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Q7TPV4 (MBB1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myb-binding protein 1A
Alternative name(s):
Myb-binding protein of 160 kDa
Gene names
Name:Mybbp1a
Synonyms:P160
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1344 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.5 Ref.7

Subunit structure

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. Ref.1 Ref.5 Ref.6 Ref.7

Subcellular location

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. Ref.1 Ref.6

Tissue specificity

Ubiquitously expressed. Ref.1

Post-translational modification

Citrullinated by PADI4.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Molecular functionActivator
Repressor
   PTMAcetylation
Citrullination
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to glucose starvation

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.7. Source: MGI

nucleocytoplasmic transport

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

respiratory electron transport chain

Inferred from direct assay Ref.7. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNLS-dependent protein nuclear import complex

Inferred from direct assay Ref.6. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.6. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.6. Source: UniProtKB

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionDNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

transcription factor binding

Traceable author statement Ref.6. Source: UniProtKB

zinc ion binding

Traceable author statement PubMed 10644447. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 13441343Myb-binding protein 1A
PRO_0000096256

Regions

Region2 – 580579Interaction with MYB
Region1152 – 1344193Required for nuclear and nucleolar localization
Motif238 – 25619Nuclear export signal 1
Motif261 – 27919Nuclear export signal 2
Compositional bias698 – 75255Asp-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.12
Modified residue691N6-acetyllysine By similarity
Modified residue1561N6-acetyllysine By similarity
Modified residue11601Phosphoserine By similarity
Modified residue11641Phosphoserine By similarity
Modified residue11871Phosphoserine By similarity
Modified residue11911Phosphothreonine By similarity
Modified residue12191Phosphoserine By similarity
Modified residue12441Phosphoserine By similarity
Modified residue12531Phosphoserine Ref.11 Ref.12
Modified residue12771Phosphothreonine Ref.10
Modified residue12801Phosphoserine Ref.10 Ref.11
Modified residue13031Phosphoserine By similarity
Modified residue13181Phosphoserine By similarity
Modified residue13221Citrulline
Modified residue13231Phosphoserine By similarity
Modified residue13251Phosphoserine By similarity
Modified residue13291Phosphoserine By similarity

Experimental info

Mutagenesis2491L → A: Reduced nuclear export; when associated with A-251. Ref.6
Mutagenesis2511V → A: Reduced nuclear export; when associated with A-249. Ref.6
Mutagenesis2721L → A: Reduced nuclear export; when associated with A-274. Ref.6
Mutagenesis2741L → A: Reduced nuclear export; when associated with A-272. Ref.6
Sequence conflict871R → T in AAC39954. Ref.1
Sequence conflict871R → T in AAL83748. Ref.2
Sequence conflict881P → A in AAC39954. Ref.1
Sequence conflict505 – 5084DRNR → HASG in AAH04078. Ref.4
Sequence conflict12821I → V in AAH52889. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q7TPV4 [UniParc].

Last modified July 19, 2005. Version 2.
Checksum: 64D3420981CD0767

FASTA1,344152,037
        10         20         30         40         50         60 
MAEMKSPTKA EPATPAEAAQ SDRHSLLEHS REFLDFFWDI AKPDQETRLR ATEKLLEYLR 

        70         80         90        100        110        120 
TRPNDSEMKY ALKRLITGLG VGREAARPCY SLALAQLLQS FEDIPLCDIL DQIQEKYSLQ 

       130        140        150        160        170        180 
AMNKAMMRPS LFANLFGVLA LFQSGRLVKD KEALMKSVQL LKILSQHPNH LQGQPIKALV 

       190        200        210        220        230        240 
DILSEVPESM FQEILPKVLK GNMKVILRSP KYLELFLLAK QRVPTKLESL MGSVDLFSED 

       250        260        270        280        290        300 
NIPSLVNILK VAANSVKKEH KLPNVALDLL RLALKESRFE LFWKKVLEEG LLKNPSWTSS 

       310        320        330        340        350        360 
YMCFRLLGAS LPLLSEEQLQ LVMRGDLIRH FGENMVISKP QNLFKIIPEI STYVGTFLEG 

       370        380        390        400        410        420 
CQDDPKRQLT MMVAFTTITN QGLPVMPTFW RVTRFLNAEA LQSYVAWLRD MFLQPDLNSL 

       430        440        450        460        470        480 
VDFSTANQKR AQDASLNVPE RAVFRLRKWI IHRLVSLVDH LHLEKDEAVV EQIARFCLFH 

       490        500        510        520        530        540 
AFFKTKKATP QIPETKQHFS FPLDDRNRGV FVSAFFSLLQ TLSVKFRQTP DLAENGKPWT 

       550        560        570        580        590        600 
YRLVQLADML LNHNRNVTSV TSLTTQQRQA WDQMMSTLKE LEARSSETRA IAFQHLLLLV 

       610        620        630        640        650        660 
GLHIFKSPAE SCDVLGDIQT CIKKSMEQNP RRSRSRAKAS QEPVWVEVMV EILLSLLAQP 

       670        680        690        700        710        720 
SNLMRQVVRS VFGHICPHLT PRCLQLILAV LSPVTNEDED DNVVVTDDAD EKQLQHGEDE 

       730        740        750        760        770        780 
DSDNEDNKNS ESDMDSEDGE ESEEEDRDKD VDPGFRQQLM EVLKAGNALG GVDNEEEEEL 

       790        800        810        820        830        840 
GDEAMMALDQ NLASLFKEQK MRIQARNEEK NKLQKEKKLR RDFQIRALDL IEVLVTKQPE 

       850        860        870        880        890        900 
HPLILELLEP LLNVIQHSMR SKGSTKQEQD LLHKTARIFM HHLCRARRYC HEVGPCAEAL 

       910        920        930        940        950        960 
HAQVERLVQQ AGSQADASVA LYYFNASLYL LRVLKGNTNK RHQDGHKLHG ADTEDSEDQA 

       970        980        990       1000       1010       1020 
ANCLDLDFVT RVYSASLESL LTKRNSSLTV PMFLSLFSRY PVICKNLLPV LAQHVAGPSR 

      1030       1040       1050       1060       1070       1080 
PRHQAQACLM LQKTLSAREL RVCFEDPEWE QLITQLLGKA TQTLQTLGEA QSKGEHQKEL 

      1090       1100       1110       1120       1130       1140 
SILELLNTLL RTVNHEKLSV DLTAPLGVLQ SKQQKLQQSL QQGNHSSGSN RLYDLYWQAM 

      1150       1160       1170       1180       1190       1200 
RMLGVQRPKS EKKNAKDIPS DTQSPVSTKR KKKGFLPETK KRKKLKSEGT TPEKNAASQQ 

      1210       1220       1230       1240       1250       1260 
DAVTEGAMPA ATGKDQPPST GKKKRKRVKA STPSQVNGIT GAKSPAPSNP TLSPSTPAKT 

      1270       1280       1290       1300       1310       1320 
PKLQKKKEKL SQVNGATPVS PIEPESKKHH QEALSTKEVI RKSPHPQSAL PKKRARLSLV 

      1330       1340 
SRSPSLLQSG VKKRRVASRR VQTP 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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]"Citrullination regulates pluripotency and histone H1 binding to chromatin."
Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S., Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C., Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.
Nature 507:104-108(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-1322.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS24986.1.
PIRT34188.
RefSeqNP_058056.2. NM_016776.2.
UniGeneMm.147946.

3D structure databases

ProteinModelPortalQ7TPV4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201999. 22 interactions.
DIPDIP-39831N.
IntActQ7TPV4. 12 interactions.
MINTMINT-1868464.

PTM databases

PhosphoSiteQ7TPV4.

Proteomic databases

MaxQBQ7TPV4.
PaxDbQ7TPV4.
PRIDEQ7TPV4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000045633; ENSMUSP00000044827; ENSMUSG00000040463.
GeneID18432.
KEGGmmu:18432.
UCSCuc007jyy.1. mouse.

Organism-specific databases

CTD10514.
MGIMGI:106181. Mybbp1a.

Phylogenomic databases

eggNOGNOG313877.
GeneTreeENSGT00390000017457.
HOGENOMHOG000113488.
HOVERGENHBG081961.
InParanoidQ7TPV4.
KOK02331.
OMAHQAQACL.
OrthoDBEOG7G7KPN.
PhylomeDBQ7TPV4.
TreeFamTF317401.

Gene expression databases

ArrayExpressQ7TPV4.
BgeeQ7TPV4.
CleanExMM_MYBBP1A.
GenevestigatorQ7TPV4.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR007015. DNA_pol_V.
[Graphical view]
PANTHERPTHR13213. PTHR13213. 1 hit.
PfamPF04931. DNA_pol_phi. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
ProtoNetSearch...

Other

ChiTaRSMYBBP1A. mouse.
NextBio294102.
PMAP-CutDBQ7TPV4.
PROQ7TPV4.
SOURCESearch...

Entry information

Entry nameMBB1A_MOUSE
AccessionPrimary (citable) accession number: Q7TPV4
Secondary accession number(s): O35851 expand/collapse secondary AC list , Q80Y66, Q8R4X2, Q99KP0
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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