ID ZMYM2_HUMAN Reviewed; 1377 AA. AC Q9UBW7; A6NDG0; A6NI02; O43212; O43434; O60898; Q5W0Q4; Q5W0T3; Q63HP0; AC Q8NE39; Q9H0V5; Q9H538; Q9UEU2; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 204. DE RecName: Full=Zinc finger MYM-type protein 2; DE AltName: Full=Fused in myeloproliferative disorders protein; DE AltName: Full=Rearranged in atypical myeloproliferative disorder protein; DE AltName: Full=Zinc finger protein 198; GN Name=ZMYM2; Synonyms=FIM, RAMP, ZNF198; 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), AND CHROMOSOMAL TRANSLOCATION. RX PubMed=9576949; DOI=10.1073/pnas.95.10.5712; RA Popovici C., Adelaide J., Ollendorff V., Chaffanet M., Guasch G., RA Jacrot M., Leroux D., Birnbaum D., Pebusque M.-J.; RT "Fibroblast growth factor receptor 1 is fused to FIM in stem-cell RT myeloproliferative disorder with t(8;13)(p12;q12)."; RL Proc. Natl. Acad. Sci. U.S.A. 95:5712-5717(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9716603; RA Reiter A., Sohal J., Kulkarni S., Chase A., Macdonald D.H.C., RA Aguiar R.C.T., Goncalves C., Hernandez J.M., Jennings B.A., Goldman J.M., RA Cross N.C.P.; RT "Consistent fusion of ZNF198 to the fibroblast growth factor receptor-1 in RT the t(8;13)(p11;q12) myeloproliferative syndrome."; RL Blood 92:1735-1742(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9889006; DOI=10.1006/geno.1998.5634; RA Kulkarni S., Reiter A.J., Smedley D., Goldman J.M., Cross N.C.P.; RT "The genomic structure of ZNF198 and location of breakpoints in the t(8;13) RT myeloproliferative syndrome."; RL Genomics 55:118-121(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Endometrial tumor; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 152-1377 (ISOFORM 1). RX PubMed=9694738; RA Still I.H., Cowell J.K.; RT "The t(8;13) atypical myeloproliferative disorder: further analysis of the RT ZNF198 gene and lack of evidence for multiple genes disrupted on chromosome RT 13."; RL Blood 92:1456-1458(1998). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 170-1020 (ISOFORM 1). RX PubMed=9499416; DOI=10.1093/hmg/7.4.637; RA Smedley D., Hamoudi R., Clark J., Warren W., Abdul-Rauf M., Somers G., RA Venter D., Fagan K., Cooper C., Shipley J.; RT "The t(8;13)(p11;q11-12) rearrangement associated with an atypical RT myeloproliferative disorder fuses the fibroblast growth factor receptor 1 RT gene to a novel gene RAMP."; RL Hum. Mol. Genet. 7:637-642(1998). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 621-1377 (ISOFORM 1). RX PubMed=9425908; DOI=10.1038/ng0198-84; RA Xiao S., Nalabolu S.R., Aster J.C., Ma J., Abruzzo L., Jaffe E.S., RA Stone R., Weissman S.M., Hudson T.J., Fletcher J.A.; RT "FGFR1 is fused with a novel zinc-finger gene, ZNF198, in the t(8;13) RT leukaemia/lymphoma syndrome."; RL Nat. Genet. 18:84-87(1998). RN [12] RP IDENTIFICATION IN THE BHC COMPLEX WITH GSE1; GTF2I; HDAC1; HDAC2; HMG20B; RP KDM1A; RCOR1; PHF21A; ZNF217 AND ZMYM3. RX PubMed=12493763; DOI=10.1074/jbc.m208992200; RA Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.; RT "A candidate X-linked mental retardation gene is a component of a new RT family of histone deacetylase-containing complexes."; RL J. Biol. Chem. 278:7234-7239(2003). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-838 AND THR-1376, AND RP IDENTIFICATION BY 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 [14] 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305 AND THR-1376, AND RP IDENTIFICATION BY 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 [16] 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 [17] 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305; SER-838 AND SER-958, AND 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159; SER-305 AND SER-838, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-88; LYS-98; LYS-104; LYS-253; RP LYS-297; LYS-441; LYS-529; LYS-532 AND LYS-649, 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 [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-88; LYS-297; LYS-325; LYS-529 AND RP LYS-576, 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 [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-88; LYS-98; LYS-441; LYS-513; RP LYS-529; LYS-532 AND LYS-700, 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 [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-88; LYS-98; LYS-104; RP LYS-147; LYS-253; LYS-297; LYS-312; LYS-325; LYS-348; LYS-366; LYS-417; RP LYS-441; LYS-491; LYS-503; LYS-513; LYS-529; LYS-532; LYS-576; LYS-603; RP LYS-649; LYS-658; LYS-688; LYS-700; LYS-709; LYS-764; LYS-788; LYS-812 AND RP LYS-829, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [24] RP VARIANTS VAL-61 DEL; ALA-126; VAL-387; ARG-649; HIS-763; LEU-763; GLU-775; RP ASP-997 DEL AND LYS-1031, CHARACTERIZATION OF VARIANTS VAL-61 DEL; ALA-126; RP VAL-387; ARG-649; HIS-763; LEU-763; GLU-775; ASP-997 DEL AND LYS-1031, RP VARIANTS NECRC 208-ARG--ASP-1377 DEL; 398-GLN--ASP-1377 DEL; RP 540-ARG--ASP-1377 DEL; 722-LEU--ASP-1377 DEL; 780-ARG--ASP-1377 DEL AND RP 1082-TRP--ASP-1377 DEL, CHARACTERIZATION OF VARIANTS NECRC RP 398-GLN--ASP-1377 DEL AND 540-ARG--ASP-1377 DEL, FUNCTION, SUBCELLULAR RP LOCATION, AND INTERACTION WITH FOXP1 AND FOXP2. RX PubMed=32891193; DOI=10.1016/j.ajhg.2020.08.013; RA Connaughton D.M., Dai R., Owen D.J., Marquez J., Mann N., RA Graham-Paquin A.L., Nakayama M., Coyaud E., Laurent E.M.N., RA St-Germain J.R., Blok L.S., Vino A., Klaembt V., Deutsch K., Wu C.W., RA Kolvenbach C.M., Kause F., Ottlewski I., Schneider R., Kitzler T.M., RA Majmundar A.J., Buerger F., Onuchic-Whitford A.C., Youying M., Kolb A., RA Salmanullah D., Chen E., van der Ven A.T., Rao J., Ityel H., Seltzsam S., RA Rieke J.M., Chen J., Vivante A., Hwang D.Y., Kohl S., Dworschak G.C., RA Hermle T., Alders M., Bartolomaeus T., Bauer S.B., Baum M.A., RA Brilstra E.H., Challman T.D., Zyskind J., Costin C.E., Dipple K.M., RA Duijkers F.A., Ferguson M., Fitzpatrick D.R., Fick R., Glass I.A., RA Hulick P.J., Kline A.D., Krey I., Kumar S., Lu W., Marco E.J., RA Wentzensen I.M., Mefford H.C., Platzer K., Povolotskaya I.S., Savatt J.M., RA Shcherbakova N.V., Senguttuvan P., Squire A.E., Stein D.R., Thiffault I., RA Voinova V.Y., Somers M.J.G., Ferguson M.A., Traum A.Z., Daouk G.H., RA Daga A., Rodig N.M., Terhal P.A., van Binsbergen E., Eid L.A., Tasic V., RA Rasouly H.M., Lim T.Y., Ahram D.F., Gharavi A.G., Reutter H.M., Rehm H.L., RA MacArthur D.G., Lek M., Laricchia K.M., Lifton R.P., Xu H., Mane S.M., RA Sanna-Cherchi S., Sharrocks A.D., Raught B., Fisher S.E., Bouchard M., RA Khokha M.K., Shril S., Hildebrandt F.; RT "Mutations of the transcriptional corepressor ZMYM2 cause syndromic urinary RT tract malformations."; RL Am. J. Hum. Genet. 107:727-742(2020). CC -!- FUNCTION: Involved in the negative regulation of transcription. CC {ECO:0000269|PubMed:32891193}. CC -!- SUBUNIT: Can form homodimers (PubMed:32891193). May be a component of a CC BHC histone deacetylase complex that contains HDAC1, HDAC2, CC HMG20B/BRAF35, KDM1A, RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, CC GSE1 and GTF2I. Interacts with FOXP1 and FOXP2 (PubMed:32891193). CC {ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:32891193}. CC -!- INTERACTION: CC Q9UBW7; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-2797576, EBI-2548508; CC Q9UBW7; Q9UHL9: GTF2IRD1; NbExp=5; IntAct=EBI-2797576, EBI-372530; CC Q9UBW7; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-2797576, EBI-747204; CC Q9UBW7; P22234: PAICS; NbExp=3; IntAct=EBI-2797576, EBI-712261; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32891193}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UBW7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UBW7-2; Sequence=VSP_039065, VSP_039066, VSP_039067; CC -!