Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P06876

- MYB_MOUSE

UniProt

P06876 - MYB_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Transcriptional activator Myb

Gene

Myb

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

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi63 – 8624H-T-H motifPROSITE-ProRule annotationAdd
BLAST
DNA bindingi115 – 13824H-T-H motifPROSITE-ProRule annotationAdd
BLAST
DNA bindingi166 – 18924H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: InterPro
  2. DNA binding Source: MGI
  3. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  4. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  5. sequence-specific DNA binding transcription factor activity Source: MGI

GO - Biological processi

  1. B cell differentiation Source: MGI
  2. calcium ion transport Source: MGI
  3. chromatin remodeling Source: Ensembl
  4. embryonic digestive tract development Source: MGI
  5. G1/S transition of mitotic cell cycle Source: MGI
  6. homeostasis of number of cells Source: MGI
  7. in utero embryonic development Source: MGI
  8. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  9. positive regulation of histone H3-K4 methylation Source: Ensembl
  10. positive regulation of histone H3-K9 methylation Source: Ensembl
  11. positive regulation of T-helper cell differentiation Source: Ensembl
  12. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  13. regulation of gene expression Source: MGI
  14. regulation of transcription, DNA-templated Source: MGI
  15. thymus development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_198649. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional activator Myb
Alternative name(s):
Proto-oncogene c-Myb
Gene namesi
Name:Myb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:97249. Myb.

Subcellular locationi

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 636636Transcriptional activator MybPRO_0000197049Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei467 – 4671N6-acetyllysineBy similarity
Modified residuei476 – 4761N6-acetyllysineBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP06876.

PTM databases

PhosphoSiteiP06876.

Expressioni

Gene expression databases

BgeeiP06876.
CleanExiMM_MYB.
ExpressionAtlasiP06876. baseline and differential.
GenevestigatoriP06876.

Interactioni

Subunit structurei

Binds to HIPK1 (By similarity). Interacts with HIPK2, MAF, MYBBP1A and NLK.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Hipk2Q9QZR52EBI-366934,EBI-366905

Protein-protein interaction databases

BioGridi201631. 11 interactions.
IntActiP06876. 2 interactions.

Structurei

Secondary structure

1
636
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 5814Combined sources
Helixi63 – 686Combined sources
Helixi75 – 8612Combined sources
Beta strandi92 – 943Combined sources
Helixi97 – 11014Combined sources
Helixi115 – 1195Combined sources
Helixi127 – 13610Combined sources
Beta strandi140 – 1423Combined sources
Beta strandi144 – 1463Combined sources
Helixi149 – 16214Combined sources
Helixi163 – 1653Combined sources
Helixi166 – 1705Combined sources
Beta strandi173 – 1753Combined sources
Helixi178 – 18811Combined sources
Helixi189 – 1913Combined sources
Helixi292 – 31120Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP06876.
SMRiP06876. Positions 38-193.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06876.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 8652HTH myb-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini87 – 14256HTH myb-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini143 – 19351HTH myb-type 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni90 – 193104Interaction with HIPK2 and NLKAdd
BLAST
Regioni275 – 32753Transcriptional activation domainBy similarityAdd
BLAST
Regioni328 – 460133Negative regulatory domainAdd
BLAST
Regioni375 – 39622Leucine-zipperAdd
BLAST

Domaini

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.
C-terminal truncated mutants display increased transactivation.

Sequence similaritiesi

Contains 3 HTH myb-type DNA-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5147.
GeneTreeiENSGT00390000001038.
HOVERGENiHBG007964.
InParanoidiP06876.
KOiK09420.
OMAiHGCLPEE.
OrthoDBiEOG7H791P.
TreeFamiTF326257.

