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Protein

Menin

Gene

Men1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). May be involved in normal hematopoiesis through the activation of HOXA9 expression. May be involved in DNA repair.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • cell cycle arrest Source: MGI
  • cellular response to DNA damage stimulus Source: MGI
  • chromatin remodeling Source: MGI
  • embryonic skeletal system morphogenesis Source: MGI
  • hemopoiesis Source: MGI
  • histone lysine methylation Source: MGI
  • histone methylation Source: MGI
  • leukocyte homeostasis Source: MGI
  • MAPK cascade Source: MGI
  • maternal process involved in female pregnancy Source: MGI
  • negative regulation of cell cycle Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: MGI
  • negative regulation of JNK cascade Source: MGI
  • negative regulation of organ growth Source: MGI
  • negative regulation of osteoblast differentiation Source: MGI
  • negative regulation of protein phosphorylation Source: MGI
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  • negative regulation of telomerase activity Source: MGI
  • negative regulation of transcription, DNA-templated Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • ossification Source: MGI
  • osteoblast development Source: MGI
  • osteoblast fate commitment Source: MGI
  • palate development Source: MGI
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of cell differentiation Source: MGI
  • positive regulation of cell division Source: MGI
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of histone methylation Source: MGI
  • positive regulation of osteoblast differentiation Source: MGI
  • positive regulation of protein binding Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of transforming growth factor beta receptor signaling pathway Source: MGI
  • regulation of gene expression Source: MGI
  • response to gamma radiation Source: MGI
  • response to UV Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-201722. Formation of the beta-catenin:TCF transactivating complex.
R-MMU-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-MMU-3769402. Deactivation of the beta-catenin transactivating complex.
R-MMU-5626467. RHO GTPases activate IQGAPs.

Names & Taxonomyi

Protein namesi
Recommended name:
Menin
Gene namesi
Name:Men1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1316736. Men1.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: MGI
  • cleavage furrow Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • histone methyltransferase complex Source: MGI
  • nuclear chromatin Source: MGI
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear matrix Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Homozygous mice die in utero at 11.5-12.5 dpc. At 9 months of age, heterozygous mice develop pancreatic islet lesions, from hyperplasia to insulin-producing islet cell tumors, and frequently parathyroid adenomas. Larger, more numerous tumors involving pancreatic islets, parathyroids, thyroid, adrenal cortex and pituitary are seen by 16 months. All tumors show loss of the wild-type allele.1 Publication

Chemistry

ChEMBLiCHEMBL3124739.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 611611MeninPRO_0000096412Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei487 – 4871PhosphoserineBy similarity
Modified residuei544 – 5441PhosphoserineBy similarity
Modified residuei595 – 5951PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO88559.
MaxQBiO88559.
PaxDbiO88559.
PRIDEiO88559.

PTM databases

iPTMnetiO88559.
PhosphoSiteiO88559.

Expressioni

Tissue specificityi

Widely expressed, with high levels in hippocampus, cerebral cortex, testis and thymus (at protein level). Also expressed at high levels in pancreatic islets, ovary and bone marrow. In the brain, highest expression in hippocampus pyramidal nerve cells (at protein level). In the testis, may be expressed in spermatogonia (at protein level). Low expression, if any, in skeletal muscle.3 Publications

Developmental stagei

First detected at 7 dpc. At 13.5 dpc, expressed throughout the embryo, including forelimb, gut, head, heart and lung. At 17 dpc, expression becomes more restricted, with high levels mainly in the thymus, skeletal muscle, brain and spinal cord.2 Publications

Gene expression databases

BgeeiO88559.
CleanExiMM_MEN1.
ExpressionAtlasiO88559. baseline and differential.
GenevisibleiO88559. MM.

Interactioni

Subunit structurei

Component of the MLL-HCF complex, at least composed of KMT2A/MLL1, MEN1, ASH2L, RBBP5, DPY30, WDR5, HCFC1 and HCFC2 (By similarity). Component of the menin-associated histone methyltransferase complex, at least composed of KMT2B/MLL4, MEN1, ASH2L, RBBP5, DPY30 and WDR5 (By similarity). Interacts with POLR2B (By similarity). Interacts with POLR2A phosphorylated at 'Ser-5', but not with the unphosphorylated, nor 'Ser-2' phosphorylated POLR2A forms (By similarity). Interacts with FANCD2 and DBF4 (By similarity). Interacts with SMAD3, but not with SMAD2, nor SMAD4 (By similarity). Directly interacts with NFKB1, NFKB2 and RELA (By similarity). Interacts with JUND.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Nr1h3Q9Z0Y93EBI-3990176,EBI-5276764
PparaP232042EBI-3990176,EBI-5273083

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201393. 8 interactions.
IntActiO88559. 6 interactions.
MINTiMINT-8212015.
STRINGi10090.ENSMUSP00000109130.

