; EEF50906695779A6 CRC64; METQADLVSQ EPQALLDSAL PSKVPAFSDK DSLGDEMLAA ALLKAKSQEL VTFEDVAVYF IRKEWKRLEP AQRDLYRDVM LENYGNVFSL DRETRTENDQ EISEDTRSHG VLLGRFQKDI SQGLKFKEAY EREVSLKRPL GNSPGERLNR KMPDFGQVTV EEKLTPRGER SEKYNDFGNS FTVNSNLISH QRLPVGDRPH KCDECSKSFN RTSDLIQHQR IHTGEKPYEC NECGKAFSQS SHLIQHQRIH TGEKPYECSD CGKTFSCSSA LILHRRIHTG EKPYECNECG KTFSWSSTLT HHQRIHTGEK PYACNECGKA FSRSSTLIHH QRIHTGEKPY ECNECGKAFS QSSHLYQHQR IHTGEKPYEC MECGGKFTYS SGLIQHQRIH TGENPYECSE CGKAFRYSSA LVRHQRIHTG EKPLNGIGMS KSSLRVTTEL NIREST //