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P48972 (MYBB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myb-related protein B

Short name=B-Myb
Alternative name(s):
Myb-like protein 2
Gene names
Name:Mybl2
Synonyms:Bmyb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length704 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor involved in the regulation of cell survival, proliferation, and differentiation. Transactivates the expression of the CLU gene By similarity.

Subunit structure

Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2 By similarity.

Subcellular location

Nucleus.

Post-translational modification

Phosphorylated by cyclin A/CDK2 during S-phase. Phosphorylation at Thr-524 is probably involved in transcriptional activity By similarity.

Sequence similarities

Contains 3 HTH myb-type DNA-binding domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 704704Myb-related protein B
PRO_0000197059

Regions

Domain26 – 7752HTH myb-type 1
Domain78 – 13356HTH myb-type 2
Domain134 – 18451HTH myb-type 3
DNA binding54 – 7724H-T-H motif By similarity
DNA binding106 – 12924H-T-H motif By similarity
DNA binding157 – 18024H-T-H motif By similarity

Amino acid modifications

Modified residue2671Phosphothreonine By similarity
Modified residue4431Phosphothreonine; by CDK2 By similarity
Modified residue4471Phosphothreonine; by CDK2 By similarity
Modified residue4901Phosphothreonine; by CDK2 By similarity
Modified residue4971Phosphothreonine; by CDK2 By similarity
Modified residue5241Phosphothreonine; by CDK2 By similarity
Modified residue5811Phosphoserine; by CDK2 By similarity

Secondary structure

......... 704
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P48972 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 0EF09C1EE2184E47

FASTA70479,103
        10         20         30         40         50         60 
MSRRTRCEDL DELHYQDVDS DLLEQRDNRC KVKWTHEEDE QLRALVRQFG QQDWKFLASH 

        70         80         90        100        110        120 
FPNRTDQQCQ YRWLRVLNPD LVKGPWTKEE DQKVIELVKK YGTKQWTLIA KHLKGRLGKQ 

       130        140        150        160        170        180 
CRERWHNHLN PEVKKSCWTE EEDRIICEAH KVLGNRWAEI AKMLPGRTDN AVKNHWNSTI 

       190        200        210        220        230        240 
KRKVDTGGFP AESRDCKPVY LLLELEDKEQ HQGVQPVDGQ GSLVSSWPLV PSIVKEESSE 

       250        260        270        280        290        300 
EEIAIAATSA KELGHEPVPA DLGEVRTPEP PESLKREYQE FSSPETSLPY KWVVEAANLL 

       310        320        330        340        350        360 
IPAVGSSLSE ALDLIESDPD AWCDLSKFDL PEEPSTEGSV VSSPVQPQTS QQQQEEALQS 

       370        380        390        400        410        420 
SQQAATPGPS VTEYRLDGHT ISDLSRSSRG ELIPISPSTE FGGSGIGTPP SVLKRQKKRR 

       430        440        450        460        470        480 
VALSPVTENS ASLSFLDSCN SLTPKSTPVK TLPFSPSQFL NFWNKQDTLE LESPSLTSTP 

       490        500        510        520        530        540 
VCSQKVVVTT PLHRDKTPLH QKYPSSEVLP DQKYSMDNTP HTPTPFKNAL EKYGPLKPLP 

       550        560        570        580        590        600 
QTPHLEEDLK EVLRSEAGME LIIEDDMRPE KQKRKPGLRR SPIKKVRKSL ALDIMDEDGK 

       610        620        630        640        650        660 
LMSSTMPKPL SLPTSVTPSS CGFTSPGSKE GNSLLNQGFL QAKPEKVVAA QKTRSHIPTP 

       670        680        690        700 
APMTHAWKTV ACGGTKDQLF MQEKARQLLS RLKSSHTSRT LILS 

« Hide

References

« Hide 'large scale' references
[1]"Characterization and cell cycle-regulated expression of mouse B-myb."
Lam E.W., Robinson C., Watson R.J.
Oncogene 7:1885-1890(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Skin.
[3]"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].
Tissue: Limb.
[4]"An E2F-binding site mediates cell-cycle regulated repression of mouse B-myb transcription."
Lam E.W., Watson R.J.
EMBO J. 12:2705-2713(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
[5]"Solution structure of RSGI RUH-050, a myb DNA-binding domain in mouse."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 31-78.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70472 mRNA. Translation: CAA49898.1.
AK028497 mRNA. Translation: BAC25979.1.
BC050842 mRNA. Translation: AAH50842.1.
X73028 Genomic DNA. Translation: CAA51511.1.
CCDSCCDS17006.1.
PIRS33704.
RefSeqNP_032678.1. NM_008652.2.
UniGeneMm.4594.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9ANMR-A31-77[»]
ProteinModelPortalP48972.
SMRP48972. Positions 31-186.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201633. 7 interactions.
IntActP48972. 1 interaction.

PTM databases

PhosphoSiteP48972.

Proteomic databases

PRIDEP48972.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018005; ENSMUSP00000018005; ENSMUSG00000017861.
GeneID17865.
KEGGmmu:17865.
UCSCuc008nsl.1. mouse.

Organism-specific databases

CTD4605.
MGIMGI:101785. Mybl2.

Phylogenomic databases

eggNOGCOG5147.
GeneTreeENSGT00390000001038.
HOGENOMHOG000231021.
HOVERGENHBG007964.
InParanoidP48972.
KOK09421.
OMAMTPKSTP.
OrthoDBEOG7G7KNQ.
PhylomeDBP48972.
TreeFamTF326257.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.

Gene expression databases

ArrayExpressP48972.
BgeeP48972.
CleanExMM_MYBL2.
GenevestigatorP48972.

Family and domain databases

Gene3D1.10.10.60. 3 hits.
InterProIPR015395. C-myb_C.
IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR028311. MYBL2.
IPR001005. SANT/Myb.
[Graphical view]
PANTHERPTHR10641:SF37. PTHR10641:SF37. 1 hit.
PfamPF09316. Cmyb_C. 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

EvolutionaryTraceP48972.
NextBio292633.
PROP48972.
SOURCESearch...

Entry information

Entry nameMYBB_MOUSE
AccessionPrimary (citable) accession number: P48972
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 128 of the entry and version 1 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