Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Menin

 MEN1_HUMAN              Reviewed;         615 AA.
O00255; A5HBC6; A5HBC7; A5HBC8; A5HBC9; A5HBD0; A5HBD1; A5HBD2;
O00632; Q9BUF0; Q9BUK2;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 4.
25-OCT-2017, entry version 176.
RecName: Full=Menin;
Name=MEN1; Synonyms=SCG2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANTS
MEN1 ARG-22; LYS-119 DEL; GLU-368 DEL AND ARG-441, AND VARIANTS
GLN-176 AND ALA-546.
TISSUE=Leukocyte;
PubMed=9103196; DOI=10.1126/science.276.5311.404;
Chandrasekharappa S.C., Guru S.C., Manickam P., Olufemi S.-E.,
Collins F.S., Emmert-Buck M.R., Debelenko L.V., Zhuang Z.,
Lubensky I.A., Liotta L.A., Crabtree J.S., Wang Y., Roe B.A.,
Weisemann J., Boguski M.S., Agarwal S.K., Kester M.B., Kim Y.S.,
Heppner C., Dong Q., Spiegel A.M., Burns A.L., Marx S.J.;
"Positional cloning of the gene for multiple endocrine neoplasia-type
1.";
Science 276:404-407(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANTS MEN1
89-LEU--ALA-95 DEL; PHE-147; ARG-418; PRO-419 AND CYS-476, AND VARIANT
ALA-546.
PubMed=17555499; DOI=10.1111/j.1365-2265.2007.02895.x;
Toledo R.A., Lourenco D.M., Coutinho F.L., Quedas E., Mackowiack I.,
Machado M.C., Montenegro F., Cunha-Neto M.B., Liberman B.,
Pereira M.A., Correa P.H., Toledo S.P.;
"Novel MEN1 germline mutations in Brazilian families with multiple
endocrine neoplasia type 1.";
Clin. Endocrinol. (Oxf.) 67:377-384(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
ALA-546.
TISSUE=Placenta, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH JUND, AND VARIANTS MEN1 LEU-12; ARG-22; ASP-139;
TYR-139; PRO-165; PRO-181; VAL-247; PRO-291; PRO-314; ARG-349 AND
ARG-441.
PubMed=9989505; DOI=10.1016/S0092-8674(00)80967-8;
Agarwal S.K., Guru S.C., Heppner C., Erdos M.R., Collins R.M.,
Park S.Y., Saggar S., Chandrasekharappa S.C., Collins F.S.,
Spiegel A.M., Marx S.J., Burns A.L.;
"Menin interacts with the AP1 transcription factor JunD and represses
JunD-activated transcription.";
Cell 96:143-152(1999).
[6]
FUNCTION, AND INTERACTION WITH NFKB1; NFKB2 AND RELA.
PubMed=11526476; DOI=10.1038/sj.onc.1204529;
Heppner C., Bilimoria K.Y., Agarwal S.K., Kester M., Whitty L.J.,
Guru S.C., Chandrasekharappa S.C., Collins F.S., Spiegel A.M.,
Marx S.J., Burns A.L.;
"The tumor suppressor protein menin interacts with NF-kappaB proteins
and inhibits NF-kappaB-mediated transactivation.";
Oncogene 20:4917-4925(2001).
[7]
FUNCTION, AND INTERACTION WITH SMAD3.
PubMed=11274402; DOI=10.1073/pnas.061358098;
Kaji H., Canaff L., Lebrun J.J., Goltzman D., Hendy G.N.;
"Inactivation of menin, a Smad3-interacting protein, blocks
transforming growth factor type beta signaling.";
Proc. Natl. Acad. Sci. U.S.A. 98:3837-3842(2001).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FANCD2.
PubMed=12874027;
Jin S., Mao H., Schnepp R.W., Sykes S.M., Silva A.C., D'Andrea A.D.,
Hua X.;
"Menin associates with FANCD2, a protein involved in repair of DNA
damage.";
Cancer Res. 63:4204-4210(2003).
[9]
FUNCTION IN TERT REPRESSION.
PubMed=12837246; DOI=10.1016/S0092-8674(03)00430-6;
Lin S.Y., Elledge S.J.;
"Multiple tumor suppressor pathways negatively regulate telomerase.";
Cell 113:881-889(2003).
[10]
INTERACTION WITH DBF4.
PubMed=15374998; DOI=10.1158/0008-5472.CAN-04-0724;
Schnepp R.W., Hou Z., Wang H., Petersen C., Silva A., Masai H.,
Hua X.;
"Functional interaction between tumor suppressor menin and activator
of S-phase kinase.";
Cancer Res. 64:6791-6796(2004).
[11]
FUNCTION IN H3K4 METHYLATION, IDENTIFICATION IN THE MEN1-ASSOCIATED
HISTONE METHYLTRANSFERASE COMPLEX, INTERACTION WITH POLR2A AND POLR2B,
AND VARIANTS MEN1 LEU-12; ARG-22; ASP-139; VAL-247; PRO-314; ARG-349
AND ARG-441.
PubMed=14992727; DOI=10.1016/S1097-2765(04)00081-4;
Hughes C.M., Rozenblatt-Rosen O., Milne T.A., Copeland T.D.,
Levine S.S., Lee J.C., Hayes D.N., Shanmugam K.S., Bhattacharjee A.,
Biondi C.A., Kay G.F., Hayward N.K., Hess J.L., Meyerson M.;
"Menin associates with a trithorax family histone methyltransferase
complex and with the hoxc8 locus.";
Mol. Cell 13:587-597(2004).
[12]
IDENTIFICATION IN THE MLL-HCF COMPLEX.
PubMed=15199122; DOI=10.1128/MCB.24.13.5639-5649.2004;
Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J.,
Kitabayashi I., Herr W., Cleary M.L.;
"Leukemia proto-oncoprotein MLL forms a SET1-like histone
methyltransferase complex with menin to regulate Hox gene
expression.";
Mol. Cell. Biol. 24:5639-5649(2004).
[13]
INTERACTION WITH DPY30.
PubMed=17500065; DOI=10.1074/jbc.M701574200;
Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T.,
Dressler G.R., Copeland T.D., Kalkum M., Ge K.;
"PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4
methyltransferase complex.";
J. Biol. Chem. 282:20395-20406(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-599, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548 AND THR-599, VARIANT
[LARGE SCALE ANALYSIS] ALA-546, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
VARIANTS MEN1.
PubMed=9215689; DOI=10.1093/hmg/6.7.1169;
Agarwal S.K., Kester M.B., Debelenko L.V., Heppner C.,
Emmert-Buck M.R., Skarulis M.C., Doppman J.L., Kim Y.S.,
Lubensky I.A., Zhuang Z., Green J.S., Guru S.C., Manickam P.,
Olufemi S.E., Liotta L.A., Chandrasekharappa S.C., Collins F.S.,
Spiegel A.M., Burns A.L., Marx S.J.;
"Germline mutations of the MEN1 gene in familial multiple endocrine
neoplasia type 1 and related states.";
Hum. Mol. Genet. 6:1169-1175(1997).
[20]
VARIANT MEN1 SER-188, AND VARIANT GLN-176.
PubMed=9215690; DOI=10.1093/hmg/6.7.1177;
The European consortium on MEN1;
Lemmens I., Van de Ven W.J.M., Kas K., Zhang C.X., Giraud S.,
Wautot V., Buisson N., De Witte K., Salandre J., Lenoir G., Pugeat M.,
Calender A., Parente F., Quincey D., Gaudray P., De Wit M.J.,
Lips C.J.M., Hoeppener J.W.M., Khodaei S., Grant A.L., Weber G.,
Kytoelae S., Teh B.T., Farnebo F., Phelan C., Hayward N., Larsson C.,
Pannett A.A.J., Forbes S.A., Basset J.H.D., Thakker R.V.;
"Identification of the multiple endocrine neoplasia type 1 (MEN1)
gene.";
Hum. Mol. Genet. 6:1177-1183(1997).
[21]
VARIANT PARATHYROID ADENOMA LYS-26.
PubMed=9241276; DOI=10.1038/ng0897-375;
Heppner C., Kester M.B., Agarwal S.K., Debelenko L.V.,
Emmert-Buck M.R., Guru S.C., Manickam P., Olufemi S.-E.,
Skarulis M.C., Doppman J.L., Alexander R.H., Kim Y.S., Saggar S.K.,
Lubensky I.A., Zhuang Z., Liotta L.A., Chandrasekharappa S.C.,
Collins F.S., Spiegel A.M., Burns A.L., Marx S.J.;
"Somatic mutation of the MEN1 gene in parathyroid tumours.";
Nat. Genet. 16:375-378(1997).
[22]
VARIANTS MEN1 ASP-42; PRO-165; ASP-169; SER-188 AND GLU-289.
PubMed=9463336; DOI=10.1086/301729;
Bassett J.H.D., Forbes S.A., Pannett A.A.J., Lloyd S.E.,
Christie P.T., Wooding C., Harding B., Besser G.M., Edwards C.R.,
Monson J.P., Sampson J., Wass J.A.H., Wheeler M.H., Thakker R.V.;
"Characterization of mutations in patients with multiple endocrine
neoplasia type 1.";
Am. J. Hum. Genet. 62:232-244(1998).
[23]
VARIANTS MEN1.
PubMed=9683585; DOI=10.1086/301953;
Giraud S., Zhang C.X., Serova-Sinilnikova O., Wautot V., Salandre J.,
Buisson N., Waterlot C., Bauters C., Porchet N., Aubert J.-P., Emy P.,
Cadiot G., Delemer B., Chabre O., Niccoli P., Leprat F., Duron F.,
Emperauger B., Cougard P., Goudet P., Sarfati E., Riou J.-P.,
Guichard S., Rodier M., Meyrier A., Caron P., Vantyghem M.-C.,
Assayag M., Peix J.-L., Pugeat M., Rohmer V., Vallotton M., Lenoir G.,
Gaudray P., Proye C., Conte-Devolx B., Chanson P., Shugart Y.Y.,
Goldgar D., Murat A., Calender A.;
"Germ-line mutation analysis in patients with multiple endocrine
neoplasia type 1 and related disorders.";
Am. J. Hum. Genet. 63:455-467(1998).
[24]
VARIANT LYS-260, AND INVOLVEMENT IN ISOLATED HYPERPARATHYROIDISM.
PubMed=9792884; DOI=10.1086/302097;
Teh B.T., Esapa C.T., Houlston R., Grandell U., Farnebo F.,
Nordenskjoeld M., Pearce C.J., Carmichael D., Larsson C., Harris P.E.;
"A family with isolated hyperparathyroidism segregating a missense
MEN1 mutation and showing loss of the wild-type alleles in the
parathyroid tumors.";
Am. J. Hum. Genet. 63:1544-1549(1998).
[25]
VARIANT GLU-189, AND INVOLVEMENT IN ISOLATED HYPERPARATHYROIDISM.
PubMed=9843042;
DOI=10.1002/(SICI)1096-8628(19981116)80:3<221::AID-AJMG8>3.0.CO;2-1;
Fujimori M., Shirahama S., Sakurai A., Hashizume K., Hama Y., Ito K.,
Shingu K., Kobayashi S., Amano J., Fukushima Y.;
"Novel V184E MEN1 germline mutation in a Japanese kindred with
familial hyperparathyroidism.";
Am. J. Med. Genet. 80:221-222(1998).
[26]
VARIANTS MEN1 LYS-26 AND PRO-173.
PubMed=9820618; DOI=10.1530/eje.0.1390416;
Bartsch D., Kopp I., Bergenfelz A., Rieder H., Muench K., Jaeger K.,
Deiss Y., Schudy A., Barth P., Arnold R., Rothmund M., Simon B.;
"MEN1 gene mutations in 12 MEN1 families and their associated
tumors.";
Eur. J. Endocrinol. 139:416-420(1998).
[27]
VARIANTS MEN1.
PubMed=9671267;
DOI=10.1002/(SICI)1098-1004(1998)12:2<75::AID-HUMU1>3.0.CO;2-T;
Agarwal S.K., Debelenko L.V., Kester M.B., Guru S.C., Manickam P.,
Olufemi S.-E., Skarulis M.C., Heppner C., Crabtree J.S.,
Lubensky I.A., Zhuang Z., Kim Y.S., Chandrasekharappa S.C.,
Collins F.S., Liotta L.A., Spiegel A.M., Burns A.L., Emmert-Buck M.R.,
Marx S.J.;
"Analysis of recurrent germline mutations in the MEN1 gene encountered
in apparently unrelated families.";
Hum. Mutat. 12:75-82(1998).
[28]
VARIANT MEN1 ARG-432.
PubMed=10660339;
Cote G.J., Lee J.E., Evans D.B., Huang E., Schultz P.N., Dang G.T.,
Qiu H., Shetelbine S., Sellin R.V., Gagel R.F.;
"Five novel mutations in the familial multiple endocrine neoplasia
type 1 (MEN1) gene.";
Hum. Mutat. 12:219-219(1998).
[29]
VARIANT MEN1 LEU-325, AND VARIANT ALA-546.
PubMed=9506756; DOI=10.1210/jcem.83.3.4653;
Tanaka C., Yoshimoto K., Yamada S., Nishioka H., Ii S., Moritani M.,
Yamaoka T., Itakura M.;
"Absence of germ-line mutations of the multiple endocrine neoplasia
type 1 (MEN1) gene in familial pituitary adenoma in contrast to MEN1
in Japanese.";
J. Clin. Endocrinol. Metab. 83:960-965(1998).
[30]
VARIANT MEN1 ASN-423, AND VARIANTS GLN-176 AND ALA-546.
PubMed=9709921; DOI=10.1210/jcem.83.8.5059;
Teh B.T., Kytoelae S., Farnebo F., Bergman L., Wong F.K., Weber G.,
Hayward N., Larsson C., Skogseid B., Beckers A., Phelan C.,
Edwards M., Epstein M., Alford F., Hurley D., Grimmond S., Silins G.,
Walters M., Stewart C., Cardinal J., Khodaei S., Parente F.,
Tranebjaerg L., Jorde R., Menon J., Khir A., Tan T.T., Chan S.P.,
Zaini A., Khalid B.A.K., Sandelin K., Thompson N., Brandi M.-L.,
Warth M., Stock J., Leisti J., Cameron D., Shepherd J.J., Oeberg K.,
Nordenskjoeld M., Salmela P.;
"Mutation analysis of the MEN1 gene in multiple endocrine neoplasia
type 1, familial acromegaly and familial isolated
hyperparathyroidism.";
J. Clin. Endocrinol. Metab. 83:2621-2626(1998).
[31]
VARIANT MEN1 ASP-139, AND VARIANT TRP-157.
PubMed=9709976; DOI=10.1210/jcem.83.8.4977;
Carling T., Correa P., Hessman O., Hedberg J., Skogseid B.,
Lindberg D., Rastad J., Westin G., Akerstrom G.;
"Parathyroid MEN1 gene mutations in relation to clinical
characteristics of nonfamilial primary hyperparathyroidism.";
J. Clin. Endocrinol. Metab. 83:2960-2963(1998).
[32]
VARIANT MEN1 SER-428.
PubMed=9709985; DOI=10.1210/jcem.83.8.5033-4;
Mayr B., Brabant G., von zur Muehlen A.;
"Menin mutations in MEN1 patients.";
J. Clin. Endocrinol. Metab. 83:3004-3005(1998).
[33]
VARIANTS MEN1 ILE-135 AND LYS-364.
PubMed=9740255; DOI=10.1046/j.1523-1747.1998.00317.x;
Boeni R., Vortmeyer A.O., Pack S., Park W.-S., Burg G., Hofbauer G.,
Darling T., Liotta L., Zhuang Z.;
"Somatic mutations of the MEN1 tumor suppressor gene detected in
sporadic angiofibromas.";
J. Invest. Dermatol. 111:539-540(1998).
[34]
VARIANTS MEN1 LYS-119 DEL AND 171-GLN--LEU-173 DEL.
PubMed=9747036; DOI=10.1007/s100380050070;
Sakurai A., Shirahama S., Fujimori M., Katai M., Itakura Y.,
Kobayashi S., Amano J., Fukushima Y., Hashizume K.;
"Novel MEN1 gene mutations in familial multiple endocrine neoplasia
type 1.";
J. Hum. Genet. 43:199-201(1998).
[35]
VARIANT MEN1 GLY-45.
PubMed=9832038; DOI=10.1136/jmg.35.11.915;
Sato M., Matsubara S., Miyauchi A., Ohye H., Imachi H., Murao K.,
Takahara J.;
"Identification of five novel germline mutations of the MEN1 gene in
Japanese multiple endocrine neoplasia type 1 (MEN1) families.";
J. Med. Genet. 35:915-919(1998).
[36]
VARIANT MEN1 ARG-139.
PubMed=10617276; DOI=10.1097/00019606-199912000-00005;
Martin-Campos J.M., Catasus L., Chico A., Mayoral C., Lagarda E.,
Gallart L., Mato E., Rodriguez-Espinosa J., Matias-Guiu X.,
De Leiva A., Blanco-Vaca F.;
"Molecular pathology of multiple endocrine neoplasia type I: two novel
germline mutations and updated classification of mutations affecting
MEN1 gene.";
Diagn. Mol. Pathol. 8:195-204(1999).
[37]
VARIANT MEN1 PRO-449.
PubMed=10229909; DOI=10.1530/eje.0.1400429;
Cetani F., Pardi E., Cianferotti L., Vignali E., Picone A.,
Miccoli P., Pinchera A., Marcocci C.;
"A new mutation of the MEN1 gene in an Italian kindred with multiple
endocrine neoplasia type 1.";
Eur. J. Endocrinol. 140:429-433(1999).
[38]
VARIANTS MEN1 ARG-188; ARG-230; TYR-246 AND PRO-258, AND VARIANT
ALA-546.
PubMed=10576763; DOI=10.1530/eje.0.1410475;
Hai N., Aoki N., Matsuda A., Mori T., Kosugi S.;
"Germline MEN1 mutations in sixteen Japanese families with multiple
endocrine neoplasia type 1 (MEN1).";
Eur. J. Endocrinol. 141:475-480(1999).
