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UniProtKB/Swiss-Prot entry P10244


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MYBB_HUMAN
Primary accession number P10244
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 1, 1989 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 107)
Name and origin of the protein
Protein name Myb-related protein B
Synonym B-Myb
Gene name
Name: MYBL2
Synonyms: BMYB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/16.23.11075; PubMed=3060855 [NCBI, ExPASy, EBI, Israel, Japan]
Nomura N., Takahashi M., Matsui M., Ishii S., Date T., Sasamoto S., Ishizaki R.;
"Isolation of human cDNA clones of myb-related genes, A-myb and B-myb.";
Nucleic Acids Res. 16:11075-11089(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Eye;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION AT THR-444; THR-487; THR-494 AND SER-577.
DOI=10.1038/sj.onc.1202503; PubMed=9840932 [NCBI, ExPASy, EBI, Israel, Japan]
Saville M.K., Watson R.J.;
"The cell-cycle regulated transcription factor B-Myb is phosphorylated by cyclin A/Cdk2 at sites that enhance its transactivation properties.";
Oncogene 17:2679-2689(1998).
[5]
PHOSPHORYLATION AT THR-440; THR-444; THR-494; THR-520 AND SER-577.
DOI=10.1046/j.1432-1327.1999.00191.x; PubMed=10095772 [NCBI, ExPASy, EBI, Israel, Japan]
Bartsch O., Horstmann S., Toprak K., Klempnauer K.H., Ferrari S.;
"Identification of cyclin A/Cdk2 phosphorylation sites in B-Myb.";
Eur. J. Biochem. 260:384-391(1999).
[6]
FUNCTION.
DOI=10.1074/jbc.M002055200; PubMed=10770937 [NCBI, ExPASy, EBI, Israel, Japan]
Cervellera M., Raschella G., Santilli G., Tanno B., Ventura A., Mancini C., Sevignani C., Calabretta B., Sala A.;
"Direct transactivation of the anti-apoptotic gene apolipoprotein J (clusterin) by B-MYB.";
J. Biol. Chem. 275:21055-21060(2000).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[8]
NUCLEAR LOCALIZATION SIGNALS.
DOI=10.1016/0014-5793(94)00733-0; PubMed=8062924 [NCBI, ExPASy, EBI, Israel, Japan]
Takemoto Y., Tashiro S., Handa H., Ishii S.;
"Multiple nuclear localization signals of the B-myb gene product.";
FEBS Lett. 350:55-60(1994).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[10]
IDENTIFICATION IN THE DREAM COMPLEX.
PubMed=17671431 [NCBI, ExPASy, EBI, Israel, Japan]
Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B., Gagrica S., Haenel F., Brehm A., Gaubatz S.;
"LINC, a human complex that is related to pRB-containing complexes in invertebrates regulates the expression of G2/M genes.";
Cell Cycle 6:1903-1913(2007).
[11]
IDENTIFICATION IN THE DREAM COMPLEX.
DOI=10.1016/j.molcel.2007.04.015; PubMed=17531812 [NCBI, ExPASy, EBI, Israel, Japan]
Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K., Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.;
"Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex represses human cell cycle-dependent genes in quiescence.";
Mol. Cell 26:539-551(2007).
Comments
  • FUNCTION: Transcription factor involved in the regulation of cell survival, proliferation, and differentiation. Transactivates the expression of the CLU gene.
  • SUBUNIT: 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 MYBL22.
  • SUBCELLULAR LOCATION: Nucleus.
  • PTM: Phosphorylated by cyclin A/CDK2 during S-phase. Phosphorylation at Thr-520 is probably involved in transcriptional activity.
  • SIMILARITY: Contains 3 HTH myb-type DNA-binding domains.
  • WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/MYBL2ID41469ch20q13.html";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X13293; CAA31655.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121886; CAC08392.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007585; AAH07585.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC053555; AAH53555.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00019993; -.
PIR S01991; S01991.
RefSeq NP_002457.1; -.
UniGene Hs.179718
3D structure databases
HSSP Q03237; 1A5J. [HSSP ENTRY / PDB]
SMR P10244; 31-181.
ModBase P10244.
PTM databases
PhosphoSite P10244; -.
Organism-specific databases
GeneCards GC20P041729; -.
H-InvDB HIX0015830; -.
HGNC HGNC:7548; MYBL2.
GenAtlas MYBL2.
HPA CAB017114; -.
MIM 601415; gene. [NCBI / EBI]
PharmGKB PA31348; -.
Gene expression databases
ArrayExpress P10244; -.
Bgee P10244; -.
CleanEx HS_MYBL2; -.
GermOnline ENSG00000101057; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003700; Molecular function: transcription factor activity (traceable author statement from ProtInc).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR015395; C-myb_C.
IPR012287; Homeodomain-rel.
IPR017930; Myb-type_HTH.
IPR014778; Myb_DNA-bd.
IPR015495; Myb_trans_fac.
IPR001005; SANT_DNA-bd.
Graphical view of domain structure.
Gene3D G3DSA:1.10.10.60; Homeodomain-rel; 3.
PANTHER PTHR10641; Myb_transfac; 1.
Pfam PF09316; Cmyb_C; 1.
PF00249; Myb_DNA-binding; 3.
Pfam graphical view of domain structure.
SMART SM00717; SANT; 3.
SMART graphical view of domain structure.
PROSITE PS51294; HTH_MYB; 3.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P10244; -.
PRIDE P10244; -.
Genome annotation databases
Ensembl ENSG00000101057; Homo sapiens. [Contig view]
GeneID 4605; -.
KEGG hsa:4605; -.
Phylogenomic databases
HOGENOM P10244; -.
HOVERGEN P10244; -.
OMA P10244; QFLNFWN.
Other
NextBio 17724; -.
SOURCE MYBL2; Homo sapiens.
ProtoNet P10244.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Repeat; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   700  700     Myb-related protein B. PRO_0000197058
DOMAIN   26    77  52     HTH myb-type 1. 
DOMAIN   78   133  56     HTH myb-type 2. 
DOMAIN   134   184  51     HTH myb-type 3. 
DNA_BIND   54    77  24     H-T-H motif (By similarity). 
DNA_BIND   106   129  24     H-T-H motif (By similarity). 
DNA_BIND   157   180  24     H-T-H motif (By similarity). 
MOTIF   411   417  7     Nuclear localization signal. 
MOTIF   564   584  21     Bipartite nuclear localization signal. 
MOD_RES   266   266        Phosphothreonine. 
MOD_RES   393   393        Phosphoserine. 
MOD_RES   440   440        Phosphothreonine; by CDK2. 
MOD_RES   444   444        Phosphothreonine; by CDK2. 
MOD_RES   487   487        Phosphothreonine; by CDK2. 
MOD_RES   494   494        Phosphothreonine; by CDK2. 
MOD_RES   520   520        Phosphothreonine; by CDK2. 
MOD_RES   577   577        Phosphoserine; by CDK2. 
VARIANT   341   341  1     N -> S (in dbSNP:rs6017146 [NCBI]). VAR_050190 
VARIANT   427   427  1     S -> G (in dbSNP:rs2070235 [NCBI]). VAR_020422 
VARIANT   595   595  1     V -> M (in dbSNP:rs7660 [NCBI]). VAR_050191 
VARIANT   624   624  1     I -> M (in dbSNP:rs11556379 [NCBI]). VAR_050192 
Sequence information
Length: 700 AA [This is the length of the unprocessed precursor] Molecular weight: 78764 Da [This is the MW of the unprocessed precursor] CRC64: D91B28B3DAB94061 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSRRTRCEDL DELHYQDTDS DVPEQRDSKC 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 
KRKVDTGGFL SESKDCKPPV YLLLELEDKD GLQSAQPTEG QGSLLTNWPS VPPTIKEEEN 

       250        260        270        280        290        300 
SEEELAAATT SKEQEPIGTD LDAVRTPEPL EEFPKREDQE GSPPETSLPY KWVVEAANLL 

       310        320        330        340        350        360 
IPAVGSSLSE ALDLIESDPD AWCDLSKFDL PEEPSAEDSI NNSLVQLQAS HQQQVLPPRQ 

       370        380        390        400        410        420 
PSALVPSVTE YRLDGHTISD LSRSSRGELI PISPSTEVGG SGIGTPPSVL KRQRKRRVAL 

       430        440        450        460        470        480 
SPVTENSTSL SFLDSCNSLT PKSTPVKTLP FSPSQFLNFW NKQDTLELES PSLTSTPVCS 

       490        500        510        520        530        540 
QKVVVTTPLH RDKTPLHQKH AAFVTPDQKY SMDNTPHTPT PFKNALEKYG PLKPLPQTPH 

       550        560        570        580        590        600 
LEEDLKEVLR SEAGIELIIE DDIRPEKQKR KPGLRRSPIK KVRKSLALDI VDEDVKLMMS 

       610        620        630        640        650        660 
TLPKSLSLPT TAPSNSSSLT LSGIKEDNSL LNQGFLQAKP EKAAVAQKPR SHFTTPAPMS 

       670        680        690        700 
SAWKTVACGG TRDQLFMQEK ARQLLGRLKP SHTSRTLILS 

P10244 in FASTA format

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