- DISEASE: Neurodevelopmental-craniofacial syndrome with variable renal CC and cardiac abnormalities (NECRC) [MIM:619522]: An autosomal dominant CC disorder characterized by dysmorphic craniofacial features, mild CC developmental delay, mildly impaired intellectual development or CC learning difficulties, speech delay, and behavioral abnormalities. CC About half of patients have congenital anomalies of the kidney and CC urinary tract and/or congenital cardiac defects, including septal CC defects. {ECO:0000269|PubMed:32891193}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Note=A chromosomal aberration involving ZMYM2 may be a cause CC of stem cell leukemia lymphoma syndrome (SCLL). Translocation CC t(8;13)(p11;q12) with FGFR1. SCLL usually presents as lymphoblastic CC lymphoma in association with a myeloproliferative disorder, often CC accompanied by pronounced peripheral eosinophilia and/or prominent CC eosinophilic infiltrates in the affected bone marrow. CC {ECO:0000269|PubMed:9716603}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB88464.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAC23591.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAA73875.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/114/ZNF198"; 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; Y13472; CAA73875.1; ALT_FRAME; mRNA. DR EMBL; AJ224901; CAA12204.1; -; mRNA. DR EMBL; AJ007676; CAA07604.1; -; Genomic_DNA. DR EMBL; AJ007677; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007678; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007679; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007680; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007681; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007682; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007683; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007684; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007685; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007686; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007687; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007688; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007689; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007690; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007691; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007692; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007693; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007694; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007695; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AJ007696; CAA07604.1; JOINED; Genomic_DNA. DR EMBL; AL136621; CAB66556.2; -; mRNA. DR EMBL; BX647944; CAH56193.1; -; mRNA. DR EMBL; AL137119; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL138688; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471075; EAX08244.1; -; Genomic_DNA. DR EMBL; CH471075; EAX08247.1; -; Genomic_DNA. DR EMBL; BC036372; AAH36372.1; -; mRNA. DR EMBL; AF060181; AAC23591.1; ALT_FRAME; mRNA. DR EMBL; AF035374; AAB88464.1; ALT_FRAME; mRNA. DR EMBL; AF012126; AAC01561.1; -; mRNA. DR CCDS; CCDS45016.1; -. [Q9UBW7-1] DR PIR; T45119; T45119. DR RefSeq; NP_001177893.1; NM_001190964.2. [Q9UBW7-1] DR RefSeq; NP_001177894.1; NM_001190965.2. [Q9UBW7-1] DR RefSeq; NP_003444.1; NM_003453.4. [Q9UBW7-1] DR RefSeq; NP_932072.1; NM_197968.3. [Q9UBW7-1] DR RefSeq; XP_005266577.1; XM_005266520.3. [Q9UBW7-1] DR RefSeq; XP_011533526.1; XM_011535224.2. DR RefSeq; XP_016876218.1; XM_017020729.1. DR AlphaFoldDB; Q9UBW7; -. DR SMR; Q9UBW7; -. DR BioGRID; 113534; 257. DR CORUM; Q9UBW7; -. DR IntAct; Q9UBW7; 78. DR MINT; Q9UBW7; -. DR STRING; 9606.ENSP00000479904; -. DR GlyGen; Q9UBW7; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UBW7; -. DR PhosphoSitePlus; Q9UBW7; -. DR SwissPalm; Q9UBW7; -. DR BioMuta; ZMYM2; -. DR DMDM; 17369677; -. DR EPD; Q9UBW7; -. DR jPOST; Q9UBW7; -. DR MassIVE; Q9UBW7; -. DR MaxQB; Q9UBW7; -. DR PaxDb; 9606-ENSP00000479904; -. DR PeptideAtlas; Q9UBW7; -. DR ProteomicsDB; 84085; -. [Q9UBW7-1] DR ProteomicsDB; 84086; -. [Q9UBW7-2] DR Pumba; Q9UBW7; -. DR Antibodypedia; 22277; 176 antibodies from 23 