ZN462_HUMAN
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 03-AUG-2022, entry version 168.
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};
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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; 43.
DR DIP; DIP-39340N; -.
DR ELM; Q96JM2; -.
DR IntAct; Q96JM2; 31.
DR MINT; Q96JM2; -.
DR STRING; 9606.ENSP00000277225; -.
DR GlyGen; Q96JM2; 2 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; Q96JM2; -.
DR PeptideAtlas; Q96JM2; -.
DR PRIDE; Q96JM2; -.
DR ProteomicsDB; 76981; -. [Q96JM2-1]
DR ProteomicsDB; 76982; -. [Q96JM2-2]
DR ProteomicsDB; 76983; -. [Q96JM2-3]
DR Antibodypedia; 14859; 75 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 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; Metopic ridging-ptosis-facial dysmorphism syndrome.
DR PharmGKB; PA134949139; -.
DR VEuPathDB; HostDB:ENSG00000148143; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156411; -.
DR InParanoid; Q96JM2; -.
DR OMA; GYYSQHI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q96JM2; -.
DR TreeFam; TF325534; -.
DR PathwayCommons; Q96JM2; -.
DR SignaLink; Q96JM2; -.
DR SIGNOR; Q96JM2; -.
DR BioGRID-ORCS; 58499; 17 hits in 1080 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 190 other tissues.
DR ExpressionAtlas; Q96JM2; baseline and differential.
DR Genevisible; Q96JM2; HS.
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:0043392; P:negative regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 34.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
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
