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Q7TPV4

- MBB1A_MOUSE

UniProt

Q7TPV4 - MBB1A_MOUSE

Protein

Myb-binding protein 1A

Gene

Mybbp1a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (19 Jul 2005)
      Previous versions | rss
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    Functioni

    May activate or repress transcription via interactions with sequence specific DNA-binding proteins. Repression may be mediated at least in part by histone deacetylase activity (HDAC activity).2 Publications

    GO - Molecular functioni

    1. DNA-directed DNA polymerase activity Source: InterPro
    2. protein binding Source: UniProtKB
    3. sequence-specific DNA binding Source: Ensembl
    4. transcription factor binding Source: UniProtKB
    5. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to glucose starvation Source: Ensembl
    2. intrinsic apoptotic signaling pathway by p53 class mediator Source: Ensembl
    3. negative regulation of transcription, DNA-templated Source: MGI
    4. nucleocytoplasmic transport Source: UniProtKB
    5. positive regulation of cell cycle arrest Source: Ensembl
    6. respiratory electron transport chain Source: MGI
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myb-binding protein 1A
    Alternative name(s):
    Myb-binding protein of 160 kDa
    Gene namesi
    Name:Mybbp1a
    Synonyms:P160
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:106181. Mybbp1a.

    Subcellular locationi

    Nucleusnucleolus. Cytoplasm
    Note: Predominantly nucleolar. Also shuttles between the nucleus and cytoplasm. Nuclear import may be mediated by KPNA2, while export appears to depend partially on XPO1/CRM1.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. NLS-dependent protein nuclear import complex Source: UniProtKB
    3. nucleolus Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi249 – 2491L → A: Reduced nuclear export; when associated with A-251. 1 Publication
    Mutagenesisi251 – 2511V → A: Reduced nuclear export; when associated with A-249. 1 Publication
    Mutagenesisi272 – 2721L → A: Reduced nuclear export; when associated with A-274. 1 Publication
    Mutagenesisi274 – 2741L → A: Reduced nuclear export; when associated with A-272. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 13441343Myb-binding protein 1APRO_0000096256Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei69 – 691N6-acetyllysineBy similarity
    Modified residuei156 – 1561N6-acetyllysineBy similarity
    Modified residuei1160 – 11601PhosphoserineBy similarity
    Modified residuei1164 – 11641PhosphoserineBy similarity
    Modified residuei1187 – 11871PhosphoserineBy similarity
    Modified residuei1191 – 11911PhosphothreonineBy similarity
    Modified residuei1219 – 12191PhosphoserineBy similarity
    Modified residuei1244 – 12441PhosphoserineBy similarity
    Modified residuei1253 – 12531Phosphoserine2 Publications
    Modified residuei1277 – 12771Phosphothreonine1 Publication
    Modified residuei1280 – 12801Phosphoserine2 Publications
    Modified residuei1303 – 13031PhosphoserineBy similarity
    Modified residuei1318 – 13181PhosphoserineBy similarity
    Modified residuei1322 – 13221Citrulline1 Publication
    Modified residuei1323 – 13231PhosphoserineBy similarity
    Modified residuei1325 – 13251PhosphoserineBy similarity
    Modified residuei1329 – 13291PhosphoserineBy similarity

    Post-translational modificationi

    Citrullinated by PADI4.1 Publication

    Keywords - PTMi

    Acetylation, Citrullination, Phosphoprotein

    Proteomic databases

    MaxQBiQ7TPV4.
    PaxDbiQ7TPV4.
    PRIDEiQ7TPV4.

    PTM databases

    PhosphoSiteiQ7TPV4.

    Miscellaneous databases

    PMAP-CutDBQ7TPV4.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ7TPV4.
    BgeeiQ7TPV4.
    CleanExiMM_MYBBP1A.
    GenevestigatoriQ7TPV4.

    Interactioni

    Subunit structurei

    Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 By similarity. Binds to and represses JUN and MYB via the leucine zipper regions present in these proteins. Also binds to and represses PPARGC1A: this interaction is abrogated when PPARGC1A is phosphorylated by MAPK1/ERK. Binds to and stimulates transcription by AHR. Binds to KPNA2.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi201999. 22 interactions.
    DIPiDIP-39831N.
    IntActiQ7TPV4. 12 interactions.
    MINTiMINT-1868464.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7TPV4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 580579Interaction with MYBAdd
    BLAST
    Regioni1152 – 1344193Required for nuclear and nucleolar localizationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi238 – 25619Nuclear export signal 1Add
    BLAST
    Motifi261 – 27919Nuclear export signal 2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi698 – 75255Asp-richAdd
    BLAST

    Phylogenomic databases

    eggNOGiNOG313877.
    GeneTreeiENSGT00390000017457.
    HOGENOMiHOG000113488.
    HOVERGENiHBG081961.
    InParanoidiQ7TPV4.
    KOiK02331.
    OMAiHQAQACL.
    OrthoDBiEOG7G7KPN.
    PhylomeDBiQ7TPV4.
    TreeFamiTF317401.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR007015. DNA_pol_V.
    [Graphical view]
    PANTHERiPTHR13213. PTHR13213. 1 hit.
    PfamiPF04931. DNA_pol_phi. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 3 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q7TPV4-1 [UniParc]FASTAAdd to Basket

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    MAEMKSPTKA EPATPAEAAQ SDRHSLLEHS REFLDFFWDI AKPDQETRLR     50
    ATEKLLEYLR TRPNDSEMKY ALKRLITGLG VGREAARPCY SLALAQLLQS 100
    FEDIPLCDIL DQIQEKYSLQ AMNKAMMRPS LFANLFGVLA LFQSGRLVKD 150
    KEALMKSVQL LKILSQHPNH LQGQPIKALV DILSEVPESM FQEILPKVLK 200
    GNMKVILRSP KYLELFLLAK QRVPTKLESL MGSVDLFSED NIPSLVNILK 250
    VAANSVKKEH KLPNVALDLL RLALKESRFE LFWKKVLEEG LLKNPSWTSS 300
    YMCFRLLGAS LPLLSEEQLQ LVMRGDLIRH FGENMVISKP QNLFKIIPEI 350
    STYVGTFLEG CQDDPKRQLT MMVAFTTITN QGLPVMPTFW RVTRFLNAEA 400
    LQSYVAWLRD MFLQPDLNSL VDFSTANQKR AQDASLNVPE RAVFRLRKWI 450
    IHRLVSLVDH LHLEKDEAVV EQIARFCLFH AFFKTKKATP QIPETKQHFS 500
    FPLDDRNRGV FVSAFFSLLQ TLSVKFRQTP DLAENGKPWT YRLVQLADML 550
    LNHNRNVTSV TSLTTQQRQA WDQMMSTLKE LEARSSETRA IAFQHLLLLV 600
    GLHIFKSPAE SCDVLGDIQT CIKKSMEQNP RRSRSRAKAS QEPVWVEVMV 650
    EILLSLLAQP SNLMRQVVRS VFGHICPHLT PRCLQLILAV LSPVTNEDED 700
    DNVVVTDDAD EKQLQHGEDE DSDNEDNKNS ESDMDSEDGE ESEEEDRDKD 750
    VDPGFRQQLM EVLKAGNALG GVDNEEEEEL GDEAMMALDQ NLASLFKEQK 800
    MRIQARNEEK NKLQKEKKLR RDFQIRALDL IEVLVTKQPE HPLILELLEP 850
    LLNVIQHSMR SKGSTKQEQD LLHKTARIFM HHLCRARRYC HEVGPCAEAL 900
    HAQVERLVQQ AGSQADASVA LYYFNASLYL LRVLKGNTNK RHQDGHKLHG 950
    ADTEDSEDQA ANCLDLDFVT RVYSASLESL LTKRNSSLTV PMFLSLFSRY 1000
    PVICKNLLPV LAQHVAGPSR PRHQAQACLM LQKTLSAREL RVCFEDPEWE 1050
    QLITQLLGKA TQTLQTLGEA QSKGEHQKEL SILELLNTLL RTVNHEKLSV 1100
    DLTAPLGVLQ SKQQKLQQSL QQGNHSSGSN RLYDLYWQAM RMLGVQRPKS 1150
    EKKNAKDIPS DTQSPVSTKR KKKGFLPETK KRKKLKSEGT TPEKNAASQQ 1200
    DAVTEGAMPA ATGKDQPPST GKKKRKRVKA STPSQVNGIT GAKSPAPSNP 1250
    TLSPSTPAKT PKLQKKKEKL SQVNGATPVS PIEPESKKHH QEALSTKEVI 1300
    RKSPHPQSAL PKKRARLSLV SRSPSLLQSG VKKRRVASRR VQTP 1344
    Length:1,344
    Mass (Da):152,037
    Last modified:July 19, 2005 - v2
    Checksum:i64D3420981CD0767
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti87 – 871R → T in AAC39954. (PubMed:9447996)Curated
    Sequence conflicti87 – 871R → T in AAL83748. 1 PublicationCurated
    Sequence conflicti88 – 881P → A in AAC39954. (PubMed:9447996)Curated
    Sequence conflicti505 – 5084DRNR → HASG in AAH04078. (PubMed:15489334)Curated
    Sequence conflicti1282 – 12821I → V in AAH52889. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U63648 mRNA. Translation: AAC39954.1.
    AF345640 Genomic DNA. Translation: AAL83748.1.
    AL662812 Genomic DNA. Translation: CAI52004.1.
    BC004078 mRNA. Translation: AAH04078.1.
    BC048858 mRNA. Translation: AAH48858.1.
    BC052889 mRNA. Translation: AAH52889.1.
    CCDSiCCDS24986.1.
    PIRiT34188.
    RefSeqiNP_058056.2. NM_016776.2.
    UniGeneiMm.147946.

    Genome annotation databases

    EnsembliENSMUST00000045633; ENSMUSP00000044827; ENSMUSG00000040463.
    GeneIDi18432.
    KEGGimmu:18432.
    UCSCiuc007jyy.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U63648 mRNA. Translation: AAC39954.1 .
    AF345640 Genomic DNA. Translation: AAL83748.1 .
    AL662812 Genomic DNA. Translation: CAI52004.1 .
    BC004078 mRNA. Translation: AAH04078.1 .
    BC048858 mRNA. Translation: AAH48858.1 .
    BC052889 mRNA. Translation: AAH52889.1 .
    CCDSi CCDS24986.1.
    PIRi T34188.
    RefSeqi NP_058056.2. NM_016776.2.
    UniGenei Mm.147946.

    3D structure databases

    ProteinModelPortali Q7TPV4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201999. 22 interactions.
    DIPi DIP-39831N.
    IntActi Q7TPV4. 12 interactions.
    MINTi MINT-1868464.

    PTM databases

    PhosphoSitei Q7TPV4.

    Proteomic databases

    MaxQBi Q7TPV4.
    PaxDbi Q7TPV4.
    PRIDEi Q7TPV4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000045633 ; ENSMUSP00000044827 ; ENSMUSG00000040463 .
    GeneIDi 18432.
    KEGGi mmu:18432.
    UCSCi uc007jyy.1. mouse.

    Organism-specific databases

    CTDi 10514.
    MGIi MGI:106181. Mybbp1a.

    Phylogenomic databases

    eggNOGi NOG313877.
    GeneTreei ENSGT00390000017457.
    HOGENOMi HOG000113488.
    HOVERGENi HBG081961.
    InParanoidi Q7TPV4.
    KOi K02331.
    OMAi HQAQACL.
    OrthoDBi EOG7G7KPN.
    PhylomeDBi Q7TPV4.
    TreeFami TF317401.

    Miscellaneous databases

    ChiTaRSi MYBBP1A. mouse.
    NextBioi 294102.
    PMAP-CutDB Q7TPV4.
    PROi Q7TPV4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7TPV4.
    Bgeei Q7TPV4.
    CleanExi MM_MYBBP1A.
    Genevestigatori Q7TPV4.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR007015. DNA_pol_V.
    [Graphical view ]
    PANTHERi PTHR13213. PTHR13213. 1 hit.
    Pfami PF04931. DNA_pol_phi. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 3 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning reveals that the p160 Myb-binding protein is a novel, predominantly nucleolar protein which may play a role in transactivation by Myb."
      Tavner F.J., Simpson R., Tashiro S., Favier D., Jenkins N.A., Gilbert D.J., Copeland N.G., Macmillan E.M., Lutwyche J., Keough R.A., Ishii S., Gonda T.J.
      Mol. Cell. Biol. 18:989-1002(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-53; 205-211; 286-290; 458-465 AND 488-496, INTERACTION WITH JUN AND MYB, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "Structural organization of the murine myb-binding protein p160 (Mybbp1a) gene."
      Keough R.A., Gonda T.J.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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].
      Strain: C3H/He.
      Tissue: Eye, Mammary gland and Osteoblast.
    5. "Myb-binding protein 1a augments AhR-dependent gene expression."
      Jones L.C., Okino S.T., Gonda T.J., Whitlock J.P. Jr.
      J. Biol. Chem. 277:22515-22519(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH AHR.
    6. "Myb-binding protein 1a is a nucleocytoplasmic shuttling protein that utilizes CRM1-dependent and independent nuclear export pathways."
      Keough R.A., Macmillan E.M., Lutwyche J.K., Gardner J.M., Tavner F.J., Jans D.A., Henderson B.R., Gonda T.J.
      Exp. Cell Res. 289:108-123(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KPNA2, MUTAGENESIS OF LEU-249; VAL-251; LEU-272 AND LEU-274, DOMAINS NES AND NLS.
    7. "Suppression of mitochondrial respiration through recruitment of p160 myb binding protein to PGC-1alpha: modulation by p38 MAPK."
      Fan M., Rhee J., St Pierre J., Handschin C., Puigserver P., Lin J., Jaeger S., Erdjument-Bromage H., Tempst P., Spiegelman B.M.
      Genes Dev. 18:278-289(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PPARGC1A.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    9. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1277 AND SER-1280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1253 AND SER-1280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    13. Cited for: CITRULLINATION AT ARG-1322.

    Entry informationi

    Entry nameiMBB1A_MOUSE
    AccessioniPrimary (citable) accession number: Q7TPV4
    Secondary accession number(s): O35851
    , Q80Y66, Q8R4X2, Q99KP0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 105 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, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3