Structurei

3D structure databases

ProteinModelPortaliO88559.
SMRiO88559. Positions 2-459, 516-609.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni214 – 390177Interaction with FANCD2By similarityAdd
BLAST

Phylogenomic databases

eggNOGiENOG410IF2R. Eukaryota.
ENOG410ZNZF. LUCA.
GeneTreeiENSGT00390000014237.
HOGENOMiHOG000007225.
HOVERGENiHBG000208.
InParanoidiO88559.
KOiK14970.
OrthoDBiEOG7QC7WH.
TreeFamiTF323888.

Family and domain databases

InterProiIPR007747. Menin.
[Graphical view]
PANTHERiPTHR12693. PTHR12693. 1 hit.
PfamiPF05053. Menin. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O88559-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGLKAAQKTL FPLRSIDDVV RLFAAELGRE EPDLVLLSLV LGFVEHFLAV
60 70 80 90 100
NRVIPTNVPE LTFQPSPAPD PPGGLTYFPV ADLSIIAALY ARFTAQIRGA
110 120 130 140 150
VDLSLYPREG GVSSRELVKK VSDVIWNSLS RSYFKDRAHI QSLFSFITGT
160 170 180 190 200
KLDSSGVAFA VVGACQALGL RDVHLALSED HAWVVFGPNG EQTAEVTWHG
210 220 230 240 250
KGNEDRRGQT VNAGVAERSW LYLKGSYMRC DRKMEVAFMV CAINPSIDLH
260 270 280 290 300
TDSLELLQLQ QKLLWLLYDL GHLERYPMAL GNLADLEELE PTPGRPDPLT
310 320 330 340 350
LYHKGIASAK TYYQDEHIYP YMYLAGYHCR NRNVREALQA WADTATVIQD
360 370 380 390 400
YNYCREDEEI YKEFFEVAND VIPNLLKEAA SLLETGEERT GEQAQGTQGQ
410 420 430 440 450
GSALQDPECF AHLLRFYDGI CKWEEGSPTP VLHVGWATFL VQSLGRFEGQ
460 470 480 490 500
VRQKVHIVSR EAEAAEAEEP WGDEAREGRR RGPRRESKPE EPPPPKKPAL
510 520 530 540 550
DKGPGSGQSA GSGPPRKTSG TVPGTTRGGQ EVGNAAQAPA PAASPPPEGP
560 570 580 590 600
VLTFQSEKMK GMKELLVATK INSSAIKLQL TAQSQVQMKK QKVSTPSDYT
610
LSFLKRQRKG L
Length:611
Mass (Da):67,501
Last modified:May 31, 2011 - v2
Checksum:iEF45DE5B5EB1B8D1
GO
Isoform 2 (identifier: O88559-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     396-450: Missing.

Note: No experimental confirmation available.
Show »
Length:556
Mass (Da):61,453
Checksum:iBE74BD285110C63E
GO

