MEN1_BOVIN
ID MEN1_BOVIN Reviewed; 610 AA.
AC Q0P5I0;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Menin;
GN Name=MEN1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential component of a MLL/SET1 histone methyltransferase
CC (HMT) complex, a complex that specifically methylates 'Lys-4' of
CC histone H3 (H3K4). Functions as a transcriptional regulator. Binds to
CC the TERT promoter and represses telomerase expression. Plays a role in
CC TGFB1-mediated inhibition of cell-proliferation, possibly regulating
CC SMAD3 transcriptional activity. Represses JUND-mediated transcriptional
CC activation on AP1 sites, as well as that mediated by NFKB subunit RELA.
CC Positively regulates HOXC8 and HOXC6 gene expression. May be involved
CC in normal hematopoiesis through the activation of HOXA9 expression. May
CC be involved in DNA repair (By similarity).
CC {ECO:0000250|UniProtKB:O00255, ECO:0000250|UniProtKB:O88559}.
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 (By
CC similarity). Interacts with KMT2A (via MBM motif) (By similarity). The
CC KMT2A-MEN1 complex interacts with PSIP1 with a greater affinity as MEN1
CC enhances interaction of KMT2A with PSIP1 (By similarity).
CC {ECO:0000250|UniProtKB:O00255}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00255}.
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DR EMBL; BC120005; AAI20006.1; -; mRNA.
DR RefSeq; NP_001069629.1; NM_001076161.2.
DR RefSeq; XP_005227211.1; XM_005227154.3.
DR RefSeq; XP_005227212.1; XM_005227155.3.
DR AlphaFoldDB; Q0P5I0; -.
DR SMR; Q0P5I0; -.
DR STRING; 9913.ENSBTAP00000002705; -.
DR PaxDb; Q0P5I0; -.
DR PRIDE; Q0P5I0; -.
DR Ensembl; ENSBTAT00000002705; ENSBTAP00000002705; ENSBTAG00000002095.
DR Ensembl; ENSBTAT00000068428; ENSBTAP00000066214; ENSBTAG00000002095.
DR GeneID; 539431; -.
DR KEGG; bta:539431; -.
DR CTD; 4221; -.
DR VEuPathDB; HostDB:ENSBTAG00000002095; -.
DR VGNC; VGNC:31385; MEN1.
DR eggNOG; ENOG502QUYK; Eukaryota.
DR GeneTree; ENSGT00390000014237; -.
DR HOGENOM; CLU_018646_0_0_1; -.
DR InParanoid; Q0P5I0; -.
DR OMA; GVNERSW; -.
DR OrthoDB; 799417at2759; -.
DR TreeFam; TF323888; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000002095; Expressed in retina and 105 other tissues.
DR ExpressionAtlas; Q0P5I0; baseline and differential.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0035097; C:histone methyltransferase complex; IBA:GO_Central.
DR GO; GO:0071339; C:MLL1 complex; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR GO; GO:0017053; C:transcription repressor complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0000400; F:four-way junction DNA binding; IEA:Ensembl.
DR GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0070412; F:R-SMAD binding; IEA:Ensembl.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0000403; F:Y-form DNA binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0045786; P:negative regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0051974; P:negative regulation of telomerase activity; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0009411; P:response to UV; IEA:Ensembl.
DR CDD; cd14456; Menin; 1.
DR InterPro; IPR007747; Menin.
DR PANTHER; PTHR12693; PTHR12693; 1.
DR Pfam; PF05053; Menin; 2.
PE 2: Evidence at transcript level;
KW Chromatin regulator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..610
FT /note="Menin"
FT /id="PRO_0000408471"
FT REGION 214..390
FT /note="Interaction with FANCD2"
FT /evidence="ECO:0000250|UniProtKB:O00255"
FT REGION 385..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..552
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 MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00255"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00255"
FT MOD_RES 594
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00255"
SQ SEQUENCE 610 AA; 67384 MW; A64C9CE51D0377B3 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 TYYRDEHIYP YMYLAGYHCR NRNVREALQA WADTATVIQD YNYCREDEEI
YKEFFEVAND VIPNLLKEAA SLLEAGEERP GEQTQGTQSQ GSALQDPECF AHLLRFYDGI
CKWEEGSPTP VLHVGWATFL VQSLGRFEGQ VRQKVRIVSR EAEAAEAEEP WGEEAREGRR
RGPRRESKPE EPPPPKKPAL DKGPGAGQGA VPGPPRKPPG TVPGTARGAE GGSAAPVPAP
AASPPPEGPV LTFQSEKMKG MKELLVATKI NSSAIKLQLT AQSQVQMKKQ KVSTPSDYTL
SFLKRQRKGL
