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P06876 (MYB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional activator Myb
Alternative name(s):
Proto-oncogene c-Myb
Gene names
Name:Myb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length636 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells.

Subunit structure

Binds to HIPK1 By similarity. Interacts with HIPK2, MAF, MYBBP1A and NLK. Ref.14 Ref.15 Ref.16 Ref.17

Subcellular location

Nucleus.

Domain

Comprised of 3 domains; an N-terminal DNA-binding domain, a centrally located transcriptional activation domain and a C-terminal domain involved in transcriptional repression. Ref.11 Ref.12 Ref.13

C-terminal truncated mutants display increased transactivation. Ref.11 Ref.12 Ref.13

Post-translational modification

Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation By similarity.

Phosphorylated by NLK on multiple sites, which induces proteasomal degradation.

Phosphorylated by HIPK1. This phosphorylation reduces MYB transcription factor activity but not MYB protein levels By similarity.

Sequence similarities

Contains 3 HTH myb-type DNA-binding domains.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DiseaseProto-oncogene
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from mutant phenotype PubMed 17927961. Source: MGI

G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 12660151. Source: MGI

calcium ion transport

Inferred from mutant phenotype PubMed 12660151. Source: MGI

chromatin remodeling

Inferred from electronic annotation. Source: Ensembl

embryonic digestive tract development

Inferred from mutant phenotype PubMed 10523863. Source: MGI

homeostasis of number of cells

Inferred from mutant phenotype PubMed 17927961. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 10523863PubMed 17927961. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of T-helper cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of histone H3-K4 methylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of histone H3-K9 methylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 15094381. Source: MGI

regulation of gene expression

Inferred from mutant phenotype PubMed 10523863. Source: MGI

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12628004. Source: MGI

thymus development

Inferred from mutant phenotype PubMed 17927961. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 12628004PubMed 16847320PubMed 8302594. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 12628004PubMed 21980308. Source: MGI

chromatin binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12628004. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Hipk2Q9QZR52EBI-366934,EBI-366905

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 636636Transcriptional activator Myb
PRO_0000197049

Regions

Domain35 – 8652HTH myb-type 1
Domain87 – 14256HTH myb-type 2
Domain143 – 19351HTH myb-type 3
DNA binding63 – 8624H-T-H motif By similarity
DNA binding115 – 13824H-T-H motif
DNA binding166 – 18924H-T-H motif
Region90 – 193104Interaction with HIPK2 and NLK
Region275 – 32753Transcriptional activation domain By similarity
Region328 – 460133Negative regulatory domain
Region375 – 39622Leucine-zipper

Amino acid modifications

Modified residue4671N6-acetyllysine By similarity
Modified residue4761N6-acetyllysine By similarity

Experimental info

Sequence conflict1051E → K in CAA26552. Ref.2
Sequence conflict2011E → K in CAA26552. Ref.2
Sequence conflict2671V → A in AAB59713. Ref.1
Sequence conflict4021F → V in AAA39786. Ref.10
Sequence conflict4111S → N in CAA26552. Ref.2
Sequence conflict5001Q → R in CAA26552. Ref.2
Sequence conflict5001Q → R in AAH11513. Ref.6
Sequence conflict5251E → A in CAA26552. Ref.2

Secondary structure

.............................. 636
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06876 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 0C6308E584726D01

FASTA63671,422
        10         20         30         40         50         60 
MARRPRHSIY SSDEDDEDIE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT 

        70         80         90        100        110        120 
DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK 

       130        140        150        160        170        180 
HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA 

       190        200        210        220        230        240 
IKNHWNSTMR RKVEQEGYLQ EPSKASQTPV ATSFQKNNHL MGFGHASPPS QLSPSGQSSV 

       250        260        270        280        290        300 
NSEYPYYHIA EAQNISSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL 

       310        320        330        340        350        360 
LLMSTENELK GQQALPTQNH TCSYPGWHST SIVDQTRPHG DSAPVSCLGE HHATPSLPAD 

       370        380        390        400        410        420 
PGSLPEESAS PARCMIVHQG TILDNVKNLL EFAETLQFID SFLNTSSNHE SSGLDAPTLP 

       430        440        450        460        470        480 
STPLIGHKLT PCRDQTVKTQ KENSIFRTPA IKRSILESSP RTPTPFKHAL AAQEIKYGPL 

       490        500        510        520        530        540 
KMLPQTPSHA VEDLQDVIKQ ESDESGIVAE FQESGPPLLK KIKQEVESPT EKSGNFFCSN 

       550        560        570        580        590        600 
HWAENSLSTQ LFSQASPVAD APNILTSSVL MTPVSEDEDN VLKAFTVPKN RPLVGPLQPC 

       610        620        630 
SGAWEPASCG KTEDQMTASG PARKYVNAFS ARTLVM 

« Hide

References

« Hide 'large scale' references
[1]"Murine myb protooncogene mRNA: cDNA sequence and evidence for 5' heterogeneity."
Bender T.P., Kuehl W.M.
Proc. Natl. Acad. Sci. U.S.A. 83:3204-3208(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"Nucleotide sequence of cDNA clones of the murine myb proto-oncogene."
Gonda T.J., Gough N.M., Dunn A.R., de Blaquiere J.
EMBO J. 4:2003-2008(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Multiple c-myb transcript cap sites are variously utilized in cells of mouse haemopoietic origin."
Watson R.J., Dyson P.J., McMahon J.
EMBO J. 6:1643-1651(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Aberrant splicing events that are induced by proviral integration: implications for myb oncogene activation."
Rosson D., Dugan D., Reddy E.P.
Proc. Natl. Acad. Sci. U.S.A. 84:3171-3175(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"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.
[6]"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: FVB/N.
Tissue: Mammary gland.
[7]"Structure and biological activity of the transcriptional initiation sequences of the murine c-myb oncogene."
Sobieszczuk P.W., Gonda T.J., Dunn A.R.
Nucleic Acids Res. 17:9593-9611(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
[8]"Two modes of c-myb activation in virus-induced mouse myeloid tumors."
Shen-Ong G.L.C., Morse H.C. III, Potter M., Mushinski F.
Mol. Cell. Biol. 6:380-392(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 72-636.
[9]"Structural organization and nucleotide sequence of mouse c-myb oncogene: activation in ABPL tumors is due to viral integration in an intron which results in the deletion of the 5' coding sequences."
Lavu S., Reddy E.P.
Nucleic Acids Res. 14:5309-5320(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 72-401.
[10]"Truncation of the c-myb gene by a retroviral integration in an interleukin 3-dependent myeloid leukemia cell line."
Weinstein Y., Ihle J.N., Lavu S., Reddy P.E.
Proc. Natl. Acad. Sci. U.S.A. 83:5010-5014(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-402.
[11]"Activation of c-myb by carboxy-terminal truncation: relationship to transformation of murine haemopoietic cells in vitro."
Gonda T.J., Buckmaster C., Ramsay R.G.
EMBO J. 8:1777-1783(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN C-TERMINAL.
[12]"Transformation by carboxyl-deleted Myb reflects increased transactivating capacity and disruption of a negative regulatory domain."
Hu Y., Ramsay R.G., Kanei-Ishii C., Ishii S., Gonda T.J.
Oncogene 6:1549-1553(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NEGATIVE REGULATORY DOMAIN.
[13]"Negative autoregulation of c-Myb activity by homodimer formation through the leucine zipper."
Nomura T., Sakai N., Sarai A., Sudo T., Kanei-Ishii C., Ramsay R.G., Favier D., Gonda T.J., Ishii S.
J. Biol. Chem. 268:21914-21923(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN LEUCINE-ZIPPER, NEGATIVE AUTOREGULATION.
[14]"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: INTERACTION WITH MYBBP1A1.
[15]"c-Maf interacts with c-Myb to regulate transcription of an early myeloid gene during differentiation."
Hedge S.P., Kumar A., Kurschner C., Shapiro L.H.
Mol. Cell. Biol. 18:2729-2737(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAF.
[16]"Wnt-1 signal induces phosphorylation and degradation of c-Myb protein via TAK1, HIPK2, and NLK."
Kanei-Ishii C., Ninomiya-Tsuji J., Tanikawa J., Nomura T., Ishitani T., Kishida S., Kokura K., Kurahashi T., Ichikawa-Iwata E., Kim Y., Matsumoto K., Ishii S.
Genes Dev. 18:816-829(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIPK2 AND NLK.
[17]"c-Maf interacts with c-Myb to down-regulate Bcl-2 expression and increase apoptosis in peripheral CD4 cells."
Peng S., Lalani S., Leavenworth J.W., Ho I.-C., Pauza M.E.
Eur. J. Immunol. 37:2868-2880(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAF.
[18]"Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic core."
Ogata K., Hojo H., Aimoto S., Nakai T., Nakamura H., Sarai A., Ishii S., Nishimura Y.
Proc. Natl. Acad. Sci. U.S.A. 89:6428-6432(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 142-193.
[19]"Secondary structure of the DNA-binding domain of the c-Myb oncoprotein in solution. A multidimensional double and triple heteronuclear NMR study."
Jamin N., Gabrielsen O.S., Gilles N., Lirsac P.-N., Toma F.
Eur. J. Biochem. 216:147-154(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 89-192.
[20]"Comparison of the free and DNA-complexed forms of the DNA-binding domain from c-Myb."
Ogata K., Morikawa S., Nakamura H., Hojo H., Yoshimura S., Zhang R., Aimoto S., Ametani Y., Hirata Z., Sarai A., Ishii S., Nishimura Y.
Nat. Struct. Biol. 2:309-320(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 38-89; 90-141 AND 142-193.
[21]"A small engineered protein lacks structural uniqueness by increasing the side-chain conformational entropy."
Furukawa K., Oda M., Nakamura H.
Proc. Natl. Acad. Sci. U.S.A. 93:13583-13588(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 140-193.
[22]"Mechanism of c-Myb-C/EBP beta cooperation from separated sites on a promoter."
Tahirov T.H., Sato K., Ichikawa-Iwata E., Sasaki M., Inoue-Bungo T., Shiina M., Kimura K., Takata S., Fujikawa A., Morii H., Kumasaka T., Yamamoto M., Ishii S., Ogata K.
Cell 108:57-70(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-193 IN COMPLEX WITH HUMAN CEBPB.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21169 Genomic DNA. Translation: AAA39782.1.
M12848 mRNA. Translation: AAB59713.1.
X02774 mRNA. Translation: CAA26552.1.
M20210 Genomic DNA. Translation: AAA39783.1.
AC153556 Genomic DNA. No translation available.
BC011513 mRNA. Translation: AAH11513.1.
X04099 expand/collapse EMBL AC list , X04100, X04101, X04102, X04103, X04104 Genomic DNA. Translation: CAA27724.1.
X16389 Genomic DNA. Translation: CAA34425.1.
X16390 Genomic DNA. Translation: CAA34426.1.
M13989 Genomic DNA. Translation: AAA39787.1.
K03547 Genomic DNA. Translation: AAA39786.1.
PIRTVMSMB. A25285.
RefSeqNP_001185843.1. NM_001198914.1.
NP_034978.3. NM_010848.3.
UniGeneMm.473872.
Mm.52109.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GUUX-ray1.60A38-89[»]
1GV2X-ray1.68A89-193[»]
1GV5X-ray1.58A90-141[»]
1GVDX-ray1.45A90-141[»]
1H88X-ray2.80C37-193[»]
1H89X-ray2.45C37-193[»]
1IDYNMR-A141-193[»]
1IDZNMR-A141-193[»]
1MBENMR-A38-89[»]
1MBFNMR-A38-89[»]
1MBGNMR-A90-141[»]
1MBHNMR-A90-141[»]
1MBJNMR-A142-193[»]
1MBKNMR-A142-193[»]
1MSENMR-C90-193[»]
1MSFNMR-C90-193[»]
1SB0NMR-B291-315[»]
2AGHNMR-A291-315[»]
ProteinModelPortalP06876.
SMRP06876. Positions 38-193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201631. 11 interactions.
IntActP06876. 2 interactions.

