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Protein

Myb-related protein B

Gene

Mybl2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi54 – 7724H-T-H motifPROSITE-ProRule annotationAdd
BLAST
DNA bindingi106 – 12924H-T-H motifPROSITE-ProRule annotationAdd
BLAST
DNA bindingi157 – 18024H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_274086. G0 and Early G1.

Names & Taxonomyi

Protein namesi
Recommended name:
Myb-related protein B
Short name:
B-Myb
Alternative name(s):
Myb-like protein 2
Gene namesi
Name:Mybl2
Synonyms:Bmyb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:101785. Mybl2.

Subcellular locationi

GO - Cellular componenti

  • Myb complex Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 704704Myb-related protein BPRO_0000197059Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei267 – 2671PhosphothreonineBy similarity
Modified residuei443 – 4431Phosphothreonine; by CDK2By similarity
Modified residuei447 – 4471Phosphothreonine; by CDK2By similarity
Modified residuei490 – 4901Phosphothreonine; by CDK2By similarity
Modified residuei497 – 4971Phosphothreonine; by CDK2By similarity
Modified residuei524 – 5241Phosphothreonine; by CDK2By similarity
Modified residuei581 – 5811Phosphoserine; by CDK2By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP48972.

PTM databases

PhosphoSiteiP48972.

Expressioni

Gene expression databases

BgeeiP48972.
CleanExiMM_MYBL2.
ExpressionAtlasiP48972. baseline and differential.
GenevisibleiP48972. MM.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi201633. 6 interactions.
IntActiP48972. 1 interaction.
STRINGi10090.ENSMUSP00000018005.

Structurei

Secondary structure

1
704
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 4813Combined sources
Helixi54 – 607Combined sources
Beta strandi62 – 643Combined sources
Helixi66 – 7510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9ANMR-A31-77[»]
ProteinModelPortaliP48972.
SMRiP48972. Positions 31-186.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48972.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 7752HTH myb-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini78 – 13356HTH myb-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini134 – 18451HTH myb-type 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5147.
GeneTreeiENSGT00390000001038.
HOGENOMiHOG000231021.
HOVERGENiHBG007964.
InParanoidiP48972.
KOiK09421.
OMAiNSMTPKS.
OrthoDBiEOG7G7KNQ.
PhylomeDBiP48972.
TreeFamiTF326257.

Family and domain databases

Gene3Di1.10.10.60. 3 hits.
InterProiIPR015395. C-myb_C.
IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR028311. MYBL2.
IPR001005. SANT/Myb.
[Graphical view]
PANTHERiPTHR10641:SF37. PTHR10641:SF37. 1 hit.
PfamiPF09316. Cmyb_C. 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.

P48972-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRRTRCEDL DELHYQDVDS DLLEQRDNRC KVKWTHEEDE QLRALVRQFG
60 70 80 90 100
QQDWKFLASH FPNRTDQQCQ YRWLRVLNPD LVKGPWTKEE DQKVIELVKK
110 120 130 140 150
YGTKQWTLIA KHLKGRLGKQ CRERWHNHLN PEVKKSCWTE EEDRIICEAH
160 170 180 190 200
KVLGNRWAEI AKMLPGRTDN AVKNHWNSTI KRKVDTGGFP AESRDCKPVY
210 220 230 240 250
LLLELEDKEQ HQGVQPVDGQ GSLVSSWPLV PSIVKEESSE EEIAIAATSA
260 270 280 290 300
KELGHEPVPA DLGEVRTPEP PESLKREYQE FSSPETSLPY KWVVEAANLL
310 320 330 340 350
IPAVGSSLSE ALDLIESDPD AWCDLSKFDL PEEPSTEGSV VSSPVQPQTS
360 370 380 390 400
QQQQEEALQS SQQAATPGPS VTEYRLDGHT ISDLSRSSRG ELIPISPSTE
410 420 430 440 450
FGGSGIGTPP SVLKRQKKRR VALSPVTENS ASLSFLDSCN SLTPKSTPVK
460 470 480 490 500
TLPFSPSQFL NFWNKQDTLE LESPSLTSTP VCSQKVVVTT PLHRDKTPLH
510 520 530 540 550
QKYPSSEVLP DQKYSMDNTP HTPTPFKNAL EKYGPLKPLP QTPHLEEDLK
560 570 580 590 600
EVLRSEAGME LIIEDDMRPE KQKRKPGLRR SPIKKVRKSL ALDIMDEDGK
610 620 630 640 650
LMSSTMPKPL SLPTSVTPSS CGFTSPGSKE GNSLLNQGFL QAKPEKVVAA
660 670 680 690 700
QKTRSHIPTP APMTHAWKTV ACGGTKDQLF MQEKARQLLS RLKSSHTSRT

LILS
Length:704
Mass (Da):79,103
Last modified:February 1, 1996 - v1
Checksum:i0EF09C1EE2184E47
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70472 mRNA. Translation: CAA49898.1.
AK028497 mRNA. Translation: BAC25979.1.
BC050842 mRNA. Translation: AAH50842.1.
X73028 Genomic DNA. Translation: CAA51511.1.
CCDSiCCDS17006.1.
PIRiS33704.
RefSeqiNP_032678.1. NM_008652.2.
UniGeneiMm.4594.

Genome annotation databases

EnsembliENSMUST00000018005; ENSMUSP00000018005; ENSMUSG00000017861.
GeneIDi17865.
KEGGimmu:17865.
UCSCiuc008nsl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70472 mRNA. Translation: CAA49898.1.
AK028497 mRNA. Translation: BAC25979.1.
BC050842 mRNA. Translation: AAH50842.1.
X73028 Genomic DNA. Translation: CAA51511.1.
CCDSiCCDS17006.1.
PIRiS33704.
RefSeqiNP_032678.1. NM_008652.2.
UniGeneiMm.4594.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9ANMR-A31-77[»]
ProteinModelPortaliP48972.
SMRiP48972. Positions 31-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201633. 6 interactions.
IntActiP48972. 1 interaction.
STRINGi10090.ENSMUSP00000018005.

PTM databases

PhosphoSiteiP48972.

Proteomic databases

PRIDEiP48972.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018005; ENSMUSP00000018005; ENSMUSG00000017861.
GeneIDi17865.
KEGGimmu:17865.
UCSCiuc008nsl.1. mouse.

Organism-specific databases

CTDi4605.
MGIiMGI:101785. Mybl2.

Phylogenomic databases

eggNOGiCOG5147.
GeneTreeiENSGT00390000001038.
HOGENOMiHOG000231021.
HOVERGENiHBG007964.
InParanoidiP48972.
KOiK09421.
OMAiNSMTPKS.
OrthoDBiEOG7G7KNQ.
PhylomeDBiP48972.
TreeFamiTF326257.

Enzyme and pathway databases

ReactomeiREACT_274086. G0 and Early G1.

Miscellaneous databases

EvolutionaryTraceiP48972.
NextBioi292633.
PROiP48972.
SOURCEiSearch...

Gene expression databases

BgeeiP48972.
CleanExiMM_MYBL2.
ExpressionAtlasiP48972. baseline and differential.
GenevisibleiP48972. MM.

Family and domain databases

Gene3Di1.10.10.60. 3 hits.
InterProiIPR015395. C-myb_C.
IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR028311. MYBL2.
IPR001005. SANT/Myb.
[Graphical view]
PANTHERiPTHR10641:SF37. PTHR10641:SF37. 1 hit.
PfamiPF09316. Cmyb_C. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiMYBB_MOUSE
AccessioniPrimary (citable) accession number: P48972
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 24, 2015
This is version 136 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.