[39]
VARIANT ADRENAL ADENOMA SER-557.
PubMed=10647896; DOI=10.1007/s004399900193;
Schulte K.-M., Heinze M., Mengel M., Simon D., Scheuring S.,
Koehrer K., Roeher H.-D.;
"MEN I gene mutations in sporadic adrenal adenomas.";
Hum. Genet. 105:603-610(1999).
[40]
VARIANTS MEN1 TRP-39; TYR-177; ASP-184 AND PRO-269, VARIANTS GLN-176;
PRO-272 AND ALA-546, AND INVOLVEMENT IN ISOLATED HYPERPARATHYROIDISM.
PubMed=9888389;
DOI=10.1002/(SICI)1098-1004(1999)13:1<54::AID-HUMU6>3.0.CO;2-K;
Poncin J., Abs R., Velkeniers B., Bonduelle M., Abramowicz M.,
Legros J.-J., Verloes A., Meurisse M., van Gaal L., Verellen C.,
Koulischer L., Beckers A.;
"Mutation analysis of the MEN1 gene in Belgian patients with multiple
endocrine neoplasia type 1 and related diseases.";
Hum. Mutat. 13:54-60(1999).
[41]
VARIANTS MEN1 ASP-161 AND ARG-246.
PubMed=10090472;
DOI=10.1002/(SICI)1098-1004(1999)13:3<175::AID-HUMU1>3.0.CO;2-R;
Mutch M.G., Dilley W.G., Sanjurjo F., Debenedetti M.K., Doherty G.M.,
Wells S.A. Jr., Goodfellow P.J., Lairmore T.C.;
"Germline mutations in the multiple endocrine neoplasia type 1 gene:
evidence for frequent splicing defects.";
Hum. Mutat. 13:175-185(1999).
[42]
VARIANT MEN1 PHE-160.
PubMed=10534569;
Engelbach M., Forst T., Hankeln T., Tratzky M., Heerdt S.,
Pfuetzner A., Kann P., Kunt T., Schneider S., Schmidt E.R., Beyer J.;
"Germline mutations in the MEN1 gene: creation of a new splice
acceptor site and insertion of 7 intron nucleotides into the mRNA.";
Int. J. Mol. Med. 4:483-485(1999).
[43]
VARIANTS MEN1 LEU-234; ASP-358; SER-378 AND PRO-420.
PubMed=10993647; DOI=10.1054/bjoc.2000.1380;
Bergman L., Teh B.T., Cardinal J., Palmer J., Walters M., Shepherd J.,
Cameron D., Hayward N.;
"Identification of MEN1 gene mutations in families with MEN 1 and
related disorders.";
Br. J. Cancer 83:1009-1014(2000).
[44]
VARIANTS PARATHYROID TUMOR ASP-161; ARG-188; TRP-258; ALA-279 AND
PRO-289.
PubMed=11034102;
Uchino S., Noguchi S., Sato M., Yamashita H., Yamashita H.,
Watanabe S., Murakami T., Toda M., Ohshima A., Futata T.,
Mizukoshi T., Koike E., Takatsu K., Terao K., Wakiya S., Nagatomo M.,
Adachi M.;
"Screening of the MEN1 gene and discovery of germ-line and somatic
mutations in apparently sporadic parathyroid tumors.";
Cancer Res. 60:5553-5557(2000).
[45]
VARIANTS MEN1 TRP-39; LYS-119 DEL; GLN-184; PRO-228; ARG-322; PRO-342;
ASN-353; VAL-390 AND SER-549.
PubMed=10849016; DOI=10.1046/j.1365-2362.2000.00664.x;
Roijers J.F.M., de Wit M.J., van der Luijt R.B.,
Ploos van Amstel H.K., Hoeppener J.W.M., Lips C.J.M.;
"Criteria for mutation analysis in MEN 1-suspected patients: MEN 1
case-finding.";
Eur. J. Clin. Invest. 30:487-492(2000).
[46]
VARIANTS MEN1 LYS-45; MET-220 AND ARG-349.
PubMed=10664520; DOI=10.1530/eje.0.1420131;
Morelli A., Falchetti A., Martineti V., Becherini L., Mark M.,
Friedman E., Brandi M.L.;
"MEN1 gene mutation analysis in Italian patients with multiple
endocrine neoplasia type 1.";
Eur. J. Endocrinol. 142:131-137(2000).
[47]
VARIANT ASP-310, AND INVOLVEMENT IN ISOLATED HYPERPARATHYROIDISM.
PubMed=10664521; DOI=10.1530/eje.0.1420138;
Honda M., Tsukada T., Tanaka H., Maruyama K., Yamaguchi K., Obara T.,
Yamaji T., Ishibashi M.;
"A novel mutation of the MEN1 gene in a Japanese kindred with familial
isolated primary hyperparathyroidism.";
Eur. J. Endocrinol. 142:138-143(2000).
[48]
VARIANT MEN1 LYS-184.
PubMed=11102994;
DOI=10.1002/1098-1004(200012)16:6<533::AID-HUMU22>3.0.CO;2-5;
Weinhaeusel A., Vierhapper H., Schlegl R., Wagner T., Muhr D.,
Scheuba C., Niederle B., Haas O.A.;
"A novel mutation E179K of the MEN1 gene predisposes for multiple
endocrine neoplasia-type 1 (MEN1).";
Hum. Mutat. 16:533-533(2000).
[49]
VARIANT PRO-265, AND INVOLVEMENT IN ISOLATED HYPERPARATHYROIDISM.
PubMed=10634381; DOI=10.1210/jcem.85.1.6299;
Kassem M., Kruse T.A., Wong F.K., Larsson C., Teh B.T.;
"Familial isolated hyperparathyroidism as a variant of multiple
endocrine neoplasia type 1 in a large Danish pedigree.";
J. Clin. Endocrinol. Metab. 85:165-167(2000).
[50]
VARIANT MEN1 ASP-139.
PubMed=11134142; DOI=10.1210/jcem.85.12.7064;
Stratakis C.A., Schussheim D.H., Freedman S.M., Keil M.F., Pack S.D.,
Agarwal S.K., Skarulis M.C., Weil R.J., Lubensky I.A., Zhuang Z.,
Oldfield E.H., Marx S.J.;
"Pituitary macroadenoma in a 5-year-old: an early expression of
multiple endocrine neoplasia type 1.";
J. Clin. Endocrinol. Metab. 85:4776-4780(2000).
[51]
VARIANT MEN1 PRO-419.
PubMed=11241849; DOI=10.1002/humu.12;
Asteria C., Faglia G., Roncoroni R., Borretta G., Ribotto P.,
Beck-Peccoz P.;
"Identification of three novel menin mutations (c.741delGTCA,
c.1348T>C, c.1785delA) in unrelated Italian families affected with
multiple endocrine neoplasia type 1: additional information for
mutational screening.";
Hum. Mutat. 17:237-237(2001).
[52]
VARIANTS MEN1 TRP-39; ASP-42; LEU-98; PRO-165; THR-165; PHE-167;
ASP-169; ARG-170; TYR-177; PRO-228; PHE-245; ARG-286; PRO-316;
PRO-319; TYR-322; ARG-322; ASP-342; ARG-346; HIS-362; ASP-373;
MET-377; ASN-423; CYS-532; ASN-560 AND ARG-560.
PubMed=12112656; DOI=10.1002/humu.10092;
Wautot V., Vercherat C., Lespinasse J., Chambe B., Lenoir G.M.,
Zhang C.X., Porchet N., Cordier M., Beroud C., Calender A.;
"Germline mutation profile of MEN1 in multiple endocrine neoplasia
type 1: search for correlation between phenotype and the functional
domains of the MEN1 protein.";
Hum. Mutat. 20:35-47(2002).
[53]
VARIANT MEN1 LEU-GLN-266 INS.
PubMed=12417605; DOI=10.1093/jjco/hyf079;
Okamoto H., Tamada A., Hai N., Doi M., Uchimura I., Hirata Y.,
Kosugi S.;
"A novel six-nucleotide insertion in exon 4 of the MEN1 gene,
878insCTGCAG, in three patients with familial insulinoma and primary
hyperparathyroidism.";
Jpn. J. Clin. Oncol. 32:368-370(2002).
[54]
VARIANTS MEN1 LYS-119 DEL; ILE-159; GLU-368 DEL AND ASN-423.
PubMed=12050235; DOI=10.1210/jcem.87.6.8607;
Turner J.J.O., Leotlela P.D., Pannett A.A.J., Forbes S.A.,
Bassett J.H.D., Harding B., Christie P.T., Bowen-Jones D., Ellard S.,
Hattersley A., Jackson C.E., Pope R., Quarrell O.W., Trembath R.,
Thakker R.V.;
"Frequent occurrence of an intron 4 mutation in multiple endocrine
neoplasia type 1.";
J. Clin. Endocrinol. Metab. 87:2688-2693(2002).
[55]
VARIANT HIS-282, AND INVOLVEMENT IN ISOLATED HYPERPARATHYROIDISM.
