ID ZN480_HUMAN Reviewed; 535 AA. AC Q8WV37; Q5JPG9; Q6P0Q4; Q8N1M5; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 28-JUN-2023, entry version 170. DE RecName: Full=Zinc finger protein 480; GN Name=ZNF480; 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 1), FUNCTION IN TRANSCRIPTIONAL RP ACTIVATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE RP SPECIFICITY. RC TISSUE=Embryonic heart; RX PubMed=15219843; DOI=10.1016/j.bbrc.2004.05.182; RA Yi Z., Li Y., Ma W., Li D., Zhu C., Luo J., Wang Y., Huang X., Yuan W., RA Liu M., Wu X.; RT "A novel KRAB zinc-finger protein, ZNF480, expresses in human heart and RT activates transcriptional activities of AP-1 and SRE."; RL Biochem. Biophys. Res. Commun. 320:409-415(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Fetal brain, and Tongue; 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 MRNA] (ISOFORM 2). RC TISSUE=Fetal brain; 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 MRNA] (ISOFORM 1). RC TISSUE=Eye, and Testis; 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-122; LYS-125; LYS-195 AND RP LYS-220, 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). RN [7] RP VARIANT [LARGE SCALE ANALYSIS] GLN-361. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Involved in transcriptional regulation as an activator. CC {ECO:0000269|PubMed:15219843}. CC -!- INTERACTION: CC Q8WV37; O95273: CCNDBP1; NbExp=3; IntAct=EBI-8490675, EBI-748961; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15219843}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8WV37-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WV37-2; Sequence=VSP_016214; CC Name=3; CC IsoId=Q8WV37-3; Sequence=VSP_016215; CC -!- TISSUE SPECIFICITY: Expressed in fetal heart, heart, skeletal muscle, CC pancreas and placenta. {ECO:0000269|PubMed:15219843}. CC -!- DEVELOPMENTAL STAGE: Expressed in heart as early as the 24th week of CC gestation. {ECO:0000269|PubMed:15219843}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-20 is the initiator. A CC 'GT' insertion (rs59214675) allows to extend the sequence in the N- CC terminus. The majority of mRNAs do not have this insertion and the CC corresponding protein sequences start at Met-20. {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; AY512662; AAR97581.1; -; mRNA. DR EMBL; AK096442; BAC04792.1; -; mRNA. DR EMBL; AK096559; BAC04817.1; -; mRNA. DR EMBL; AL832560; CAI46140.1; -; mRNA. DR EMBL; AC010320; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC018783; AAH18783.1; -; mRNA. DR EMBL; BC065503; AAH65503.1; -; mRNA. DR CCDS; CCDS12850.2; -. [Q8WV37-1] DR CCDS; CCDS74437.1; -. [Q8WV37-2] DR RefSeq; NP_001284553.1; NM_001297624.1. DR RefSeq; NP_001284554.1; NM_001297625.1. [Q8WV37-2] DR RefSeq; NP_653285.2; NM_144684.3. [Q8WV37-1] DR RefSeq; XP_011524767.1; XM_011526465.2. [Q8WV37-1] DR AlphaFoldDB; Q8WV37; -. DR SMR; Q8WV37; -. DR BioGRID; 127068; 8. DR IntAct; Q8WV37; 2. DR MINT; Q8WV37; -. DR STRING; 9606.ENSP00000471754; -. DR iPTMnet; Q8WV37; -. DR PhosphoSitePlus; Q8WV37; -. DR BioMuta; ZNF480; -. DR DMDM; 296453042; -. DR EPD; Q8WV37; -. DR jPOST; Q8WV37; -. DR MassIVE; Q8WV37; -. DR MaxQB; Q8WV37; -. DR PaxDb; Q8WV37; -. DR PeptideAtlas; Q8WV37; -. DR ProteomicsDB; 74743; -. [Q8WV37-1] DR ProteomicsDB; 74744; -. [Q8WV37-2] DR ProteomicsDB; 74745; -. [Q8WV37-3] DR Antibodypedia; 32583; 138 antibodies from 18 providers. DR DNASU; 147657; -. DR Ensembl; ENST00000335090.6; ENSP00000335670.6; ENSG00000198464.14. [Q8WV37-2] DR Ensembl; ENST00000468240.6; ENSP00000417424.1; ENSG00000198464.14. [Q8WV37-1] DR Ensembl; ENST00000595962.6; ENSP00000471754.1; ENSG00000198464.14. [Q8WV37-1] DR GeneID; 147657; -. DR KEGG; hsa:147657; -. DR MANE-Select; ENST00000595962.6; ENSP00000471754.1; NM_144684.4; NP_653285.2. DR