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P10244 (MYBB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length700 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. Ref.9

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 MYBL22. Ref.12 Ref.13

Subcellular location

Nucleus.

Post-translational modification

Phosphorylated by cyclin A/CDK2 during S-phase. Phosphorylation at Thr-520 is probably involved in transcriptional activity. Ref.7 Ref.8

Sequence similarities

Contains 3 HTH myb-type DNA-binding domains.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P10244-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P10244-2)

The sequence of this isoform differs from the canonical sequence as follows:
     39-62: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 700700Myb-related protein B
PRO_0000197058

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
Motif411 – 4177Nuclear localization signal Ref.10
Motif564 – 58421Bipartite nuclear localization signal

Amino acid modifications

Modified residue2411Phosphoserine Ref.15 Ref.16 Ref.17
Modified residue2661Phosphothreonine Ref.11
Modified residue4401Phosphothreonine; by CDK2 Ref.8
Modified residue4441Phosphothreonine; by CDK2 Ref.7 Ref.8
Modified residue4871Phosphothreonine; by CDK2 Ref.7
Modified residue4941Phosphothreonine; by CDK2 Ref.7 Ref.8
Modified residue5201Phosphothreonine; by CDK2 Ref.8
Modified residue5771Phosphoserine; by CDK2 Ref.7 Ref.8

Natural variations

Alternative sequence39 – 6224Missing in isoform 2.
VSP_053987
Natural variant3411N → S.
Corresponds to variant rs6017146 [ dbSNP | Ensembl ].
VAR_050190
Natural variant4271S → G. Ref.2
Corresponds to variant rs2070235 [ dbSNP | Ensembl ].
VAR_020422
Natural variant5951V → M.
Corresponds to variant rs7660 [ dbSNP | Ensembl ].
VAR_050191
Natural variant6241I → M.
Corresponds to variant rs11556379 [ dbSNP | Ensembl ].
VAR_050192

Experimental info

Sequence conflict1841V → A in BAD97202. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: D91B28B3DAB94061

FASTA70078,764
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 322D482BEFD9A724
Show »

FASTA67675,865

References

« Hide 'large scale' references
[1]"Isolation of human cDNA clones of myb-related genes, A-myb and B-myb."
Nomura N., Takahashi M., Matsui M., Ishii S., Date T., Sasamoto S., Ishizaki R.
Nucleic Acids Res. 16:11075-11089(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT GLY-427.
Tissue: Brain and Thymus.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"The DNA sequence and comparative analysis of human chromosome 20."
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. expand/collapse author list , 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.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 1).
Tissue: Brain and Eye.
[7]"The cell-cycle regulated transcription factor B-Myb is phosphorylated by cyclin A/Cdk2 at sites that enhance its transactivation properties."
Saville M.K., Watson R.J.
Oncogene 17:2679-2689(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-444; THR-487; THR-494 AND SER-577.
[8]"Identification of cyclin A/Cdk2 phosphorylation sites in B-Myb."
Bartsch O., Horstmann S., Toprak K., Klempnauer K.H., Ferrari S.
Eur. J. Biochem. 260:384-391(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-440; THR-444; THR-494; THR-520 AND SER-577.
[9]"Direct transactivation of the anti-apoptotic gene apolipoprotein J (clusterin) by B-MYB."
Cervellera M., Raschella G., Santilli G., Tanno B., Ventura A., Mancini C., Sevignani C., Calabretta B., Sala A.
J. Biol. Chem. 275:21055-21060(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Multiple nuclear localization signals of the B-myb gene product."
Takemoto Y., Tashiro S., Handa H., Ishii S.
FEBS Lett. 350:55-60(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR LOCALIZATION SIGNALS.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"LINC, a human complex that is related to pRB-containing complexes in invertebrates regulates the expression of G2/M genes."
Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B., Gagrica S., Haenel F., Brehm A., Gaubatz S.
Cell Cycle 6:1903-1913(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
[13]"Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex represses human cell cycle-dependent genes in quiescence."
Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K., Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.
Mol. Cell 26:539-551(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13293 mRNA. Translation: CAA31655.1.
AK303249 mRNA. Translation: BAH13925.1.
AK314791 mRNA. Translation: BAG37322.1.
AK223482 mRNA. Translation: BAD97202.1.
AL121886 Genomic DNA. Translation: CAC08392.1.
CH471077 Genomic DNA. Translation: EAW75951.1.
BC007585 mRNA. Translation: AAH07585.1.
BC053555 mRNA. Translation: AAH53555.1.
CCDSCCDS13322.1.
PIRS01991.
RefSeqNP_001265539.1. NM_001278610.1. [P10244-2]
NP_002457.1. NM_002466.3. [P10244-1]
UniGeneHs.179718.

3D structure databases

ProteinModelPortalP10244.
SMRP10244. Positions 28-186.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110690. 36 interactions.
IntActP10244. 12 interactions.
MINTMINT-125947.
STRING9606.ENSP00000217026.

PTM databases

PhosphoSiteP10244.

Polymorphism databases

DMDM127584.

Proteomic databases

MaxQBP10244.
PaxDbP10244.
PeptideAtlasP10244.
PRIDEP10244.

Protocols and materials databases

DNASU4605.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217026; ENSP00000217026; ENSG00000101057.
ENST00000396863; ENSP00000380072; ENSG00000101057.
GeneID4605.
KEGGhsa:4605.
UCSCuc002xlb.1. human. [P10244-1]

Organism-specific databases

CTD4605.
GeneCardsGC20P042295.
HGNCHGNC:7548. MYBL2.
HPACAB017114.
HPA030530.
HPA055416.
MIM601415. gene.
neXtProtNX_P10244.
PharmGKBPA31348.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5147.
HOGENOMHOG000231021.
HOVERGENHBG007964.
InParanoidP10244.
KOK09421.
OMAMTPKSTP.
OrthoDBEOG7G7KNQ.
PhylomeDBP10244.
TreeFamTF326257.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressP10244.
BgeeP10244.
CleanExHS_MYBL2.
GenevestigatorP10244.

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

ChiTaRSMYBL2. human.
GeneWikiMYBL2.
GenomeRNAi4605.
NextBio17724.
PROP10244.
SOURCESearch...

Entry information

Entry nameMYBB_HUMAN
AccessionPrimary (citable) accession number: P10244
Secondary accession number(s): B2RBS5 expand/collapse secondary AC list , B7Z8D9, F8W6N6, Q53F07
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM