ZMYM2_HUMAN
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 03-AUG-2022, entry version 195.
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="http://atlasgeneticsoncology.org/Genes/ZNF198ID114.html";
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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; 136.
DR CORUM; Q9UBW7; -.
DR IntAct; Q9UBW7; 75.
DR MINT; Q9UBW7; -.
DR STRING; 9606.ENSP00000479904; -.
DR iPTMnet; Q9UBW7; -.
DR PhosphoSitePlus; Q9UBW7; -.
DR BioMuta; ZMYM2; -.
DR DMDM; 17369677; -.
DR EPD; Q9UBW7; -.
DR jPOST; Q9UBW7; -.
DR MassIVE; Q9UBW7; -.
DR MaxQB; Q9UBW7; -.
DR PaxDb; Q9UBW7; -.
DR PeptideAtlas; Q9UBW7; -.
DR PRIDE; Q9UBW7; -.
DR ProteomicsDB; 84085; -. [Q9UBW7-1]
DR ProteomicsDB; 84086; -. [Q9UBW7-2]
DR Antibodypedia; 22277; 149 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 CTD; 7750; -.
DR DisGeNET; 7750; -.
DR GeneCards; ZMYM2; -.
DR HGNC; HGNC:12989; ZMYM2.
DR HPA; ENSG00000121741; Low tissue specificity.
DR MIM; 602221; gene.
DR MIM; 619522; phenotype.
DR neXtProt; NX_Q9UBW7; -.
DR OpenTargets; ENSG00000121741; -.
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; EMKQFCD; -.
DR OrthoDB; 587724at2759; -.
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 BioGRID-ORCS; 7750; 24 hits in 1081 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 205 other tissues.
DR ExpressionAtlas; Q9UBW7; baseline and differential.
DR Genevisible; Q9UBW7; HS.
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 transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR021893; DUF3504.
DR InterPro; IPR011017; TRASH_dom.
DR InterPro; IPR010507; Znf_MYM.
DR Pfam; PF12012; DUF3504; 1.
DR Pfam; PF06467; zf-FCS; 8.
DR SMART; SM00746; TRASH; 9.
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 352..386
FT /note="MYM-type 1"
FT ZN_FING 398..436
FT /note="MYM-type 2"
FT ZN_FING 445..480
FT /note="MYM-type 3"
FT ZN_FING 491..549
FT /note="MYM-type 4"
FT ZN_FING 559..597
FT /note="MYM-type 5"
FT ZN_FING 605..652
FT /note="MYM-type 6"
FT ZN_FING 660..694
FT /note="MYM-type 7"
FT ZN_FING 701..740
FT /note="MYM-type 8"
FT ZN_FING 747..781
FT /note="MYM-type 9"
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 (likely benign variant; found in a patient
FT with congenital anomalies of the kidney and urinary tract;
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 (likely benign variant; found in a patient
FT with congenital anomalies of the kidney and urinary tract;
FT no effect 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 (likely benign variant; found in a patient
FT with congenital anomalies of the kidney and urinary tract;
FT no effect 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 (likely benign variant; found in a patient
FT with congenital anomalies of the kidney and urinary tract;
FT no effect 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 (likely benign variant; found in a patient
FT with congenital anomalies of the kidney and urinary tract;
FT no effect 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 (likely benign variant; found in a patient
FT with congenital anomalies of the kidney and urinary tract;
FT requires 2 nucleotide substitutions; no effect on
FT localization to the nucleus)"
FT /evidence="ECO:0000269|PubMed:32891193"
FT /id="VAR_086283"
FT VARIANT 775
FT /note="G -> E (likely benign variant; found in a patient
FT with congenital anomalies of the kidney and urinary tract;
FT no effect 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 (likely benign variant; found in a patient
FT with congenital anomalies of the kidney and urinary tract;
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 (likely benign variant; found in a patient
FT with congenital anomalies of the kidney and urinary tract;
FT no effect 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
