ID ZN462_HUMAN Reviewed; 2506 AA. AC Q96JM2; Q5T0T4; Q8N408; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 3. DT 27-MAR-2024, entry version 177. DE RecName: Full=Zinc finger protein 462 {ECO:0000305}; DE AltName: Full=Zinc finger PBX1-interacting protein {ECO:0000250|UniProtKB:B1AWL2}; DE Short=ZFPIP {ECO:0000250|UniProtKB:B1AWL2}; GN Name=ZNF462 {ECO:0000312|HGNC:HGNC:21684}; Synonyms=KIAA1803; 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 2). RC TISSUE=Brain; RX PubMed=11347906; DOI=10.1093/dnares/8.2.85; RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XX. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 8:85-95(2001). RN [2] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1118-2506 (ISOFORM 3). RC TISSUE=Placenta; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1576-2506 (ISOFORM 1). RC TISSUE=Liver; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [7] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=20219459; DOI=10.1016/j.yexcr.2010.02.024; RA Masse J., Laurent A., Nicol B., Guerrier D., Pellerin I., Deschamps S.; RT "Involvement of ZFPIP/Zfp462 in chromatin integrity and survival of P19 RT pluripotent cells."; RL Exp. Cell Res. 316:1190-1201(2010). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21570965; DOI=10.1016/j.yexcr.2011.04.015; RA Masse J., Piquet-Pellorce C., Viet J., Guerrier D., Pellerin I., RA Deschamps S.; RT "ZFPIP/Zfp462 is involved in P19 cell pluripotency and in their neuronal RT fate."; RL Exp. Cell Res. 317:1922-1934(2011). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350; SER-354; SER-688; RP SER-1090; SER-1166; SER-2172 AND SER-2177, AND IDENTIFICATION BY MASS RP 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 [10] RP GLYCOSYLATION AT SER-292 AND SER-309, AND PHOSPHORYLATION AT SER-292 AND RP SER-309. RC TISSUE=Embryonic stem cell; RX PubMed=22826440; DOI=10.1074/mcp.m112.019760; RA Hahne H., Kuster B.; RT "Discovery of O-GlcNAc-6-phosphate modified proteins in large-scale RT phosphoproteomics data."; RL Mol. Cell. Proteomics 11:1063-1069(2012). RN [11] RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-2004, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [12] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20 AND LYS-1946, AND RP IDENTIFICATION BY MASS 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 [13] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-271 AND LYS-1946, AND RP 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 [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20, SUMOYLATION [LARGE SCALE RP ANALYSIS] AT LYS-849 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-234; LYS-271; LYS-337; RP LYS-347; LYS-349; LYS-428; LYS-484; LYS-631; LYS-657; LYS-668; LYS-706; RP LYS-986; LYS-1135; LYS-1206; LYS-1214; LYS-1220; LYS-1243; LYS-1499; RP LYS-1571; LYS-1591; LYS-1698; LYS-1780; LYS-1946; LYS-2104; LYS-2293; RP LYS-2444 AND LYS-2504, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-849 RP (ISOFORM 2), 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). RN [17] RP STRUCTURE BY NMR OF 1874-1948. RG RIKEN structural genomics initiative (RSGI); RT "Solution structures of the C2H2 type zinc finger domain of human zinc RT finger protein 462."; RL Submitted (NOV-2005) to the PDB data bank. RN [18] RP INVOLVEMENT IN WSKA, AND VARIANT WSKA 1263-ARG--GLU-2506 DEL. RX PubMed=28513610; DOI=10.1038/ejhg.2017.86; RA Weiss K., Wigby K., Fannemel M., Henderson L.B., Beck N., Ghali N., RA Study D.D.D., Anderlid B.M., Lundin J., Hamosh A., Jones M.C., Ghedia S., RA Muenke M., Kruszka P.; RT "Haploinsufficiency of ZNF462 is associated with craniofacial anomalies, RT corpus callosum dysgenesis, ptosis, and developmental delay."; RL Eur. J. Hum. Genet. 25:946-951(2017). RN [19] RP INVOLVEMENT IN WSKA. RX PubMed=29427787; DOI=10.1016/j.ejmg.2018.02.002; RA Cosemans N., Vandenhove L., Maljaars J., Van Esch H., Devriendt K., RA Baldwin A., Fryns J.P., Noens I., Peeters H.; RT "ZNF462 and KLF12 are disrupted by a de novo translocation in a patient RT with syndromic intellectual disability and autism spectrum disorder."; RL Eur. J. Med. Genet. 61:376-383(2018). RN [20] RP INVOLVEMENT IN WSKA, AND VARIANTS WSKA 255-ARG--GLU-2506 DEL; RP 412-SER--GLU-2506 DEL; 864-ARG--GLU-2506 DEL; 899-GLU--GLU-2506 DEL; RP 1389-GLN--GLU-2506 DEL AND 2265-TYR--GLU-2506 DEL. RX PubMed=31361404; DOI=10.1002/ajmg.a.61306; RA Kruszka P., Hu T., Hong S., Signer R., Cogne B., Isidor B., Mazzola S.E., RA Giltay J.C., van Gassen K.L.I., England E.M., Pais L., Ockeloen C.W., RA Sanchez-Lara P.A., Kinning E., Adams D.J., Treat K., Torres-Martinez W., RA Bedeschi M.F., Iascone M., Blaney S., Bell O., Tan T.Y., Delrue M.A., RA Jurgens J., Barry B.J., Engle E.C., Savage S.K., Fleischer N., RA Martinez-Agosto J.A., Boycott K., Zackai E.H., Muenke M.; RT "Phenotype delineation of ZNF462 related syndrome."; RL Am. J. Med. Genet. A 179:2075-2082(2019). CC -!- FUNCTION: Zinc finger nuclear factor involved in transcription by CC regulating chromatin structure and organization (PubMed:20219459, CC PubMed:21570965). Involved in the pluripotency and differentiation of CC embryonic stem cells by regulating SOX2, POU5F1/OCT4, and NANOG CC (PubMed:21570965). By binding PBX1, prevents the heterodimerization of CC PBX1 and HOXA9 and their binding to DNA (By similarity). Regulates CC neuronal development and neural cell differentiation (PubMed:21570965). CC {ECO:0000250|UniProtKB:B1AWL2, ECO:0000269|PubMed:20219459, CC ECO:0000269|PubMed:21570965}. CC -!- SUBUNIT: Interacts with PBX1; this interaction prevents PBX1-HOXA9 CC heterodimer from forming and binding to DNA. CC {ECO:0000250|UniProtKB:B1AWL2}. CC -!- INTERACTION: CC Q96JM2; Q96KQ7: EHMT2; NbExp=4; IntAct=EBI-1210359, EBI-744366; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20219459, CC ECO:0000269|PubMed:21570965}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96JM2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96JM2-2; Sequence=VSP_037407, VSP_037408; CC Name=3; CC IsoId=Q96JM2-3; Sequence=VSP_037409; CC -!- PTM: O-GlcNAcylated with O-GlcNAc-6-phosphate. CC {ECO:0000269|PubMed:22826440}. CC -!- DISEASE: Weiss-Kruszka syndrome (WSKA) [MIM:618619]: An autosomal CC dominant, multiple congenital anomaly syndrome with variable CC expressivity and complete penetrance. Patients manifest developmental CC delay, hypotonia, feeding difficulties, craniofacial abnormalities CC including ptosis, abnormal head shape, downslanting palpebral fissures, CC metopic ridging, and craniosynostosis. Variable congenital heart CC defects can be observed in some patients. A few patients show agenesis CC of the corpus callosum on brain imaging. {ECO:0000269|PubMed:28513610, CC ECO:0000269|PubMed:29427787, ECO:0000269|PubMed:31361404}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAH36884.1; Type=Erroneous initiation; Note=Truncated 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; AB058706; BAB47432.2; -; mRNA. DR EMBL; AL512593; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK027866; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC036884; AAH36884.1; ALT_INIT; mRNA. DR CCDS; CCDS35096.1; -. [Q96JM2-1] DR RefSeq; NP_067047.4; NM_021224.5. [Q96JM2-1] DR RefSeq; XP_006717278.1; XM_006717215.3. [Q96JM2-3] DR RefSeq; XP_006717279.1; XM_006717216.3. [Q96JM2-1] DR PDB; 1X6F; NMR; -; A=1874-1948. DR PDBsum; 1X6F; -. DR AlphaFoldDB; Q96JM2; -. DR BMRB; Q96JM2; -. DR SMR; Q96JM2; -. DR BioGRID; 121829; 57. DR DIP; DIP-39340N; -. DR ELM; Q96JM2; -. DR IntAct; Q96JM2; 31. DR MINT; Q96JM2; -. DR STRING; 9606.ENSP00000277225; -. DR GlyCosmos; Q96JM2; 2 sites, No reported glycans. DR GlyGen; Q96JM2; 5 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q96JM2; -. DR PhosphoSitePlus; Q96JM2; -. DR BioMuta; ZNF462; -. DR DMDM; 238054352; -. DR EPD; Q96JM2; -. DR jPOST; Q96JM2; -. DR MassIVE; Q96JM2; -. DR MaxQB; Q96JM2; -. DR PaxDb; 9606-ENSP00000277225; -. DR PeptideAtlas; Q96JM2; -. DR ProteomicsDB; 76981; -. [Q96JM2-1] DR ProteomicsDB; 76982; -. [Q96JM2-2] DR ProteomicsDB; 76983; -. [Q96JM2-3] DR Pumba; Q96JM2; -. DR Antibodypedia; 14859; 91 antibodies from 19 providers. DR DNASU; 58499; -. DR Ensembl; ENST00000277225.10; ENSP00000277225.5; ENSG00000148143.13. [Q96JM2-1] DR Ensembl; ENST00000441147.6; ENSP00000397306.2; ENSG00000148143.13. [Q96JM2-2] DR GeneID; 58499; -. DR KEGG; hsa:58499; -. DR MANE-Select; ENST00000277225.10; ENSP00000277225.5; NM_021224.6; NP_067047.4. DR UCSC; uc004bcz.4; human. [Q96JM2-1] DR AGR; HGNC:21684; -. DR CTD; 58499; -. DR DisGeNET; 58499; -. DR GeneCards; ZNF462; -. DR GeneReviews; ZNF462; -. DR HGNC; HGNC:21684; ZNF462. DR HPA; ENSG00000148143; Low tissue specificity. DR MalaCards; ZNF462; -. DR MIM; 617371; gene. DR MIM; 618619; phenotype. DR neXtProt; NX_Q96JM2; -. DR OpenTargets; ENSG00000148143; -. DR Orphanet; 502430; Weiss-Kruszka Syndrome. DR PharmGKB; PA134949139; -. DR VEuPathDB; HostDB:ENSG00000148143; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000156411; -. DR InParanoid; Q96JM2; -. DR OMA; CAFQSFS; -. DR OrthoDB; 4041258at2759; -. DR PhylomeDB; Q96JM2; -. DR TreeFam; TF325534; -. DR PathwayCommons; Q96JM2; -. DR SignaLink; Q96JM2; -. DR SIGNOR; Q96JM2; -. DR BioGRID-ORCS; 58499; 21 hits in 1161 CRISPR screens. DR ChiTaRS; ZNF462; human. DR EvolutionaryTrace; Q96JM2; -. DR GenomeRNAi; 58499; -. DR Pharos; Q96JM2; Tbio. DR PRO; PR:Q96JM2; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q96JM2; Protein. DR Bgee; ENSG00000148143; Expressed in buccal mucosa cell and 192 other cell types or tissues. DR ExpressionAtlas; Q96JM2; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006325; P:chromatin organization; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 9. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24403; ZINC FINGER PROTEIN; 1. DR PANTHER; PTHR24403:SF58; ZINC FINGER PROTEIN 462; 1. DR SMART; SM00355; ZnF_C2H2; 34. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9. DR Genevisible; Q96JM2; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Disease variant; DNA-binding; KW Glycoprotein; Isopeptide bond; Metal-binding; Methylation; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..2506 FT /note="Zinc finger protein 462" FT /id="PRO_0000047601" FT ZN_FING 4..27 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 108..131 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 162..185 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 439..462 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 470..492 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 600..623 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 843..866 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 886..908 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 925..948 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1030..1053 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1265..1288 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1470..1493 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1515..1538 FT /note="C2H2-type 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1577..1600 FT /note="C2H2-type 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1660..1683 FT /note="C2H2-type 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1697..1720 FT /note="C2H2-type 16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1892..1914 FT /note="C2H2-type 17" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1968..1992 FT /note="C2H2-type 18; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 2025..2048 FT /note="C2H2-type 19" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 2054..2077 FT /note="C2H2-type 20" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 2083..2106 FT /note="C2H2-type 21" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 2191..2214 FT /note="C2H2-type 22" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 2220..2243 FT /note="C2H2-type 23" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 2254..2276 FT /note="C2H2-type 24" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 2300..2322 FT /note="C2H2-type 25" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 2328..2351 FT /note="C2H2-type 26" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 2414..2436 FT /note="C2H2-type 27" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 215..241 FT /note="Interaction with PBX1" FT /evidence="ECO:0000250|UniProtKB:B1AWL2" FT REGION 280..299 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 337..356 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 535..596 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 636..661 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1157..1186 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2122..2152 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2371..2396 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 539..595 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 638..661 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 350 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 354 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 688 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692" FT MOD_RES 1090 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1166 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 2004 FT /note="N6-methyllysine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 2172 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 2177 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT CARBOHYD 292 FT /note="O-linked (GlcNAc6P) serine" FT /evidence="ECO:0000269|PubMed:22826440" FT CARBOHYD 309 FT /note="O-linked (GlcNAc6P) serine" FT /evidence="ECO:0000269|PubMed:22826440" FT CROSSLNK 20 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 20 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 234 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 271 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 337 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 347 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 349 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 428 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 484 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 631 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 657 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 668 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 706 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 986 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1135 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1206 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1214 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1220 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1243 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1499 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1571 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1591 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1698 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1780 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1946 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 2104 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 2293 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 2444 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 2504 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..1155 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11347906" FT /id="VSP_037407" FT VAR_SEQ 2004 FT /note="K -> KQEADDPAHLFLDGLEAAKDASGALVGRVDGEHCLLDGMLEDETRPG FT GYHCSQCDRVLMSMQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11347906" FT /id="VSP_037408" FT VAR_SEQ 2004 FT /note="K -> KEADDPAHLFLDGLEAAKDASGALVGRVDGEHCLLDGMLEDETRPGG FT YHCSQCDRVLMSMQ (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037409" FT VARIANT 255..2506 FT /note="Missing (in WSKA)" FT /evidence="ECO:0000269|PubMed:31361404" FT /id="VAR_083319" FT VARIANT 404 FT /note="M -> V (in dbSNP:rs17723637)" FT /id="VAR_058301" FT VARIANT 412..2506 FT /note="Missing (in WSKA)" FT /evidence="ECO:0000269|PubMed:31361404" FT /id="VAR_083320" FT VARIANT 864..2506 FT /note="Missing (in WSKA)" FT /evidence="ECO:0000269|PubMed:31361404" FT /id="VAR_083321" FT VARIANT 899..2506 FT /note="Missing (in WSKA)" FT /evidence="ECO:0000269|PubMed:31361404" FT /id="VAR_083322" FT VARIANT 1187 FT /note="P -> S (in dbSNP:rs3814541)" FT /id="VAR_058302" FT VARIANT 1263..2506 FT /note="Missing (in WSKA)" FT /evidence="ECO:0000269|PubMed:28513610" FT /id="VAR_083323" FT VARIANT 1389..2506 FT /note="Missing (in WSKA)" FT /evidence="ECO:0000269|PubMed:31361404" FT /id="VAR_083324" FT VARIANT 1828 FT /note="N -> S (in dbSNP:rs3814538)" FT /id="VAR_058303" FT VARIANT 2052 FT /note="K -> R (in dbSNP:rs7020769)" FT /id="VAR_058304" FT VARIANT 2265..2506 FT /note="Missing (in WSKA)" FT /evidence="ECO:0000269|PubMed:31361404" FT /id="VAR_083325" FT VARIANT 2452 FT /note="H -> L (in dbSNP:rs10217192)" FT /id="VAR_058305" FT CONFLICT 1241 FT /note="Q -> R (in Ref. 4; AK027866)" FT /evidence="ECO:0000305" FT CONFLICT 1250 FT /note="V -> I (in Ref. 4; AK027866)" FT /evidence="ECO:0000305" FT CONFLICT 1332 FT /note="Q -> R (in Ref. 4; AK027866)" FT /evidence="ECO:0000305" FT CONFLICT 1424 FT /note="A -> T (in Ref. 4; AK027866)" FT /evidence="ECO:0000305" FT CONFLICT 1430 FT /note="E -> A (in Ref. 4; AK027866)" FT /evidence="ECO:0000305" FT CONFLICT 1936 FT /note="K -> E (in Ref. 4; AK027866)" FT /evidence="ECO:0000305" FT CONFLICT 2030 FT /note="C -> S (in Ref. 4; AK027866)" FT /evidence="ECO:0000305" FT CONFLICT 2277 FT /note="Missing (in Ref. 4; AK027866)" FT /evidence="ECO:0000305" FT STRAND 1895..1897 FT /evidence="ECO:0007829|PDB:1X6F" FT STRAND 1900..1903 FT /evidence="ECO:0007829|PDB:1X6F" FT HELIX 1904..1921 FT /evidence="ECO:0007829|PDB:1X6F" FT STRAND 1941..1943 FT /evidence="ECO:0007829|PDB:1X6F" FT CROSSLNK Q96JM2-2:849 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" SQ SEQUENCE 2506 AA; 284688 MW; BE921753A66384DB CRC64; MEVLQCDGCD FRAPSYEDLK AHIQDVHTAF LQPTDVAEDN VNELRCGSVN ASNQTEVEFS SIKDEFAIAE DLSGQNATSL GTGGYYGHSP GYYGQHIAAN PKPTNKFFQC KFCVRYFRSK NLLIEHTRKV HGAQAEGSSS GPPVPGSLNY NIMMHEGFGK VFSCQFCTYK SPRRARIIKH QKMYHKNNLK ETTAPPPAPA PMPDPVVPPV SLQDPCKELP AEVVERSILE SMVKPLTKSR GNFCCEWCSY QTPRRERWCD HMMKKHRSMV KILSSLRQQQ EGTNLPDVPN KSAPSPTSNS TYLTMNAASR EIPNTTVSNF RGSMGNSIMR PNSSASKFSP MSYPQMKPKS PHNSGLVNLT ERSRYGMTDM TNSSADLETN SMLNDSSSDE ELNEIDSENG LSAMDHQTSG LSAEQLMGSD GNKLLETKGI PFRRFMNRFQ CPFCPFLTMH RRSISRHIEN IHLSGKTAVY KCDECPFTCK SSLKLGAHKQ CHTGTTSDWD AVNSQSESIS SSLNEGVVSY ESSSINGRKS GVMLDPLQQQ QPPQPPPPPP PPPPSQPQPL QQPQPPQLQP PHQVPPQPQT QPPPTQQPQP PTQAAPLHPY KCTMCNYSTT TLKGLRVHQQ HKHSFCDNLP KFEGQPSSLP LENETDSHPS SSNTVKKSQT SILGLSSKNN FVAKASRKLA NDFPLDLSPV KKRTRIDEIA SNLQSKINQT KQQEDAVINV EDDEEEEEDN EVEIEVELDR EEEPTEPIIE VPTSFSAQQI WVRDTSEPQK EPNFRNITHD YNATNGAEIE LTLSEDEEDY YGSSTNLKDH QVSNTALLNT QTPIYGTEHN SENTDFGDSG RLYYCKHCDF NNKSARSVST HYQRMHPYIK FSFRYILDPN DHSAVYRCLE CYIDYTNFED LQQHYGEHHP EAMNVLNFDH SDLIYRCRFC SYTSPNVRSL MPHYQRMHPT VKINNAMIFS SYVVEQQEGL NTESQTLREI LNSAPKNMAT STPVARGGGL PATFNKNTPK TFTPECENQK DPLVNTVVVY DCDVCSFASP NMHSVLVHYQ KKHPEEKASY FRIQKTMRMV SVDRGSALSQ LSFEVGAPMS PKMSNMGSPP PPQPPPPDLS TELYYCKHCS YSNRSVVGVL VHYQKRHPEI KVTAKYIRQA PPTAAMMRGV EGPQGSPRPP APIQQLNRSS SERDGPPVEN EMFFCQHCDY GNRTVKGVLI HYQKKHRDFK ANADVIRQHT ATIRSLCDRN QKKPASCVLV SPSNLERDKT KLRALKCRQC SYTSPYFYAL RKHIKKDHPA LKATVTSIMR WAFLDGLIEA GYHCEWCIYS HTEPNGLLLH YQRRHPEHYV DYTYMATKLW AGPDPSPPSL TMPAEAKTYR CRDCVFEAVS IWDITNHYQA FHPWAMNGDE SVLLDIIKEK DAVEKPILSS EELAGPVNCE NSIPTPFPEQ EAECPEDARL SPEKSLQLAS ANPAISSTPY QCTVCQSEYN NLHGLLTHYG KKHPGMKVKA ADFAQDIDIN PGAVYKCRHC PYINTRIHGV LTHYQKRHPS IKVTAEDFVH DVEQSADISQ NDVEETSRIF KQGYGAYRCK LCPYTHGTLE KLKIHYEKYH NQPEFDVFSQ SPPKLPVPLE PEMTTEVSPS QVSITEEEVG EEPVSTSHFS TSHLVSHTVF RCQLCKYFCS TRKGIARHYR IKHNNVRAQP EGKNNLFKCA LCAYTNPIRK GLAAHYQKRH DIDAYYTHCL AASRTISDKP NKVIIPSPPK DDSPQLSEEL RRAVEKKKCS LCSFQSFSKK GIVSHYMKRH PGVFPKKQHA SKLGGYFTAV YADEHEKPTL MEEEERGNFE KAEVEGEAQE IEWLPFRCIK CFKLSFSTAE LLCMHYTDHH SRDLKRDFII LGNGPRLQNS TYQCKHCDSK LQSTAELTSH LNIHNEEFQK RAKRQERRKQ LLSKQKYADG AFADFKQERP FGHLEEVPKI KERKVVGYKC KFCVEVHPTL RAICNHLRKH VQYGNVPAVS AAVKGLRSHE RSHLALAMFT REDKYSCQYC SFVSAFRHNL DRHMQTHHGH HKPFRCKLCS FKSSYNSRLK THILKAHAGE HAYKCSWCSF STMTISQLKE HSLKVHGKAL TLPRPRIVSL LSSHSHHSSQ KATPAEEVED SNDSSYSEPP DVQQQLNHYQ SAALARNNSR VSPVPLSGAA AGTEQKTEAV LHCEFCEFSS GYIQSIRRHY RDKHGGKKLF KCKDCSFYTG FKSAFTMHVE AGHSAVPEEG PKDLRCPLCL YHTKYKRNMI DHIVLHREER VVPIEVCRSK LSKYLQGVVF RCDKCTFTCS SDESLQQHIE KHNELKPYKC QLCYYETKHT EELDSHLRDE HKVSRNFELV GRVNLDQLEQ MKEKMESSSS DDEDKEEEMN SKAEDRELMR FSDHGAALNT EKRFPCEFCG RAFSQGSEWE RHVLRHGMAL NDTKQVSREE IHPKEIMENS VKMPSIEEKE DDEAIGIDFS LKNETVAICV VTADKSLLEN AEAKKE //