UCSC; uc010ydl.3; human. [Q8WV37-1] DR AGR; HGNC:23305; -. DR CTD; 147657; -. DR DisGeNET; 147657; -. DR GeneCards; ZNF480; -. DR HGNC; HGNC:23305; ZNF480. DR HPA; ENSG00000198464; Low tissue specificity. DR MIM; 613910; gene. DR neXtProt; NX_Q8WV37; -. DR OpenTargets; ENSG00000198464; -. DR PharmGKB; PA134876563; -. DR VEuPathDB; HostDB:ENSG00000198464; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000163746; -. DR HOGENOM; CLU_002678_94_1_1; -. DR InParanoid; Q8WV37; -. DR OMA; HWTTHTR; -. DR OrthoDB; 4710132at2759; -. DR PhylomeDB; Q8WV37; -. DR TreeFam; TF341892; -. DR PathwayCommons; Q8WV37; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; Q8WV37; -. DR BioGRID-ORCS; 147657; 23 hits in 1170 CRISPR screens. DR ChiTaRS; ZNF480; human. DR GenomeRNAi; 147657; -. DR Pharos; Q8WV37; Tdark. DR PRO; PR:Q8WV37; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q8WV37; protein. DR Bgee; ENSG00000198464; Expressed in granulocyte and 92 other tissues. DR ExpressionAtlas; Q8WV37; baseline and differential. DR Genevisible; Q8WV37; HS. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. 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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro. DR CDD; cd07765; KRAB_A-box; 1. DR Gene3D; 6.10.140.140; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 12. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24404; ZINC FINGER PROTEIN; 1. DR PANTHER; PTHR24404:SF92; ZINC FINGER PROTEIN 845; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 11. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 12. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Isopeptide bond; Metal-binding; Nucleus; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..535 FT /note="Zinc finger protein 480" FT /id="PRO_0000047607" FT DOMAIN 27..98 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 203..225 FT /note="C2H2-type 1; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 231..253 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 259..281 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 287..309 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 315..337 FT /note="C2H2-type 5; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 343..365 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 371..393 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 399..421 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 427..449 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 455..477 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 483..505 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 511..533 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT CROSSLNK 122 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 195 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 220 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..169 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016215" FT VAR_SEQ 1..77 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_016214" FT VARIANT 177 FT /note="P -> S (in dbSNP:rs13343641)" FT /id="VAR_033569" FT VARIANT 361 FT /note="H -> Q (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035584" SQ SEQUENCE 535 AA; 61708 MW; 444D121FE8B9C44C CRC64; MLCDEKAQKR RKRKAKESGM ALPQGHLTFR DVAIEFSQAE WKCLDPAQRA LYKDVMLENY RNLVSLGISL PDLNINSMLE QRREPWSGES EVKIAKNSDG RECIKGVNTG SSYALGSNAE DKPIKKQLGV SFHLHLSELE LFPDERVING CNQVENFINH SSSVSCLQEM SSSVKTPIFN RNDFDDSSFL PQEQKVHLRE KPYECNEHSK VFRVSSSLTK HQVIHTVEKP YKCNSCGKVF SRNSHLAEHC RIHTGEKPYK CNVCGKVFSY NSNFARHQRI HTREKPYECN ECGKVFSNNS YLARHQRIHA EEKPYKCNEC GKGFSHKSSL ANHWRIYTGE KPYKCDECGK AFYRIALLVR HQKIHTGEKP YKCNECGKVF IQNSHLAQHW RIHTGEKPYK CNECGKVFNQ LSNLARHRRI HTGEKPYKCN ECGKAFSEYS GLSAHLVIHT GEKPYKCSEC GKAFRHKLSL TNHQRIHTGE RPYKCNECGK VFNRIAHLAR HRKIHTGEKP YKCNECGKAF SRISYLAQHW TIHMG //