PubMed=12016470; DOI=10.1007/s00268-002-6617-9;
Perrier N.D., Villablanca A., Larsson C., Wong M., Ituarte P.,
Teh B.T., Clark O.H.;
"Genetic screening for MEN1 mutations in families presenting with
familial primary hyperparathyroidism.";
World J. Surg. 26:907-913(2002).
[56]
VARIANTS MEN1 VAL-158 AND PRO-416, AND INVOLVEMENT IN ISOLATED
HYPERPARATHYROIDISM.
PubMed=12699448; DOI=10.1046/j.1365-2265.2003.01765.x;
Pannett A.A.J., Kennedy A.M., Turner J.J.O., Forbes S.A., Cavaco B.M.,
Bassett J.H.D., Cianferotti L., Harding B., Shine B., Flinter F.,
Maidment C.G.H., Trembath R., Thakker R.V.;
"Multiple endocrine neoplasia type 1 (MEN1) germline mutations in
familial isolated primary hyperparathyroidism.";
Clin. Endocrinol. (Oxf.) 58:639-646(2003).
[57]
VARIANT MEN1 PRO-330.
PubMed=12791038; DOI=10.1034/j.1399-0004.2003.00091.x;
Park J.-H., Kim I.-J., Kang H.C., Lee S.-H., Shin Y., Kim K.-H.,
Lim S.-B., Kang S.-B., Lee K.U., Kim S.Y., Lee M.-S., Lee M.-K.,
Park J.-H., Moon S.-D., Park J.-G.;
"Germline mutations of the MEN1 gene in Korean families with multiple
endocrine neoplasia type 1 (MEN1) or MEN1-related disorders.";
Clin. Genet. 64:48-53(2003).
[58]
VARIANTS MEN1 ARG-170; PRO-228; PHE-246; ARG-286; PRO-316; TYR-322;
ASN-423 AND SER-545.
PubMed=12652570; DOI=10.1002/elps.200390023;
Groupe d'etude des neoplasies endocriniennes multiples;
Crepin M., Escande F., Pigny P., Buisine M.-P., Calender A.,
Porchet N., Odou M.-F.;
"Efficient mutation detection in MEN1 gene using a combination of
single-strand conformation polymorphism (MDGA) and heteroduplex
analysis.";
Electrophoresis 24:26-33(2003).
[59]
VARIANT MEN1 PRO-347.
PubMed=14686752;
Ukita C., Yamaguchi M., Tanaka T., Shigeta H., Nishikawa M.;
"A novel missense mutation of the MEN1 gene in a multiple endocrine
neoplasia type 1 patient associated with carcinoid syndrome.";
Intern. Med. 42:1112-1116(2003).
[60]
VARIANTS MEN1 LYS-45 AND PRO-139, AND VARIANTS GLN-176 AND ALA-546.
PubMed=12746426; DOI=10.1136/jmg.40.5.e72;
Cebrian A., Ruiz-Llorente S., Cascon A., Pollan M., Diez J.J.,
Pico A., Telleria D., Benitez J., Robledo M.;
"Mutational and gross deletion study of the MEN1 gene and correlation
with clinical features in Spanish patients.";
J. Med. Genet. 40:E72-E72(2003).
[61]
VARIANT GLN-176.
PubMed=15205994; DOI=10.1007/s10038-004-0163-2;
Balogh K., Patocs A., Majnik J., Varga F., Illyes G., Hunyady L.,
Racz K.;
"Unusual presentation of multiple endocrine neoplasia type 1 in a
young woman with a novel mutation of the MEN1 gene.";
J. Hum. Genet. 49:380-386(2004).
[62]
VARIANTS MEN1 GLU-110 AND HIS-423.
PubMed=15730416; DOI=10.1111/j.1365-2265.2005.02219.x;
Jap T.-S., Chiu C.-Y., Won J.G.-S., Wu Y.-C., Chen H.-S.;
"Novel mutations in the MEN1 gene in subjects with multiple endocrine
neoplasia-1.";
Clin. Endocrinol. (Oxf.) 62:336-342(2005).
[63]
VARIANTS MEN1 VAL-144; ASP-161; ASP-184; LYS-184; ARG-186; MET-220;
ARG-264; ARG-325; TRP-360; TYR-426; CYS-441 AND ARG-441.
PubMed=15714081; DOI=10.1097/01.GIM.0000153663.62300.F8;
Klein R.D., Salih S., Bessoni J., Bale A.E.;
"Clinical testing for multiple endocrine neoplasia type 1 in a DNA
diagnostic laboratory.";
Genet. Med. 7:131-138(2005).
[64]
VARIANT PHE-220, AND ASSOCIATION WITH PARATHYROID CARCINOMA.
PubMed=17555500; DOI=10.1111/j.1365-2265.2007.02894.x;
Haven C.J., van Puijenbroek M., Tan M.H., Teh B.T., Fleuren G.J.,
van Wezel T., Morreau H.;
"Identification of MEN1 and HRPT2 somatic mutations in paraffin-
embedded (sporadic) parathyroid carcinomas.";
Clin. Endocrinol. (Oxf.) 67:370-376(2007).
[65]
VARIANT [LARGE SCALE ANALYSIS] ALA-546, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[66]
VARIANT [LARGE SCALE ANALYSIS] ALA-546, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
-!- FUNCTION: Essential component of a MLL/SET1 histone
methyltransferase (HMT) complex, a complex that specifically
methylates 'Lys-4' of histone H3 (H3K4). Functions as a
transcriptional regulator. Binds to the TERT promoter and
represses telomerase expression. Plays a role in TGFB1-mediated
inhibition of cell-proliferation, possibly regulating SMAD3
transcriptional activity. Represses JUND-mediated transcriptional
activation on AP1 sites, as well as that mediated by NFKB subunit
RELA. Positively regulates HOXC8 and HOXC6 gene expression. May be
involved in normal hematopoiesis through the activation of HOXA9
expression (By similarity). May be involved in DNA repair.
{ECO:0000250, ECO:0000269|PubMed:11274402,
ECO:0000269|PubMed:11526476, ECO:0000269|PubMed:12837246,
ECO:0000269|PubMed:12874027, ECO:0000269|PubMed:14992727}.
-!- SUBUNIT: Component of the MLL-HCF complex, at least composed of
KMT2A/MLL1, MEN1, ASH2L, RBBP5, DPY30, WDR5, HCFC1 and HCFC2.
Component of the menin-associated histone methyltransferase
complex, at least composed of KMT2B/MLL4, MEN1, ASH2L, RBBP5,
DPY30 and WDR5. Interacts with POLR2B. Interacts with POLR2A
phosphorylated at 'Ser-5', but not with the unphosphorylated, nor
'Ser-2' phosphorylated POLR2A forms. Interacts with FANCD2 and
DBF4. Interacts with JUND. Interacts with SMAD3, but not with
SMAD2, nor SMAD4. Directly interacts with NFKB1, NFKB2 and RELA.
{ECO:0000269|PubMed:11274402, ECO:0000269|PubMed:11526476,
ECO:0000269|PubMed:12874027, ECO:0000269|PubMed:14992727,
ECO:0000269|PubMed:15199122, ECO:0000269|PubMed:15374998,
ECO:0000269|PubMed:17500065, ECO:0000269|PubMed:9989505}.
-!- INTERACTION:
O14757:CHEK1; NbExp=2; IntAct=EBI-592789, EBI-974488;
Q9BXW9:FANCD2; NbExp=4; IntAct=EBI-592789, EBI-359343;
P17535:JUND; NbExp=6; IntAct=EBI-9869387, EBI-2682803;
Q03164:KMT2A; NbExp=12; IntAct=EBI-9869387, EBI-591370;
P35579:MYH9; NbExp=4; IntAct=EBI-9869387, EBI-350338;
P19838:NFKB1; NbExp=4; IntAct=EBI-9869387, EBI-697771;
Q00653:NFKB2; NbExp=3; IntAct=EBI-9869387, EBI-9869360;
Q05982:Nme1 (xeno); NbExp=5; IntAct=EBI-9869387, EBI-1165329;
Q04206:RELA; NbExp=4; IntAct=EBI-9869387, EBI-73886;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12874027}.
