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P81947 (TBA1B_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Tubulin alpha-1B chain
Alternative name(s):
Alpha-tubulin ubiquitous
Tubulin K-alpha-1
Tubulin alpha-ubiquitous chain
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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 By similarity.

Subcellular location

Cytoplasm › cytoskeleton.

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 By similarity.

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.

Sequence similarities

Belongs to the tubulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Tubulin alpha-1B chain
PRO_0000048114

Regions

Nucleotide binding142 – 1487GTP Potential

Sites

Site4511Involved in polymerization By similarity

Amino acid modifications

Modified residue401N6-acetyllysine By similarity
Modified residue411Phosphothreonine By similarity
Modified residue481Phosphoserine By similarity
Modified residue2321Phosphoserine By similarity
Modified residue2721Phosphotyrosine By similarity
Modified residue3341Phosphothreonine By similarity
Modified residue3391Omega-N-methylarginine By similarity
Modified residue3401Phosphoserine By similarity
Modified residue4321Phosphotyrosine By similarity
Modified residue4391Phosphoserine By similarity
Modified residue4511Phosphotyrosine By similarity
Cross-link326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Secondary structure

1 .................................................................... 451
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P81947 [UniParc].

Last modified February 10, 2009. Version 2.
Checksum: 94355B4EC2086429

FASTA45150,152
        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 GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA 

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

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

       310        320        330        340        350        360 
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP 

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

       430        440        450 
AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Uterus.
[2]"Differential assembly kinetics of alpha-tubulin isoforms in the presence of paclitaxel."
Banerjee A., Kasmala L.T.
Biochem. Biophys. Res. Commun. 245:349-351(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 430-451.
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC146060 mRNA. Translation: AAI46061.1.
IPIIPI00700865.
RefSeqNP_001108328.1. NM_001114856.1.
UniGeneBt.106995.
Bt.109492.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DCOelectron microscopy1.90A1-451[»]
3EDLelectron microscopy28.00A/F1-451[»]
3J1Telectron microscopy9.70B1-451[»]
3J1Uelectron microscopy9.70B1-451[»]
3J2Uelectron microscopy10.80A/C1-451[»]
4I4TX-ray1.80A/C1-450[»]
4I50X-ray2.30A/C1-451[»]
4I55X-ray2.20A/C1-450[»]
4IHJX-ray2.00A/C1-450[»]
4IIJX-ray2.60A/C1-451[»]
ProteinModelPortalP81947.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-235448.

Proteomic databases

PaxDbP81947.
PRIDEP81947.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000016242; ENSBTAP00000016242; ENSBTAG00000012244.
GeneID539882.
KEGGbta:539882.

Organism-specific databases

CTD10376.

Phylogenomic databases

eggNOGCOG5023.
GeneTreeENSGT00690000101720.
HOGENOMHOG000165711.
HOVERGENHBG000089.
InParanoidA6H700.
KOK07374.
OMAKRATHES.
OrthoDBEOG4JWVDD.

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]
SUPFAMSSF55307. Tub_FtsZ_C. 1 hit.
SSF52490. Tubulin_FtsZ. 1 hit.
PROSITEPS00227. TUBULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP81947.
NextBio20878279.

Entry information

Entry nameTBA1B_BOVIN
AccessionPrimary (citable) accession number: P81947
Secondary accession number(s): A6H700
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: February 10, 2009
Last modified: May 1, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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