MEN1_MOUSE
ID MEN1_MOUSE Reviewed; 611 AA.
AC O88559; Q3U491; Q8CI72; Q91UZ7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Menin;
GN Name=Men1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9824159; DOI=10.1038/sj.onc.1202164;
RA Stewart C., Parente F., Piehl F., Farnebo F., Quincey D., Silins G.,
RA Bergman L., Carle G.F., Lemmens I., Grimmond S., Xian C.Z., Khodei S.,
RA Teh B.T., Lagercrantz J., Siggers P., Calender A., van de Vem V., Kas K.,
RA Weber G., Hayward N., Gaudray P., Larsson C.;
RT "Characterization of the mouse Men1 gene and its expression during
RT development.";
RL Oncogene 17:2485-2493(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/c X CBA;
RX PubMed=10524203; DOI=10.1016/s0167-4781(99)00089-5;
RA Karges W., Maier S., Wissmann A., Dralle H., Dosch H.M., Boehm B.O.;
RT "Primary structure, gene expression and chromosomal mapping of rodent
RT homologs of the MEN1 tumor suppressor gene.";
RL Biochim. Biophys. Acta 1446:286-294(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=129/Ola;
RX PubMed=9893060; DOI=10.1359/jbmr.1999.14.1.3;
RA Bassett J.H.D., Rashbass P., Harding B., Forbes S.A., Pannett A.A.,
RA Thakker R.V.;
RT "Studies of the murine homolog of the multiple endocrine neoplasia type 1
RT (MEN1) gene, men1.";
RL J. Bone Miner. Res. 14:3-10(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=129/Sv;
RX PubMed=10341092; DOI=10.1007/s003359901051;
RA Guru S.C., Crabtree J.S., Brown K.D., Dunn K.J., Manickam P., Prasad N.B.,
RA Wangsa D., Burns A.L., Spiegel A.M., Marx S.J., Pavan W.J., Collins F.S.,
RA Chandrasekharappa S.C.;
RT "Isolation, genomic organization, and expression analysis of Men1, the
RT murine homolog of the MEN1 gene.";
RL Mamm. Genome 10:592-596(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=10612420; DOI=10.1016/s0303-7207(99)00150-1;
RA Maruyama K., Tsukada T., Hosono T., Ohkura N., Kishi M., Honda M.,
RA Nara-Ashizawa N., Nagasaki K., Yamaguchi K.;
RT "Structure and distribution of rat menin mRNA.";
RL Mol. Cell. Endocrinol. 156:25-33(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NOD; TISSUE=Dendritic cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INTERACTION WITH JUND.
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 [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=11158604; DOI=10.1073/pnas.98.3.1118;
RA Crabtree J.S., Scacheri P.C., Ward J.M., Garrett-Beal L., Emmert-Buck M.R.,
RA Edgemon K.A., Lorang D., Libutti S.K., Chandrasekharappa S.C., Marx S.J.,
RA Spiegel A.M., Collins F.S.;
RT "A mouse model of multiple endocrine neoplasia, type 1, develops multiple
RT endocrine tumors.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1118-1123(2001).
RN [11]
RP FUNCTION.
RX PubMed=16415155; DOI=10.1073/pnas.0510347103;
RA Chen Y.X., Yan J., Keeshan K., Tubbs A.T., Wang H., Silva A., Brown E.J.,
RA Hess J.L., Pear W.S., Hua X.;
RT "The tumor suppressor menin regulates hematopoiesis and myeloid
RT transformation by influencing Hox gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:1018-1023(2006).
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 (By similarity).
CC May be involved in normal hematopoiesis through the activation of HOXA9
CC expression. May be involved in DNA repair.
CC {ECO:0000250|UniProtKB:O00255, ECO:0000269|PubMed:16415155}.
CC -!- SUBUNIT: Component of the MLL-HCF complex, at least composed of
CC KMT2A/MLL1, MEN1, ASH2L, RBBP5, DPY30, WDR5, HCFC1 and HCFC2 (By
CC similarity). Component of the menin-associated histone
CC methyltransferase complex, at least composed of KMT2B/MLL4, MEN1,
CC ASH2L, RBBP5, DPY30 and WDR5 (By similarity). Interacts with POLR2B (By
CC similarity). Interacts with POLR2A phosphorylated at 'Ser-5', but not
CC with the unphosphorylated, nor 'Ser-2' phosphorylated POLR2A forms (By
CC similarity). Interacts with FANCD2 and DBF4 (By similarity). Interacts
CC with SMAD3, but not with SMAD2, nor SMAD4 (By similarity). Directly
CC interacts with NFKB1, NFKB2 and RELA (By similarity). Interacts with
CC JUND (via MBM motif); inhibits the interaction of JUND with MAPK10 and
CC the phosphorylation of JUND by MAP kinases MAPK8 and MAPK10
CC (PubMed:9989505). Interacts with KMT2A (via MBM motif) (By similarity).
CC The KMT2A-MEN1 complex interacts with PSIP1 with a greater affinity as
CC MEN1 enhances interaction of KMT2A with PSIP1 (By similarity).