providers. DR DNASU; 7750; -. DR Ensembl; ENST00000382871.3; ENSP00000372324.2; ENSG00000121741.17. [Q9UBW7-1] DR Ensembl; ENST00000382874.6; ENSP00000372327.2; ENSG00000121741.17. [Q9UBW7-1] DR Ensembl; ENST00000610343.5; ENSP00000479904.1; ENSG00000121741.17. [Q9UBW7-1] DR GeneID; 7750; -. DR KEGG; hsa:7750; -. DR MANE-Select; ENST00000610343.5; ENSP00000479904.1; NM_197968.4; NP_932072.1. DR UCSC; uc031zxt.2; human. [Q9UBW7-1] DR AGR; HGNC:12989; -. DR CTD; 7750; -. DR DisGeNET; 7750; -. DR GeneCards; ZMYM2; -. DR HGNC; HGNC:12989; ZMYM2. DR HPA; ENSG00000121741; Low tissue specificity. DR MalaCards; ZMYM2; -. DR MIM; 602221; gene. DR MIM; 619522; phenotype. DR neXtProt; NX_Q9UBW7; -. DR OpenTargets; ENSG00000121741; -. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR PharmGKB; PA37569; -. DR VEuPathDB; HostDB:ENSG00000121741; -. DR eggNOG; ENOG502QQQ9; Eukaryota. DR GeneTree; ENSGT00940000157028; -. DR HOGENOM; CLU_004099_0_0_1; -. DR InParanoid; Q9UBW7; -. DR OMA; KEPTCHF; -. DR OrthoDB; 5399298at2759; -. DR PhylomeDB; Q9UBW7; -. DR TreeFam; TF336988; -. DR PathwayCommons; Q9UBW7; -. DR Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants. DR Reactome; R-HSA-5655302; Signaling by FGFR1 in disease. DR Reactome; R-HSA-9703465; Signaling by FLT3 fusion proteins. DR SignaLink; Q9UBW7; -. DR SIGNOR; Q9UBW7; -. DR BioGRID-ORCS; 7750; 25 hits in 1170 CRISPR screens. DR ChiTaRS; ZMYM2; human. DR GeneWiki; ZMYM2; -. DR GenomeRNAi; 7750; -. DR Pharos; Q9UBW7; Tbio. DR PRO; PR:Q9UBW7; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q9UBW7; Protein. DR Bgee; ENSG00000121741; Expressed in sperm and 207 other cell types or tissues. DR ExpressionAtlas; Q9UBW7; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0016605; C:PML body; IDA:UniProtKB. DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR InterPro; IPR021893; DUF3504. DR InterPro; IPR011017; TRASH_dom. DR InterPro; IPR010507; Znf_MYM. DR PANTHER; PTHR45736; ZINC FINGER MYM-TYPE PROTEIN; 1. DR PANTHER; PTHR45736:SF6; ZINC FINGER MYM-TYPE PROTEIN 2; 1. DR Pfam; PF12012; DUF3504; 1. DR Pfam; PF06467; zf-FCS; 8. DR SMART; SM00746; TRASH; 9. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR Genevisible; Q9UBW7; HS. PE 1: Evidence at protein level; KW Alternative splicing; Chromosomal rearrangement; Disease variant; KW Intellectual disability; Isopeptide bond; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..1377 FT /note="Zinc finger MYM-type protein 2" FT /id="PRO_0000191382" FT ZN_FING 327..363 FT /note="MYM-type 1" FT /evidence="ECO:0000255" FT ZN_FING 369..409 FT /note="MYM-type 2" FT /evidence="ECO:0000255" FT ZN_FING 421..456 FT /note="MYM-type 3" FT /evidence="ECO:0000255" FT ZN_FING 463..502 FT /note="MYM-type 4" FT /evidence="ECO:0000255" FT ZN_FING 533..570 FT /note="MYM-type 5" FT /evidence="ECO:0000255" FT ZN_FING 636..671 FT /note="MYM-type 6" FT /evidence="ECO:0000255" FT ZN_FING 723..758 FT /note="MYM-type 7" FT /evidence="ECO:0000255" FT ZN_FING 764..799 FT /note="MYM-type 8" FT /evidence="ECO:0000255" FT REGION 85..177 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 273..305 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 983..1002 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1028..1064 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 85..115 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 150..177 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 913..914 FT /note="Breakpoint for translocation to form ZMYM2-FGFR1" FT MOD_RES 159 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 305 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 838 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 958 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1064 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CU65" FT MOD_RES 1376 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT CROSSLNK 48 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 88 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 98 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:28112733" FT CROSSLNK 104 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 147 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 253 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 297 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 312 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:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 348 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 366 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 417 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 441 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:28112733" FT CROSSLNK 491 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 503 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 513 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" FT CROSSLNK 529 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 532 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:28112733" FT CROSSLNK 576 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 603 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 649 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 658 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 688 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 700 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" FT CROSSLNK 709 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 764 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 788 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 812 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 829 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 165..251 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11230166" FT /id="VSP_039065" FT VAR_SEQ 529..549 FT /note="KYGKLTTCTGCRTQCRFFDMT -> VSRNVNGVQGLNIFEHCYYCH (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:11230166" FT /id="VSP_039066" FT VAR_SEQ 550..1377 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11230166" FT /id="VSP_039067" FT VARIANT 61 FT /note="Missing (found in a patient with congenital FT anomalies of the kidney and urinary tract; likely benign; FT no effect on localization to the nucleus)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086274" FT VARIANT 126 FT /note="E -> A (found in a patient with congenital anomalies FT of the kidney and urinary tract; likely benign; no effect FT on localization to the nucleus; no effect on FT transcriptional repression activity)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086275" FT VARIANT 208..1377 FT /note="Missing (in NECRC)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086276" FT VARIANT 387 FT /note="I -> V (found in a patient with congenital anomalies FT of the kidney and urinary tract; likely benign; no effect FT on localization to the nucleus; no effect on FT transcriptional repression activity)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086277" FT VARIANT 398..1377 FT /note="Missing (in NECRC; does not localize to the nucleus; FT decreased interaction with FOXP1 and FOXP2)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086278" FT VARIANT 540..1377 FT /note="Missing (in NECRC; does not localize to the nucleus; FT loss of interaction with FOXP1 and FOXP2)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086279" FT VARIANT 649 FT /note="K -> R (found in a patient with congenital anomalies FT of the kidney and urinary tract; likely benign; no effect FT on localization to the nucleus; no effect on FT transcriptional repression activity)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086280" FT VARIANT 722..1377 FT /note="Missing (in NECRC)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086281" FT VARIANT 763 FT /note="Y -> H (found in a patient with congenital anomalies FT of the kidney and urinary tract; likely benign; no effect FT on localization to the nucleus; no effect on FT transcriptional repression activity)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086282" FT VARIANT 763 FT /note="Y -> L (found in a patient with congenital anomalies FT of the kidney and urinary tract; likely benign; no effect FT on localization to the nucleus; requires 2 nucleotide FT substitutions)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086283" FT VARIANT 775 FT /note="G -> E (found in a patient with congenital anomalies FT of the kidney and urinary tract; likely benign; no effect FT on localization to the nucleus; no effect on FT transcriptional repression activity)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086284" FT VARIANT 780..1377 FT /note="Missing (in NECRC)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086285" FT VARIANT 997 FT /note="Missing (found in a patient with congenital FT anomalies of the kidney and urinary tract; likely benign; FT no effect on localization to the nucleus)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086286" FT VARIANT 1031 FT /note="E -> K (found in a patient with congenital anomalies FT of the kidney and urinary tract; likely benign; no effect FT on localization to the nucleus; no effect on FT transcriptional repression activity)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086287" FT VARIANT 1082..1377 FT /note="Missing (in NECRC)" FT /evidence="ECO:0000269|PubMed:32891193" FT /id="VAR_086288" FT CONFLICT 102 FT /note="S -> P (in Ref. 4; CAH56193)" FT /evidence="ECO:0000305" FT CONFLICT 110 FT /note="K -> E (in Ref. 7; AAH36372)" FT /evidence="ECO:0000305" FT CONFLICT 304 FT /note="L -> V (in Ref. 4; CAB66556)" FT /evidence="ECO:0000305" FT CONFLICT 330 FT /note="T -> S (in Ref. 4; CAB66556)" FT /evidence="ECO:0000305" FT CONFLICT 411..412 FT /note="DK -> EQ (in Ref. 1; CAA73875)" FT /evidence="ECO:0000305" FT CONFLICT 424 FT /note="R -> G (in Ref. 4; CAB66556)" FT /evidence="ECO:0000305" FT CONFLICT 736 FT /note="K -> G (in Ref. 1; CAA73875)" FT /evidence="ECO:0000305" FT CONFLICT 856 FT /note="T -> I (in Ref. 7; AAH36372)" FT /evidence="ECO:0000305" FT CONFLICT 967 FT /note="Missing (in Ref. 9; AAB88464)" FT /evidence="ECO:0000305" FT CONFLICT 1009..1010 FT /note="DF -> IS (in Ref. 9; AAB88464)" FT /evidence="ECO:0000305" FT CONFLICT 1016 FT /note="Missing (in Ref. 9; AAB88464)" FT /evidence="ECO:0000305" FT CONFLICT 1259 FT /note="C -> R (in Ref. 7; AAH36372)" FT /evidence="ECO:0000305" SQ SEQUENCE 1377 AA; 154911 MW; 2652D4C766492FF9 CRC64; MDTSSVGGLE LTDQTPVLLG STAMATSLTN VGNSFSGPAN PLVSRSNKFQ NSSVEDDDDV VFIEPVQPPP PSVPVVADQR TITFTSSKNE ELQGNDSKIT PSSKELASQK GSVSETIVID DEEDMETNQG QEKNSSNFIE RRPPETKNRT NDVDFSTSSF SRSKVNAGMG NSGITTEPDS EIQIANVTTL ETGVSSVNDG QLENTDGRDM NLMITHVTSL QNTNLGDVSN GLQSSNFGVN IQTYTPSLTS QTKTGVGPFN PGRMNVAGDV FQNGESATHH NPDSWISQSA SFPRNQKQPG VDSLSPVASL PKQIFQPSVQ QQPTKPVKVT CANCKKPLQK GQTAYQRKGS AHLFCSTTCL SSFSHKPAPK KLCVMCKKDI TTMKGTIVAQ VDSSESFQEF CSTSCLSLYE DKQNPTKGAL NKSRCTICGK LTEIRHEVSF KNMTHKLCSD HCFNRYRMAN GLIMNCCEQC GEYLPSKGAG NNVLVIDGQQ KRFCCQSCVS EYKQVGSHPS FLKEVRDHMQ DSFLMQPEKY GKLTTCTGCR TQCRFFDMTQ CIGPNGYMEP YCSTACMNSH KTKYAKSQSL GIICHFCKRN SLPQYQATMP DGKLYNFCNS SCVAKFQALS MQSSPNGQFV APSDIQLKCN YCKNSFCSKP EILEWENKVH QFCSKTCSDD YKKLHCIVTY CEYCQEEKTL HETVNFSGVK RPFCSEGCKL LYKQDFARRL GLRCVTCNYC SQLCKKGATK ELDGVVRDFC SEDCCKKFQD WYYKAARCDC CKSQGTLKER VQWRGEMKHF CDQHCLLRFY CQQNEPNMTT QKGPENLHYD QGCQTSRTKM TGSAPPPSPT PNKEMKNKAV LCKPLTMTKA TYCKPHMQTK SCQTDDTWRT EYVPVPIPVP VYIPVPMHMY SQNIPVPTTV PVPVPVPVFL PAPLDSSEKI PAAIEELKSK VSSDALDTEL LTMTDMMSED EGKTETTNIN SVIIETDIIG SDLLKNSDPE TQSSMPDVPY EPDLDIEIDF PRAAEELDME NEFLLPPVFG EEYEEQPRPR SKKKGAKRKA VSGYQSHDDS SDNSECSFPF KYTYGVNAWK HWVKTRQLDE DLLVLDELKS SKSVKLKEDL LSHTTAELNY GLAHFVNEIR RPNGENYAPD SIYYLCLGIQ EYLCGSNRKD NIFIDPGYQT FEQELNKILR SWQPSILPDG SIFSRVEEDY LWRIKQLGSH SPVALLNTLF YFNTKYFGLK TVEQHLRLSF GTVFRHWKKN PLTMENKACL RYQVSSLCGT DNEDKITTGK RKHEDDEPVF EQIENTANPS RCPVKMFECY LSKSPQNLNQ RMDVFYLQPE CSSSTDSPVW YTSTSLDRNT LENMLVRVLL VKDIYDKDNY ELDEDTD //