ID ZN281_HUMAN Reviewed; 895 AA. AC Q9Y2X9; A6NF48; B3KMX2; Q5RKW5; Q9NY92; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 200. DE RecName: Full=Zinc finger protein 281; DE AltName: Full=GC-box-binding zinc finger protein 1; DE AltName: Full=Transcription factor ZBP-99; DE AltName: Full=Zinc finger DNA-binding protein 99; GN Name=ZNF281; Synonyms=GZP1, ZBP99; 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, AND SUBCELLULAR LOCATION. RX PubMed=10448078; DOI=10.1006/bbrc.1999.1180; RA Law D.J., Du M., Law G.L., Merchant J.L.; RT "ZBP-99 defines a conserved family of transcription factors and regulates RT ornithine decarboxylase gene expression."; RL Biochem. Biophys. Res. Commun. 262:113-120(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=10405178; DOI=10.1016/s0014-5793(99)00754-1; RA Lisowsky T., Loguercio Polosa P., Sagliano A., Roberti M., Gadaleta M.N., RA Cantatore P.; RT "Identification of human GC-box-binding zinc finger protein, a new RT Krueppel-like zinc finger protein, by the yeast one-hybrid screening with a RT GC-rich target sequence."; RL FEBS Lett. 453:369-374(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta, 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 [6] RP FUNCTION. RX PubMed=12771217; DOI=10.1093/nar/gkg380; RA Zhang X., Diab I.H., Zehner Z.E.; RT "ZBP-89 represses vimentin gene transcription by interacting with the RT transcriptional activator, Sp1."; RL Nucleic Acids Res. 31:2900-2914(2003). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; SER-785 AND SER-807, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [8] RP IDENTIFICATION BY 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 SER-484, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651, 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND THR-888, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-128; LYS-213; LYS-232; LYS-409; RP LYS-416; LYS-622; LYS-787 AND LYS-795, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-128; LYS-225; LYS-498 AND RP LYS-795, AND IDENTIFICATION BY MASS 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 [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-128, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2; LYS-101; LYS-128; LYS-213; RP LYS-219; LYS-225; LYS-232; LYS-242; LYS-259; LYS-301; LYS-325; LYS-373; RP LYS-409; LYS-416; LYS-460; LYS-477; LYS-493; LYS-498; LYS-539; LYS-599; RP LYS-617; LYS-622; LYS-661; LYS-670; LYS-787; LYS-792; LYS-795; LYS-818 AND RP LYS-840, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-65 (ISOFORM 2), AND RP 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 [21] RP VARIANT [LARGE SCALE ANALYSIS] THR-527. 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: Transcription repressor that plays a role in regulation of CC embryonic stem cells (ESCs) differentiation. Required for ESCs CC differentiation and acts by mediating autorepression of NANOG in ESCs: CC binds to the NANOG promoter and promotes association of NANOG protein CC to its own promoter and recruits the NuRD complex, which deacetylates CC histones. Not required for establishement and maintenance of ESCs (By CC similarity). Represses the transcription of a number of genes including CC GAST, ODC1 and VIM. Binds to the G-rich box in the enhancer region of CC these genes. {ECO:0000250, ECO:0000269|PubMed:10448078, CC ECO:0000269|PubMed:12771217}. CC -!- INTERACTION: CC Q9Y2X9; P42858: HTT; NbExp=3; IntAct=EBI-396200, EBI-466029; CC Q9Y2X9; Q96CV9: OPTN; NbExp=3; IntAct=EBI-396200, EBI-748974; CC Q9Y2X9; D3DTS7: PMP22; NbExp=3; IntAct=EBI-396200, EBI-25882629; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10448078}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y2X9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y2X9-2; Sequence=VSP_054815; CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB70967.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AF125158; AAD21084.1; -; mRNA. DR EMBL; AJ132591; CAB70967.1; ALT_INIT; mRNA. DR EMBL; AJ132592; CAB70968.1; -; mRNA. DR EMBL; AK022916; BAG51134.1; -; mRNA. DR EMBL; AC104461; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC051905; AAH51905.1; -; mRNA. DR EMBL; BC060820; AAH60820.1; -; mRNA. DR CCDS; CCDS1402.1; -. [Q9Y2X9-1] DR CCDS; CCDS60384.1; -. [Q9Y2X9-2] DR PIR; JC7089; JC7089. DR RefSeq; NP_001268222.1; NM_001281293.1. [Q9Y2X9-1] DR RefSeq; NP_001268223.1; NM_001281294.1. [Q9Y2X9-2] DR RefSeq; NP_036614.1; NM_012482.4. [Q9Y2X9-1] DR RefSeq; XP_016856376.1; XM_017000887.1. DR RefSeq; XP_016856377.1; XM_017000888.1. DR AlphaFoldDB; Q9Y2X9; -. DR SMR; Q9Y2X9; -. DR BioGRID; 117074; 166. DR CORUM; Q9Y2X9; -. DR ELM; Q9Y2X9; -. DR IntAct; Q9Y2X9; 106. DR MINT; Q9Y2X9; -. DR STRING; 9606.ENSP00000294740; -. DR GlyConnect; 2864; 1 O-GlcNAc glycan (1 site). DR GlyCosmos; Q9Y2X9; 22 sites, 2 glycans. DR GlyGen; Q9Y2X9; 29 sites, 2 O-linked glycans (29 sites). DR iPTMnet; Q9Y2X9; -. DR PhosphoSitePlus; Q9Y2X9; -. DR BioMuta; ZNF281; -. DR DMDM; 13124664; -. DR EPD; Q9Y2X9; -. DR jPOST; Q9Y2X9; -. DR MassIVE; Q9Y2X9; -. DR MaxQB; Q9Y2X9; -. DR PaxDb; 9606-ENSP00000294740; -. DR PeptideAtlas; Q9Y2X9; -. DR ProteomicsDB; 1027; -. DR ProteomicsDB; 85932; -. [Q9Y2X9-1] DR Pumba; Q9Y2X9; -. DR Antibodypedia; 20632; 229 antibodies from 32 providers. DR DNASU; 23528; -. DR Ensembl; ENST00000294740.3; ENSP00000294740.2; ENSG00000162702.8. [Q9Y2X9-1] DR Ensembl; ENST00000367352.3; ENSP00000356321.3; ENSG00000162702.8. [Q9Y2X9-2] DR Ensembl; ENST00000367353.2; ENSP00000356322.1; ENSG00000162702.8. [Q9Y2X9-1] DR GeneID; 23528; -. DR KEGG; hsa:23528; -. DR MANE-Select; ENST00000367353.2; ENSP00000356322.1; NM_001281293.2; NP_001268222.1. DR UCSC; uc001gve.5; human. [Q9Y2X9-1] DR AGR; HGNC:13075; -. DR CTD; 23528; -. DR DisGeNET; 23528; -. DR GeneCards; ZNF281; -. DR HGNC; HGNC:13075; ZNF281. DR HPA; ENSG00000162702; Tissue enhanced (bone). DR MIM; 618703; gene. DR neXtProt; NX_Q9Y2X9; -. DR OpenTargets; ENSG00000162702; -. DR PharmGKB; PA37651; -. DR VEuPathDB; HostDB:ENSG00000162702; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000161586; -. DR HOGENOM; CLU_017625_0_0_1; -. DR InParanoid; Q9Y2X9; -. DR OMA; NVGHMTS; -. DR OrthoDB; 5318724at2759; -. DR PhylomeDB; Q9Y2X9; -. DR TreeFam; TF331779; -. DR PathwayCommons; Q9Y2X9; -. DR SignaLink; Q9Y2X9; -. DR SIGNOR; Q9Y2X9; -. DR BioGRID-ORCS; 23528; 26 hits in 1174 CRISPR screens. DR ChiTaRS; ZNF281; human. DR GeneWiki; ZNF281; -. DR GenomeRNAi; 23528; -. DR Pharos; Q9Y2X9; Tbio. DR PRO; PR:Q9Y2X9; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9Y2X9; Protein. DR Bgee; ENSG00000162702; Expressed in secondary oocyte and 206 other cell types or tissues. DR Genevisible; Q9Y2X9; HS. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB. 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; IDA:NTNU_SB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0010172; P:embryonic body morphogenesis; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 4. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1. DR PANTHER; PTHR24394:SF23; ZINC FINGER PROTEIN 281-LIKE ISOFORM X1; 1. DR Pfam; PF00096; zf-C2H2; 2. DR SMART; SM00355; ZnF_C2H2; 4. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4. PE 1: Evidence at protein level; KW Alternative splicing; Differentiation; DNA-binding; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..895 FT /note="Zinc finger protein 281" FT /id="PRO_0000047505" FT ZN_FING 261..283 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 289..311 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 317..339 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 345..367 FT /note="C2H2-type 4; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..44 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 63..113 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 130..149 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 183..253 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 377..427 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 638..660 