Family and domain databases

Gene3Di1.10.10.60. 3 hits.
InterProiIPR015395. C-myb_C.
IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
IPR012642. Tscrpt_reg_Wos2-domain.
[Graphical view]
PfamiPF09316. Cmyb_C. 1 hit.
PF07988. LMSTEN. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 3 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51294. HTH_MYB. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P06876-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARRPRHSIY SSDEDDEDIE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK
60 70 80 90 100
LKKLVEQNGT DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED
110 120 130 140 150
QRVIELVQKY GPKRWSVIAK HLKGRIGKQC RERWHNHLNP EVKKTSWTEE
160 170 180 190 200
EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA IKNHWNSTMR RKVEQEGYLQ
210 220 230 240 250
EPSKASQTPV ATSFQKNNHL MGFGHASPPS QLSPSGQSSV NSEYPYYHIA
260 270 280 290 300
EAQNISSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL
310 320 330 340 350
LLMSTENELK GQQALPTQNH TCSYPGWHST SIVDQTRPHG DSAPVSCLGE
360 370 380 390 400
HHATPSLPAD PGSLPEESAS PARCMIVHQG TILDNVKNLL EFAETLQFID
410 420 430 440 450
SFLNTSSNHE SSGLDAPTLP STPLIGHKLT PCRDQTVKTQ KENSIFRTPA
460 470 480 490 500
IKRSILESSP RTPTPFKHAL AAQEIKYGPL KMLPQTPSHA VEDLQDVIKQ
510 520 530 540 550
ESDESGIVAE FQESGPPLLK KIKQEVESPT EKSGNFFCSN HWAENSLSTQ
560 570 580 590 600
LFSQASPVAD APNILTSSVL MTPVSEDEDN VLKAFTVPKN RPLVGPLQPC
610 620 630
SGAWEPASCG KTEDQMTASG PARKYVNAFS ARTLVM
Length:636
Mass (Da):71,422
Last modified:July 27, 2011 - v2
Checksum:i0C6308E584726D01
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051E → K in CAA26552. (PubMed:2998780)Curated
Sequence conflicti201 – 2011E → K in CAA26552. (PubMed:2998780)Curated
Sequence conflicti267 – 2671V → A in AAB59713. (PubMed:3010282)Curated
Sequence conflicti402 – 4021F → V in AAA39786. (PubMed:3014527)Curated
Sequence conflicti411 – 4111S → N in CAA26552. (PubMed:2998780)Curated
Sequence conflicti500 – 5001Q → R in CAA26552. (PubMed:2998780)Curated
Sequence conflicti500 – 5001Q → R in AAH11513. (PubMed:15489334)Curated
Sequence conflicti525 – 5251E → A in CAA26552. (PubMed:2998780)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35861.1.
PIRiA25285. TVMSMB.
RefSeqiNP_001185843.1. NM_001198914.1.
NP_034978.3. NM_010848.3.
UniGeneiMm.473872.
Mm.52109.

Genome annotation databases

EnsembliENSMUST00000020158; ENSMUSP00000020158; ENSMUSG00000019982.
GeneIDi17863.
KEGGimmu:17863.
UCSCiuc007eog.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS35861.1.
PIRi A25285. TVMSMB.
RefSeqi NP_001185843.1. NM_001198914.1.
NP_034978.3. NM_010848.3.
UniGenei Mm.473872.
Mm.52109.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P06876.
SMRi P06876. Positions 38-193.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201631. 11 interactions.
IntActi P06876. 2 interactions.

PTM databases

PhosphoSitei P06876.

Proteomic databases

PRIDEi P06876.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020158 ; ENSMUSP00000020158 ; ENSMUSG00000019982 .
GeneIDi 17863.
KEGGi mmu:17863.
UCSCi uc007eog.1. mouse.

Organism-specific databases

CTDi 4602.
MGIi MGI:97249. Myb.

Phylogenomic databases

eggNOGi COG5147.
GeneTreei ENSGT00390000001038.
HOVERGENi HBG007964.
InParanoidi P06876.
KOi K09420.
OMAi HGCLPEE.
OrthoDBi EOG7H791P.
TreeFami TF326257.

Enzyme and pathway databases

Reactomei REACT_198649. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTracei P06876.
NextBioi 292625.
PROi P06876.
SOURCEi Search...

Gene expression databases

Bgeei P06876.
CleanExi MM_MYB.
ExpressionAtlasi P06876. baseline and differential.
Genevestigatori P06876.

Family and domain databases

Gene3Di 1.10.10.60. 3 hits.
InterProi IPR015395. C-myb_C.
IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
IPR012642. Tscrpt_reg_Wos2-domain.
[Graphical view ]
Pfami PF09316. Cmyb_C. 1 hit.
PF07988. LMSTEN. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view ]
SMARTi SM00717. SANT. 3 hits.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 2 hits.
PROSITEi PS51294. HTH_MYB. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-193 IN COMPLEX WITH HUMAN CEBPB.

Entry informationi

Entry nameiMYB_MOUSE
AccessioniPrimary (citable) accession number: P06876
Secondary accession number(s): E9QMG8, Q61929
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 153 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3