Note=Concentrated in nuclear body-like structures. Relocates to
the nuclear matrix upon gamma irradiation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Long;
IsoId=O00255-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=O00255-2; Sequence=VSP_004323;
Name=3;
IsoId=O00255-3; Sequence=VSP_004323, VSP_015854;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DISEASE: Familial multiple endocrine neoplasia type I (MEN1)
[MIM:131100]: Autosomal dominant disorder characterized by tumors
of the parathyroid glands, gastro-intestinal endocrine tissue, the
anterior pituitary and other tissues. Cutaneous lesions and
nervous-tissue tumors can exist. Prognosis in MEN1 patients is
related to hormonal hypersecretion by tumors, such as
hypergastrinemia causing severe peptic ulcer disease (Zollinger-
Ellison syndrome, ZES), primary hyperparathyroidism, and acute
forms of hyperinsulinemia. {ECO:0000269|PubMed:10090472,
ECO:0000269|PubMed:10229909, ECO:0000269|PubMed:10534569,
ECO:0000269|PubMed:10576763, ECO:0000269|PubMed:10617276,
ECO:0000269|PubMed:10660339, ECO:0000269|PubMed:10664520,
ECO:0000269|PubMed:10849016, ECO:0000269|PubMed:10993647,
ECO:0000269|PubMed:11102994, ECO:0000269|PubMed:11134142,
ECO:0000269|PubMed:11241849, ECO:0000269|PubMed:12050235,
ECO:0000269|PubMed:12112656, ECO:0000269|PubMed:12417605,
ECO:0000269|PubMed:12652570, ECO:0000269|PubMed:12699448,
ECO:0000269|PubMed:12746426, ECO:0000269|PubMed:12791038,
ECO:0000269|PubMed:14686752, ECO:0000269|PubMed:14992727,
ECO:0000269|PubMed:15714081, ECO:0000269|PubMed:15730416,
ECO:0000269|PubMed:17555499, ECO:0000269|PubMed:9103196,
ECO:0000269|PubMed:9215689, ECO:0000269|PubMed:9215690,
ECO:0000269|PubMed:9463336, ECO:0000269|PubMed:9506756,
ECO:0000269|PubMed:9671267, ECO:0000269|PubMed:9683585,
ECO:0000269|PubMed:9709921, ECO:0000269|PubMed:9709976,
ECO:0000269|PubMed:9709985, ECO:0000269|PubMed:9740255,
ECO:0000269|PubMed:9747036, ECO:0000269|PubMed:9820618,
ECO:0000269|PubMed:9832038, ECO:0000269|PubMed:9888389,
ECO:0000269|PubMed:9989505}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=MEN1 inactivating mutations are responsible for
hyperfunctioning of the parathyroid glands and subsequent primary
hyperparathyroidism. Primary hyperparathyroidism can occur in
isolation or in association with multiple endocrine neoplasia.
{ECO:0000269|PubMed:10634381, ECO:0000269|PubMed:10664521,
ECO:0000269|PubMed:12016470, ECO:0000269|PubMed:12699448,
ECO:0000269|PubMed:9792884, ECO:0000269|PubMed:9843042,
ECO:0000269|PubMed:9888389}.
-!- SEQUENCE CAUTION:
Sequence=ABQ12624.1; Type=Frameshift; Positions=383; Note=The frameshift is caused by a single nucleotide deletion which is found in a MEN1 kindred.; Evidence={ECO:0000305};
Sequence=ABQ12627.1; Type=Frameshift; Positions=97; Note=The frameshift is caused by a single nucleotide deletion which is found in a MEN1 kindred.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MEN1ID148.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U93236; AAC51228.1; -; mRNA.
EMBL; U93237; AAC51229.1; -; Genomic_DNA.
EMBL; U93237; AAC51230.1; -; Genomic_DNA.
EMBL; AP001462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; EF443091; ABQ12621.1; -; Genomic_DNA.
EMBL; EF443092; ABQ12622.1; -; Genomic_DNA.
EMBL; EF443093; ABQ12623.1; -; Genomic_DNA.
EMBL; EF443094; ABQ12624.1; ALT_FRAME; Genomic_DNA.
EMBL; EF443095; ABQ12625.1; -; Genomic_DNA.
EMBL; EF443096; ABQ12626.1; -; Genomic_DNA.
EMBL; EF443097; ABQ12627.1; ALT_FRAME; Genomic_DNA.
EMBL; BC002544; AAH02544.1; -; mRNA.
EMBL; BC002664; AAH02664.2; -; mRNA.
CCDS; CCDS31600.1; -. [O00255-2]
CCDS; CCDS8083.1; -. [O00255-1]
RefSeq; NP_000235.2; NM_000244.3.
RefSeq; NP_570711.1; NM_130799.2.
RefSeq; NP_570712.1; NM_130800.2.
RefSeq; NP_570713.1; NM_130801.2.
RefSeq; NP_570714.1; NM_130802.2.
RefSeq; NP_570715.1; NM_130803.2.
RefSeq; NP_570716.1; NM_130804.2.
RefSeq; XP_005274058.1; XM_005274001.4. [O00255-2]
RefSeq; XP_016873258.1; XM_017017769.1. [O00255-2]
RefSeq; XP_016873259.1; XM_017017770.1. [O00255-2]
UniGene; Hs.423348; -.
PDB; 3U84; X-ray; 2.50 A; A/B=2-615.
PDB; 3U85; X-ray; 3.00 A; A=2-615.
PDB; 3U86; X-ray; 2.84 A; A=2-615.
PDB; 3U88; X-ray; 3.00 A; A/B=2-615.
PDB; 4GPQ; X-ray; 1.46 A; A=1-598.
PDB; 4GQ3; X-ray; 1.56 A; A=1-598.
PDB; 4GQ4; X-ray; 1.27 A; A=1-598.
PDB; 4GQ6; X-ray; 1.55 A; A=1-598.
PDB; 4I80; X-ray; 3.10 A; A=2-615.
PDB; 4OG3; X-ray; 2.01 A; A=1-598.
PDB; 4OG4; X-ray; 1.45 A; A=1-598.
PDB; 4OG5; X-ray; 1.63 A; A=1-598.
PDB; 4OG6; X-ray; 1.49 A; A=1-598.
PDB; 4OG7; X-ray; 2.08 A; A=1-598.
PDB; 4OG8; X-ray; 1.53 A; A=1-598.
PDB; 4X5Y; X-ray; 1.59 A; A=1-432, A=537-593.
PDB; 4X5Z; X-ray; 1.86 A; A=1-432, A=537-598.
PDB; 5DB0; X-ray; 1.50 A; A=1-593.
PDB; 5DB1; X-ray; 1.86 A; A=1-593.
PDB; 5DB2; X-ray; 1.54 A; A=1-593.
PDB; 5DB3; X-ray; 1.71 A; A=1-593.
PDB; 5DD9; X-ray; 1.62 A; A=1-598.
PDB; 5DDA; X-ray; 1.83 A; A=1-593.
PDB; 5DDB; X-ray; 1.54 A; A=1-598.
PDB; 5DDC; X-ray; 1.62 A; A=1-598.
PDB; 5DDD; X-ray; 2.14 A; A=1-593.
PDB; 5DDE; X-ray; 1.78 A; A=1-593.
PDB; 5DDF; X-ray; 1.66 A; A=1-593.
PDBsum; 3U84; -.
PDBsum; 3U85; -.
PDBsum; 3U86; -.
PDBsum; 3U88; -.
PDBsum; 4GPQ; -.
PDBsum; 4GQ3; -.
PDBsum; 4GQ4; -.
PDBsum; 4GQ6; -.
PDBsum; 4I80; -.
PDBsum; 4OG3; -.
PDBsum; 4OG4; -.
PDBsum; 4OG5; -.
PDBsum; 4OG6; -.
PDBsum; 4OG7; -.
PDBsum; 4OG8; -.
PDBsum; 4X5Y; -.
PDBsum; 4X5Z; -.
PDBsum; 5DB0; -.
PDBsum; 5DB1; -.
PDBsum; 5DB2; -.
PDBsum; 5DB3; -.
PDBsum; 5DD9; -.
PDBsum; 5DDA; -.
PDBsum; 5DDB; -.
PDBsum; 5DDC; -.
PDBsum; 5DDD; -.
PDBsum; 5DDE; -.
PDBsum; 5DDF; -.
ProteinModelPortal; O00255; -.
SMR; O00255; -.
BioGrid; 110384; 66.
CORUM; O00255; -.
DIP; DIP-24236N; -.
IntAct; O00255; 28.
MINT; MINT-1543749; -.
STRING; 9606.ENSP00000337088; -.
BindingDB; O00255; -.
ChEMBL; CHEMBL1615381; -.
iPTMnet; O00255; -.
PhosphoSitePlus; O00255; -.
BioMuta; MEN1; -.
EPD; O00255; -.
MaxQB; O00255; -.
PaxDb; O00255; -.
PeptideAtlas; O00255; -.
PRIDE; O00255; -.
DNASU; 4221; -.
Ensembl; ENST00000312049; ENSP00000308975; ENSG00000133895. [O00255-2]
Ensembl; ENST00000315422; ENSP00000323747; ENSG00000133895. [O00255-2]
Ensembl; ENST00000337652; ENSP00000337088; ENSG00000133895. [O00255-1]
Ensembl; ENST00000377313; ENSP00000366530; ENSG00000133895. [O00255-1]
Ensembl; ENST00000377321; ENSP00000366538; ENSG00000133895. [O00255-3]
Ensembl; ENST00000377326; ENSP00000366543; ENSG00000133895. [O00255-2]
Ensembl; ENST00000394374; ENSP00000377899; ENSG00000133895. [O00255-1]
Ensembl; ENST00000394376; ENSP00000377901; ENSG00000133895. [O00255-1]
GeneID; 4221; -.
KEGG; hsa:4221; -.
UCSC; uc001obl.4; human. [O00255-1]
CTD; 4221; -.
DisGeNET; 4221; -.
EuPathDB; HostDB:ENSG00000133895.14; -.
GeneCards; MEN1; -.
GeneReviews; MEN1; -.
HGNC; HGNC:7010; MEN1.
HPA; HPA030342; -.
MalaCards; MEN1; -.
