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Q7TPV4

- MBB1A_MOUSE

UniProt

Q7TPV4 - MBB1A_MOUSE

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Protein

Myb-binding protein 1A

Gene
Mybbp1a, P160
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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/CRM1.2 Publications

GO - Cellular componenti

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

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-acetyllysine By similarity
Modified residuei156 – 1561N6-acetyllysine By similarity
Modified residuei1160 – 11601Phosphoserine By similarity
Modified residuei1164 – 11641Phosphoserine By similarity
Modified residuei1187 – 11871Phosphoserine By similarity
Modified residuei1191 – 11911Phosphothreonine By similarity
Modified residuei1219 – 12191Phosphoserine By similarity
Modified residuei1244 – 12441Phosphoserine By similarity
Modified residuei1253 – 12531Phosphoserine2 Publications
Modified residuei1277 – 12771Phosphothreonine1 Publication
Modified residuei1280 – 12801Phosphoserine2 Publications
Modified residuei1303 – 13031Phosphoserine By similarity
Modified residuei1318 – 13181Phosphoserine By similarity
Modified residuei1322 – 13221Citrulline
Modified residuei1323 – 13231Phosphoserine By similarity
Modified residuei1325 – 13251Phosphoserine By similarity
Modified residuei1329 – 13291Phosphoserine By similarity

Post-translational modificationi

Citrullinated by PADI4.

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 KPNA2.4 Publications

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ7TPV4.

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

« Hide

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

Sequence conflict

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

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 104 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

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