Myb-binding protein 1A - Mus musculus (Mouse)

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Q7TPV4 (MBB1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Myb-binding protein 1A

Alternative name(s):
Myb-binding protein of 160 kDa

Gene names

Name:	Mybbp1a
Synonyms:	P160

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1344 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleolus. 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

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Molecular function	Activator Repressor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to glucose starvation Inferred from electronic annotation. Source: Compara intrinsic apoptotic signaling pathway by p53 class mediator Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent 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: Compara respiratory electron transport chain Inferred from direct assay Ref.7. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	NLS-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
Molecular_function	DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding Inferred from electronic annotation. Source: Compara 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1344

1344

Myb-binding protein 1A

PRO_0000096256

Regions

Region

1 – 580

580

Interaction with MYB

Region

1152 – 1344

193

Required for nuclear and nucleolar localization

Motif

238 – 256

Nuclear export signal 1

Motif

261 – 279

Nuclear export signal 2

Compositional bias

698 – 752

Asp-rich

Amino acid modifications

Modified residue

Phosphoserine Ref.9

Modified residue

N6-acetyllysine By similarity

Modified residue

156

N6-acetyllysine By similarity

Modified residue

722

Phosphoserine Ref.10

Modified residue

1160

Phosphoserine By similarity

Modified residue

1164

Phosphoserine Ref.9

Modified residue

1187

Phosphoserine By similarity

Modified residue

1191

Phosphothreonine By similarity

Modified residue

1198

Phosphoserine Ref.9

Modified residue

1219

Phosphoserine By similarity

Modified residue

1244

Phosphoserine By similarity

Modified residue

1253

Phosphoserine Ref.8 Ref.9 Ref.11

Modified residue

1277

Phosphothreonine Ref.9

Modified residue

1280

Phosphoserine Ref.9

Modified residue

1318

Phosphoserine By similarity

Modified residue

1323

Phosphoserine By similarity

Modified residue

1325

Phosphoserine By similarity

Modified residue

1329

Phosphoserine By similarity

Experimental info

Mutagenesis

249

L → A: Reduced nuclear export; when associated with A-251. Ref.6

Mutagenesis

251

V → A: Reduced nuclear export; when associated with A-249. Ref.6

Mutagenesis

272

L → A: Reduced nuclear export; when associated with A-274. Ref.6

Mutagenesis

274

L → A: Reduced nuclear export; when associated with A-272. Ref.6

Sequence conflict

R → T in AAC39954. Ref.1

Sequence conflict

R → T in AAL83748. Ref.2

Sequence conflict

P → A in AAC39954. Ref.1

Sequence conflict

505 – 508

DRNR → HASG in AAH04078. Ref.4

Sequence conflict

1282

I → V in AAH52889. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

Q7TPV4 [UniParc].

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

1,344

152,037

        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' referencesShow '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. 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1253, MASS SPECTROMETRY. Tissue: Embryonic brain.
[9]	"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 SER-6; SER-1164; SER-1198; SER-1253; THR-1277 AND SER-1280, MASS SPECTROMETRY. Tissue: Liver.
[10]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-722, MASS SPECTROMETRY. Tissue: Melanoma.
[11]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1253, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	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.
IPI	IPI00331361.
PIR	T34188.
RefSeq	NP_058056.2. NM_016776.2.
UniGene	Mm.147946.
3D structure databases
ProteinModelPortal	Q7TPV4.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-39831N.
IntAct	Q7TPV4. 8 interactions.
PTM databases
PhosphoSite	Q7TPV4.
Proteomic databases
PaxDb	Q7TPV4.
PRIDE	Q7TPV4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000045633; ENSMUSP00000044827; ENSMUSG00000040463.
GeneID	18432.
KEGG	mmu:18432.
Organism-specific databases
CTD	10514.
MGI	MGI:106181. Mybbp1a.
Phylogenomic databases
eggNOG	NOG313877.
GeneTree	ENSGT00390000017457.
HOGENOM	HOG000113488.
HOVERGEN	HBG081961.
InParanoid	Q7TPV4.
KO	K02331.
OMA	HKTARIF.
OrthoDB	EOG4RFKRW.
Gene expression databases
ArrayExpress	Q7TPV4.
Bgee	Q7TPV4.
CleanEx	MM_MYBBP1A.
Genevestigator	Q7TPV4.
GermOnline	ENSMUSG00000040463. Mus musculus.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR007015. DNA_pol_V. [Graphical view]
PANTHER	PTHR13213. PTHR13213. 1 hit.
Pfam	PF04931. DNA_pol_phi. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	MYBBP1A. mouse.
NextBio	294102.
PMAP-CutDB	Q7TPV4.
SOURCE	Search...

Entry information

Entry name

MBB1A_MOUSE

Accession

Primary (citable) accession number: Q7TPV4
Secondary accession number(s): O35851

Q99KP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	April 3, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents