MEN1_HUMAN
ID MEN1_HUMAN Reviewed; 615 AA.
AC O00255; A5HBC6; A5HBC7; A5HBC8; A5HBC9; A5HBD0; A5HBD1; A5HBD2; O00632;
AC Q9BUF0; Q9BUK2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Menin;
GN Name=MEN1; Synonyms=SCG2;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANTS MEN1
RP ARG-22; LYS-119 DEL; GLU-368 DEL AND ARG-441, AND VARIANTS GLN-176 AND
RP ALA-546.
RC TISSUE=Leukocyte;
RX PubMed=9103196; DOI=10.1126/science.276.5311.404;
RA Chandrasekharappa S.C., Guru S.C., Manickam P., Olufemi S.-E.,
RA Collins F.S., Emmert-Buck M.R., Debelenko L.V., Zhuang Z., Lubensky I.A.,
RA Liotta L.A., Crabtree J.S., Wang Y., Roe B.A., Weisemann J., Boguski M.S.,
RA Agarwal S.K., Kester M.B., Kim Y.S., Heppner C., Dong Q., Spiegel A.M.,
RA Burns A.L., Marx S.J.;
RT "Positional cloning of the gene for multiple endocrine neoplasia-type 1.";
RL Science 276:404-407(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANTS MEN1 89-LEU--ALA-95
RP DEL; PHE-147; ARG-418; PRO-419 AND CYS-476, AND VARIANT ALA-546.
RX PubMed=17555499; DOI=10.1111/j.1365-2265.2007.02895.x;
RA Toledo R.A., Lourenco D.M., Coutinho F.L., Quedas E., Mackowiack I.,
RA Machado M.C., Montenegro F., Cunha-Neto M.B., Liberman B., Pereira M.A.,
RA Correa P.H., Toledo S.P.;
RT "Novel MEN1 germline mutations in Brazilian families with multiple
RT endocrine neoplasia type 1.";
RL Clin. Endocrinol. (Oxf.) 67:377-384(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ALA-546.
RC TISSUE=Placenta, and Uterus;
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 [5]
RP INTERACTION WITH JUND, AND VARIANTS MEN1 LEU-12; ARG-22; ASP-139; TYR-139;
RP PRO-165; PRO-181; VAL-247; PRO-291; PRO-314; ARG-349 AND ARG-441.
RX PubMed=9989505; DOI=10.1016/s0092-8674(00)80967-8;
RA Agarwal S.K., Guru S.C., Heppner C., Erdos M.R., Collins R.M., Park S.Y.,
RA Saggar S., Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Marx S.J.,
RA Burns A.L.;
RT "Menin interacts with the AP1 transcription factor JunD and represses JunD-
RT activated transcription.";
RL Cell 96:143-152(1999).
RN [6]
RP FUNCTION, AND INTERACTION WITH NFKB1; NFKB2 AND RELA.
RX PubMed=11526476; DOI=10.1038/sj.onc.1204529;
RA Heppner C., Bilimoria K.Y., Agarwal S.K., Kester M., Whitty L.J.,
RA Guru S.C., Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Marx S.J.,
RA Burns A.L.;
RT "The tumor suppressor protein menin interacts with NF-kappaB proteins and
RT inhibits NF-kappaB-mediated transactivation.";
RL Oncogene 20:4917-4925(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH SMAD3.
RX PubMed=11274402; DOI=10.1073/pnas.061358098;
RA Kaji H., Canaff L., Lebrun J.J., Goltzman D., Hendy G.N.;
RT "Inactivation of menin, a Smad3-interacting protein, blocks transforming
RT growth factor type beta signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3837-3842(2001).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FANCD2.
RX PubMed=12874027;
RA Jin S., Mao H., Schnepp R.W., Sykes S.M., Silva A.C., D'Andrea A.D.,
RA Hua X.;
RT "Menin associates with FANCD2, a protein involved in repair of DNA
RT damage.";
RL Cancer Res. 63:4204-4210(2003).
RN [9]
RP FUNCTION IN TERT REPRESSION.
RX PubMed=12837246; DOI=10.1016/s0092-8674(03)00430-6;
RA Lin S.Y., Elledge S.J.;
RT "Multiple tumor suppressor pathways negatively regulate telomerase.";
RL Cell 113:881-889(2003).
RN [10]
RP INTERACTION WITH DBF4.
RX PubMed=15374998; DOI=10.1158/0008-5472.can-04-0724;
RA Schnepp R.W., Hou Z., Wang H., Petersen C., Silva A., Masai H., Hua X.;
RT "Functional interaction between tumor suppressor menin and activator of S-
RT phase kinase.";
RL Cancer Res. 64:6791-6796(2004).
RN [11]
RP FUNCTION IN H3K4 METHYLATION, IDENTIFICATION IN THE MEN1-ASSOCIATED HISTONE
RP METHYLTRANSFERASE COMPLEX, INTERACTION WITH POLR2A AND POLR2B, AND VARIANTS
RP MEN1 LEU-12; ARG-22; ASP-139; VAL-247; PRO-314; ARG-349 AND ARG-441.
RX PubMed=14992727; DOI=10.1016/s1097-2765(04)00081-4;
RA Hughes C.M., Rozenblatt-Rosen O., Milne T.A., Copeland T.D., Levine S.S.,
RA Lee J.C., Hayes D.N., Shanmugam K.S., Bhattacharjee A., Biondi C.A.,
RA Kay G.F., Hayward N.K., Hess J.L., Meyerson M.;
RT "Menin associates with a trithorax family histone methyltransferase complex
RT and with the hoxc8 locus.";
RL Mol. Cell 13:587-597(2004).
RN [12]
RP IDENTIFICATION IN THE MLL-HCF COMPLEX.
RX PubMed=15199122; DOI=10.1128/mcb.24.13.5639-5649.2004;
RA Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J., Kitabayashi I.,
RA Herr W., Cleary M.L.;
RT "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase
RT complex with menin to regulate Hox gene expression.";
RL Mol. Cell. Biol. 24:5639-5649(2004).
RN [13]
RP INTERACTION WITH DPY30.
RX PubMed=17500065; DOI=10.1074/jbc.m701574200;
RA Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T.,
RA Dressler G.R., Copeland T.D., Kalkum M., Ge K.;
RT "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4
RT methyltransferase complex.";
RL J. Biol. Chem. 282:20395-20406(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-599, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548 AND THR-599, VARIANT
RP [LARGE SCALE ANALYSIS] ALA-546, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [18]
RP INTERACTION WITH KMT2A AND FUSION PROTEIN KMT2A-MLLT3, AND INTERACTION OF
RP KMT2A-MEN1 COMPLEX WITH PSIP1.
RX PubMed=25305204; DOI=10.1182/blood-2014-01-550079;
RA Murai M.J., Pollock J., He S., Miao H., Purohit T., Yokom A., Hess J.L.,
RA Muntean A.G., Grembecka J., Cierpicki T.;
RT "The same site on the integrase-binding domain of lens epithelium-derived
RT growth factor is a therapeutic target for MLL leukemia and HIV.";
RL Blood 124:3730-3737(2014).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20] {ECO:0007744|PDB:4GPQ, ECO:0007744|PDB:4GQ3, ECO:0007744|PDB:4GQ4, ECO:0007744|PDB:4GQ6}
RP X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) OF 1-598 IN COMPLEX WITH KMT2A AND
RP INHIBITORS MI-2 AND MI-2-2, AND INTERACTION WITH KMT2A AND FUSION PROTEIN
RP KMT2A-MLLT3.
RX PubMed=22936661; DOI=10.1182/blood-2012-05-429274;
RA Shi A., Murai M.J., He S., Lund G., Hartley T., Purohit T., Reddy G.,
RA Chruszcz M., Grembecka J., Cierpicki T.;
RT "Structural insights into inhibition of the bivalent menin-MLL interaction
RT by small molecules in leukemia.";
RL Blood 120:4461-4469(2012).
RN [21] {ECO:0007744|PDB:3U84, ECO:0007744|PDB:3U85, ECO:0007744|PDB:3U86, ECO:0007744|PDB:3U88}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-615 IN COMPLEX WITH KMT2A;
RP PSIP1 AND JUND, INTERACTION WITH KMT2A AND JUND, INTERACTION OF KMT2A-MEN1
RP COMPLEX WITH PSIP1, CHARACTERIZATION OF VARIANTS MEN1 ASP-139; PHE-246;
RP VAL-247; ARG-286 AND ARG-349, CHARACTERIZATION OF VARIANT GLN-289,
RP MUTAGENESIS OF ALA-187; MET-283; ASP-290; GLU-293; GLU-295; TYR-324;
RP TYR-328; GLU-371 AND ASP-375, AND FUNCTION.
RX PubMed=22327296; DOI=10.1038/nature10806;
RA Huang J., Gurung B., Wan B., Matkar S., Veniaminova N.A., Wan K.,
RA Merchant J.L., Hua X., Lei M.;
RT "The same pocket in menin binds both MLL and JUND but has opposite effects
RT on transcription.";
RL Nature 482:542-546(2012).
RN [22]
RP VARIANTS MEN1.
RX PubMed=9215689; DOI=10.1093/hmg/6.7.1169;
RA Agarwal S.K., Kester M.B., Debelenko L.V., Heppner C., Emmert-Buck M.R.,
RA Skarulis M.C., Doppman J.L., Kim Y.S., Lubensky I.A., Zhuang Z.,
RA Green J.S., Guru S.C., Manickam P., Olufemi S.E., Liotta L.A.,
RA Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Burns A.L., Marx S.J.;
RT "Germline mutations of the MEN1 gene in familial multiple endocrine
RT neoplasia type 1 and related states.";
RL Hum. Mol. Genet. 6:1169-1175(1997).
RN [23]
RP VARIANT MEN1 SER-188, AND VARIANT GLN-176.
RX PubMed=9215690; DOI=10.1093/hmg/6.7.1177;
RG The European consortium on MEN1;
RA Lemmens I., Van de Ven W.J.M., Kas K., Zhang C.X., Giraud S., Wautot V.,
RA Buisson N., De Witte K., Salandre J., Lenoir G., Pugeat M., Calender A.,
RA Parente F., Quincey D., Gaudray P., De Wit M.J., Lips C.J.M.,
RA Hoeppener J.W.M., Khodaei S., Grant A.L., Weber G., Kytoelae S., Teh B.T.,
RA Farnebo F., Phelan C., Hayward N., Larsson C., Pannett A.A.J., Forbes S.A.,
RA Basset J.H.D., Thakker R.V.;
RT "Identification of the multiple endocrine neoplasia type 1 (MEN1) gene.";
RL Hum. Mol. Genet. 6:1177-1183(1997).
RN [24]
RP VARIANT PARATHYROID ADENOMA LYS-26.
RX PubMed=9241276; DOI=10.1038/ng0897-375;
RA Heppner C., Kester M.B., Agarwal S.K., Debelenko L.V., Emmert-Buck M.R.,
RA Guru S.C., Manickam P., Olufemi S.-E., Skarulis M.C., Doppman J.L.,
RA Alexander R.H., Kim Y.S., Saggar S.K., Lubensky I.A., Zhuang Z.,
RA Liotta L.A., Chandrasekharappa S.C., Collins F.S., Spiegel A.M.,
RA Burns A.L., Marx S.J.;
RT "Somatic mutation of the MEN1 gene in parathyroid tumours.";
RL Nat. Genet. 16:375-378(1997).
RN [25]
RP VARIANTS MEN1 ASP-42; PRO-165; ASP-169; SER-188 AND GLU-289.
RX PubMed=9463336; DOI=10.1086/301729;
RA Bassett J.H.D., Forbes S.A., Pannett A.A.J., Lloyd S.E., Christie P.T.,
RA Wooding C., Harding B., Besser G.M., Edwards C.R., Monson J.P., Sampson J.,
RA Wass J.A.H., Wheeler M.H., Thakker R.V.;
RT "Characterization of mutations in patients with multiple endocrine
RT neoplasia type 1.";
RL Am. J. Hum. Genet. 62:232-244(1998).
RN [26]
RP VARIANTS MEN1.
RX PubMed=9683585; DOI=10.1086/301953;
RA Giraud S., Zhang C.X., Serova-Sinilnikova O., Wautot V., Salandre J.,
RA Buisson N., Waterlot C., Bauters C., Porchet N., Aubert J.-P., Emy P.,
RA Cadiot G., Delemer B., Chabre O., Niccoli P., Leprat F., Duron F.,
RA Emperauger B., Cougard P., Goudet P., Sarfati E., Riou J.-P., Guichard S.,
RA Rodier M., Meyrier A., Caron P., Vantyghem M.-C., Assayag M., Peix J.-L.,
RA Pugeat M., Rohmer V., Vallotton M., Lenoir G., Gaudray P., Proye C.,
RA Conte-Devolx B., Chanson P., Shugart Y.Y., Goldgar D., Murat A.,
RA Calender A.;
RT "Germ-line mutation analysis in patients with multiple endocrine neoplasia
RT type 1 and related disorders.";
RL Am. J. Hum. Genet. 63:455-467(1998).
RN [27]
RP VARIANT LYS-260, AND INVOLVEMENT IN ISOLATED HYPERPARATHYROIDISM.
RX PubMed=9792884; DOI=10.1086/302097;
RA Teh B.T., Esapa C.T., Houlston R., Grandell U., Farnebo F.,
RA Nordenskjoeld M., Pearce C.J., Carmichael D., Larsson C., Harris P.E.;
RT "A family with isolated hyperparathyroidism segregating a missense MEN1
RT mutation and showing loss of the wild-type alleles in the parathyroid
RT tumors.";
RL Am. J. Hum. Genet. 63:1544-1549(1998).
RN [28]
RP VARIANT GLU-189, AND INVOLVEMENT IN ISOLATED HYPERPARATHYROIDISM.
RX PubMed=9843042;
RX DOI=10.1002/(sici)1096-8628(19981116)80:3<221::aid-ajmg8>3.0.co;2-1;
RA Fujimori M., Shirahama S., Sakurai A., Hashizume K., Hama Y., Ito K.,
RA Shingu K., Kobayashi S., Amano J., Fukushima Y.;
RT "Novel V184E MEN1 germline mutation in a Japanese kindred with familial
RT hyperparathyroidism.";
RL Am. J. Med. Genet. 80:221-222(1998).
RN [29]
RP VARIANTS MEN1 LYS-26 AND PRO-173.
RX PubMed=9820618; DOI=10.1530/eje.0.1390416;
RA Bartsch D., Kopp I., Bergenfelz A., Rieder H., Muench K., Jaeger K.,
RA Deiss Y., Schudy A., Barth P., Arnold R., Rothmund M., Simon B.;
RT "MEN1 gene mutations in 12 MEN1 families and their associated tumors.";
RL Eur. J. Endocrinol. 139:416-420(1998).
RN [30]
RP VARIANTS MEN1.
RX PubMed=9671267;
RX DOI=10.1002/(sici)1098-1004(1998)12:2<75::aid-humu1>3.0.co;2-t;
RA Agarwal S.K., Debelenko L.V., Kester M.B., Guru S.C., Manickam P.,
RA Olufemi S.-E., Skarulis M.C., Heppner C., Crabtree J.S., Lubensky I.A.,
RA Zhuang Z., Kim Y.S., Chandrasekharappa S.C., Collins F.S., Liotta L.A.,
RA Spiegel A.M., Burns A.L., Emmert-Buck M.R., Marx S.J.;
RT "Analysis of recurrent germline mutations in the MEN1 gene encountered in
RT apparently unrelated families.";
RL Hum. Mutat. 12:75-82(1998).
RN [31]
RP VARIANT MEN1 ARG-432.
RX PubMed=10660339;
RA Cote G.J., Lee J.E., Evans D.B., Huang E., Schultz P.N., Dang G.T., Qiu H.,
RA Shetelbine S., Sellin R.V., Gagel R.F.;
RT "Five novel mutations in the familial multiple endocrine neoplasia type 1
RT (MEN1) gene.";
RL Hum. Mutat. 12:219-219(1998).
RN [32]
RP VARIANT MEN1 LEU-325, AND VARIANT ALA-546.
RX PubMed=9506756; DOI=10.1210/jcem.83.3.4653;
RA Tanaka C., Yoshimoto K., Yamada S., Nishioka H., Ii S., Moritani M.,
RA Yamaoka T., Itakura M.;
RT "Absence of germ-line mutations of the multiple endocrine neoplasia type 1
RT (MEN1) gene in familial pituitary adenoma in contrast to MEN1 in
RT Japanese.";
RL J. Clin. Endocrinol. Metab. 83:960-965(1998).
RN [33]
RP VARIANT MEN1 ASN-423, AND VARIANTS GLN-176 AND ALA-546.
RX PubMed=9709921; DOI=10.1210/jcem.83.8.5059;
RA Teh B.T., Kytoelae S., Farnebo F., Bergman L., Wong F.K., Weber G.,
RA Hayward N., Larsson C., Skogseid B., Beckers A., Phelan C., Edwards M.,
RA Epstein M., Alford F., Hurley D., Grimmond S., Silins G., Walters M.,
RA Stewart C., Cardinal J., Khodaei S., Parente F., Tranebjaerg L., Jorde R.,
RA Menon J., Khir A., Tan T.T., Chan S.P., Zaini A., Khalid B.A.K.,
RA Sandelin K., Thompson N., Brandi M.-L., Warth M., Stock J., Leisti J.,
RA Cameron D., Shepherd J.J., Oeberg K., Nordenskjoeld M., Salmela P.;
RT "Mutation analysis of the MEN1 gene in multiple endocrine neoplasia type 1,
RT familial acromegaly and familial isolated hyperparathyroidism.";
RL J. Clin. Endocrinol. Metab. 83:2621-2626(1998).
RN [34]
RP VARIANT MEN1 ASP-139, AND VARIANT TRP-157.
RX PubMed=9709976; DOI=10.1210/jcem.83.8.4977;
RA Carling T., Correa P., Hessman O., Hedberg J., Skogseid B., Lindberg D.,
RA Rastad J., Westin G., Akerstrom G.;
RT "Parathyroid MEN1 gene mutations in relation to clinical characteristics of
RT nonfamilial primary hyperparathyroidism.";
RL J. Clin. Endocrinol. Metab. 83:2960-2963(1998).
RN [35]
RP VARIANT MEN1 SER-428.
RX PubMed=9709985; DOI=10.1210/jcem.83.8.5033-4;
RA Mayr B., Brabant G., von zur Muehlen A.;
RT "Menin mutations in MEN1 patients.";
RL J. Clin. Endocrinol. Metab. 83:3004-3005(1998).
RN [36]
RP VARIANTS MEN1 ILE-135 AND LYS-364.
RX PubMed=9740255; DOI=10.1046/j.1523-1747.1998.00317.x;
RA Boeni R., Vortmeyer A.O., Pack S., Park W.-S., Burg G., Hofbauer G.,
RA Darling T., Liotta L., Zhuang Z.;
RT "Somatic mutations of the MEN1 tumor suppressor gene detected in sporadic
RT angiofibromas.";
RL J. Invest. Dermatol. 111:539-540(1998).
RN [37]
RP VARIANTS MEN1 LYS-119 DEL AND 171-GLN--LEU-173 DEL.
RX PubMed=9747036; DOI=10.1007/s100380050070;
RA Sakurai A., Shirahama S., Fujimori M., Katai M., Itakura Y., Kobayashi S.,
RA Amano J., Fukushima Y., Hashizume K.;
RT "Novel MEN1 gene mutations in familial multiple endocrine neoplasia type
RT 1.";
RL J. Hum. Genet. 43:199-201(1998).
RN [38]
RP VARIANT MEN1 GLY-45.
RX PubMed=9832038; DOI=10.1136/jmg.35.11.915;
RA Sato M., Matsubara S., Miyauchi A., Ohye H., Imachi H., Murao K.,
RA Takahara J.;
RT "Identification of five novel germline mutations of the MEN1 gene in
RT Japanese multiple endocrine neoplasia type 1 (MEN1) families.";
RL J. Med. Genet. 35:915-919(1998).
RN [39]
RP VARIANT MEN1 ARG-139.
RX PubMed=10617276; DOI=10.1097/00019606-199912000-00005;
RA Martin-Campos J.M., Catasus L., Chico A., Mayoral C., Lagarda E.,
RA Gallart L., Mato E., Rodriguez-Espinosa J., Matias-Guiu X., De Leiva A.,
RA Blanco-Vaca F.;
RT "Molecular pathology of multiple endocrine neoplasia type I: two novel
RT germline mutations and updated classification of mutations affecting MEN1
RT gene.";
RL Diagn. Mol. Pathol. 8:195-204(1999).
RN [40]
RP VARIANT MEN1 PRO-449.
RX PubMed=10229909; DOI=10.1530/eje.0.1400429;
RA Cetani F., Pardi E., Cianferotti L., Vignali E., Picone A., Miccoli P.,
RA Pinchera A., Marcocci C.;
RT "A new mutation of the MEN1 gene in an Italian kindred with multiple
RT endocrine neoplasia type 1.";
RL Eur. J. Endocrinol. 140:429-433(1999).
RN [41]
RP VARIANTS MEN1 ARG-188; ARG-230; TYR-246 AND PRO-258, AND VARIANT ALA-546.
RX PubMed=10576763; DOI=10.1530/eje.0.1410475;
RA Hai N., Aoki N., Matsuda A., Mori T., Kosugi S.;
RT "Germline MEN1 mutations in sixteen Japanese families with multiple
RT endocrine neoplasia type 1 (MEN1).";
RL Eur. J. Endocrinol. 141:475-480(1999).
RN [42]
RP VARIANT ADRENAL ADENOMA SER-557.
RX PubMed=10647896; DOI=10.1007/s004399900193;
RA Schulte K.-M., Heinze M., Mengel M., Simon D., Scheuring S., Koehrer K.,
RA Roeher H.-D.;
RT "MEN I gene mutations in sporadic adrenal adenomas.";
RL Hum. Genet. 105:603-610(1999).
RN [43]
RP VARIANTS MEN1 TRP-39; TYR-177; ASP-184 AND PRO-269, VARIANTS GLN-176;
RP PRO-272 AND ALA-546, AND INVOLVEMENT IN ISOLATED HYPERPARATHYROIDISM.
RX PubMed=9888389;
RX DOI=10.1002/(sici)1098-1004(1999)13:1<54::aid-humu6>3.0.co;2-k;
RA Poncin J., Abs R., Velkeniers B., Bonduelle M., Abramowicz M.,
RA Legros J.-J., Verloes A., Meurisse M., van Gaal L., Verellen C.,
RA Koulischer L., Beckers A.;
RT "Mutation analysis of the MEN1 gene in Belgian patients with multiple
RT endocrine neoplasia type 1 and related diseases.";
RL Hum. Mutat. 13:54-60(1999).
RN [44]
RP VARIANTS MEN1 ASP-161 AND ARG-246.
RX PubMed=10090472;
RX DOI=10.1002/(sici)1098-1004(1999)13:3<175::aid-humu1>3.0.co;2-r;
RA Mutch M.G., Dilley W.G., Sanjurjo F., Debenedetti M.K., Doherty G.M.,
RA Wells S.A. Jr., Goodfellow P.J., Lairmore T.C.;
RT "Germline mutations in the multiple endocrine neoplasia type 1 gene:
RT evidence for frequent splicing defects.";
RL Hum. Mutat. 13:175-185(1999).
RN [45]
RP VARIANT MEN1 PHE-160.
RX PubMed=10534569; DOI=10.3892/ijmm.4.5.483;
RA Engelbach M., Forst T., Hankeln T., Tratzky M., Heerdt S., Pfuetzner A.,
RA Kann P., Kunt T., Schneider S., Schmidt E.R., Beyer J.;
RT "Germline mutations in the MEN1 gene: creation of a new splice acceptor
RT site and insertion of 7 intron nucleotides into the mRNA.";
RL Int. J. Mol. Med. 4:483-485(1999).
RN [46]
RP VARIANTS MEN1 LEU-234; ASP-358; SER-378 AND PRO-420.
RX PubMed=10993647; DOI=10.1054/bjoc.2000.1380;
RA Bergman L., Teh B.T., Cardinal J., Palmer J., Walters M., Shepherd J.,
RA Cameron D., Hayward N.;
RT "Identification of MEN1 gene mutations in families with MEN 1 and related
RT disorders.";
RL Br. J. Cancer 83:1009-1014(2000).
RN [47]
RP VARIANTS PARATHYROID TUMOR ASP-161; ARG-188; TRP-258; ALA-279 AND PRO-289.
RX PubMed=11034102;
RA Uchino S., Noguchi S., Sato M., Yamashita H., Yamashita H., Watanabe S.,
RA Murakami T., Toda M., Ohshima A., Futata T., Mizukoshi T., Koike E.,
RA Takatsu K., Terao K., Wakiya S., Nagatomo M., Adachi M.;
RT "Screening of the MEN1 gene and discovery of germ-line and somatic
RT mutations in apparently sporadic parathyroid tumors.";
RL Cancer Res. 60:5553-5557(2000).
RN [48]
RP VARIANTS MEN1 TRP-39; LYS-119 DEL; GLN-184; PRO-228; ARG-322; PRO-342;
RP ASN-353; VAL-390 AND SER-549.
RX PubMed=10849016; DOI=10.1046/j.1365-2362.2000.00664.x;
RA Roijers J.F.M., de Wit M.J., van der Luijt R.B., Ploos van Amstel H.K.,
RA Hoeppener J.W.M., Lips C.J.M.;
RT "Criteria for mutation analysis in MEN 1-suspected patients: MEN 1 case-
RT finding.";
RL Eur. J. Clin. Invest. 30:487-492(2000).
RN [49]
RP VARIANTS MEN1 LYS-45; MET-220 AND ARG-349.
RX PubMed=10664520; DOI=10.1530/eje.0.1420131;
RA Morelli A., Falchetti A., Martineti V., Becherini L., Mark M., Friedman E.,
RA Brandi M.L.;
RT "MEN1 gene mutation analysis in Italian patients with multiple endocrine
RT neoplasia type 1.";
RL Eur. J. Endocrinol. 142:131-137(2000).
RN [50]
RP VARIANT ASP-310, AND INVOLVEMENT IN ISOLATED HYPERPARATHYROIDISM.
RX PubMed=10664521; DOI=10.1530/eje.0.1420138;
RA Honda M., Tsukada T., Tanaka H., Maruyama K., Yamaguchi K., Obara T.,
RA Yamaji T., Ishibashi M.;
RT "A novel mutation of the MEN1 gene in a Japanese kindred with familial
RT isolated primary hyperparathyroidism.";
RL Eur. J. Endocrinol. 142:138-143(2000).
RN [51]
RP VARIANT MEN1 LYS-184.
RX PubMed=11102994;
RX DOI=10.1002/1098-1004(200012)16:6<533::aid-humu22>3.0.co;2-5;
RA Weinhaeusel A., Vierhapper H., Schlegl R., Wagner T., Muhr D., Scheuba C.,
RA Niederle B., Haas O.A.;
RT "A novel mutation E179K of the MEN1 gene predisposes for multiple endocrine
RT neoplasia-type 1 (MEN1).";
RL Hum. Mutat. 16:533-533(2000).
RN [52]
RP VARIANT PRO-265, AND INVOLVEMENT IN ISOLATED HYPERPARATHYROIDISM.
RX PubMed=10634381; DOI=10.1210/jcem.85.1.6299;
RA Kassem M., Kruse T.A., Wong F.K., Larsson C., Teh B.T.;
RT "Familial isolated hyperparathyroidism as a variant of multiple endocrine
RT neoplasia type 1 in a large Danish pedigree.";
RL J. Clin. Endocrinol. Metab. 85:165-167(2000).
RN [53]
RP VARIANT MEN1 ASP-139.
RX PubMed=11134142; DOI=10.1210/jcem.85.12.7064;
RA Stratakis C.A., Schussheim D.H., Freedman S.M., Keil M.F., Pack S.D.,
RA Agarwal S.K., Skarulis M.C., Weil R.J., Lubensky I.A., Zhuang Z.,
RA Oldfield E.H., Marx S.J.;
RT "Pituitary macroadenoma in a 5-year-old: an early expression of multiple
RT endocrine neoplasia type 1.";
RL J. Clin. Endocrinol. Metab. 85:4776-4780(2000).
RN [54]
RP VARIANT MEN1 PRO-419.
RX PubMed=11241849; DOI=10.1002/humu.12;
RA Asteria C., Faglia G., Roncoroni R., Borretta G., Ribotto P.,
RA Beck-Peccoz P.;
RT "Identification of three novel menin mutations (c.741delGTCA, c.1348T>C,
RT c.1785delA) in unrelated Italian families affected with multiple endocrine
RT neoplasia type 1: additional information for mutational screening.";
RL Hum. Mutat. 17:237-237(2001).
RN [55]
RP VARIANTS MEN1 TRP-39; ASP-42; LEU-98; PRO-165; THR-165; PHE-167; ASP-169;
RP ARG-170; TYR-177; PRO-228; PHE-245; ARG-286; PRO-316; PRO-319; TYR-322;
RP ARG-322; ASP-342; ARG-346; HIS-362; ASP-373; MET-377; ASN-423; CYS-532;
RP ASN-560 AND ARG-560.
RX PubMed=12112656; DOI=10.1002/humu.10092;
RA Wautot V., Vercherat C., Lespinasse J., Chambe B., Lenoir G.M., Zhang C.X.,
RA Porchet N., Cordier M., Beroud C., Calender A.;
RT "Germline mutation profile of MEN1 in multiple endocrine neoplasia type 1:
RT search for correlation between phenotype and the functional domains of the
RT MEN1 protein.";
RL Hum. Mutat. 20:35-47(2002).
RN [56]
RP VARIANT MEN1 LEU-GLN-266 INS.
RX PubMed=12417605; DOI=10.1093/jjco/hyf079;
RA Okamoto H., Tamada A., Hai N., Doi M., Uchimura I., Hirata Y., Kosugi S.;
RT "A novel six-nucleotide insertion in exon 4 of the MEN1 gene, 878insCTGCAG,
RT in three patients with familial insulinoma and primary
RT hyperparathyroidism.";
RL Jpn. J. Clin. Oncol. 32:368-370(2002).
RN [57]
RP VARIANTS MEN1 LYS-119 DEL; ILE-159; GLU-368 DEL AND ASN-423.
RX PubMed=12050235; DOI=10.1210/jcem.87.6.8607;
RA Turner J.J.O., Leotlela P.D., Pannett A.A.J., Forbes S.A., Bassett J.H.D.,
RA Harding B., Christie P.T., Bowen-Jones D., Ellard S., Hattersley A.,
RA Jackson C.E., Pope R., Quarrell O.W., Trembath R., Thakker R.V.;
RT "Frequent occurrence of an intron 4 mutation in multiple endocrine
RT neoplasia type 1.";
RL J. Clin. Endocrinol. Metab. 87:2688-2693(2002).
RN [58]
RP VARIANT HIS-282, AND INVOLVEMENT IN ISOLATED HYPERPARATHYROIDISM.
RX PubMed=12016470; DOI=10.1007/s00268-002-6617-9;
RA Perrier N.D., Villablanca A., Larsson C., Wong M., Ituarte P., Teh B.T.,
RA Clark O.H.;
RT "Genetic screening for MEN1 mutations in families presenting with familial
RT primary hyperparathyroidism.";
RL World J. Surg. 26:907-913(2002).
RN [59]
RP VARIANTS MEN1 VAL-158 AND PRO-416, AND INVOLVEMENT IN ISOLATED
RP HYPERPARATHYROIDISM.
RX PubMed=12699448; DOI=10.1046/j.1365-2265.2003.01765.x;
RA Pannett A.A.J., Kennedy A.M., Turner J.J.O., Forbes S.A., Cavaco B.M.,
RA Bassett J.H.D., Cianferotti L., Harding B., Shine B., Flinter F.,
RA Maidment C.G.H., Trembath R., Thakker R.V.;
RT "Multiple endocrine neoplasia type 1 (MEN1) germline mutations in familial
RT isolated primary hyperparathyroidism.";
RL Clin. Endocrinol. (Oxf.) 58:639-646(2003).
RN [60]
RP VARIANT MEN1 PRO-330.
RX PubMed=12791038; DOI=10.1034/j.1399-0004.2003.00091.x;
RA Park J.-H., Kim I.-J., Kang H.C., Lee S.-H., Shin Y., Kim K.-H., Lim S.-B.,
RA Kang S.-B., Lee K.U., Kim S.Y., Lee M.-S., Lee M.-K., Park J.-H.,
RA Moon S.-D., Park J.-G.;
RT "Germline mutations of the MEN1 gene in Korean families with multiple
RT endocrine neoplasia type 1 (MEN1) or MEN1-related disorders.";
RL Clin. Genet. 64:48-53(2003).
RN [61]
RP VARIANTS MEN1 ARG-170; PRO-228; PHE-246; ARG-286; PRO-316; TYR-322; ASN-423
RP AND SER-545.
RX PubMed=12652570; DOI=10.1002/elps.200390023;
RG Groupe d'etude des neoplasies endocriniennes multiples;
RA Crepin M., Escande F., Pigny P., Buisine M.-P., Calender A., Porchet N.,
RA Odou M.-F.;
RT "Efficient mutation detection in MEN1 gene using a combination of single-
RT strand conformation polymorphism (MDGA) and heteroduplex analysis.";
RL Electrophoresis 24:26-33(2003).
RN [62]
RP VARIANT MEN1 PRO-347.
RX PubMed=14686752; DOI=10.2169/internalmedicine.42.1112;
RA Ukita C., Yamaguchi M., Tanaka T., Shigeta H., Nishikawa M.;
RT "A novel missense mutation of the MEN1 gene in a multiple endocrine
RT neoplasia type 1 patient associated with carcinoid syndrome.";
RL Intern. Med. 42:1112-1116(2003).
RN [63]
RP VARIANTS MEN1 LYS-45 AND PRO-139, AND VARIANTS GLN-176 AND ALA-546.
RX PubMed=12746426; DOI=10.1136/jmg.40.5.e72;
RA Cebrian A., Ruiz-Llorente S., Cascon A., Pollan M., Diez J.J., Pico A.,
RA Telleria D., Benitez J., Robledo M.;
RT "Mutational and gross deletion study of the MEN1 gene and correlation with
RT clinical features in Spanish patients.";
RL J. Med. Genet. 40:E72-E72(2003).
RN [64]
RP VARIANT GLN-176.
RX PubMed=15205994; DOI=10.1007/s10038-004-0163-2;
RA Balogh K., Patocs A., Majnik J., Varga F., Illyes G., Hunyady L., Racz K.;
RT "Unusual presentation of multiple endocrine neoplasia type 1 in a young
RT woman with a novel mutation of the MEN1 gene.";
RL J. Hum. Genet. 49:380-386(2004).
RN [65]
RP VARIANTS MEN1 GLU-110 AND HIS-423.
RX PubMed=15730416; DOI=10.1111/j.1365-2265.2005.02219.x;
RA Jap T.-S., Chiu C.-Y., Won J.G.-S., Wu Y.-C., Chen H.-S.;
RT "Novel mutations in the MEN1 gene in subjects with multiple endocrine
RT neoplasia-1.";
RL Clin. Endocrinol. (Oxf.) 62:336-342(2005).
RN [66]
RP VARIANTS MEN1 VAL-144; ASP-161; ASP-184; LYS-184; ARG-186; MET-220;
RP ARG-264; ARG-325; TRP-360; TYR-426; CYS-441 AND ARG-441.
RX PubMed=15714081; DOI=10.1097/01.gim.0000153663.62300.f8;
RA Klein R.D., Salih S., Bessoni J., Bale A.E.;
RT "Clinical testing for multiple endocrine neoplasia type 1 in a DNA
RT diagnostic laboratory.";
RL Genet. Med. 7:131-138(2005).
RN [67]
RP VARIANT PHE-220, AND ASSOCIATION WITH PARATHYROID CARCINOMA.
RX PubMed=17555500; DOI=10.1111/j.1365-2265.2007.02894.x;
RA Haven C.J., van Puijenbroek M., Tan M.H., Teh B.T., Fleuren G.J.,
RA van Wezel T., Morreau H.;
RT "Identification of MEN1 and HRPT2 somatic mutations in paraffin-embedded
RT (sporadic) parathyroid carcinomas.";
RL Clin. Endocrinol. (Oxf.) 67:370-376(2007).
RN [68]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-546, AND IDENTIFICATION BY MASS
RP 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 [69]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-546, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Essential component of a MLL/SET1 histone methyltransferase
CC (HMT) complex, a complex that specifically methylates 'Lys-4' of
CC histone H3 (H3K4). Functions as a transcriptional regulator. Binds to
CC the TERT promoter and represses telomerase expression. Plays a role in
CC TGFB1-mediated inhibition of cell-proliferation, possibly regulating
CC SMAD3 transcriptional activity. Represses JUND-mediated transcriptional
CC activation on AP1 sites, as well as that mediated by NFKB subunit RELA.
CC Positively regulates HOXC8 and HOXC6 gene expression. May be involved
CC in normal hematopoiesis through the activation of HOXA9 expression (By
CC similarity). May be involved in DNA repair.
CC {ECO:0000250|UniProtKB:O88559, ECO:0000269|PubMed:11274402,
CC ECO:0000269|PubMed:11526476, ECO:0000269|PubMed:12837246,
CC ECO:0000269|PubMed:12874027, ECO:0000269|PubMed:14992727,
CC ECO:0000269|PubMed:22327296}.
CC -!- SUBUNIT: Component of the MLL-HCF complex, at least composed of
CC KMT2A/MLL1, MEN1, ASH2L, RBBP5, DPY30, WDR5, HCFC1 and HCFC2. Component
CC of the menin-associated histone methyltransferase complex, at least
CC composed of KMT2B/MLL4, MEN1, ASH2L, RBBP5, DPY30 and WDR5. Interacts
CC with POLR2B. Interacts with POLR2A phosphorylated at 'Ser-5', but not
CC with the unphosphorylated, nor 'Ser-2' phosphorylated POLR2A forms.
CC Interacts with FANCD2 and DBF4. Interacts with JUND (via MBM motif);
CC inhibits the interaction of JUND with MAPK10 and the phosphorylation of
CC JUND by MAP kinases MAPK8 and MAPK10 (PubMed:9989505, PubMed:22327296).
CC Interacts with SMAD3, but not with SMAD2, nor SMAD4. Directly interacts
CC with NFKB1, NFKB2 and RELA. Interacts with KMT2A (via MBM motif)
CC (PubMed:25305204, PubMed:22936661, PubMed:22327296). The KMT2A-MEN1
CC complex interacts with PSIP1 with a greater affinity as MEN1 enhances
CC interaction of KMT2A with PSIP1 (PubMed:25305204, PubMed:22327296).
CC Interacts with the fusion protein KMT2A-MLLT3 (PubMed:25305204,
CC PubMed:22936661). {ECO:0000269|PubMed:11274402,
CC ECO:0000269|PubMed:11526476, ECO:0000269|PubMed:12874027,
CC ECO:0000269|PubMed:14992727, ECO:0000269|PubMed:15199122,
CC ECO:0000269|PubMed:15374998, ECO:0000269|PubMed:17500065,
CC ECO:0000269|PubMed:22327296, ECO:0000269|PubMed:22936661,
CC ECO:0000269|PubMed:25305204, ECO:0000269|PubMed:9989505}.
CC -!- INTERACTION:
CC O00255; O14757: CHEK1; NbExp=2; IntAct=EBI-592789, EBI-974488;
CC O00255; Q9BXW9: FANCD2; NbExp=4; IntAct=EBI-592789, EBI-359343;
CC O00255; P35579: MYH9; NbExp=3; IntAct=EBI-592789, EBI-350338;
CC O00255; PRO_0000030311 [P19838]: NFKB1; NbExp=2; IntAct=EBI-592789, EBI-697771;
CC O00255; P61964: WDR5; NbExp=4; IntAct=EBI-592789, EBI-540834;
CC O00255-2; P17535: JUND; NbExp=6; IntAct=EBI-9869387, EBI-2682803;
CC O00255-2; Q03164: KMT2A; NbExp=12; IntAct=EBI-9869387, EBI-591370;
CC O00255-2; P35579: MYH9; NbExp=4; IntAct=EBI-9869387, EBI-350338;
CC O00255-2; PRO_0000030311 [P19838]: NFKB1; NbExp=4; IntAct=EBI-9869387, EBI-697771;
CC O00255-2; PRO_0000030322 [Q00653]: NFKB2; NbExp=3; IntAct=EBI-9869387, EBI-9869360;
CC O00255-2; Q04206: RELA; NbExp=4; IntAct=EBI-9869387, EBI-73886;
CC O00255-2; Q05982: Nme1; Xeno; NbExp=5; IntAct=EBI-9869387, EBI-1165329;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12874027}.
CC Note=Concentrated in nuclear body-like structures. Relocates to the
CC nuclear matrix upon gamma irradiation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=O00255-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=O00255-2; Sequence=VSP_004323;
CC Name=3;
CC IsoId=O00255-3; Sequence=VSP_004323, VSP_015854;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DISEASE: Familial multiple endocrine neoplasia type I (MEN1)
CC [MIM:131100]: Autosomal dominant disorder characterized by tumors of
CC the parathyroid glands, gastro-intestinal endocrine tissue, the
CC anterior pituitary and other tissues. Cutaneous lesions and nervous-
CC tissue tumors can exist. Prognosis in MEN1 patients is related to
CC hormonal hypersecretion by tumors, such as hypergastrinemia causing
CC severe peptic ulcer disease (Zollinger-Ellison syndrome, ZES), primary
CC hyperparathyroidism, and acute forms of hyperinsulinemia.
