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P06876

- MYB_MOUSE

UniProt

P06876 - MYB_MOUSE

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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 motif By similarity
Add
BLAST
DNA bindingi115 – 13824H-T-H motif
Add
BLAST
DNA bindingi166 – 18924H-T-H motif
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. chromatin binding Source: InterPro
  3. protein binding Source: IntAct
  4. sequence-specific DNA binding transcription factor activity Source: MGI

GO - Biological processi

  1. B cell differentiation Source: MGI
  2. G1/S transition of mitotic cell cycle Source: MGI
  3. calcium ion transport Source: MGI
  4. chromatin remodeling Source: Ensembl
  5. embryonic digestive tract development 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 T-helper cell differentiation Source: Ensembl
  10. positive regulation of histone H3-K4 methylation Source: Ensembl
  11. positive regulation of histone H3-K9 methylation Source: Ensembl
  12. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  13. regulation of gene expression Source: MGI
  14. regulation of transcription, DNA-templated Source: MGI
  15. thymus development Source: MGI
  16. transcription, DNA-templated Source: UniProtKB-KW
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 Myb
PRO_0000197049Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP06876.

PTM databases

PhosphoSiteiP06876.

Expressioni

Gene expression databases

ArrayExpressiP06876.
BgeeiP06876.
CleanExiMM_MYB.
GenevestigatoriP06876.

Interactioni

Subunit structurei

Binds to HIPK1 By similarity. Interacts with HIPK2, MAF, MYBBP1A and NLK.4 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi201631. 11 interactions.
IntActiP06876. 2 interactions.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP06876.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni90 – 193104Interaction with HIPK2 and NLK
Add
BLAST
Regioni275 – 32753Transcriptional activation domain By similarity
Add
BLAST
Regioni328 – 460133Negative regulatory domain
Add
BLAST
Regioni375 – 39622Leucine-zipper
Add
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.3 Publications
C-terminal truncated mutants display increased transactivation.3 Publications

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5147.
GeneTreeiENSGT00390000001038.
HOVERGENiHBG007964.
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

MARRPRHSIY SSDEDDEDIE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK    50
LKKLVEQNGT DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED 100
QRVIELVQKY GPKRWSVIAK HLKGRIGKQC RERWHNHLNP EVKKTSWTEE 150
EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA IKNHWNSTMR RKVEQEGYLQ 200
EPSKASQTPV ATSFQKNNHL MGFGHASPPS QLSPSGQSSV NSEYPYYHIA 250
EAQNISSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL 300
LLMSTENELK GQQALPTQNH TCSYPGWHST SIVDQTRPHG DSAPVSCLGE 350
HHATPSLPAD PGSLPEESAS PARCMIVHQG TILDNVKNLL EFAETLQFID 400
SFLNTSSNHE SSGLDAPTLP STPLIGHKLT PCRDQTVKTQ KENSIFRTPA 450
IKRSILESSP RTPTPFKHAL AAQEIKYGPL KMLPQTPSHA VEDLQDVIKQ 500
ESDESGIVAE FQESGPPLLK KIKQEVESPT EKSGNFFCSN HWAENSLSTQ 550
LFSQASPVAD APNILTSSVL MTPVSEDEDN VLKAFTVPKN RPLVGPLQPC 600
SGAWEPASCG KTEDQMTASG PARKYVNAFS ARTLVM 636
Length:636
Mass (Da):71,422
Last modified:July 27, 2011 - v2
Checksum:i0C6308E584726D01
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051E → K in CAA26552. 1 Publication
Sequence conflicti201 – 2011E → K in CAA26552. 1 Publication
Sequence conflicti267 – 2671V → A in AAB59713. 1 Publication
Sequence conflicti402 – 4021F → V in AAA39786. 1 Publication
Sequence conflicti411 – 4111S → N in CAA26552. 1 Publication
Sequence conflicti500 – 5001Q → R in CAA26552. 1 Publication
Sequence conflicti500 – 5001Q → R in AAH11513. 1 Publication
Sequence conflicti525 – 5251E → A in CAA26552. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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.
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

ArrayExpressi P06876.
Bgeei P06876.
CleanExi MM_MYB.
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: September 3, 2014
This is version 150 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

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