MIM; 131100; phenotype.
MIM; 613733; gene.
neXtProt; NX_O00255; -.
OpenTargets; ENSG00000133895; -.
Orphanet; 99879; Familial isolated hyperparathyroidism.
Orphanet; 99877; Familial parathyroid adenoma.
Orphanet; 652; Multiple endocrine neoplasia type 1.
PharmGKB; PA30746; -.
eggNOG; ENOG410IF2R; Eukaryota.
eggNOG; ENOG410ZNZF; LUCA.
GeneTree; ENSGT00390000014237; -.
HOVERGEN; HBG000208; -.
InParanoid; O00255; -.
KO; K14970; -.
OMA; NNEHIYP; -.
OrthoDB; EOG091G066V; -.
PhylomeDB; O00255; -.
TreeFam; TF323888; -.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; O00255; -.
ChiTaRS; MEN1; human.
GeneWiki; MEN1; -.
GenomeRNAi; 4221; -.
PRO; PR:O00255; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000133895; -.
CleanEx; HS_MEN1; -.
CleanEx; HS_SCG2; -.
ExpressionAtlas; O00255; baseline and differential.
Genevisible; O00255; HS.
GO; GO:0000785; C:chromatin; IDA:UniProtKB.
GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0035097; C:histone methyltransferase complex; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0000784; C:nuclear chromosome, telomeric region; ISS:BHF-UCL.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0000400; F:four-way junction DNA binding; IDA:UniProtKB.
GO; GO:0030674; F:protein binding, bridging; IDA:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0000403; F:Y-form DNA binding; IDA:UniProtKB.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
GO; GO:0046697; P:decidualization; IEA:Ensembl.
GO; GO:0006281; P:DNA repair; NAS:UniProtKB.
GO; GO:0034968; P:histone lysine methylation; IEA:GOC.
GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0046329; P:negative regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IGI:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0051974; P:negative regulation of telomerase activity; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0002076; P:osteoblast development; IGI:MGI.
GO; GO:0032092; P:positive regulation of protein binding; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0032925; P:regulation of activin receptor signaling pathway; IEA:Ensembl.
GO; GO:0061469; P:regulation of type B pancreatic cell proliferation; IEA:Ensembl.
GO; GO:0010332; P:response to gamma radiation; IDA:UniProtKB.
GO; GO:0071559; P:response to transforming growth factor beta; IEA:Ensembl.
GO; GO:0009411; P:response to UV; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0003309; P:type B pancreatic cell differentiation; IEA:Ensembl.
CDD; cd14456; Menin; 1.
InterPro; IPR007747; Menin.
PANTHER; PTHR12693; PTHR12693; 1.
Pfam; PF05053; Menin; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; Disease mutation; DNA-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repressor;
Transcription; Transcription regulation.
CHAIN 1 615 Menin.
/FTId=PRO_0000096411.
REGION 219 395 Interaction with FANCD2.
{ECO:0000269|PubMed:12874027}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 548 548 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 599 599 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 149 153 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9103196}.
/FTId=VSP_004323.
VAR_SEQ 189 223 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015854.
VARIANT 12 12 P -> L (in MEN1; no effect on histone
methylation; almost no effect on JUND-
binding; dbSNP:rs794728614).
{ECO:0000269|PubMed:14992727,
ECO:0000269|PubMed:9989505}.
/FTId=VAR_005425.
VARIANT 22 22 L -> R (in MEN1; no effect on histone
methylation; almost no effect on JUND-
binding; no repression of JUND
transactivation; dbSNP:rs104894256).
{ECO:0000269|PubMed:14992727,
ECO:0000269|PubMed:9103196,
ECO:0000269|PubMed:9989505}.
/FTId=VAR_005426.
VARIANT 26 26 E -> K (in parathyroid adenoma and MEN1;
dbSNP:rs28931612).
{ECO:0000269|PubMed:9241276,
ECO:0000269|PubMed:9820618}.
/FTId=VAR_005427.
VARIANT 39 39 L -> W (in MEN1).
{ECO:0000269|PubMed:10849016,
ECO:0000269|PubMed:12112656,
ECO:0000269|PubMed:9888389}.
/FTId=VAR_005428.
VARIANT 42 42 G -> D (in MEN1).
{ECO:0000269|PubMed:12112656,
ECO:0000269|PubMed:9463336}.
/FTId=VAR_005429.
VARIANT 45 45 E -> G (in MEN1).
{ECO:0000269|PubMed:9832038}.
/FTId=VAR_005430.
VARIANT 45 45 E -> K (in MEN1).
{ECO:0000269|PubMed:10664520,
ECO:0000269|PubMed:12746426}.
/FTId=VAR_039587.
VARIANT 89 95 Missing (in MEN1).
{ECO:0000269|PubMed:17555499}.
/FTId=VAR_065152.
VARIANT 98 98 R -> L (in MEN1).
{ECO:0000269|PubMed:12112656}.
/FTId=VAR_039588.
VARIANT 110 110 G -> E (in MEN1).
{ECO:0000269|PubMed:15730416}.
/FTId=VAR_039589.
VARIANT 119 119 Missing (in MEN1).
{ECO:0000269|PubMed:10849016,
ECO:0000269|PubMed:12050235,
ECO:0000269|PubMed:9103196,
ECO:0000269|PubMed:9747036}.
/FTId=VAR_005431.
VARIANT 135 135 K -> I (in MEN1).
{ECO:0000269|PubMed:9740255}.
/FTId=VAR_005434.
VARIANT 139 139 H -> D (in MEN1; almost complete loss of
histone methylation; strong decrease in
JUND-binding; no repression of JUND
transactivation; dbSNP:rs104894263).
{ECO:0000269|PubMed:11134142,
ECO:0000269|PubMed:14992727,
ECO:0000269|PubMed:9709976,
ECO:0000269|PubMed:9989505}.
/FTId=VAR_005432.
VARIANT 139 139 H -> P (in MEN1).
{ECO:0000269|PubMed:12746426}.
/FTId=VAR_039590.
VARIANT 139 139 H -> R (in MEN1).
{ECO:0000269|PubMed:10617276}.
/FTId=VAR_039591.
VARIANT 139 139 H -> Y (in MEN1; familial and sporadic
cases; almost no effect on JUND-binding;
no repression of JUND transactivation).
{ECO:0000269|PubMed:9989505}.
/FTId=VAR_005433.
VARIANT 144 144 F -> V (in MEN1).
{ECO:0000269|PubMed:15714081}.
/FTId=VAR_005436.
VARIANT 147 147 I -> F (in MEN1).
{ECO:0000269|PubMed:17555499}.
/FTId=VAR_065153.
VARIANT 157 157 L -> W (in parathyroid tumors; somatic).
{ECO:0000269|PubMed:9709976}.
/FTId=VAR_065154.
VARIANT 158 158 D -> V (in MEN1; also found in isolated
hyperparathyroidism).
{ECO:0000269|PubMed:12699448}.
/FTId=VAR_039592.
VARIANT 159 159 S -> I (in MEN1).
{ECO:0000269|PubMed:12050235}.
/FTId=VAR_039593.
VARIANT 160 160 S -> F (in MEN1).
{ECO:0000269|PubMed:10534569}.
/FTId=VAR_039594.
VARIANT 161 161 G -> D (in MEN1 and parathyroid tumor).
{ECO:0000269|PubMed:10090472,
ECO:0000269|PubMed:11034102,
ECO:0000269|PubMed:15714081}.
/FTId=VAR_008017.
VARIANT 165 165 A -> P (in MEN1; strong decrease in JUND-
binding). {ECO:0000269|PubMed:12112656,
ECO:0000269|PubMed:9463336,
ECO:0000269|PubMed:9989505}.
/FTId=VAR_005437.
VARIANT 165 165 A -> T (in MEN1).
{ECO:0000269|PubMed:12112656}.
/FTId=VAR_039595.
VARIANT 167 167 V -> F (in MEN1).
{ECO:0000269|PubMed:12112656}.
/FTId=VAR_039596.
VARIANT 169 169 A -> D (in MEN1).
{ECO:0000269|PubMed:12112656,
ECO:0000269|PubMed:9463336}.
/FTId=VAR_005438.
VARIANT 170 170 C -> R (in MEN1).
{ECO:0000269|PubMed:12112656,
ECO:0000269|PubMed:12652570}.
/FTId=VAR_039597.
VARIANT 171 173 Missing (in MEN1).
{ECO:0000269|PubMed:9747036}.
/FTId=VAR_005439.
VARIANT 173 173 L -> P (in MEN1; dbSNP:rs386134256).
{ECO:0000269|PubMed:9820618}.
/FTId=VAR_039598.
VARIANT 176 176 R -> Q (in dbSNP:rs607969).
{ECO:0000269|PubMed:12746426,
ECO:0000269|PubMed:15205994,
ECO:0000269|PubMed:9103196,
ECO:0000269|PubMed:9215690,
ECO:0000269|PubMed:9709921,
ECO:0000269|PubMed:9888389}.
/FTId=VAR_005440.
VARIANT 177 177 D -> Y (in MEN1).
{ECO:0000269|PubMed:12112656,
ECO:0000269|PubMed:9888389}.