CC {ECO:0000250|UniProtKB:O00255, ECO:0000269|PubMed:9989505}.
CC -!- INTERACTION:
CC O88559; Q9Z0Y9: Nr1h3; NbExp=3; IntAct=EBI-3990176, EBI-5276764;
CC O88559; P23204: Ppara; NbExp=2; IntAct=EBI-3990176, EBI-5273083;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9824159}. Note=May be
CC perinuclear in testis. {ECO:0000269|PubMed:9824159}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88559-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88559-2; Sequence=VSP_041100;
CC -!- TISSUE SPECIFICITY: Widely expressed, with high levels in hippocampus,
CC cerebral cortex, testis and thymus (at protein level). Also expressed
CC at high levels in pancreatic islets, ovary and bone marrow. In the
CC brain, highest expression in hippocampus pyramidal nerve cells (at
CC protein level). In the testis, may be expressed in spermatogonia (at
CC protein level). Low expression, if any, in skeletal muscle.
CC {ECO:0000269|PubMed:10341092, ECO:0000269|PubMed:10524203,
CC ECO:0000269|PubMed:9824159}.
CC -!- DEVELOPMENTAL STAGE: First detected at 7 dpc. At 13.5 dpc, expressed
CC throughout the embryo, including forelimb, gut, head, heart and lung.
CC At 17 dpc, expression becomes more restricted, with high levels mainly
CC in the thymus, skeletal muscle, brain and spinal cord.
CC {ECO:0000269|PubMed:10341092, ECO:0000269|PubMed:9824159}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mice die in utero at 11.5-12.5 dpc. At
CC 9 months of age, heterozygous mice develop pancreatic islet lesions,
CC from hyperplasia to insulin-producing islet cell tumors, and frequently
CC parathyroid adenomas. Larger, more numerous tumors involving pancreatic
CC islets, parathyroids, thyroid, adrenal cortex and pituitary are seen by
CC 16 months. All tumors show loss of the wild-type allele.
CC {ECO:0000269|PubMed:11158604}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE32542.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF016398; AAC79938.1; -; mRNA.
DR EMBL; AF024513; AAC79939.1; -; Genomic_DNA.
DR EMBL; AF130368; AAF01352.1; -; mRNA.
DR EMBL; AF072755; AAC26001.1; -; mRNA.
DR EMBL; AF093756; AAC78843.1; -; Genomic_DNA.
DR EMBL; AF109389; AAD37498.1; -; mRNA.
DR EMBL; AF109390; AAD38333.1; -; Genomic_DNA.
DR EMBL; AB023401; BAA74964.1; -; mRNA.
DR EMBL; AK154371; BAE32542.1; ALT_INIT; mRNA.
DR EMBL; AK170713; BAE41971.1; -; mRNA.
DR EMBL; CH466612; EDL33234.1; -; Genomic_DNA.
DR EMBL; CH466612; EDL33236.1; -; Genomic_DNA.
DR EMBL; BC036287; AAH36287.1; -; mRNA.
DR CCDS; CCDS29502.1; -. [O88559-1]
DR CCDS; CCDS50367.1; -. [O88559-2]
DR RefSeq; NP_001161960.1; NM_001168488.1.
DR RefSeq; NP_001161961.1; NM_001168489.1. [O88559-1]
DR RefSeq; NP_001161962.1; NM_001168490.1. [O88559-2]
DR RefSeq; NP_032609.1; NM_008583.2. [O88559-1]
DR AlphaFoldDB; O88559; -.
DR SMR; O88559; -.
DR BioGRID; 201393; 11.
DR ComplexPortal; CPX-628; Menin-JUND transcription inhibition complex.
DR IntAct; O88559; 6.
DR MINT; O88559; -.
DR STRING; 10090.ENSMUSP00000058149; -.
DR ChEMBL; CHEMBL3124739; -.
DR iPTMnet; O88559; -.
DR PhosphoSitePlus; O88559; -.
DR EPD; O88559; -.
DR jPOST; O88559; -.
DR MaxQB; O88559; -.
DR PaxDb; O88559; -.
DR PeptideAtlas; O88559; -.
DR PRIDE; O88559; -.
DR ProteomicsDB; 295884; -. [O88559-1]
DR ProteomicsDB; 295885; -. [O88559-2]
DR Antibodypedia; 15626; 548 antibodies from 44 providers.
DR DNASU; 17283; -.
DR Ensembl; ENSMUST00000056391; ENSMUSP00000058149; ENSMUSG00000024947. [O88559-1]
DR Ensembl; ENSMUST00000078137; ENSMUSP00000077272; ENSMUSG00000024947. [O88559-2]
DR Ensembl; ENSMUST00000079327; ENSMUSP00000078306; ENSMUSG00000024947. [O88559-1]
DR Ensembl; ENSMUST00000113500; ENSMUSP00000109128; ENSMUSG00000024947. [O88559-1]
DR Ensembl; ENSMUST00000113504; ENSMUSP00000109132; ENSMUSG00000024947. [O88559-1]
DR GeneID; 17283; -.
DR KEGG; mmu:17283; -.
DR UCSC; uc008gib.2; mouse. [O88559-1]
DR UCSC; uc012bhl.1; mouse. [O88559-2]
DR CTD; 4221; -.
DR MGI; MGI:1316736; Men1.
DR VEuPathDB; HostDB:ENSMUSG00000024947; -.
DR eggNOG; ENOG502QUYK; Eukaryota.
DR GeneTree; ENSGT00390000014237; -.
DR HOGENOM; CLU_018646_0_0_1; -.
DR InParanoid; O88559; -.
DR OrthoDB; 799417at2759; -.
DR TreeFam; TF323888; -.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-MMU-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 17283; 19 hits in 76 CRISPR screens.
DR ChiTaRS; Men1; mouse.
DR PRO; PR:O88559; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; O88559; protein.
DR Bgee; ENSMUSG00000024947; Expressed in undifferentiated genital tubercle and 89 other tissues.
DR ExpressionAtlas; O88559; baseline and differential.
DR Genevisible; O88559; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0032154; C:cleavage furrow; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR GO; GO:0071339; C:MLL1 complex; ISO:MGI.
DR GO; GO:0044665; C:MLL1/2 complex; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000400; F:four-way junction DNA binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0000403; F:Y-form DNA binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0044346; P:fibroblast apoptotic process; IDA:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0051568; P:histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:0016571; P:histone methylation; IDA:MGI.
DR GO; GO:0001776; P:leukocyte homeostasis; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; ISO:MGI.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IDA:MGI.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISO:MGI.
DR GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISO:MGI.
DR GO; GO:0046621; P:negative regulation of organ growth; IDA:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0051974; P:negative regulation of telomerase activity; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:1904691; P:negative regulation of type B pancreatic cell proliferation; IDA:MGI.
DR GO; GO:0035265; P:organ growth; IDA:MGI.
DR GO; GO:0001503; P:ossification; IMP:MGI.
DR GO; GO:0002076; P:osteoblast development; IGI:MGI.
DR GO; GO:0002051; P:osteoblast fate commitment; IGI:MGI.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0031062; P:positive regulation of histone methylation; IMP:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IGI:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0032925; P:regulation of activin receptor signaling pathway; ISO:MGI.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0010332; P:response to gamma radiation; ISO:MGI.
DR GO; GO:0071559; P:response to transforming growth factor beta; ISO:MGI.
DR GO; GO:0009411; P:response to UV; ISO:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0048863; P:stem cell differentiation; IMP:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0003309; P:type B pancreatic cell differentiation; ISO:MGI.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; IDA:MGI.
DR CDD; cd14456; Menin; 1.
DR InterPro; IPR007747; Menin.
DR PANTHER; PTHR12693; PTHR12693; 1.
DR Pfam; PF05053; Menin; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..611
FT /note="Menin"
FT /id="PRO_0000096412"
FT REGION 214..390
FT /note="Interaction with FANCD2"
FT /evidence="ECO:0000250|UniProtKB:O00255"
FT REGION 460..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00255"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00255"
FT MOD_RES 595
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00255"
FT VAR_SEQ 396..450
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041100"
FT CONFLICT 457
FT /note="I -> M (in Ref. 2; AAC26001/AAC78843)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="E -> G (in Ref. 2; AAC26001/AAC78843)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="S -> L (in Ref. 2; AAC26001/AAC78843 and 8;
FT AAH36287)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 67501 MW; EF45DE5B5EB1B8D1 CRC64;
MGLKAAQKTL FPLRSIDDVV RLFAAELGRE EPDLVLLSLV LGFVEHFLAV NRVIPTNVPE
LTFQPSPAPD PPGGLTYFPV ADLSIIAALY ARFTAQIRGA VDLSLYPREG GVSSRELVKK
VSDVIWNSLS RSYFKDRAHI QSLFSFITGT KLDSSGVAFA VVGACQALGL RDVHLALSED
HAWVVFGPNG EQTAEVTWHG KGNEDRRGQT VNAGVAERSW LYLKGSYMRC DRKMEVAFMV
CAINPSIDLH TDSLELLQLQ QKLLWLLYDL GHLERYPMAL GNLADLEELE PTPGRPDPLT
LYHKGIASAK TYYQDEHIYP YMYLAGYHCR NRNVREALQA WADTATVIQD YNYCREDEEI
YKEFFEVAND VIPNLLKEAA SLLETGEERT GEQAQGTQGQ GSALQDPECF AHLLRFYDGI
CKWEEGSPTP VLHVGWATFL VQSLGRFEGQ VRQKVHIVSR EAEAAEAEEP WGDEAREGRR
RGPRRESKPE EPPPPKKPAL DKGPGSGQSA GSGPPRKTSG TVPGTTRGGQ EVGNAAQAPA
PAASPPPEGP VLTFQSEKMK GMKELLVATK INSSAIKLQL TAQSQVQMKK QKVSTPSDYT
LSFLKRQRKG L