PTM databases

PhosphoSiteP06876.

Proteomic databases

PRIDEP06876.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020158; ENSMUSP00000020158; ENSMUSG00000019982.
GeneID17863.
KEGGmmu:17863.
UCSCuc007eog.1. mouse.

Organism-specific databases

CTD4602.
MGIMGI:97249. Myb.

Phylogenomic databases

eggNOGCOG5147.
GeneTreeENSGT00390000001038.
HOVERGENHBG007964.
KOK09420.
OMAHGCLPEE.
OrthoDBEOG7H791P.
TreeFamTF326257.

Gene expression databases

ArrayExpressP06876.
BgeeP06876.
CleanExMM_MYB.
GenevestigatorP06876.

Family and domain databases

Gene3D1.10.10.60. 3 hits.
InterProIPR015395. C-myb_C.
IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
IPR012642. Tscrpt_reg_Wos2-domain.
[Graphical view]
PfamPF09316. Cmyb_C. 1 hit.
PF07988. LMSTEN. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTSM00717. SANT. 3 hits.
[Graphical view]
SUPFAMSSF46689. SSF46689. 2 hits.
PROSITEPS51294. HTH_MYB. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06876.
NextBio292625.
PROP06876.
SOURCESearch...

Entry information

Entry nameMYB_MOUSE
AccessionPrimary (citable) accession number: P06876
Secondary accession number(s): E9QMG8, Q61929
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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