ID ZN493_HUMAN Reviewed; 646 AA. AC Q6ZR52; G5E974; Q59GM3; Q6ZSF6; Q8N1Z6; Q8N965; Q9BR99; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 3. DT 27-MAR-2024, entry version 168. DE RecName: Full=Zinc finger protein 493; GN Name=ZNF493; 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] (ISOFORM 1), AND VARIANTS PHE-195 RP AND VAL-292. RC TISSUE=Brain, Kidney, Thalamus, and Trachea; 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] (ISOFORM 1), AND VARIANT PHE-195. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PHE-195. RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [5] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=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). CC -!- FUNCTION: May be involved in transcriptional regulation. CC -!- INTERACTION: CC Q6ZR52-3; Q9H3R5: CENPH; NbExp=3; IntAct=EBI-12856290, EBI-1003700; CC Q6ZR52-3; Q14696: MESD; NbExp=3; IntAct=EBI-12856290, EBI-6165891; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q6ZR52-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6ZR52-2; Sequence=VSP_038298; CC Name=3; CC IsoId=Q6ZR52-3; Sequence=VSP_046656, VSP_046657; CC -!- SEQUENCE CAUTION: CC Sequence=BAC04591.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC86997.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAD92323.1; Type=Erroneous initiation; Evidence={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; AK095616; BAC04591.1; ALT_INIT; mRNA. DR EMBL; AK127476; BAC86997.1; ALT_INIT; mRNA. DR EMBL; AK128494; BAC87465.1; -; mRNA. DR EMBL; AB209086; BAD92323.1; ALT_INIT; mRNA. DR EMBL; BX648842; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC010615; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471106; EAW84898.1; -; Genomic_DNA. DR EMBL; BC006408; AAH06408.1; -; mRNA. DR CCDS; CCDS12411.1; -. [Q6ZR52-3] DR CCDS; CCDS12412.1; -. [Q6ZR52-1] DR CCDS; CCDS42536.1; -. [Q6ZR52-2] DR RefSeq; NP_001070146.1; NM_001076678.2. [Q6ZR52-2] DR RefSeq; NP_663299.2; NM_145326.2. [Q6ZR52-3] DR RefSeq; NP_787106.4; NM_175910.6. [Q6ZR52-1] DR AlphaFoldDB; Q6ZR52; -. DR SMR; Q6ZR52; -. DR BioGRID; 129880; 4. DR IntAct; Q6ZR52; 2. DR GlyGen; Q6ZR52; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6ZR52; -. DR PhosphoSitePlus; Q6ZR52; -. DR SwissPalm; Q6ZR52; -. DR BioMuta; ZNF493; -. DR DMDM; 145559547; -. DR jPOST; Q6ZR52; -. DR MassIVE; Q6ZR52; -. DR MaxQB; Q6ZR52; -. DR PaxDb; 9606-ENSP00000376110; -. DR PeptideAtlas; Q6ZR52; -. DR ProteomicsDB; 68112; -. [Q6ZR52-1] DR ProteomicsDB; 68113; -. [Q6ZR52-2] DR Antibodypedia; 55042; 61 antibodies from 12 providers. DR DNASU; 284443; -. DR Ensembl; ENST00000339914.6; ENSP00000340651.6; ENSG00000196268.12. [Q6ZR52-3] DR Ensembl; ENST00000355504.4; ENSP00000347691.4; ENSG00000196268.12. [Q6ZR52-1] DR Ensembl; ENST00000392288.7; ENSP00000376110.2; ENSG00000196268.12. [Q6ZR52-2] DR GeneID; 284443; -. DR KEGG; hsa:284443; -. DR MANE-Select; ENST00000392288.7; ENSP00000376110.2; NM_001076678.3; NP_001070146.1. [Q6ZR52-2] DR UCSC; uc002npu.4; human. [Q6ZR52-1] DR AGR; HGNC:23708; -. DR CTD; 284443; -. DR DisGeNET; 284443; -. DR GeneCards; ZNF493; -. DR HGNC; HGNC:23708; ZNF493. DR HPA; ENSG00000196268; Low tissue specificity. DR neXtProt; NX_Q6ZR52; -. DR OpenTargets; ENSG00000196268; -. DR PharmGKB; PA134932599; -. DR VEuPathDB; HostDB:ENSG00000196268; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000161765; -. DR HOGENOM; CLU_002678_17_1_1; -. DR InParanoid; Q6ZR52; -. DR OMA; RSSILXI; -. DR OrthoDB; 4625752at2759; -. DR PhylomeDB; Q6ZR52; -. DR TreeFam; TF343410; -. DR PathwayCommons; Q6ZR52; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; Q6ZR52; -. DR BioGRID-ORCS; 284443; 11 hits in 1141 CRISPR screens. DR ChiTaRS; ZNF493; human. DR GenomeRNAi; 284443; -. DR Pharos; Q6ZR52; Tdark. DR PRO; PR:Q6ZR52; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q6ZR52; Protein. DR Bgee; ENSG00000196268; Expressed in visceral pleura and 187 other cell types or tissues. DR ExpressionAtlas; Q6ZR52; baseline and differential. 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 21. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24399:SF66; NOVEL KRAB BOX AND ZINC FINGER, C2H2 TYPE DOMAIN CONTAINING PROTEIN-RELATED; 1. DR PANTHER; PTHR24399; ZINC FINGER AND BTB DOMAIN-CONTAINING; 1. DR Pfam; PF00096; zf-C2H2; 17. DR SMART; SM00355; ZnF_C2H2; 21. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 11. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 18. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 22. DR Genevisible; Q6ZR52; HS. PE 1: Evidence at protein level; KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1..646 FT /note="Zinc finger protein 493" FT /id="PRO_0000047616" FT ZN_FING 26..48 FT /note="C2H2-type 1; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 54..76 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 82..104 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 109..131 FT /note="C2H2-type 4; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 137..159 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 165..187 FT /note="C2H2-type 6; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 193..215 FT /note="C2H2-type 7; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 221..243 FT /note="C2H2-type 8; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 249..271 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 277..299 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 305..327 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 333..355 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 361..383 FT /note="C2H2-type 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 389..411 FT /note="C2H2-type 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 417..439 FT /note="C2H2-type 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 445..467 FT /note="C2H2-type 16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 473..495 FT /note="C2H2-type 17" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 501..523 FT /note="C2H2-type 18" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 529..551 FT /note="C2H2-type 19" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 557..579 FT /note="C2H2-type 20" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 585..607 FT /note="C2H2-type 21" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 613..635 FT /note="C2H2-type 22" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT VAR_SEQ 1 FT /note="M -> MPGPPESLDMGPLTFRDVAIEFSLEEWQCLDTAQQDLYRKVMLENYR FT NLVFLGIAVSKPDLVTCLEQGKDPWNMKGHSTVVKPPVICSHFAEDFCPGPGIKDSFQK FT VILREYVKCGHKDLQLRKGCKSM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_038298" FT VAR_SEQ 1 FT /note="M -> MPGPPESLDMGPLTFRDVAIEFSLEEWQCLDTAQQDLYRKVMLENYR FT NLVFLAGIAVSKPDLVTCLEQGKDPWNMKGHSTVVKPPVETGFHRFSQDGLYLLTS FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_046656" FT VAR_SEQ 2..646 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_046657" FT VARIANT 195 FT /note="C -> F (in dbSNP:rs4621113)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.2" FT /id="VAR_052846" FT VARIANT 292 FT /note="L -> V (in dbSNP:rs10414834)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_052847" FT CONFLICT 181 FT /note="T -> I (in Ref. 1; BAC87465)" FT /evidence="ECO:0000305" FT CONFLICT 202 FT /note="F -> L (in Ref. 1; BAC87465)" FT /evidence="ECO:0000305" FT CONFLICT 335 FT /note="C -> R (in Ref. 1; BAC04591)" FT /evidence="ECO:0000305" FT CONFLICT 448 FT /note="K -> E (in Ref. 2; BAD92323)" FT /evidence="ECO:0000305" FT CONFLICT 547 FT /note="H -> Y (in Ref. 1; BAC86997)" FT /evidence="ECO:0000305" FT CONFLICT Q6ZR52-3:94 FT /note="S -> G (in Ref. 6; AAH06408)" FT /evidence="ECO:0000305" SQ SEQUENCE 646 AA; 75342 MW; F6F677DF4F48FF55 CRC64; MNECNVHKEG YNELNQYLTT TQSKIFQCDK YVKVFHKLLN SNRHNTKHTG KKPFKCKKCG KSFCMLLHLC QHKRIHIREN SYRCEECGKA FIWFSTLTRH RRVHTGEKSY KYECGKSFNQ DSNLTTHKRI HTGQKPYKCE ECGTSFYQFS YLTRHKLIHT REKPYKCEQY GKTFNQSSTL TGHKIIHNGE KPYKCEECGK AFSIFSTPTK HKIIHTEEKS HRCEEYCKAY KESSHLTTHK RIHTGEKPYK CEECGKAFSI FSTLTKHKII HTEEKSHRCE ECGKAYKESS HLTTHKRIHT GEKPYKCEEC GKTFSVFSIL TKHKIIHTEE KPYKCEECGK AFKRSSTLTK HRIIHTEEKP YKCEECGKAF NQSSTLSIHK IIHTGEKPYK CEECGKAFKR SSTLTIHKMI HTGEKPYKCE ECGKAFNRSS HLTTHKRIHT GHKPYKCKEC GKSFSVFSTL TKHKIIHTDK KPYKCEECGK AFNRSSILSI HKKIHTGEKP YKCEECGKAF KRSSHLAGHK QIHSVQKPYK CEECGKAFSI FSTLTKHKII HTEEKPYKCE KCGKTFYRFS NLNTHKIIHT GEKPCKCEEC GKAFNHSSNL IKHKLIHTGD KPYKCEACGK AFRRSSHLSR HKIIHIGIHT EETVQK //