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P02554 (TBB_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tubulin beta chain
Alternative name(s):
Beta-tubulin
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceEvidence 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. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Subcellular location

Cytoplasmcytoskeleton.

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 C-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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Tubulin beta chain
PRO_0000048261

Regions

Nucleotide binding140 – 1467GTP Potential

Amino acid modifications

Modified residue1721Phosphoserine; by CDK1 By similarity

Natural variations

Natural variant371H → V in 2nd form.
Natural variant481N → S in 2nd form.
Natural variant55 – 573AGN → SSH in 2nd form.
Natural variant2751S → A in 2nd form.

Secondary structure

............................................................................. 445
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02554 [UniParc].

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

FASTA44549,861
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRUBPGB. A02973.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFXX-ray3.95B/D1-445[»]
1IA0electron microscopy15.00B1-445[»]
1JFFX-ray3.50B1-445[»]
1TUBX-ray3.70B1-427[»]
2HXFelectron microscopy10.00B1-435[»]
2HXHelectron microscopy11.00B1-435[»]
2WBEelectron microscopy9.40B1-445[»]
4ABOelectron microscopy8.60A/C/E/G1-445[»]
ProteinModelPortalP02554.
SMRP02554. Positions 1-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP02554. 2 interactions.
STRING9823.ENSSSCP00000001076.

Chemistry

BindingDBP02554.
ChEMBLCHEMBL2111354.

Proteomic databases

PaxDbP02554.
PRIDEP02554.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG5023.
HOGENOMHOG000165710.
HOVERGENHBG000089.

Family and domain databases

Gene3D1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProIPR013838. 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]
PANTHERPTHR11588. PTHR11588. 1 hit.
PfamPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02554.

Entry information

Entry nameTBB_PIG
AccessionPrimary (citable) accession number: P02554
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 22, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references