Tubulin beta chain - Sus scrofa (Pig)

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Reviewed, UniProtKB/Swiss-Prot P02554 (TBB_PIG)

Last modified November 25, 2008. Version 74. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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.
Sequence processing	The displayed sequence is not processed.
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.
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	cytoplasm Inferred from electronic annotation. Source: InterPro microtubule Inferred from electronic annotation. Source: InterPro protein complex Inferred from electronic annotation. Source: InterPro
Molecular function	GTP binding Inferred from electronic annotation. Source: InterPro 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

445

Tubulin beta chain

PRO_0000048261

Regions

Nucleotide binding

7

GTP Potential

Natural variations

Natural variant

1

H → V in 2nd form.

Natural variant

1

N → S in 2nd form.

Natural variant

3

AGN → SSH in 2nd form.

Natural variant

1

S → A in 2nd form.

Secondary structure

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445

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P02554-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: EF71423B12C5E1B2
Show »

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

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	electron microscopy	3.50	B	1-445	[»]
1SA0	X-ray	3.58	B/D	1-445	[»]
1SA1	X-ray	4.20	B/D	1-445	[»]
1TUB	electron microscopy	3.70	B	1-427	[»]
1TVK	electron microscopy	2.89	B	1-427	[»]
2HXF	electron microscopy	10.00	B	1-445	[»]
2HXH	electron microscopy	11.00	B	1-445	[»]

ModBase

Phylogenomic databases

HOVERGEN

Family and domain databases

InterPro

IPR013838. Beta-tubulin_BS.
IPR002453. Beta_tubulin.
IPR000158. Cell_division_FtsZ_N.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR003008. Tubulin_FtsZ.
[Graphical view]

Gene3D

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.
PR00423. CELLDVISFTSZ.
PR01161. TUBULIN.

PROSITE

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

ProtoNet

Other Resources

LinkHub

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 25, 2008
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents