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Q2HJ86 (TBA1D_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 48. 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-1D chain
Gene names
Name:TUBA1D
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length452 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 By similarity.

Subunit structure

Dimer of alpha and beta chains By similarity.

Subcellular location

Cytoplasm › cytoskeleton By similarity.

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-tubulins 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 – 452452Tubulin alpha-1D chain
PRO_0000288849

Regions

Nucleotide binding142 – 1487GTP Potential

Sites

Site4521Involved in polymerization By similarity

Amino acid modifications

Modified residue61Phosphoserine By similarity
Modified residue401N6-acetyllysine By similarity
Modified residue2721Phosphotyrosine By similarity

Secondary structure

1 ........................................................ 452
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q2HJ86 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: BF41F4296CAC7A56

FASTA45250,283
        10         20         30         40         50         60 
MRECISVHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK 

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

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

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

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

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

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

       430        440        450 
AREDMAALEK DYEEVGMDSV EGEGEEEEGD EY

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Uterus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC113253 mRNA. Translation: AAI13254.1.
IPIIPI00705899.
RefSeqNP_001039875.1. NM_001046410.1.
UniGeneBt.55718.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JFFX-ray3.50A1-447[»]
1SA0X-ray3.58A/C1-447[»]
1SA1X-ray4.20A/C1-447[»]
1TVKX-ray2.89A1-440[»]
1Z2BX-ray4.10A/C1-448[»]
2XRPelectron microscopy8.20B/D/F/H1-449[»]
ProteinModelPortalQ2HJ86.
SMRQ2HJ86. Positions 1-440.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2HJ86.

Proteomic databases

PRIDEQ2HJ86.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000038369; ENSBTAP00000038183; ENSBTAG00000030973.
GeneID535605.
KEGGbta:535605.

Organism-specific databases

CTD535605.

Phylogenomic databases

eggNOGmaNOG08063.
GeneTreeENSGT00600000084100.
HOVERGENHBG000089.
InParanoidQ2HJ86.
OMAPNFDSLN.
OrthoDBEOG44J2HZ.
PhylomeDBQ2HJ86.

Family and domain databases

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]
Gene3DG3DSA:3.30.1330.20. Tubulin/FtsZ_2-layer-sand-dom. 1 hit.
G3DSA:1.10.287.600. Tubulin_C. 1 hit.
G3DSA:3.40.50.1440. Tubulin_FtsZ. 1 hit.
KOK07374.
PANTHERPTHR11588. Tubulin. 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...

Entry information

Entry nameTBA1D_BOVIN
AccessionPrimary (citable) accession number: Q2HJ86
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: March 21, 2006
Last modified: November 16, 2011
This is version 48 of the entry and version 1 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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