P06876 (MYB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcriptional activator Myb

Alternative name(s):
Proto-oncogene c-Myb

Gene names

Name:

Myb

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	636 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Disease	Proto-oncogene
Domain	Repeat
Ligand	DNA-binding
Molecular function	Activator
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B 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: Compara 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: Compara positive regulation of T-helper cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of histone H3-K4 methylation Inferred from electronic annotation. Source: Compara positive regulation of histone H3-K9 methylation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction PubMed 15094381. Source: MGI thymus development Inferred from mutant phenotype PubMed 17927961. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA 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
Hipk2	Q9QZR5	2	EBI-366934,EBI-366905

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 636

636

Transcriptional activator Myb

PRO_0000197049

Regions

Domain

35 – 86

52

HTH myb-type 1

Domain

87 – 142

56

HTH myb-type 2

Domain

143 – 193

51

HTH myb-type 3

DNA binding

63 – 86

24

H-T-H motif By similarity

DNA binding

115 – 138

24

H-T-H motif

DNA binding

166 – 189

24

H-T-H motif

Region

90 – 193

104

Interaction with HIPK2 and NLK

Region

275 – 327

53

Transcriptional activation domain By similarity

Region

328 – 460

133

Negative regulatory domain

Region

375 – 396

22

Leucine-zipper

Amino acid modifications

Modified residue

467

1

N6-acetyllysine By similarity

Modified residue

476

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

105

1

E → K in CAA26552. Ref.2

Sequence conflict

201

1

E → K in CAA26552. Ref.2

Sequence conflict

267

1

V → A in AAB59713. Ref.1

Sequence conflict

402

1

F → V in AAA39786. Ref.10

Sequence conflict

411

1

S → N in CAA26552. Ref.2

Sequence conflict

500

1

Q → R in CAA26552. Ref.2

Sequence conflict

500

1

Q → R in AAH11513. Ref.6

Sequence conflict

525

1

E → A in CAA26552. Ref.2

Secondary structure

1

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636

Helix Strand Turn

Details...

Helix

45 – 58

14

Helix

63 – 68

6

Helix

75 – 86

12

Beta strand

92 – 94

3

Helix

97 – 110

14

Helix

115 – 119

5

Helix

127 – 136

10

Beta strand

140 – 142

3

Beta strand

144 – 146

3

Helix

149 – 162

14

Helix

163 – 165

3

Helix

166 – 170

5

Beta strand

173 – 175

3

Helix

178 – 188

11

Helix

189 – 191

3

Helix

292 – 311

20

Sequences

	Sequence		Length	Mass (Da)
	P06876 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 0C6308E584726D01	FASTA	636	71,422
	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

References

	« Hide 'large scale' referencesShow '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. , 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 , 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.

IPI

IPI00323266.

PIR

TVMSMB. A25285.

RefSeq

NP_001185843.1. NM_001198914.1.
NP_034978.3. NM_010848.3.

UniGene

Mm.52109.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GUU	X-ray	1.60	A	38-89	[»]
1GV2	X-ray	1.68	A	89-193	[»]
1GV5	X-ray	1.58	A	90-141	[»]
1GVD	X-ray	1.45	A	90-141	[»]
1H88	X-ray	2.80	C	37-193	[»]
1H89	X-ray	2.45	C	37-193	[»]
1IDY	NMR	-	A	141-193	[»]
1IDZ	NMR	-	A	141-193	[»]
1MBE	NMR	-	A	38-89	[»]
1MBF	NMR	-	A	38-89	[»]
1MBG	NMR	-	A	90-141	[»]
1MBH	NMR	-	A	90-141	[»]
1MBJ	NMR	-	A	142-193	[»]
1MBK	NMR	-	A	142-193	[»]
1MSE	NMR	-	C	90-193	[»]
1MSF	NMR	-	C	90-193	[»]
1SB0	NMR	-	B	291-315	[»]
2AGH	NMR	-	A	291-315	[»]

ProteinModelPortal

P06876.

SMR

P06876. Positions 38-193.

ModBase

Search...

Protein-protein interaction databases

IntAct

P06876. 2 interactions.

PTM databases

PhosphoSite

P06876.

Proteomic databases

PRIDE

P06876.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000020158; ENSMUSP00000020158; ENSMUSG00000019982.

GeneID

17863.

KEGG

mmu:17863.

UCSC

uc007eog.1. mouse.

Organism-specific databases

CTD

4602.

MGI

MGI:97249. Myb.

Phylogenomic databases

eggNOG

COG5147.

GeneTree

ENSGT00390000001038.

HOVERGEN

HBG007964.

KO

K09420.

OMA

HLMGFAH.

OrthoDB

EOG4H9XKD.

Gene expression databases

ArrayExpress

P06876.

Bgee

P06876.

CleanEx

MM_MYB.

Genevestigator

P06876.

GermOnline

ENSMUSG00000019982. Mus musculus.

Family and domain databases

Gene3D

1.10.10.60. 3 hits.

InterPro

IPR015395. C-myb_C.
IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
IPR012642. Tscrpt_reg_Wos2-domain.
[Graphical view]

Pfam

PF09316. Cmyb_C. 1 hit.
PF07988. LMSTEN. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]

SMART

SM00717. SANT. 3 hits.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 2 hits.

PROSITE

PS51294. HTH_MYB. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P06876.

NextBio

292625.

SOURCE

Search...

Entry information

Entry name

MYB_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 141 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program