CC {ECO:0000269|PubMed:10090472, ECO:0000269|PubMed:10229909,
CC ECO:0000269|PubMed:10534569, ECO:0000269|PubMed:10576763,
CC ECO:0000269|PubMed:10617276, ECO:0000269|PubMed:10660339,
CC ECO:0000269|PubMed:10664520, ECO:0000269|PubMed:10849016,
CC ECO:0000269|PubMed:10993647, ECO:0000269|PubMed:11102994,
CC ECO:0000269|PubMed:11134142, ECO:0000269|PubMed:11241849,
CC ECO:0000269|PubMed:12050235, ECO:0000269|PubMed:12112656,
CC ECO:0000269|PubMed:12417605, ECO:0000269|PubMed:12652570,
CC ECO:0000269|PubMed:12699448, ECO:0000269|PubMed:12746426,
CC ECO:0000269|PubMed:12791038, ECO:0000269|PubMed:14686752,
CC ECO:0000269|PubMed:14992727, ECO:0000269|PubMed:15714081,
CC ECO:0000269|PubMed:15730416, ECO:0000269|PubMed:17555499,
CC ECO:0000269|PubMed:22327296, ECO:0000269|PubMed:9103196,
CC ECO:0000269|PubMed:9215689, ECO:0000269|PubMed:9215690,
CC ECO:0000269|PubMed:9463336, ECO:0000269|PubMed:9506756,
CC ECO:0000269|PubMed:9671267, ECO:0000269|PubMed:9683585,
CC ECO:0000269|PubMed:9709921, ECO:0000269|PubMed:9709976,
CC ECO:0000269|PubMed:9709985, ECO:0000269|PubMed:9740255,
CC ECO:0000269|PubMed:9747036, ECO:0000269|PubMed:9820618,
CC ECO:0000269|PubMed:9832038, ECO:0000269|PubMed:9888389,
CC ECO:0000269|PubMed:9989505}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=MEN1 inactivating mutations are responsible for
CC hyperfunctioning of the parathyroid glands and subsequent primary
CC hyperparathyroidism. Primary hyperparathyroidism can occur in isolation
CC or in association with multiple endocrine neoplasia.
CC {ECO:0000269|PubMed:10634381, ECO:0000269|PubMed:10664521,
CC ECO:0000269|PubMed:12016470, ECO:0000269|PubMed:12699448,
CC ECO:0000269|PubMed:9792884, ECO:0000269|PubMed:9843042,
CC ECO:0000269|PubMed:9888389}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABQ12624.1; Type=Frameshift; Note=The frameshift is caused by a single nucleotide deletion which is found in a MEN1 kindred.; Evidence={ECO:0000305};
CC Sequence=ABQ12627.1; Type=Frameshift; Note=The frameshift is caused by a single nucleotide deletion which is found in a MEN1 kindred.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MEN1ID148.html";
CC ---------------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
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DR EMBL; U93236; AAC51228.1; -; mRNA.
DR EMBL; U93237; AAC51229.1; -; Genomic_DNA.
DR EMBL; U93237; AAC51230.1; -; Genomic_DNA.
DR EMBL; AP001462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EF443091; ABQ12621.1; -; Genomic_DNA.
DR EMBL; EF443092; ABQ12622.1; -; Genomic_DNA.
DR EMBL; EF443093; ABQ12623.1; -; Genomic_DNA.
DR EMBL; EF443094; ABQ12624.1; ALT_FRAME; Genomic_DNA.
DR EMBL; EF443095; ABQ12625.1; -; Genomic_DNA.
DR EMBL; EF443096; ABQ12626.1; -; Genomic_DNA.
DR EMBL; EF443097; ABQ12627.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BC002544; AAH02544.1; -; mRNA.
DR EMBL; BC002664; AAH02664.2; -; mRNA.
DR CCDS; CCDS31600.1; -. [O00255-2]
DR CCDS; CCDS8083.1; -. [O00255-1]
DR RefSeq; NP_000235.2; NM_000244.3.
DR RefSeq; NP_570711.1; NM_130799.2.
DR RefSeq; NP_570712.1; NM_130800.2.
DR RefSeq; NP_570713.1; NM_130801.2.
DR RefSeq; NP_570714.1; NM_130802.2.
DR RefSeq; NP_570715.1; NM_130803.2.
DR RefSeq; NP_570716.1; NM_130804.2.
DR RefSeq; XP_005274058.1; XM_005274001.4.
DR RefSeq; XP_016873258.1; XM_017017769.1.
DR RefSeq; XP_016873259.1; XM_017017770.1.
DR PDB; 3U84; X-ray; 2.50 A; A/B=2-615.
DR PDB; 3U85; X-ray; 3.00 A; A=2-615.
DR PDB; 3U86; X-ray; 2.84 A; A=2-615.
DR PDB; 3U88; X-ray; 3.00 A; A/B=2-615.
DR PDB; 4GPQ; X-ray; 1.46 A; A=1-598.
DR PDB; 4GQ3; X-ray; 1.56 A; A=1-598.
DR PDB; 4GQ4; X-ray; 1.27 A; A=1-598.
DR PDB; 4GQ6; X-ray; 1.55 A; A=1-598.
DR PDB; 4I80; X-ray; 3.10 A; A=2-615.
DR PDB; 4OG3; X-ray; 2.01 A; A=1-598.
DR PDB; 4OG4; X-ray; 1.45 A; A=1-598.
DR PDB; 4OG5; X-ray; 1.63 A; A=1-598.
DR PDB; 4OG6; X-ray; 1.49 A; A=1-598.
DR PDB; 4OG7; X-ray; 2.08 A; A=1-598.
DR PDB; 4OG8; X-ray; 1.53 A; A=1-598.
DR PDB; 4X5Y; X-ray; 1.59 A; A=1-464, A=542-598.
DR PDB; 4X5Z; X-ray; 1.86 A; A=1-464, A=542-598.
DR PDB; 5DB0; X-ray; 1.50 A; A=1-593.
DR PDB; 5DB1; X-ray; 1.86 A; A=1-593.
DR PDB; 5DB2; X-ray; 1.54 A; A=1-593.
DR PDB; 5DB3; X-ray; 1.71 A; A=1-593.
DR PDB; 5DD9; X-ray; 1.62 A; A=1-598.
DR PDB; 5DDA; X-ray; 1.83 A; A=1-593.
DR PDB; 5DDB; X-ray; 1.54 A; A=1-598.
DR PDB; 5DDC; X-ray; 1.62 A; A=1-598.
DR PDB; 5DDD; X-ray; 2.14 A; A=1-593.
DR PDB; 5DDE; X-ray; 1.78 A; A=1-593.
DR PDB; 5DDF; X-ray; 1.66 A; A=1-593.
DR PDB; 6B41; X-ray; 2.61 A; A=2-615.
DR PDB; 6BXH; X-ray; 2.44 A; A=1-464.
DR PDB; 6BXY; X-ray; 1.82 A; A=1-598.
DR PDB; 6BY8; X-ray; 1.90 A; A=1-598.
DR PDB; 6E1A; X-ray; 3.10 A; A=2-615.
DR PDB; 6O5I; X-ray; 1.24 A; A=1-598.
DR PDB; 6OPJ; X-ray; 1.50 A; A=1-598.
DR PDB; 6PKC; X-ray; 1.90 A; A/B=2-588.
DR PDB; 6S2K; X-ray; 3.10 A; A/B=1-589.
DR PDB; 6WNH; X-ray; 2.10 A; A=2-615.
DR PDB; 7M4T; X-ray; 2.74 A; A=2-615.
DR PDBsum; 3U84; -.
DR PDBsum; 3U85; -.
DR PDBsum; 3U86; -.
DR PDBsum; 3U88; -.
DR PDBsum; 4GPQ; -.
DR PDBsum; 4GQ3; -.
DR PDBsum; 4GQ4; -.
DR PDBsum; 4GQ6; -.
DR PDBsum; 4I80; -.
DR PDBsum; 4OG3; -.
DR PDBsum; 4OG4; -.
DR PDBsum; 4OG5; -.
DR PDBsum; 4OG6; -.
DR PDBsum; 4OG7; -.
DR PDBsum; 4OG8; -.
DR PDBsum; 4X5Y; -.
DR PDBsum; 4X5Z; -.
DR PDBsum; 5DB0; -.
DR PDBsum; 5DB1; -.
DR PDBsum; 5DB2; -.
DR PDBsum; 5DB3; -.
DR PDBsum; 5DD9; -.
DR PDBsum; 5DDA; -.
DR PDBsum; 5DDB; -.
DR PDBsum; 5DDC; -.
DR PDBsum; 5DDD; -.
DR PDBsum; 5DDE; -.
DR PDBsum; 5DDF; -.
DR PDBsum; 6B41; -.
DR PDBsum; 6BXH; -.
DR PDBsum; 6BXY; -.
DR PDBsum; 6BY8; -.
DR PDBsum; 6E1A; -.
DR PDBsum; 6O5I; -.
DR PDBsum; 6OPJ; -.
DR PDBsum; 6PKC; -.
DR PDBsum; 6S2K; -.
DR PDBsum; 6WNH; -.
DR PDBsum; 7M4T; -.
DR AlphaFoldDB; O00255; -.
DR SMR; O00255; -.
DR BioGRID; 110384; 160.
DR ComplexPortal; CPX-497; Menin-JUND transcription inhibition complex.
DR ComplexPortal; CPX-5850; Histone-lysine N-methyltransferase complex, KMT2A variant.
DR ComplexPortal; CPX-7062; Histone-lysine N-methyltransferase complex, KMT2B variant.
DR CORUM; O00255; -.
DR DIP; DIP-24236N; -.
DR IntAct; O00255; 32.
DR MINT; O00255; -.
DR STRING; 9606.ENSP00000337088; -.
DR BindingDB; O00255; -.
DR ChEMBL; CHEMBL1615381; -.
DR DrugCentral; O00255; -.
DR iPTMnet; O00255; -.
DR PhosphoSitePlus; O00255; -.
DR BioMuta; MEN1; -.
DR EPD; O00255; -.
DR jPOST; O00255; -.
DR MassIVE; O00255; -.
DR MaxQB; O00255; -.
DR PaxDb; O00255; -.
DR PeptideAtlas; O00255; -.
DR PRIDE; O00255; -.
DR ProteomicsDB; 47808; -. [O00255-1]
DR ProteomicsDB; 47809; -. [O00255-2]
DR ProteomicsDB; 47810; -. [O00255-3]
DR ABCD; O00255; 2 sequenced antibodies.
DR Antibodypedia; 15626; 548 antibodies from 44 providers.
DR CPTC; O00255; 1 antibody.
DR DNASU; 4221; -.
DR Ensembl; ENST00000312049.11; ENSP00000308975.6; ENSG00000133895.18. [O00255-2]
DR Ensembl; ENST00000315422.9; ENSP00000323747.4; ENSG00000133895.18. [O00255-2]
DR Ensembl; ENST00000377313.6; ENSP00000366530.1; ENSG00000133895.18. [O00255-1]
DR Ensembl; ENST00000377321.5; ENSP00000366538.1; ENSG00000133895.18. [O00255-3]
DR Ensembl; ENST00000377326.7; ENSP00000366543.3; ENSG00000133895.18. [O00255-2]
DR Ensembl; ENST00000440873.6; ENSP00000413944.2; ENSG00000133895.18. [O00255-2]
DR Ensembl; ENST00000450708.7; ENSP00000394933.3; ENSG00000133895.18. [O00255-2]
DR GeneID; 4221; -.
DR KEGG; hsa:4221; -.
DR MANE-Select; ENST00000450708.7; ENSP00000394933.3; NM_001370259.2; NP_001357188.2. [O00255-2]
DR UCSC; uc001obl.4; human. [O00255-1]
DR CTD; 4221; -.
DR DisGeNET; 4221; -.
DR GeneCards; MEN1; -.
DR GeneReviews; MEN1; -.
DR HGNC; HGNC:7010; MEN1.
DR HPA; ENSG00000133895; Low tissue specificity.
DR MalaCards; MEN1; -.
DR MIM; 131100; phenotype.
DR MIM; 613733; gene.
DR neXtProt; NX_O00255; -.
DR OpenTargets; ENSG00000133895; -.
DR Orphanet; 99879; Familial isolated hyperparathyroidism.
DR Orphanet; 97279; Insulinoma.
DR Orphanet; 652; Multiple endocrine neoplasia type 1.
DR Orphanet; 314790; Null pituitary adenoma.
DR Orphanet; 99725; Pituitary gigantism.
DR Orphanet; 2965; Prolactinoma.
DR Orphanet; 314786; Silent pituitary adenoma.
DR PharmGKB; PA30746; -.
DR VEuPathDB; HostDB:ENSG00000133895; -.
DR eggNOG; ENOG502QUYK; Eukaryota.
DR GeneTree; ENSGT00390000014237; -.
DR HOGENOM; CLU_018646_0_0_1; -.
DR InParanoid; O00255; -.
DR OrthoDB; 799417at2759; -.
DR PhylomeDB; O00255; -.
DR TreeFam; TF323888; -.
DR PathwayCommons; O00255; -.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; O00255; -.
DR SIGNOR; O00255; -.
DR BioGRID-ORCS; 4221; 164 hits in 1097 CRISPR screens.
DR ChiTaRS; MEN1; human.
DR GeneWiki; MEN1; -.
DR GenomeRNAi; 4221; -.
DR Pharos; O00255; Tchem.
DR PRO; PR:O00255; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O00255; protein.
DR Bgee; ENSG00000133895; Expressed in granulocyte and 179 other tissues.
DR ExpressionAtlas; O00255; baseline and differential.
DR Genevisible; O00255; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:BHF-UCL.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:MGI.
DR GO; GO:0071339; C:MLL1 complex; IPI:ComplexPortal.
DR GO; GO:0044665; C:MLL1/2 complex; IPI:ComplexPortal.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IPI:ComplexPortal.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0000400; F:four-way junction DNA binding; IDA:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:UniProtKB.
DR GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0000403; F:Y-form DNA binding; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; NAS:UniProtKB.
DR GO; GO:0051568; P:histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IGI:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0051974; P:negative regulation of telomerase activity; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0002076; P:osteoblast development; IGI:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0032925; P:regulation of activin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0061469; P:regulation of type B pancreatic cell proliferation; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IDA:UniProtKB.
DR GO; GO:0071559; P:response to transforming growth factor beta; IEA:Ensembl.
DR GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR GO; GO:0003309; P:type B pancreatic cell differentiation; IEA:Ensembl.
DR CDD; cd14456; Menin; 1.
DR IDEAL; IID00404; -.
DR InterPro; IPR007747; Menin.
DR PANTHER; PTHR12693; PTHR12693; 1.
DR Pfam; PF05053; Menin; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Disease variant;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..615
FT /note="Menin"
FT /id="PRO_0000096411"
FT REGION 219..395
FT /note="Interaction with FANCD2"
FT /evidence="ECO:0000269|PubMed:12874027"
FT REGION 465..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 599
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 149..153
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9103196"
FT /id="VSP_004323"
FT VAR_SEQ 189..223
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015854"
FT VARIANT 12
FT /note="P -> L (in MEN1; no effect on histone methylation;
FT almost no effect on JUND-binding; dbSNP:rs794728614)"
FT /evidence="ECO:0000269|PubMed:14992727,
FT ECO:0000269|PubMed:9989505"
FT /id="VAR_005425"
FT VARIANT 22
FT /note="L -> R (in MEN1; no effect on histone methylation;
FT almost no effect on JUND-binding; no repression of JUND
FT transactivation; dbSNP:rs104894256)"
FT /evidence="ECO:0000269|PubMed:14992727,
FT ECO:0000269|PubMed:9103196, ECO:0000269|PubMed:9989505"
FT /id="VAR_005426"
FT VARIANT 26
FT /note="E -> K (in parathyroid adenoma and MEN1;
FT dbSNP:rs28931612)"
FT /evidence="ECO:0000269|PubMed:9241276,
FT ECO:0000269|PubMed:9820618"
FT /id="VAR_005427"
FT VARIANT 39
FT /note="L -> W (in MEN1)"
FT /evidence="ECO:0000269|PubMed:10849016,
FT ECO:0000269|PubMed:12112656, ECO:0000269|PubMed:9888389"
FT /id="VAR_005428"
FT VARIANT 42
FT /note="G -> D (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656,
FT ECO:0000269|PubMed:9463336"
FT /id="VAR_005429"
FT VARIANT 45
FT /note="E -> G (in MEN1; dbSNP:rs1592660101)"
FT /evidence="ECO:0000269|PubMed:9832038"
FT /id="VAR_005430"
FT VARIANT 45
FT /note="E -> K (in MEN1; dbSNP:rs1114167491)"
FT /evidence="ECO:0000269|PubMed:10664520,
FT ECO:0000269|PubMed:12746426"
FT /id="VAR_039587"
FT VARIANT 89..95
FT /note="Missing (in MEN1)"
FT /evidence="ECO:0000269|PubMed:17555499"
FT /id="VAR_065152"
FT VARIANT 98
FT /note="R -> L (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656"
FT /id="VAR_039588"
FT VARIANT 110
FT /note="G -> E (in MEN1; dbSNP:rs1389398299)"
FT /evidence="ECO:0000269|PubMed:15730416"
FT /id="VAR_039589"
FT VARIANT 119
FT /note="Missing (in MEN1)"
FT /evidence="ECO:0000269|PubMed:10849016,
FT ECO:0000269|PubMed:12050235, ECO:0000269|PubMed:9103196,
FT ECO:0000269|PubMed:9747036"
FT /id="VAR_005431"
FT VARIANT 135
FT /note="K -> I (in MEN1)"
FT /evidence="ECO:0000269|PubMed:9740255"
FT /id="VAR_005434"
FT VARIANT 139
FT /note="H -> D (in MEN1; almost complete loss of histone
FT methylation; strong decrease in JUND-binding; no repression
FT of JUND transactivation; reduced interaction with KMT2A;
FT dbSNP:rs104894263)"
FT /evidence="ECO:0000269|PubMed:11134142,
FT ECO:0000269|PubMed:14992727, ECO:0000269|PubMed:22327296,
FT ECO:0000269|PubMed:9709976, ECO:0000269|PubMed:9989505"
FT /id="VAR_005432"
FT VARIANT 139
FT /note="H -> P (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12746426"
FT /id="VAR_039590"
FT VARIANT 139
FT /note="H -> R (in MEN1; dbSNP:rs1114167515)"
FT /evidence="ECO:0000269|PubMed:10617276"
FT /id="VAR_039591"
FT VARIANT 139
FT /note="H -> Y (in MEN1; familial and sporadic cases; almost
FT no effect on JUND-binding; no repression of JUND
FT transactivation)"
FT /evidence="ECO:0000269|PubMed:9989505"
FT /id="VAR_005433"
FT VARIANT 144
FT /note="F -> V (in MEN1; dbSNP:rs1114167543)"
FT /evidence="ECO:0000269|PubMed:15714081"
FT /id="VAR_005436"
FT VARIANT 147
FT /note="I -> F (in MEN1)"
FT /evidence="ECO:0000269|PubMed:17555499"
FT /id="VAR_065153"
FT VARIANT 157
FT /note="L -> W (in parathyroid tumors; somatic)"
FT /evidence="ECO:0000269|PubMed:9709976"
FT /id="VAR_065154"
FT VARIANT 158
FT /note="D -> V (in MEN1; also found in isolated
FT hyperparathyroidism; dbSNP:rs1565648789)"
FT /evidence="ECO:0000269|PubMed:12699448"
FT /id="VAR_039592"
FT VARIANT 159
FT /note="S -> I (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12050235"
FT /id="VAR_039593"
FT VARIANT 160
FT /note="S -> F (in MEN1)"
FT /evidence="ECO:0000269|PubMed:10534569"
FT /id="VAR_039594"
FT VARIANT 161
FT /note="G -> D (in MEN1 and parathyroid tumor;
FT dbSNP:rs794728648)"
FT /evidence="ECO:0000269|PubMed:10090472,
FT ECO:0000269|PubMed:11034102, ECO:0000269|PubMed:15714081"
FT /id="VAR_008017"
FT VARIANT 165
FT /note="A -> P (in MEN1; strong decrease in JUND-binding;
FT dbSNP:rs1565648656)"
