Reviewed, UniProtKB/Swiss-Prot P02554 (TBB_PIG)

Names and origin

Protein names	Recommended name:     Tubulin beta chain Alternative name(s):     Beta-tubulin
Organism	Sus scrofa (Pig)
Taxonomic identifier	9823 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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.
Subunit structure	Dimer of alpha and beta chains.
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.
Miscellaneous	The highly acidic carboxyl-terminal region may bind cations such as calcium. Pig brain contains at least two forms of this protein.
Sequence similarities	Belongs to the tubulin family.

Ontologies

Keywords
Cellular component	Microtubule
Ligand	GTP-binding Nucleotide-binding
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	microtubule-based movement Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro
Cellular component	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 chain

PRO_0000048261

Regions

Nucleotide binding

140 – 146

7

GTP Potential

Natural variations

Natural variant

37

1

H → V in 2nd form.

Natural variant

48

1

N → S in 2nd form.

Natural variant

55 – 57

3

AGN → SSH in 2nd form.

Natural variant

275

1

S → A in 2nd form.

Secondary structure

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445

Helix Strand Turn

Details...

Beta strand

3 – 6

4

Helix

10 – 20

11

Turn

21 – 25

5

Helix

26 – 28

3

Beta strand

32 – 34

3

Beta strand

39 – 42

4

Helix

47 – 49

3

Beta strand

53 – 55

3

Turn

70 – 72

3

Helix

73 – 77

5

Turn

81 – 84

4

Helix

101 – 104

4

Turn

105 – 112

8

Helix

116 – 124

9

Beta strand

126 – 128

3

Beta strand

130 – 134

5

Beta strand

136 – 142

7

Turn

143 – 145

3

Helix

146 – 155

10

Turn

156 – 158

3

Beta strand

160 – 164

5

Beta strand

167 – 170

4

Beta strand

177 – 180

4

Helix

181 – 192

12

Turn

193 – 195

3

Helix

206 – 212

7

Helix

222 – 236

15

Helix

238 – 240

3

Helix

250 – 257

8

Turn

276 – 278

3

Helix

289 – 293

5

Beta strand

295 – 303

9

Helix

305 – 307

3

Beta strand

316 – 320

5

Helix

323 – 335

13

Helix

338 – 340

3

Beta strand

343 – 345

3

Beta strand

352 – 356

5

Beta strand

364 – 368

5

Turn

372 – 376

5

Helix

377 – 389

13

Turn

390 – 394

5

Helix

395 – 399

5

Helix

407 – 423

17

Sequences

	Sequence		Length	Mass (Da)
	P02554-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: EF71423B12C5E1B2	FASTA	445	49,861
	10 20 30 40 50 60 MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV 70 80 90 100 110 120 PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV 130 140 150 160 170 180 RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV 190 200 210 220 230 240 EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL 250 260 270 280 290 300 RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM 310 320 330 340 350 360 AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG 370 380 390 400 410 420 LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS 430 440 EYQQYQDATA DEQGEFEEEG EEDEA

References

[1]	"Complete amino acid sequence of beta-tubulin from porcine brain." Krauhs E., Little M., Kempf T., Hofer-Warbinek R., Ade W., Ponstingl H. Proc. Natl. Acad. Sci. U.S.A. 78:4156-4160(1981) [PubMed: 6945576] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Brain.
[2]	"The GTP-binding peptide of beta-tubulin. Localization by direct photoaffinity labeling and comparison with nucleotide-binding proteins." Linse K., Mandelkow E.M. J. Biol. Chem. 263:15205-15210(1988) [PubMed: 3170578] [Abstract] Cited for: PROTEIN SEQUENCE OF 63-77.
[3]	"Localization of the ATP binding site on alpha-tubulin." Zabrecky J.R., Cole R.D. Arch. Biochem. Biophys. 225:475-481(1983) [PubMed: 6688710] [Abstract] Cited for: GUANINE NUCLEOTIDE-BINDING SITES.
[4]	"The 4 A X-ray structure of a tubulin:stathmin-like domain complex." Gigant B., Curmi P.A., Martin-Barbey C., Charbaut E., Lachkar S., Lebeau L., Siavoshian S., Sobel A., Knossow M. Cell 102:809-816(2000) [PubMed: 11030624] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.95 ANGSTROMS).
[5]	"Structure of the alpha beta tubulin dimer by electron crystallography." Nogales E., Wolf S.G., Downing K.H. Nature 391:199-203(1998) [PubMed: 9428769] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.7 ANGSTROMS) OF 1-427.
[6]	"15 A resolution model of the monomeric kinesin motor, KIF1A." Kikkawa M., Okada Y., Hirokawa N. Cell 100:241-252(2000) [PubMed: 10660047] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (15.0 ANGSTROMS).
[7]	"Refined structure of alpha beta-tubulin at 3.5 A resolution." Loewe J., Li H., Downing K.H., Nogales E. J. Mol. Biol. 313:1045-1057(2001) [PubMed: 11700061] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

UBPGB. A02973.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFX	X-ray	3.95	B/D	1-445	[»]
1IA0	electron microscopy	15.00	B	1-445	[»]
1JFF	X-ray	3.50	B	1-445	[»]
1TUB	X-ray	3.70	B	1-427	[»]
2HXF	electron microscopy	10.00	B	1-435	[»]
2HXH	electron microscopy	11.00	B	1-435	[»]
2WBE	electron microscopy	9.40	B	1-445	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSSSCT00000001098; ENSSSCP00000001076; ENSSSCG00000001006; Sus scrofa. [Genome view]

Phylogenomic databases

HOVERGEN

P02554.

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.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
IPR019746. Tubulin_FtsZ_N.
[Graphical view]

Gene3D

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

PANTHER

PTHR11588:SF9. Beta_tubulin. 1 hit.
PTHR11588. Tubulin. 1 hit.

Pfam

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

PRINTS

PR01163. BETATUBULIN.
PR01161. TUBULIN.

SMART

SM00865. Tubulin_C. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

TBB_PIG

Accession

Primary (citable) accession number: P02554

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 24, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)