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Protein

Tubulin alpha-1A chain

Gene

Tuba1a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei451 – 4511Involved in polymerization

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1487GTPSequence analysis

GO - Molecular functioni

  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • protein domain specific binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  • microtubule-based process Source: RGD
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-RNO-380259. Loss of Nlp from mitotic centrosomes.
R-RNO-380270. Recruitment of mitotic centrosome proteins and complexes.
R-RNO-5610787. Hedgehog 'off' state.
R-RNO-5620912. Anchoring of the basal body to the plasma membrane.
R-RNO-5620924. Intraflagellar transport.
R-RNO-5632684. Hedgehog 'on' state.
R-RNO-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-1A chain
Alternative name(s):
Alpha-tubulin 1
Tubulin alpha-1 chain
Gene namesi
Name:Tuba1a
Synonyms:Tuba1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi619717. Tuba1a.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic microtubule Source: Ensembl
  • cytoplasmic ribonucleoprotein granule Source: Ensembl
  • extracellular exosome Source: Ensembl
  • microtubule Source: RGD
  • myelin sheath Source: UniProtKB
  • nucleus Source: Ensembl
  • recycling endosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4139.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Tubulin alpha-1A chainPRO_0000048126Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei282 – 2821Nitrated tyrosineBy similarity
Modified residuei439 – 4391PhosphoserineBy similarity
Modified residuei445 – 44515-glutamyl polyglutamateBy similarity

Post-translational modificationi

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.1 Publication
Some glutamate residues at the C-terminus are polyglycylated, resulting in 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 polyglycylation is still unclear.By similarity
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity).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).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Nitration, Phosphoprotein

Proteomic databases

PaxDbiP68370.
PRIDEiP68370.

PTM databases

iPTMnetiP68370.
PhosphoSiteiP68370.

Expressioni

Gene expression databases

GenevisibleiP68370. RN.

Interactioni

Subunit structurei

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.

GO - Molecular functioni

  • protein domain specific binding Source: RGD
  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi248985. 20 interactions.
IntActiP68370. 6 interactions.
MINTiMINT-236000.
STRINGi10116.ENSRNOP00000006322.

Chemistry

BindingDBiP68370.

Structurei

3D structure databases

ProteinModelPortaliP68370.
SMRiP68370. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP68370.
KOiK07374.
OMAiGSKRECI.
OrthoDBiEOG7TBC1W.
PhylomeDBiP68370.
TreeFamiTF300314.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. 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]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P68370-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN
60 70 80 90 100
TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440 450
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE

Y
Length:451
Mass (Da):50,136
Last modified:July 21, 1986 - v1
Checksum:i00F8429A4A10E5FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti326 – 3261K → R in AAH62238 (PubMed:15489334).Curated
Sequence conflicti340 – 3401T → S in CAA24536 (PubMed:6269058).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01227 mRNA. Translation: CAA24537.1.
J00798, J00797 Genomic DNA. Translation: AAA42306.1.
BC062238 mRNA. Translation: AAH62238.1.
BC078830 mRNA. Translation: AAH78830.1.
V01226 mRNA. Translation: CAA24536.1.
PIRiA92869. UBRTA.
RefSeqiNP_071634.1. NM_022298.1.
UniGeneiRn.234326.
Rn.99661.

Genome annotation databases

EnsembliENSRNOT00000083156; ENSRNOP00000075232; ENSRNOG00000060728.
GeneIDi64158.
KEGGirno:64158.
UCSCiRGD:619717. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01227 mRNA. Translation: CAA24537.1.
J00798, J00797 Genomic DNA. Translation: AAA42306.1.
BC062238 mRNA. Translation: AAH62238.1.
BC078830 mRNA. Translation: AAH78830.1.
V01226 mRNA. Translation: CAA24536.1.
PIRiA92869. UBRTA.
RefSeqiNP_071634.1. NM_022298.1.
UniGeneiRn.234326.
Rn.99661.

3D structure databases

ProteinModelPortaliP68370.
SMRiP68370. Positions 1-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248985. 20 interactions.
IntActiP68370. 6 interactions.
MINTiMINT-236000.
STRINGi10116.ENSRNOP00000006322.

Chemistry

BindingDBiP68370.
ChEMBLiCHEMBL4139.

PTM databases

iPTMnetiP68370.
PhosphoSiteiP68370.

Proteomic databases

PaxDbiP68370.
PRIDEiP68370.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000083156; ENSRNOP00000075232; ENSRNOG00000060728.
GeneIDi64158.
KEGGirno:64158.
UCSCiRGD:619717. rat.

Organism-specific databases

CTDi7846.
RGDi619717. Tuba1a.

Phylogenomic databases

eggNOGiKOG1376. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP68370.
KOiK07374.
OMAiGSKRECI.
OrthoDBiEOG7TBC1W.
PhylomeDBiP68370.
TreeFamiTF300314.

Enzyme and pathway databases

ReactomeiR-RNO-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-RNO-380259. Loss of Nlp from mitotic centrosomes.
R-RNO-380270. Recruitment of mitotic centrosome proteins and complexes.
R-RNO-5610787. Hedgehog 'off' state.
R-RNO-5620912. Anchoring of the basal body to the plasma membrane.
R-RNO-5620924. Intraflagellar transport.
R-RNO-5632684. Hedgehog 'on' state.
R-RNO-8854518. AURKA Activation by TPX2.

Miscellaneous databases

PROiP68370.

Gene expression databases

GenevisibleiP68370. RN.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. 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]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence and evolution of a mammalian alpha-tubulin messenger RNA."
    Lemischka I.R., Farmer S., Racaniello V.R., Sharp P.A.
    J. Mol. Biol. 151:101-120(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The sequences of an expressed rat alpha-tubulin gene and a pseudogene with an inserted repetitive element."
    Lemischka I., Sharp P.A.
    Nature 300:330-335(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney, Pituitary and Testis.
  4. Lubec G., Chen W.-Q., Afjehi-Sadat L., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 41-60; 65-79; 85-96; 113-121; 216-280; 312-320; 340-370; 391-401 AND 403-422, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  5. "The nucleotide sequence of rat alpha-tubulin: 3'-end characteristics, and evolutionary conservation."
    Ginzburg I., Behar L., Givol D., Littauer U.Z.
    Nucleic Acids Res. 9:2691-2697(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 307-451.
  6. "Tubulin tyrosine ligase: protein and mRNA expression in developing rat skeletal muscle."
    Arregui C.O., Mas C.R., Argarana C.E., Barra H.S.
    Dev. Growth Differ. 39:167-178(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TYROSINATION.

Entry informationi

Entry nameiTBA1A_RAT
AccessioniPrimary (citable) accession number: P68370
Secondary accession number(s): P02551
, P05210, P05212, Q6P6G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 6, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.