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 778..817 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 197..232 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 377..406 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 407..421 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 644..660 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 395 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 484 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 651 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 785 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 807 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 888 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT CROSSLNK 2 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 101 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 128 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 213 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 219 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 225 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 232 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 242 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 259 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 301 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 325 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 373 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 409 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 416 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 460 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 477 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 493 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 498 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 539 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 599 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 617 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 622 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 661 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 670 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 787 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 792 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 795 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 818 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 840 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 49..84 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_054815" FT VARIANT 527 FT /note="I -> T (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035576" FT CONFLICT 63 FT /note="F -> L (in Ref. 3; BAG51134)" FT /evidence="ECO:0000305" FT CONFLICT 206 FT /note="H -> Y (in Ref. 5; AAH51905)" FT /evidence="ECO:0000305" FT CONFLICT 482 FT /note="F -> L (in Ref. 3; BAG51134)" FT /evidence="ECO:0000305" FT CONFLICT 635 FT /note="L -> I (in Ref. 3; BAG51134)" FT /evidence="ECO:0000305" FT CROSSLNK Q9Y2X9-2:65 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" SQ SEQUENCE 895 AA; 96915 MW; 556FAAEA8D095FB7 CRC64; MKIGSGFLSG GGGTGSSGGS GSGGGGSGGG GGGGSSGRRA EMEPTFPQGM VMFNHRLPPV TSFTRPAGSA APPPQCVLSS STSAAPAAEP PPPPAPDMTF KKEPAASAAA FPSQRTSWGF LQSLVSIKQE KPADPEEQQS HHHHHHHHYG GLFAGAEERS PGLGGGEGGS HGVIQDLSIL HQHVQQQPAQ HHRDVLLSSS SRTDDHHGTE EPKQDTNVKK AKRPKPESQG IKAKRKPSAS SKPSLVGDGE GAILSPSQKP HICDHCSAAF RSSYHLRRHV LIHTGERPFQ CSQCSMGFIQ KYLLQRHEKI HSREKPFGCD QCSMKFIQKY HMERHKRTHS GEKPYKCDTC QQYFSRTDRL LKHRRTCGEV IVKGATSAEP GSSNHTNMGN LAVLSQGNTS SSRRKTKSKS IAIENKEQKT GKTNESQISN NINMQSYSVE MPTVSSSGGI IGTGIDELQK RVPKLIFKKG SRKNTDKNYL NFVSPLPDIV GQKSLSGKPS GSLGIVSNNS VETIGLLQST SGKQGQISSN YDDAMQFSKK RRYLPTASSN SAFSINVGHM VSQQSVIQSA GVSVLDNEAP LSLIDSSALN AEIKSCHDKS GIPDEVLQSI LDQYSNKSES QKEDPFNIAE PRVDLHTSGE HSELVQEENL SPGTQTPSND KASMLQEYSK YLQQAFEKST NASFTLGHGF QFVSLSSPLH NHTLFPEKQI YTTSPLECGF GQSVTSVLPS SLPKPPFGML FGSQPGLYLS ALDATHQQLT PSQELDDLID SQKNLETSSA FQSSSQKLTS QKEQKNLESS TGFQIPSQEL ASQIDPQKDI EPRTTYQIEN FAQAFGSQFK SGSRVPMTFI TNSNGEVDHR VRTSVSDFSG YTNMMSDVSE PCSTRVKTPT SQSYR //