Q6B856 (TBB2B_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin beta-2B chain

Gene names

Name:

TUBB2B

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain By similarity.
Subunit structure	Dimer of alpha and beta chains By similarity.
Subcellular location	Cytoplasm › cytoskeleton By similarity.
Post-translational modification	Some glutamate residues at the C-terminus are either polyglutamylated or polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they are regulate the assembly and dynamics of axonemal microtubules By similarity.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	microtubule-based movement Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 445

445

Tubulin beta-2B chain

PRO_0000262654

Amino acid modifications

Modified residue

36

1

Phosphotyrosine By similarity

Experimental info

Sequence conflict

201

1

C → S in AAT84374. Ref.1

Secondary structure

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445

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Helix

11 – 28

18

Helix

44 – 47

4

Turn

48 – 50

3

Beta strand

55 – 57

3

Beta strand

63 – 66

4

Beta strand

68 – 70

3

Helix

72 – 77

6

Beta strand

78 – 81

4

Helix

87 – 89

3

Helix

101 – 105

5

Turn

106 – 109

4

Helix

110 – 124

15

Beta strand

127 – 129

3

Beta strand

132 – 142

11

Helix

145 – 155

11

Turn

156 – 158

3

Beta strand

160 – 170

11

Helix

181 – 195

15

Beta strand

197 – 203

7

Helix

204 – 212

9

Turn

213 – 215

3

Helix

223 – 237

15

Helix

238 – 240

3

Helix

251 – 257

7

Turn

261 – 263

3

Beta strand

265 – 272

8

Helix

287 – 293

7

Helix

296 – 298

3

Beta strand

299 – 303

5

Beta strand

310 – 320

11

Helix

324 – 336

13

Helix

338 – 340

3

Beta strand

343 – 345

3

Beta strand

349 – 354

6

Beta strand

365 – 371

7

Helix

372 – 374

3

Helix

375 – 386

12

Turn

387 – 392

6

Helix

396 – 399

4

Turn

400 – 402

3

Helix

406 – 422

17

Turn

423 – 425

3

Sequences

	Sequence		Length	Mass (Da)
	Q6B856 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: 4DC3956EFF880746	FASTA	445	49,953
	10 20 30 40 50 60 MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEATGNKYV 70 80 90 100 110 120 PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV 130 140 150 160 170 180 RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM PSPKVSDTVV 190 200 210 220 230 240 EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL 250 260 270 280 290 300 RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM 310 320 330 340 350 360 AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG 370 380 390 400 410 420 LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS 430 440 EYQQYQDATA DEQGEFEEEE GEDEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differentially expressed genes in bovine 8-cell embryo." Hwang K.C., Park S.Y., Cui X.S., Kim N.H. Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence of taurine cattle: a window to ruminant biology and evolution." The bovine genome sequencing and analysis consortium Science 324:522-528(2009) [PubMed: 19390049] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hereford.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY675081 mRNA. Translation: AAT84374.1.

IPI

IPI00697107.

RefSeq

NP_001003900.1. NM_001003900.1.

UniGene

Bt.105119.
Bt.21484.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SA0	X-ray	3.58	B/D	1-445	[»]
1SA1	X-ray	4.20	B/D	1-445	[»]
1TVK	X-ray	2.89	B	1-427	[»]
1Z2B	X-ray	4.10	B/D	1-445	[»]
2P4N	electron microscopy	9.00	B	1-445	[»]
2XRP	electron microscopy	8.20	A/C/E/G	1-445	[»]
3DCO	electron microscopy	1.90	B	1-445	[»]
3DU7	X-ray	4.10	B/D	1-445	[»]
3E22	X-ray	3.80	B/D	1-445	[»]

ProteinModelPortal

Q6B856.

SMR

Q6B856. Positions 2-428.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-6604256.

STRING

Q6B856.

Proteomic databases

PRIDE

Q6B856.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000005346; ENSBTAP00000005346; ENSBTAG00000004093.

GeneID

281555.

KEGG

bta:281555.

Organism-specific databases

CTD

7280.

Phylogenomic databases

GeneTree

ENSGT00600000084255.

HOVERGEN

HBG000089.

OrthoDB

EOG4DFPNJ.

PhylomeDB

Q6B856.

Family and domain databases

InterPro

IPR013838. Beta-tubulin_BS.
IPR002453. Beta_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]

Gene3D

G3DSA:3.30.1330.20. Tubulin/FtsZ_2-layer-sand-dom. 1 hit.
G3DSA:1.10.287.600. Tubulin_C. 1 hit.
G3DSA:3.40.50.1440. Tubulin_FtsZ. 1 hit.

KO

K07375.

PANTHER

PTHR11588. Tubulin. 1 hit.

Pfam

PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]

PRINTS

PR01163. BETATUBULIN.
PR01161. TUBULIN.

SMART

SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]

SUPFAM

SSF55307. Tub_FtsZ_C. 1 hit.
SSF52490. Tubulin_FtsZ. 1 hit.

PROSITE

PS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

TBB2B_BOVIN

Accession

Primary (citable) accession number: Q6B856

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	November 28, 2006
Last modified:	November 16, 2011
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program