FT /evidence="ECO:0000269|PubMed:12112656,
FT ECO:0000269|PubMed:9463336, ECO:0000269|PubMed:9989505"
FT /id="VAR_005437"
FT VARIANT 165
FT /note="A -> T (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656"
FT /id="VAR_039595"
FT VARIANT 167
FT /note="V -> F (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656"
FT /id="VAR_039596"
FT VARIANT 169
FT /note="A -> D (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656,
FT ECO:0000269|PubMed:9463336"
FT /id="VAR_005438"
FT VARIANT 170
FT /note="C -> R (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656,
FT ECO:0000269|PubMed:12652570"
FT /id="VAR_039597"
FT VARIANT 171..173
FT /note="Missing (in MEN1)"
FT /evidence="ECO:0000269|PubMed:9747036"
FT /id="VAR_005439"
FT VARIANT 173
FT /note="L -> P (in MEN1; dbSNP:rs386134256)"
FT /evidence="ECO:0000269|PubMed:9820618"
FT /id="VAR_039598"
FT VARIANT 176
FT /note="R -> Q (in dbSNP:rs607969)"
FT /evidence="ECO:0000269|PubMed:12746426,
FT ECO:0000269|PubMed:15205994, ECO:0000269|PubMed:9103196,
FT ECO:0000269|PubMed:9215690, ECO:0000269|PubMed:9709921,
FT ECO:0000269|PubMed:9888389"
FT /id="VAR_005440"
FT VARIANT 177
FT /note="D -> Y (in MEN1; dbSNP:rs1114167494)"
FT /evidence="ECO:0000269|PubMed:12112656,
FT ECO:0000269|PubMed:9888389"
FT /id="VAR_005441"
FT VARIANT 181
FT /note="A -> P (in MEN1; loss of JUND-binding;
FT dbSNP:rs376872829)"
FT /evidence="ECO:0000269|PubMed:9989505"
FT /id="VAR_005442"
FT VARIANT 184
FT /note="E -> D (in MEN1; dbSNP:rs1555165811)"
FT /evidence="ECO:0000269|PubMed:15714081,
FT ECO:0000269|PubMed:9888389"
FT /id="VAR_005443"
FT VARIANT 184
FT /note="E -> K (in MEN1; dbSNP:rs1064793167)"
FT /evidence="ECO:0000269|PubMed:11102994,
FT ECO:0000269|PubMed:15714081"
FT /id="VAR_039599"
FT VARIANT 184
FT /note="E -> Q (in MEN1)"
FT /evidence="ECO:0000269|PubMed:10849016"
FT /id="VAR_039600"
FT VARIANT 186
FT /note="H -> R (in MEN1)"
FT /evidence="ECO:0000269|PubMed:15714081"
FT /id="VAR_039601"
FT VARIANT 188
FT /note="W -> R (in MEN1 and parathyroid tumor;
FT dbSNP:rs1555165791)"
FT /evidence="ECO:0000269|PubMed:10576763,
FT ECO:0000269|PubMed:11034102"
FT /id="VAR_039602"
FT VARIANT 188
FT /note="W -> S (in MEN1)"
FT /evidence="ECO:0000269|PubMed:9215690,
FT ECO:0000269|PubMed:9463336"
FT /id="VAR_005444"
FT VARIANT 189
FT /note="V -> E (probable disease-associated variant found in
FT isolated hyperparathyroidism; dbSNP:rs104894262)"
FT /evidence="ECO:0000269|PubMed:9843042"
FT /id="VAR_005445"
FT VARIANT 220
FT /note="V -> F (found in a parathyroid carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17555500"
FT /id="VAR_064937"
FT VARIANT 220
FT /note="V -> M (in MEN1; dbSNP:rs794728621)"
FT /evidence="ECO:0000269|PubMed:10664520,
FT ECO:0000269|PubMed:15714081"
FT /id="VAR_039603"
FT VARIANT 228
FT /note="L -> P (in MEN1; dbSNP:rs886039415)"
FT /evidence="ECO:0000269|PubMed:10849016,
FT ECO:0000269|PubMed:12112656, ECO:0000269|PubMed:12652570"
FT /id="VAR_005446"
FT VARIANT 230
FT /note="G -> R (in MEN1; dbSNP:rs1057521110)"
FT /evidence="ECO:0000269|PubMed:10576763"
FT /id="VAR_039604"
FT VARIANT 234
FT /note="R -> L (in MEN1)"
FT /evidence="ECO:0000269|PubMed:10993647"
FT /id="VAR_039605"
FT VARIANT 245
FT /note="V -> F (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656"
FT /id="VAR_039606"
FT VARIANT 246
FT /note="C -> F (in MEN1; loss of interaction with KMT2A and
FT JUND)"
FT /evidence="ECO:0000269|PubMed:12652570,
FT ECO:0000269|PubMed:22327296"
FT /id="VAR_039607"
FT VARIANT 246
FT /note="C -> R (in MEN1; dbSNP:rs1592649108)"
FT /evidence="ECO:0000269|PubMed:10090472"
FT /id="VAR_008018"
FT VARIANT 246
FT /note="C -> Y (in MEN1; dbSNP:rs794728624)"
FT /evidence="ECO:0000269|PubMed:10576763"
FT /id="VAR_039608"
FT VARIANT 247
FT /note="A -> V (in MEN1; almost complete loss of histone
FT methylation; loss of JUND-binding; no repression of JUND
FT transactivation; reduced interaction with KMT2A)"
FT /evidence="ECO:0000269|PubMed:14992727,
FT ECO:0000269|PubMed:22327296, ECO:0000269|PubMed:9989505"
FT /id="VAR_005447"
FT VARIANT 258
FT /note="S -> P (in MEN1)"
FT /evidence="ECO:0000269|PubMed:10576763"
FT /id="VAR_039609"
FT VARIANT 258
FT /note="S -> W (in parathyroid tumor; dbSNP:rs386134259)"
FT /evidence="ECO:0000269|PubMed:11034102"
FT /id="VAR_039610"
FT VARIANT 260
FT /note="E -> K (probable disease-associated variant found in
FT isolated hyperparathyroidism; dbSNP:rs104894268)"
FT /evidence="ECO:0000269|PubMed:9792884"
FT /id="VAR_005448"
FT VARIANT 264
FT /note="L -> R (in MEN1)"
FT /evidence="ECO:0000269|PubMed:15714081"
FT /id="VAR_039611"
FT VARIANT 265
FT /note="Q -> P (probable disease-associated variant found in
FT isolated hyperparathyroidism)"
FT /evidence="ECO:0000269|PubMed:10634381"
FT /id="VAR_039612"
FT VARIANT 266
FT /note="Q -> QLQ (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12417605"
FT /id="VAR_039613"
FT VARIANT 269
FT /note="L -> P (in MEN1)"
FT /evidence="ECO:0000269|PubMed:9888389"
FT /id="VAR_005449"
FT VARIANT 272
FT /note="L -> P (probable disease-associated variant found in
FT isolated hyperparathyroidism)"
FT /evidence="ECO:0000269|PubMed:9888389"
FT /id="VAR_005450"
FT VARIANT 279
FT /note="E -> A (in parathyroid tumor)"
FT /evidence="ECO:0000269|PubMed:11034102"
FT /id="VAR_039614"
FT VARIANT 282
FT /note="P -> H (probable disease-associated variant found in
FT isolated hyperparathyroidism; dbSNP:rs1060499973)"
FT /evidence="ECO:0000269|PubMed:12016470"
FT /id="VAR_039615"
FT VARIANT 286
FT /note="G -> R (in MEN1; loss of interaction with KMT2A and
FT JUND; dbSNP:rs1114167493)"
FT /evidence="ECO:0000269|PubMed:12112656,
FT ECO:0000269|PubMed:12652570, ECO:0000269|PubMed:22327296"
FT /id="VAR_039616"
FT VARIANT 289
FT /note="A -> E (in MEN1; dbSNP:rs1565645563)"
FT /evidence="ECO:0000269|PubMed:9463336"
FT /id="VAR_005451"
FT VARIANT 289
FT /note="A -> P (in parathyroid tumor)"
FT /evidence="ECO:0000269|PubMed:11034102"
FT /id="VAR_039617"
FT VARIANT 289
FT /note="A -> Q (requires 2 nucleotide substitutions; yields
FT insoluble protein)"
FT /evidence="ECO:0000269|PubMed:22327296"
FT /id="VAR_082607"
FT VARIANT 291
FT /note="L -> P (in MEN1; almost no effect on JUND-binding)"
FT /evidence="ECO:0000269|PubMed:9989505"
FT /id="VAR_005452"
FT VARIANT 310
FT /note="G -> D (probable disease-associated variant found in
FT isolated hyperparathyroidism)"
FT /evidence="ECO:0000269|PubMed:10664521"
FT /id="VAR_039618"
FT VARIANT 314
FT /note="A -> P (in MEN1; no effect on histone methylation;
FT almost no effect on JUND-binding)"
FT /evidence="ECO:0000269|PubMed:14992727,
FT ECO:0000269|PubMed:9989505"
FT /id="VAR_005453"
FT VARIANT 316
FT /note="T -> P (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656,
FT ECO:0000269|PubMed:12652570"
FT /id="VAR_039619"
FT VARIANT 319
FT /note="R -> P (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656"
FT /id="VAR_005454"
FT VARIANT 322
FT /note="H -> R (in MEN1; dbSNP:rs1114167495)"
FT /evidence="ECO:0000269|PubMed:10849016,
FT ECO:0000269|PubMed:12112656"
FT /id="VAR_039620"
FT VARIANT 322
FT /note="H -> Y (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656,
FT ECO:0000269|PubMed:12652570"
FT /id="VAR_039621"
FT VARIANT 325
FT /note="P -> L (in MEN1; dbSNP:rs1114167469)"
FT /evidence="ECO:0000269|PubMed:9506756"
FT /id="VAR_039622"
FT VARIANT 325
FT /note="P -> R (in MEN1)"
FT /evidence="ECO:0000269|PubMed:15714081"
FT /id="VAR_039623"
FT VARIANT 330
FT /note="A -> P (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12791038"
FT /id="VAR_039624"
FT VARIANT 342
FT /note="A -> D (in MEN1; dbSNP:rs2071312)"
FT /evidence="ECO:0000269|PubMed:12112656"
FT /id="VAR_005455"
FT VARIANT 342
FT /note="A -> P (in MEN1; dbSNP:rs2071312)"
FT /evidence="ECO:0000269|PubMed:10849016"
FT /id="VAR_039625"
FT VARIANT 346
FT /note="W -> R (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656"
FT /id="VAR_005456"
FT VARIANT 347
FT /note="A -> P (in MEN1; dbSNP:rs776561706)"
FT /evidence="ECO:0000269|PubMed:14686752"
FT /id="VAR_039626"
FT VARIANT 349
FT /note="T -> R (in MEN1; almost complete loss of histone
FT methylation; almost no effect on JUND-binding; yields
FT insoluble protein)"
FT /evidence="ECO:0000269|PubMed:10664520,
FT ECO:0000269|PubMed:14992727, ECO:0000269|PubMed:22327296,
FT ECO:0000269|PubMed:9989505"
FT /id="VAR_005457"
FT VARIANT 353
FT /note="I -> N (in MEN1)"
FT /evidence="ECO:0000269|PubMed:10849016"
FT /id="VAR_039627"
FT VARIANT 358
FT /note="Y -> D (in MEN1)"
FT /evidence="ECO:0000269|PubMed:10993647"
FT /id="VAR_039628"
FT VARIANT 360
FT /note="R -> W (in MEN1; dbSNP:rs863224807)"
FT /evidence="ECO:0000269|PubMed:15714081"
FT /id="VAR_039629"
FT VARIANT 362
FT /note="D -> H (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656"
FT /id="VAR_039630"
FT VARIANT 364
FT /note="E -> K (in MEN1; dbSNP:rs387906552)"
FT /evidence="ECO:0000269|PubMed:9740255"
FT /id="VAR_005458"
FT VARIANT 368
FT /note="Missing (in MEN1; dbSNP:rs869025185)"
FT /evidence="ECO:0000269|PubMed:12050235,
FT ECO:0000269|PubMed:9103196"
FT /id="VAR_005459"
FT VARIANT 373
FT /note="A -> D (in MEN1; dbSNP:rs1555164707)"
FT /evidence="ECO:0000269|PubMed:12112656"
FT /id="VAR_005460"
FT VARIANT 377
FT /note="I -> M (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656"
FT /id="VAR_039631"
FT VARIANT 378
FT /note="P -> S (in MEN1; dbSNP:rs794728627)"
FT /evidence="ECO:0000269|PubMed:10993647"
FT /id="VAR_039632"
FT VARIANT 390
FT /note="A -> V (in MEN1; dbSNP:rs1298484645)"
FT /evidence="ECO:0000269|PubMed:10849016"
FT /id="VAR_039633"
FT VARIANT 416
FT /note="A -> P (in MEN1; also found in isolated
FT hyperparathyroidism)"
FT /evidence="ECO:0000269|PubMed:12699448"
FT /id="VAR_039634"
FT VARIANT 418
FT /note="L -> R (in MEN1)"
FT /evidence="ECO:0000269|PubMed:17555499"
FT /id="VAR_065155"
FT VARIANT 419
FT /note="L -> P (in MEN1)"
FT /evidence="ECO:0000269|PubMed:11241849,
FT ECO:0000269|PubMed:17555499"
FT /id="VAR_039635"
FT VARIANT 420
FT /note="R -> P (in MEN1; dbSNP:rs1446518998)"
FT /evidence="ECO:0000269|PubMed:10993647"
FT /id="VAR_039636"
FT VARIANT 423..426
FT /note="Missing (in MEN1)"
FT /id="VAR_005463"
FT VARIANT 423
FT /note="D -> H (in MEN1; dbSNP:rs104894264)"
FT /evidence="ECO:0000269|PubMed:15730416"
FT /id="VAR_039637"
FT VARIANT 423
FT /note="D -> N (in MEN1; dbSNP:rs104894264)"
FT /evidence="ECO:0000269|PubMed:12050235,
FT ECO:0000269|PubMed:12112656, ECO:0000269|PubMed:12652570,
FT ECO:0000269|PubMed:9709921"
FT /id="VAR_005461"
FT VARIANT 423
FT /note="Missing (in MEN1)"
FT /id="VAR_005462"
FT VARIANT 426
FT /note="C -> Y (in MEN1; dbSNP:rs386134249)"
FT /evidence="ECO:0000269|PubMed:15714081"
FT /id="VAR_039638"
FT VARIANT 428
FT /note="W -> S (in MEN1)"
FT /evidence="ECO:0000269|PubMed:9709985"
FT /id="VAR_039639"
FT VARIANT 432
FT /note="S -> R (in MEN1; dbSNP:rs1114167528)"
FT /evidence="ECO:0000269|PubMed:10660339"
FT /id="VAR_039640"
FT VARIANT 441
FT /note="W -> C (in MEN1; dbSNP:rs398124435)"
FT /evidence="ECO:0000269|PubMed:15714081"
FT /id="VAR_039641"
FT VARIANT 441
FT /note="W -> R (in MEN1; no effect on histone methylation;
FT almost no effect on JUND-binding; modest repression of JUND
FT transactivation; dbSNP:rs104894259)"
FT /evidence="ECO:0000269|PubMed:14992727,
FT ECO:0000269|PubMed:15714081, ECO:0000269|PubMed:9103196,
FT ECO:0000269|PubMed:9989505"
FT /id="VAR_005464"
FT VARIANT 449
FT /note="L -> P (in MEN1)"
FT /evidence="ECO:0000269|PubMed:10229909"
FT /id="VAR_039642"
FT VARIANT 452
FT /note="F -> S (in MEN1; sporadic; with Zollinger-Ellison
FT syndrome)"
FT /id="VAR_005465"
FT VARIANT 476
FT /note="W -> C (in MEN1)"
FT /evidence="ECO:0000269|PubMed:17555499"
FT /id="VAR_065156"
FT VARIANT 532
FT /note="R -> C (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656"
FT /id="VAR_039643"
FT VARIANT 545
FT /note="P -> S (in MEN1; dbSNP:rs745404679)"
FT /evidence="ECO:0000269|PubMed:12652570"
FT /id="VAR_039644"
FT VARIANT 546
FT /note="T -> A (in dbSNP:rs2959656)"
FT /evidence="ECO:0000269|PubMed:10576763,
FT ECO:0000269|PubMed:12746426, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17555499, ECO:0000269|PubMed:9103196,
FT ECO:0000269|PubMed:9506756, ECO:0000269|PubMed:9709921,
FT ECO:0000269|PubMed:9888389, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT /id="VAR_005466"
FT VARIANT 549
FT /note="P -> S (in MEN1; dbSNP:rs1387157979)"
FT /evidence="ECO:0000269|PubMed:10849016"
FT /id="VAR_039645"
FT VARIANT 557
FT /note="T -> S (in adrenal adenoma; somatic;
FT dbSNP:rs121913035)"
FT /evidence="ECO:0000269|PubMed:10647896"
FT /id="VAR_039646"
FT VARIANT 560
FT /note="S -> N (in MEN1; dbSNP:rs863224527)"
FT /evidence="ECO:0000269|PubMed:12112656"
FT /id="VAR_005467"
FT VARIANT 560
FT /note="S -> R (in MEN1)"
FT /evidence="ECO:0000269|PubMed:12112656"
FT /id="VAR_039647"
FT MUTAGEN 187
FT /note="A->F: Reduced interaction with KMT2A."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 283
FT /note="M->W: Loss of interaction with KMT2A and JUND."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 290
FT /note="D->R: Reduced interaction with KMT2A; when
FT associated with R-293 and R-295."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 293
FT /note="E->R: Reduced interaction with KMT2A; when
FT associated with R-290 and R-295."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 295
FT /note="E->R: Reduced interaction with KMT2A; when
FT associated with R-290 and R-293."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 324
FT /note="Y->A: Reduced interaction with KMT2A."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 328
FT /note="Y->A: Reduced interaction with KMT2A."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 371
FT /note="E->A: Reduced interaction with KMT2A; when
FT associated with A-375."
FT /evidence="ECO:0000269|PubMed:22327296"
FT MUTAGEN 375
FT /note="D->A: Reduced interaction with KMT2A; when
FT associated with A-371."
FT /evidence="ECO:0000269|PubMed:22327296"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:6O5I"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 34..49
FT /evidence="ECO:0007829|PDB:6O5I"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:6WNH"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3U84"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:6BXY"
FT HELIX 83..100
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:6O5I"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6BXH"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:4GQ6"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 159..172
FT /evidence="ECO:0007829|PDB:6O5I"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6O5I"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6O5I"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:6O5I"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:3U84"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:6O5I"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 259..275
FT /evidence="ECO:0007829|PDB:6O5I"
FT TURN 276..280
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 282..294
FT /evidence="ECO:0007829|PDB:6O5I"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:6B41"
FT HELIX 303..317
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 324..335
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 339..353
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:5DDB"
FT HELIX 363..374
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 376..389
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 412..429
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 439..450
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 454..457
FT /evidence="ECO:0007829|PDB:6O5I"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:4GQ4"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:6E1A"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:4GQ4"
FT HELIX 561..566
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 567..569
FT /evidence="ECO:0007829|PDB:6O5I"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:4OG6"
FT HELIX 577..585
FT /evidence="ECO:0007829|PDB:6O5I"
FT HELIX 603..612
FT /evidence="ECO:0007829|PDB:3U84"
SQ SEQUENCE 615 AA; 68023 MW; DDDF850EA5AB77B4 CRC64;
MGLKAAQKTL FPLRSIDDVV RLFAAELGRE EPDLVLLSLV LGFVEHFLAV NRVIPTNVPE
LTFQPSPAPD PPGGLTYFPV ADLSIIAALY ARFTAQIRGA VDLSLYPREG GVSSRELVKK
VSDVIWNSLS RSYFKDRAHI QSLFSFITGW SPVGTKLDSS GVAFAVVGAC QALGLRDVHL
ALSEDHAWVV FGPNGEQTAE VTWHGKGNED RRGQTVNAGV AERSWLYLKG SYMRCDRKME
VAFMVCAINP SIDLHTDSLE LLQLQQKLLW LLYDLGHLER YPMALGNLAD LEELEPTPGR
PDPLTLYHKG IASAKTYYRD EHIYPYMYLA GYHCRNRNVR EALQAWADTA TVIQDYNYCR
EDEEIYKEFF EVANDVIPNL LKEAASLLEA GEERPGEQSQ GTQSQGSALQ DPECFAHLLR
FYDGICKWEE GSPTPVLHVG WATFLVQSLG RFEGQVRQKV RIVSREAEAA EAEEPWGEEA
REGRRRGPRR ESKPEEPPPP KKPALDKGLG TGQGAVSGPP RKPPGTVAGT ARGPEGGSTA
QVPAPTASPP PEGPVLTFQS EKMKGMKELL VATKINSSAI KLQLTAQSQV QMKKQKVSTP
SDYTLSFLKR QRKGL
