Reviewed, UniProtKB/Swiss-Prot Q03237 (MYBB_CHICK)

Names and origin

Protein names

Recommended name:
    Myb-related protein B
Alternative name(s):
    B-Myb

Gene names

Name:	MYBL2
Synonyms:	BMYB

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	686 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Represses v-myb- and c-myb-mediated activation of the mim-1 gene, probably by competing with other myb proteins for binding sites. It is an inhibitory member of the myb family.
Subunit structure	Component of the DREAM complex By similarity.
Subcellular location	Nucleus.
Tissue specificity	Expressed in hematopoietic and non hematopoietic cells.
Sequence similarities	Contains 3 HTH myb-type DNA-binding domains.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat
Ligand	DNA-binding
Technical term	3D-structure
Gene Ontology (GO)
Biological process	regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 686

686

Myb-related protein B

PRO_0000197060

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

DNA binding

157 – 180

24

H-T-H motif

Secondary structure

1

.

.

.

.

.

.

.

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.

.

.

.

.

.

.

.

686

Helix Strand Turn

Details...

Helix

88 – 101

14

Helix

106 – 112

7

Helix

122 – 125

4

Beta strand

133 – 137

5

Helix

140 – 147

8

Turn

148 – 152

5

Helix

157 – 163

7

Helix

169 – 178

10

Sequences

	Sequence		Length	Mass (Da)
	Q03237-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 2D1209EAD6489D7B	FASTA	686	77,737
	10 20 30 40 50 60 MARRSRGEDQ DELHCQDTDS DVPEQRDGRC KVKWTQEEDE QLKMLVRHYG QNDWKFLASH 70 80 90 100 110 120 FPNRSDQQCQ YRWLRVLNPD LVKGPWTKEE DQKVIELVKK YGTKQWTLIA KHLKGRLGKQ 130 140 150 160 170 180 CRERWHNHLN PEVKKSSWTE EEDRIIFEAH KVLGNRWAEI AKLLPGRTDN AVKNHWNSTI 190 200 210 220 230 240 KRKVDTGGFL NETKESQPLY LLVEVDDNES QSGTRAESQT IVPNWPVDIS EIKEEDVSDE 250 260 270 280 290 300 EVTGLQELPS ELPAADLAEH NEEGTPDDVV PEDASASVAS PYKWVVEAAN YLCPTSVPAL 310 320 330 340 350 360 NEALDMIESD PDGWCDLTQF DLPEEPSAGS SSSSNSPVRQ TPSKPTPSLP NVTEYRLDGH 370 380 390 400 410 420 TISDLSKSRK GELIPISPHA EVSFGTPPSV LKRQKKRKIS LSPVTENAPS TSLSFLDSCN 430 440 450 460 470 480 SMTPKSTPVK TLPFSPSQFL NFWTKQDTLE LENPSLTSTP VCSQKVIVTT PLHRDKTPLL 490 500 510 520 530 540 QKNSAFVTPD QKYVVDNTPH TPTPFKNALE KYGPIRPLPQ TPHLEEDLKE VLRSEAGIEL 550 560 570 580 590 600 IIEDDVKPHK QKRKQGLRRS PIKKVRKSLA LDIVDEDMTQ NMPALPKTIC FKRTQPVNFL 610 620 630 640 650 660 SRSLNLSSSN RKNDSGLLNR AFVQVQSEKM SYRKMPSHFR PPAPMTRAWK AVACGGTQDQ 670 680 LFMQEKARQF LGTLKQSHTS RTLILS

References

[1]	"Functional antagonism between members of the myb family: B-myb inhibits v-myb-induced gene activation." Foos G., Grimm S., Klempnauer K.-H. EMBO J. 11:4619-4629(1992) [PubMed: 1425593] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Solution structure of the B-Myb DNA-binding domain: a possible role for conformational instability of the protein in DNA binding and control of gene expression." McIntosh P.B., Frenkiel T.A., Wollborn U., McCormick J.E., Klempnauer K.H., Feeney J., Carr M.D. Biochemistry 37:9619-9629(1998) [PubMed: 9657674] [Abstract] Cited for: STRUCTURE BY NMR OF 79-186.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X67505 mRNA. Translation: CAA47839.1.

IPI

IPI00581971.

PIR

S28050.

RefSeq

NP_990649.1.

UniGene

Gga.4532

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A5J	NMR	-	A	79-186	[»]

SMR

Q03237. Positions 31-181.

ModBase

Search...

Protein-protein interaction databases

STRING

Q03237.

Genome annotation databases

GeneID

396258.

KEGG

gga:396258.

Organism-specific databases

CTD

396258.

Phylogenomic databases

HOVERGEN

Q03237.

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]

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]

PROSITE

PS51294. HTH_MYB. 3 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MYBB_CHICK

Accession

Primary (citable) accession number: Q03237

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	September 22, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)