/FTId=VAR_005441.
VARIANT 181 181 A -> P (in MEN1; loss of JUND-binding;
dbSNP:rs376872829).
{ECO:0000269|PubMed:9989505}.
/FTId=VAR_005442.
VARIANT 184 184 E -> D (in MEN1).
{ECO:0000269|PubMed:15714081,
ECO:0000269|PubMed:9888389}.
/FTId=VAR_005443.
VARIANT 184 184 E -> K (in MEN1).
{ECO:0000269|PubMed:11102994,
ECO:0000269|PubMed:15714081}.
/FTId=VAR_039599.
VARIANT 184 184 E -> Q (in MEN1).
{ECO:0000269|PubMed:10849016}.
/FTId=VAR_039600.
VARIANT 186 186 H -> R (in MEN1).
{ECO:0000269|PubMed:15714081}.
/FTId=VAR_039601.
VARIANT 188 188 W -> R (in MEN1 and parathyroid tumor;
dbSNP:rs794728649).
{ECO:0000269|PubMed:10576763,
ECO:0000269|PubMed:11034102}.
/FTId=VAR_039602.
VARIANT 188 188 W -> S (in MEN1).
{ECO:0000269|PubMed:9215690,
ECO:0000269|PubMed:9463336}.
/FTId=VAR_005444.
VARIANT 189 189 V -> E (probable disease-associated
mutation found in isolated
hyperparathyroidism; dbSNP:rs104894262).
{ECO:0000269|PubMed:9843042}.
/FTId=VAR_005445.
VARIANT 220 220 V -> F (found in a parathyroid carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17555500}.
/FTId=VAR_064937.
VARIANT 220 220 V -> M (in MEN1; dbSNP:rs794728621).
{ECO:0000269|PubMed:10664520,
ECO:0000269|PubMed:15714081}.
/FTId=VAR_039603.
VARIANT 228 228 L -> P (in MEN1).
{ECO:0000269|PubMed:10849016,
ECO:0000269|PubMed:12112656,
ECO:0000269|PubMed:12652570}.
/FTId=VAR_005446.
VARIANT 230 230 G -> R (in MEN1).
{ECO:0000269|PubMed:10576763}.
/FTId=VAR_039604.
VARIANT 234 234 R -> L (in MEN1).
{ECO:0000269|PubMed:10993647}.
/FTId=VAR_039605.
VARIANT 245 245 V -> F (in MEN1).
{ECO:0000269|PubMed:12112656}.
/FTId=VAR_039606.
VARIANT 246 246 C -> F (in MEN1).
{ECO:0000269|PubMed:12652570}.
/FTId=VAR_039607.
VARIANT 246 246 C -> R (in MEN1).
{ECO:0000269|PubMed:10090472}.
/FTId=VAR_008018.
VARIANT 246 246 C -> Y (in MEN1; dbSNP:rs794728624).
{ECO:0000269|PubMed:10576763}.
/FTId=VAR_039608.
VARIANT 247 247 A -> V (in MEN1; almost complete loss of
histone methylation; loss of JUND-
binding; no repression of JUND
transactivation).
{ECO:0000269|PubMed:14992727,
ECO:0000269|PubMed:9989505}.
/FTId=VAR_005447.
VARIANT 258 258 S -> P (in MEN1).
{ECO:0000269|PubMed:10576763}.
/FTId=VAR_039609.
VARIANT 258 258 S -> W (in parathyroid tumor).
{ECO:0000269|PubMed:11034102}.
/FTId=VAR_039610.
VARIANT 260 260 E -> K (probable disease-associated
mutation found in isolated
hyperparathyroidism; dbSNP:rs104894268).
{ECO:0000269|PubMed:9792884}.
/FTId=VAR_005448.
VARIANT 264 264 L -> R (in MEN1).
{ECO:0000269|PubMed:15714081}.
/FTId=VAR_039611.
VARIANT 265 265 Q -> P (probable disease-associated
mutation found in isolated
hyperparathyroidism).
{ECO:0000269|PubMed:10634381}.
/FTId=VAR_039612.
VARIANT 266 266 Q -> QLQ (in MEN1).
{ECO:0000269|PubMed:12417605}.
/FTId=VAR_039613.
VARIANT 269 269 L -> P (in MEN1).
{ECO:0000269|PubMed:9888389}.
/FTId=VAR_005449.
VARIANT 272 272 L -> P (probable disease-associated
mutation found in isolated
hyperparathyroidism).
{ECO:0000269|PubMed:9888389}.
/FTId=VAR_005450.
VARIANT 279 279 E -> A (in parathyroid tumor).
{ECO:0000269|PubMed:11034102}.
/FTId=VAR_039614.
VARIANT 282 282 P -> H (probable disease-associated
mutation found in isolated
hyperparathyroidism).
{ECO:0000269|PubMed:12016470}.
/FTId=VAR_039615.
VARIANT 286 286 G -> R (in MEN1).
{ECO:0000269|PubMed:12112656,
ECO:0000269|PubMed:12652570}.
/FTId=VAR_039616.
VARIANT 289 289 A -> E (in MEN1).
{ECO:0000269|PubMed:9463336}.
/FTId=VAR_005451.
VARIANT 289 289 A -> P (in parathyroid tumor).
{ECO:0000269|PubMed:11034102}.
/FTId=VAR_039617.
VARIANT 291 291 L -> P (in MEN1; almost no effect on
JUND-binding).
{ECO:0000269|PubMed:9989505}.
/FTId=VAR_005452.
VARIANT 310 310 G -> D (probable disease-associated
mutation found in isolated
hyperparathyroidism).
{ECO:0000269|PubMed:10664521}.
/FTId=VAR_039618.
VARIANT 314 314 A -> P (in MEN1; no effect on histone
methylation; almost no effect on JUND-
binding). {ECO:0000269|PubMed:14992727,
ECO:0000269|PubMed:9989505}.
/FTId=VAR_005453.
VARIANT 316 316 T -> P (in MEN1).
{ECO:0000269|PubMed:12112656,
ECO:0000269|PubMed:12652570}.
/FTId=VAR_039619.
VARIANT 319 319 R -> P (in MEN1).
{ECO:0000269|PubMed:12112656}.
/FTId=VAR_005454.
VARIANT 322 322 H -> R (in MEN1).
{ECO:0000269|PubMed:10849016,
ECO:0000269|PubMed:12112656}.
/FTId=VAR_039620.
VARIANT 322 322 H -> Y (in MEN1).
{ECO:0000269|PubMed:12112656,
ECO:0000269|PubMed:12652570}.
/FTId=VAR_039621.
VARIANT 325 325 P -> L (in MEN1).
{ECO:0000269|PubMed:9506756}.
/FTId=VAR_039622.
VARIANT 325 325 P -> R (in MEN1).
{ECO:0000269|PubMed:15714081}.
/FTId=VAR_039623.
VARIANT 330 330 A -> P (in MEN1).
{ECO:0000269|PubMed:12791038}.
/FTId=VAR_039624.
VARIANT 342 342 A -> D (in MEN1; dbSNP:rs2071312).
{ECO:0000269|PubMed:12112656}.
/FTId=VAR_005455.
VARIANT 342 342 A -> P (in MEN1).
{ECO:0000269|PubMed:10849016}.
/FTId=VAR_039625.
VARIANT 346 346 W -> R (in MEN1).
{ECO:0000269|PubMed:12112656}.
/FTId=VAR_005456.
VARIANT 347 347 A -> P (in MEN1).
{ECO:0000269|PubMed:14686752}.
/FTId=VAR_039626.
VARIANT 349 349 T -> R (in MEN1; almost complete loss of
histone methylation; almost no effect on
JUND-binding).
{ECO:0000269|PubMed:10664520,
ECO:0000269|PubMed:14992727,
ECO:0000269|PubMed:9989505}.
/FTId=VAR_005457.
VARIANT 353 353 I -> N (in MEN1).
{ECO:0000269|PubMed:10849016}.
/FTId=VAR_039627.
VARIANT 358 358 Y -> D (in MEN1).
{ECO:0000269|PubMed:10993647}.
/FTId=VAR_039628.
VARIANT 360 360 R -> W (in MEN1).
{ECO:0000269|PubMed:15714081}.
/FTId=VAR_039629.
VARIANT 362 362 D -> H (in MEN1).
{ECO:0000269|PubMed:12112656}.
/FTId=VAR_039630.
VARIANT 364 364 E -> K (in MEN1; dbSNP:rs387906552).
{ECO:0000269|PubMed:9740255}.
/FTId=VAR_005458.
VARIANT 368 368 Missing (in MEN1).
{ECO:0000269|PubMed:12050235,
ECO:0000269|PubMed:9103196}.
/FTId=VAR_005459.
VARIANT 373 373 A -> D (in MEN1).
{ECO:0000269|PubMed:12112656}.
/FTId=VAR_005460.
VARIANT 377 377 I -> M (in MEN1).
{ECO:0000269|PubMed:12112656}.
/FTId=VAR_039631.
VARIANT 378 378 P -> S (in MEN1).
{ECO:0000269|PubMed:10993647}.
/FTId=VAR_039632.
VARIANT 390 390 A -> V (in MEN1).
{ECO:0000269|PubMed:10849016}.
/FTId=VAR_039633.
VARIANT 416 416 A -> P (in MEN1; also found in isolated
hyperparathyroidism).
{ECO:0000269|PubMed:12699448}.
/FTId=VAR_039634.
VARIANT 418 418 L -> R (in MEN1).
{ECO:0000269|PubMed:17555499}.
/FTId=VAR_065155.
VARIANT 419 419 L -> P (in MEN1).
{ECO:0000269|PubMed:11241849,
ECO:0000269|PubMed:17555499}.
/FTId=VAR_039635.
VARIANT 420 420 R -> P (in MEN1).
{ECO:0000269|PubMed:10993647}.
/FTId=VAR_039636.
VARIANT 423 426 Missing (in MEN1).
/FTId=VAR_005463.
VARIANT 423 423 D -> H (in MEN1; dbSNP:rs104894264).
{ECO:0000269|PubMed:15730416}.
/FTId=VAR_039637.
VARIANT 423 423 D -> N (in MEN1; dbSNP:rs104894264).
{ECO:0000269|PubMed:12050235,
ECO:0000269|PubMed:12112656,
ECO:0000269|PubMed:12652570,
ECO:0000269|PubMed:9709921}.
/FTId=VAR_005461.
VARIANT 423 423 Missing (in MEN1).
/FTId=VAR_005462.
VARIANT 426 426 C -> Y (in MEN1; dbSNP:rs386134249).
{ECO:0000269|PubMed:15714081}.
/FTId=VAR_039638.
VARIANT 428 428 W -> S (in MEN1).
{ECO:0000269|PubMed:9709985}.
/FTId=VAR_039639.
VARIANT 432 432 S -> R (in MEN1).
{ECO:0000269|PubMed:10660339}.
/FTId=VAR_039640.
VARIANT 441 441 W -> C (in MEN1; dbSNP:rs398124435).
{ECO:0000269|PubMed:15714081}.
/FTId=VAR_039641.
VARIANT 441 441 W -> R (in MEN1; no effect on histone
methylation; almost no effect on JUND-
binding; modest repression of JUND
transactivation; dbSNP:rs104894259).
{ECO:0000269|PubMed:14992727,
ECO:0000269|PubMed:15714081,
ECO:0000269|PubMed:9103196,
ECO:0000269|PubMed:9989505}.
/FTId=VAR_005464.
VARIANT 449 449 L -> P (in MEN1).
{ECO:0000269|PubMed:10229909}.
/FTId=VAR_039642.
VARIANT 452 452 F -> S (in MEN1; sporadic; with
Zollinger-Ellison syndrome).
/FTId=VAR_005465.
VARIANT 476 476 W -> C (in MEN1).
{ECO:0000269|PubMed:17555499}.
/FTId=VAR_065156.
VARIANT 532 532 R -> C (in MEN1).
{ECO:0000269|PubMed:12112656}.
/FTId=VAR_039643.
VARIANT 545 545 P -> S (in MEN1; dbSNP:rs745404679).
{ECO:0000269|PubMed:12652570}.
/FTId=VAR_039644.
VARIANT 546 546 T -> A (in dbSNP:rs2959656).
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10576763,
ECO:0000269|PubMed:12746426,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17555499,
ECO:0000269|PubMed:9103196,
ECO:0000269|PubMed:9506756,
ECO:0000269|PubMed:9709921,
ECO:0000269|PubMed:9888389}.
/FTId=VAR_005466.
VARIANT 549 549 P -> S (in MEN1).
{ECO:0000269|PubMed:10849016}.
/FTId=VAR_039645.
VARIANT 557 557 T -> S (in adrenal adenoma; somatic;
dbSNP:rs121913035).
{ECO:0000269|PubMed:10647896}.
/FTId=VAR_039646.
VARIANT 560 560 S -> N (in MEN1; dbSNP:rs863224527).
{ECO:0000269|PubMed:12112656}.
/FTId=VAR_005467.
VARIANT 560 560 S -> R (in MEN1).
{ECO:0000269|PubMed:12112656}.
/FTId=VAR_039647.
HELIX 5 8 {ECO:0000244|PDB:4GQ4}.
HELIX 16 27 {ECO:0000244|PDB:4GQ4}.
STRAND 29 31 {ECO:0000244|PDB:4GQ4}.
HELIX 34 49 {ECO:0000244|PDB:4GQ4}.
STRAND 63 67 {ECO:0000244|PDB:3U84}.
TURN 70 72 {ECO:0000244|PDB:3U84}.
STRAND 74 79 {ECO:0000244|PDB:3U84}.
HELIX 83 100 {ECO:0000244|PDB:4GQ4}.
HELIX 103 105 {ECO:0000244|PDB:4GQ4}.
HELIX 109 111 {ECO:0000244|PDB:4GQ4}.
HELIX 115 127 {ECO:0000244|PDB:4GQ4}.
STRAND 137 139 {ECO:0000244|PDB:4GQ6}.
HELIX 143 149 {ECO:0000244|PDB:4GQ4}.
HELIX 159 172 {ECO:0000244|PDB:4GQ4}.
STRAND 179 182 {ECO:0000244|PDB:4GQ4}.
STRAND 187 192 {ECO:0000244|PDB:4GQ4}.
HELIX 193 195 {ECO:0000244|PDB:4GQ4}.
STRAND 197 199 {ECO:0000244|PDB:4GQ4}.
STRAND 205 207 {ECO:0000244|PDB:4GQ4}.
HELIX 209 211 {ECO:0000244|PDB:3U84}.
HELIX 217 221 {ECO:0000244|PDB:4GQ4}.
HELIX 225 230 {ECO:0000244|PDB:4GQ4}.
HELIX 237 246 {ECO:0000244|PDB:4GQ4}.
STRAND 251 253 {ECO:0000244|PDB:4GQ4}.
HELIX 259 275 {ECO:0000244|PDB:4GQ4}.
TURN 276 280 {ECO:0000244|PDB:4GQ4}.
HELIX 282 294 {ECO:0000244|PDB:4GQ4}.
HELIX 303 317 {ECO:0000244|PDB:4GQ4}.
HELIX 324 335 {ECO:0000244|PDB:4GQ4}.
HELIX 339 353 {ECO:0000244|PDB:4GQ4}.
HELIX 360 362 {ECO:0000244|PDB:5DDB}.
HELIX 363 374 {ECO:0000244|PDB:4GQ4}.
HELIX 376 389 {ECO:0000244|PDB:4GQ4}.
HELIX 408 410 {ECO:0000244|PDB:4GQ4}.
HELIX 412 429 {ECO:0000244|PDB:4GQ4}.
HELIX 439 450 {ECO:0000244|PDB:4GQ4}.
HELIX 454 457 {ECO:0000244|PDB:4GQ4}.
STRAND 461 463 {ECO:0000244|PDB:4GQ4}.
STRAND 555 557 {ECO:0000244|PDB:4GQ4}.
HELIX 561 566 {ECO:0000244|PDB:4GQ4}.
HELIX 567 569 {ECO:0000244|PDB:4GQ4}.
STRAND 572 574 {ECO:0000244|PDB:4OG6}.
HELIX 577 585 {ECO:0000244|PDB:4GQ4}.
HELIX 603 612 {ECO:0000244|PDB:3U84}.
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


Related products :

Catalog number Product name Quantity
BLP044 MENIN BLOCKING PEPTIDE, Product Type Blocking Peptide, Specificity MENIN , Target Species Human, Host N_A, Format Purified, Isotypes , Applications IP, WB, Clone 50 µg
SCH-BLP044 MENIN BLOCKING PEPTIDE, Product Type Blocking Peptide, Specificity MENIN , Target Species Human, Host N_A, Format Purified, Isotypes , Applications IP, WB, Clone 50 µg
SCH-AHP1527 RABBIT ANTI MENIN, Product Type Polyclonal Antibody, Specificity MENIN, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications IP, P*, WB, Clone 50 µg
AHP1527 RABBIT ANTI MENIN, Product Type Polyclonal Antibody, Specificity MENIN, Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Applications IP, P*, WB, Clone 50 µg
18-272-195559 Menin - Rabbit polyclonal to Menin Polyclonal 0.05 mg
18-272-195558 Menin - Rabbit polyclonal to Menin Polyclonal 0.05 mg
18-272-197142 Menin - Rabbit polyclonal to Menin Polyclonal 0.05 mg
AP14058PU-N Menin 0.1 mg
AP14059PU-N Menin 0.1 mg
AP05751PU-N Menin 50 µg
NB100-215 Menin 0.1 mg
NB100-287 Menin 0.1 mg
NB100-398 Menin 0.1 ml
NB100-399 Menin 0.1 ml
GTX11893 Menin 50 µg
GTX11894 Menin 50 µg
GTX19206 Menin 100 µg
GTX22605 Menin 50 µg
GTX30319 Menin 100 µg
GTX24452 Menin 50 µg
GTX22605 Menin 50 µg
AP14059PU-N Menin 0.1 mg
GTX11893 Menin 50 µg
GTX11894 Menin 50 µg
GTX19206 Menin 100 µg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur