Reviewed, UniProtKB/Swiss-Prot P10244 (MYBB_HUMAN)

Names and origin

Protein names

Recommended name:
Myb-related protein B
Short name=B-Myb

Alternative name(s):
Myb-like protein 2

Gene names

Name:	MYBL2
Synonyms:	BMYB

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	700 AA.
Sequence status	Complete.
Protein existence	Evidence 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.8
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.
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.6 Ref.7 Ref.9 Ref.11 Ref.14 Ref.15
Sequence similarities	Contains 3 HTH myb-type DNA-binding domains.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular transcription Inferred from electronic annotation. Source: UniProtKB-KW regulation of cellular transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	transcription factor activity Ref.8 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 700	700	Myb-related protein B		PRO_0000197058
Regions
	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 binding	54 – 77	24	H-T-H motif By similarity
	DNA binding	106 – 129	24	H-T-H motif By similarity
	DNA binding	157 – 180	24	H-T-H motif By similarity
	Motif	411 – 417	7	Nuclear localization signal Ref.10
	Motif	564 – 584	21	Bipartite nuclear localization signal
Amino acid modifications
	Modified residue	241	1	Phosphoserine Ref.14 Ref.15
	Modified residue	266	1	Phosphothreonine Ref.11
	Modified residue	393	1	Phosphoserine Ref.9
	Modified residue	405	1	Phosphothreonine Ref.15
	Modified residue	440	1	Phosphothreonine; by CDK2 Ref.7
	Modified residue	444	1	Phosphothreonine; by CDK2 Ref.6 Ref.7
	Modified residue	487	1	Phosphothreonine; by CDK2 Ref.6
	Modified residue	494	1	Phosphothreonine; by CDK2 Ref.6 Ref.7
	Modified residue	520	1	Phosphothreonine; by CDK2 Ref.7
	Modified residue	577	1	Phosphoserine; by CDK2 Ref.6 Ref.7
Natural variations
	Natural variant	341	1	N → S: dbSNP rs6017146.		VAR_050190
	Natural variant	427	1	S → G: dbSNP rs2070235.		VAR_020422
	Natural variant	595	1	V → M: dbSNP rs7660.		VAR_050191
	Natural variant	624	1	I → M: dbSNP rs11556379.		VAR_050192

Sequences

	Sequence		Length	Mass (Da)
	P10244-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: D91B28B3DAB94061	FASTA	700	78,764
	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

References

	« Hide 'large scale' referencesShow '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: 3060855] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"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. , 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: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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. , 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].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Eye.
[6]	"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: 9840932] [Abstract] Cited for: PHOSPHORYLATION AT THR-444; THR-487; THR-494 AND SER-577.
[7]	"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: 10095772] [Abstract] Cited for: PHOSPHORYLATION AT THR-440; THR-444; THR-494; THR-520 AND SER-577.
[8]	"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: 10770937] [Abstract] Cited for: FUNCTION.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 8062924] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 17671431] [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: 17531812] [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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, MASS SPECTROMETRY.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND THR-405, MASS SPECTROMETRY. Tissue: T-cell.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	X13293 mRNA. Translation: CAA31655.1. AK314791 mRNA. Translation: BAG37322.1. AL121886 Genomic DNA. Translation: CAC08392.1. CH471077 Genomic DNA. Translation: EAW75951.1. BC007585 mRNA. Translation: AAH07585.1. BC053555 mRNA. Translation: AAH53555.1.
IPI	IPI00019993.
PIR	S01991.
RefSeq	NP_002457.1.
UniGene	Hs.179718
3D structure databases
SMR	P10244. Positions 31-181, 83-219.
ModBase	Search...
Protein-protein interaction databases
STRING	P10244.
PTM databases
PhosphoSite	P10244.
Proteomic databases
PeptideAtlas	P10244.
PRIDE	P10244.
Genome annotation databases
Ensembl	ENST00000217026; ENSP00000217026; ENSG00000101057; Homo sapiens. [Genome view]
GeneID	4605.
KEGG	hsa:4605.
UCSC	uc002xlb.1. human.
Organism-specific databases
CTD	4605.
GeneCards	GC20P041729.
H-InvDB	HIX0015830.
HGNC	HGNC:7548. MYBL2.
HPA	CAB017114.
MIM	601415. gene.
PharmGKB	PA31348.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07008.
HOGENOM	HBG713828.
HOVERGEN	HBG007964.
InParanoid	P10244.
OMA	QFLNFWN.
OrthoDB	EOG96DPN9.
PhylomeDB	P10244.
Gene expression databases
ArrayExpress	P10244.
Bgee	P10244.
CleanEx	HS_MYBL2.
Genevestigator	P10244.
GermOnline	ENSG00000101057. Homo sapiens.
Family and domain databases
InterPro	IPR015395. C-myb_C. IPR009057. Homeodomain-like. IPR012287. Homeodomain-rel. IPR017930. HTH_Myb-type_DNA-bd. IPR014778. Myb_DNA-bd. IPR015495. Myb_trans_fac. IPR001005. SANT_DNA-bd. [Graphical view]
Gene3D	G3DSA:1.10.10.60. Homeodomain-rel. 3 hits.
PANTHER	PTHR10641. Myb_transfac. 1 hit.
Pfam	PF09316. Cmyb_C. 1 hit. PF00249. Myb_DNA-binding. 3 hits. [Graphical view]
SMART	SM00717. SANT. 3 hits. [Graphical view]
SUPFAM	SSF46689. Homeodomain_like. 3 hits.
PROSITE	PS51294. HTH_MYB. 3 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	17724.
SOURCE	Search...

Entry information

Entry name

MYBB_HUMAN

Accession

Primary (citable) accession number: P10244
Secondary accession number(s): B2RBS5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	March 2, 2010
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.