Sequence cautioni

The sequence BAE32542.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti457 – 4571I → M in AAC26001 (PubMed:10524203).Curated
Sequence conflicti457 – 4571I → M in AAC78843 (PubMed:10524203).Curated
Sequence conflicti466 – 4661E → G in AAC26001 (PubMed:10524203).Curated
Sequence conflicti466 – 4661E → G in AAC78843 (PubMed:10524203).Curated
Sequence conflicti512 – 5121S → L in AAC26001 (PubMed:10524203).Curated
Sequence conflicti512 – 5121S → L in AAC78843 (PubMed:10524203).Curated
Sequence conflicti512 – 5121S → L in AAH36287 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei396 – 45055Missing in isoform 2. 1 PublicationVSP_041100Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF016398 mRNA. Translation: AAC79938.1.
AF024513 Genomic DNA. Translation: AAC79939.1.
AF130368 mRNA. Translation: AAF01352.1.
AF072755 mRNA. Translation: AAC26001.1.
AF093756 Genomic DNA. Translation: AAC78843.1.
AF109389 mRNA. Translation: AAD37498.1.
AF109390 Genomic DNA. Translation: AAD38333.1.
AB023401 mRNA. Translation: BAA74964.1.
AK154371 mRNA. Translation: BAE32542.1. Different initiation.
AK170713 mRNA. Translation: BAE41971.1.
CH466612 Genomic DNA. Translation: EDL33234.1.
CH466612 Genomic DNA. Translation: EDL33236.1.
BC036287 mRNA. Translation: AAH36287.1.
CCDSiCCDS29502.1. [O88559-1]
CCDS50367.1. [O88559-2]
RefSeqiNP_001161960.1. NM_001168488.1.
NP_001161961.1. NM_001168489.1. [O88559-1]
NP_001161962.1. NM_001168490.1. [O88559-2]
NP_032609.1. NM_008583.2. [O88559-1]
UniGeneiMm.12917.

Genome annotation databases

EnsembliENSMUST00000056391; ENSMUSP00000058149; ENSMUSG00000024947. [O88559-1]
ENSMUST00000078137; ENSMUSP00000077272; ENSMUSG00000024947. [O88559-2]
ENSMUST00000079327; ENSMUSP00000078306; ENSMUSG00000024947. [O88559-1]
ENSMUST00000113500; ENSMUSP00000109128; ENSMUSG00000024947. [O88559-1]
ENSMUST00000113504; ENSMUSP00000109132; ENSMUSG00000024947. [O88559-1]
ENSMUST00000201284; ENSMUSP00000144549; ENSMUSG00000106695. [O88559-1]
ENSMUST00000202062; ENSMUSP00000143849; ENSMUSG00000106695. [O88559-2]
ENSMUST00000202424; ENSMUSP00000144028; ENSMUSG00000106695. [O88559-1]
ENSMUST00000202550; ENSMUSP00000144083; ENSMUSG00000106695. [O88559-1]
ENSMUST00000202978; ENSMUSP00000143830; ENSMUSG00000106695. [O88559-1]
GeneIDi17283.
KEGGimmu:17283.
UCSCiuc008gib.2. mouse. [O88559-1]
uc012bhl.1. mouse. [O88559-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF016398 mRNA. Translation: AAC79938.1.
AF024513 Genomic DNA. Translation: AAC79939.1.
AF130368 mRNA. Translation: AAF01352.1.
AF072755 mRNA. Translation: AAC26001.1.
AF093756 Genomic DNA. Translation: AAC78843.1.
AF109389 mRNA. Translation: AAD37498.1.
AF109390 Genomic DNA. Translation: AAD38333.1.
AB023401 mRNA. Translation: BAA74964.1.
AK154371 mRNA. Translation: BAE32542.1. Different initiation.
AK170713 mRNA. Translation: BAE41971.1.
CH466612 Genomic DNA. Translation: EDL33234.1.
CH466612 Genomic DNA. Translation: EDL33236.1.
BC036287 mRNA. Translation: AAH36287.1.
CCDSiCCDS29502.1. [O88559-1]
CCDS50367.1. [O88559-2]
RefSeqiNP_001161960.1. NM_001168488.1.
NP_001161961.1. NM_001168489.1. [O88559-1]
NP_001161962.1. NM_001168490.1. [O88559-2]
NP_032609.1. NM_008583.2. [O88559-1]
UniGeneiMm.12917.

3D structure databases

ProteinModelPortaliO88559.
SMRiO88559. Positions 2-459, 516-609.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201393. 8 interactions.
IntActiO88559. 6 interactions.
MINTiMINT-8212015.
STRINGi10090.ENSMUSP00000109130.

Chemistry

ChEMBLiCHEMBL3124739.

PTM databases

iPTMnetiO88559.
PhosphoSiteiO88559.

Proteomic databases

EPDiO88559.
MaxQBiO88559.
PaxDbiO88559.
PRIDEiO88559.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056391; ENSMUSP00000058149; ENSMUSG00000024947. [O88559-1]
ENSMUST00000078137; ENSMUSP00000077272; ENSMUSG00000024947. [O88559-2]
ENSMUST00000079327; ENSMUSP00000078306; ENSMUSG00000024947. [O88559-1]
ENSMUST00000113500; ENSMUSP00000109128; ENSMUSG00000024947. [O88559-1]
ENSMUST00000113504; ENSMUSP00000109132; ENSMUSG00000024947. [O88559-1]
ENSMUST00000201284; ENSMUSP00000144549; ENSMUSG00000106695. [O88559-1]
ENSMUST00000202062; ENSMUSP00000143849; ENSMUSG00000106695. [O88559-2]
ENSMUST00000202424; ENSMUSP00000144028; ENSMUSG00000106695. [O88559-1]
ENSMUST00000202550; ENSMUSP00000144083; ENSMUSG00000106695. [O88559-1]
ENSMUST00000202978; ENSMUSP00000143830; ENSMUSG00000106695. [O88559-1]
GeneIDi17283.
KEGGimmu:17283.
UCSCiuc008gib.2. mouse. [O88559-1]
uc012bhl.1. mouse. [O88559-2]

Organism-specific databases

CTDi4221.
MGIiMGI:1316736. Men1.

Phylogenomic databases

eggNOGiENOG410IF2R. Eukaryota.
ENOG410ZNZF. LUCA.
GeneTreeiENSGT00390000014237.
HOGENOMiHOG000007225.
HOVERGENiHBG000208.
InParanoidiO88559.
KOiK14970.
OrthoDBiEOG7QC7WH.
TreeFamiTF323888.

Enzyme and pathway databases

ReactomeiR-MMU-201722. Formation of the beta-catenin:TCF transactivating complex.
R-MMU-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-MMU-3769402. Deactivation of the beta-catenin transactivating complex.
R-MMU-5626467. RHO GTPases activate IQGAPs.

Miscellaneous databases

ChiTaRSiMen1. mouse.
NextBioi291788.
PROiO88559.
SOURCEiSearch...

Gene expression databases

BgeeiO88559.
CleanExiMM_MEN1.
ExpressionAtlasiO88559. baseline and differential.
GenevisibleiO88559. MM.

Family and domain databases

InterProiIPR007747. Menin.
[Graphical view]
PANTHERiPTHR12693. PTHR12693. 1 hit.
PfamiPF05053. Menin. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "Primary structure, gene expression and chromosomal mapping of rodent homologs of the MEN1 tumor suppressor gene."
    Karges W., Maier S., Wissmann A., Dralle H., Dosch H.M., Boehm B.O.
    Biochim. Biophys. Acta 1446:286-294(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Strain: BALB/c X CBA.
  3. "Studies of the murine homolog of the multiple endocrine neoplasia type 1 (MEN1) gene, men1."
    Bassett J.H.D., Rashbass P., Harding B., Forbes S.A., Pannett A.A., Thakker R.V.
    J. Bone Miner. Res. 14:3-10(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    Strain: 129/Ola.
  4. "Isolation, genomic organization, and expression analysis of Men1, the murine homolog of the MEN1 gene."
    Guru S.C., Crabtree J.S., Brown K.D., Dunn K.J., Manickam P., Prasad N.B., Wangsa D., Burns A.L., Spiegel A.M., Marx S.J., Pavan W.J., Collins F.S., Chandrasekharappa S.C.
    Mamm. Genome 10:592-596(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: 129/Sv.
  5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: ICR.
    Tissue: Brain.
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: NOD.
    Tissue: Dendritic cell.
  7. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: FVB/N.
    Tissue: Salivary gland.
  9. "Menin interacts with the AP1 transcription factor JunD and represses JunD-activated transcription."
    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.
    Cell 96:143-152(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH JUND.
  10. Cited for: DISRUPTION PHENOTYPE.
  11. "The tumor suppressor menin regulates hematopoiesis and myeloid transformation by influencing Hox gene expression."
    Chen Y.X., Yan J., Keeshan K., Tubbs A.T., Wang H., Silva A., Brown E.J., Hess J.L., Pear W.S., Hua X.
    Proc. Natl. Acad. Sci. U.S.A. 103:1018-1023(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMEN1_MOUSE
AccessioniPrimary (citable) accession number: O88559
Secondary accession number(s): Q3U491, Q8CI72, Q91UZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 31, 2011
Last modified: May 11, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.