Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P02550 (TBA1A_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 104. 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 alpha-1A chain
Alternative name(s):
Alpha-tubulin 1
Tubulin alpha-1 chain
Gene names
Name:TUBA1A
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length451 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

Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.

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.

Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling By similarity.

Miscellaneous

The highly acidic C-terminal region may bind cations such as calcium.

Sequence similarities

Belongs to the tubulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Tubulin alpha-1A chain
PRO_0000048131

Regions

Nucleotide binding142 – 1487GTP Potential

Sites

Site4511Involved in polymerization

Amino acid modifications

Modified residue481Phosphoserine By similarity
Modified residue831Nitrated tyrosine By similarity
Modified residue2821Nitrated tyrosine By similarity
Modified residue4321Phosphotyrosine By similarity
Modified residue4391Phosphoserine By similarity

Natural variations

Natural variant2651A → G.
Natural variant2651A → I.
Natural variant2661H → I.
Natural variant271 – 2733TYA → RFB.

Secondary structure

................................................................................... 451
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02550 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 48D7112D182B33CA

FASTA45150,068
        10         20         30         40         50         60 
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK 

        70         80         90        100        110        120 
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD 

       130        140        150        160        170        180 
RIRKLADQCT GLQGFSVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA 

       190        200        210        220        230        240 
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA 

       250        260        270        280        290        300 
SLRFDGALNV DLTEFQTNLV PYPRAHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 

       310        320        330        340        350        360 
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYEPP 

       370        380        390        400        410        420 
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE 

       430        440        450 
AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y 

« Hide

References

[1]"Complete amino acid sequence of alpha-tubulin from porcine brain."
Ponstingl H., Krauhs E., Little M., Kempf T.
Proc. Natl. Acad. Sci. U.S.A. 78:2757-2761(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Brain.
[2]"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: BINDING SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRUBPGA. A93874.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFXX-ray3.95A/C1-451[»]
1IA0electron microscopy15.00A1-451[»]
1TUBX-ray3.70A1-440[»]
2HXFelectron microscopy10.00A1-451[»]
2HXHelectron microscopy11.00A1-451[»]
2P4Nelectron microscopy9.00A1-451[»]
2WBEelectron microscopy9.40A1-451[»]
4ABOelectron microscopy8.60B/D/F/H1-451[»]
ProteinModelPortalP02550.
SMRP02550. Positions 1-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP02550. 3 interactions.
MINTMINT-6439698.

Chemistry

BindingDBP02550.
ChEMBLCHEMBL2111354.

Proteomic databases

PaxDbP02550.
PRIDEP02550.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG5023.
HOGENOMHOG000165711.
HOVERGENHBG000089.

Family and domain databases

Gene3D1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProIPR002452. Alpha_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]
PRINTSPR01162. ALPHATUBULIN.
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.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02550.

Entry information

Entry nameTBA1A_PIG
AccessionPrimary (citable) accession number: P02550
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 22, 2014
This is version 104 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