Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tubulin alpha chain

Gene

tuba

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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
Sitei449 – 4491Involved in polymerization

Regions

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

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  1. GTP catabolic process Source: InterPro
  2. microtubule-based process Source: InterPro
  3. protein polymerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha chain
Gene namesi
Name:tuba
Synonyms:tuba1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6464328. tuba3e.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Tubulin alpha chainPRO_0000048238Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401N6-acetyllysineBy 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.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

Proteomic databases

PRIDEiP08537.

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.

Protein-protein interaction databases

IntActiP08537. 1 interaction.
MINTiMINT-1204896.

Structurei

3D structure databases

ProteinModelPortaliP08537.
SMRiP08537. Positions 1-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

HOVERGENiHBG000089.
KOiK07374.

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.

P08537-1 [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 YGKKSKLEFA IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLTVAD ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGADSA DAEDEGEEY
Length:449
Mass (Da):49,879
Last modified:November 14, 2006 - v2
Checksum:i9A5B8497FA27FF8C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541M → L in CAA30094 (PubMed:3342025).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07046 mRNA. Translation: CAA30094.1.
X07045 Genomic DNA. Translation: CAA30093.1.
BC097546 mRNA. Translation: AAH97546.1.
BC106207 mRNA. Translation: AAI06208.1.
PIRiS00253.
RefSeqiNP_001095253.1. NM_001101783.1.
NP_001165669.1. NM_001172198.1.
UniGeneiXl.13561.
Xl.66058.

Genome annotation databases

GeneIDi100337592.
399313.
KEGGixla:100337592.
xla:399313.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07046 mRNA. Translation: CAA30094.1.
X07045 Genomic DNA. Translation: CAA30093.1.
BC097546 mRNA. Translation: AAH97546.1.
BC106207 mRNA. Translation: AAI06208.1.
PIRiS00253.
RefSeqiNP_001095253.1. NM_001101783.1.
NP_001165669.1. NM_001172198.1.
UniGeneiXl.13561.
Xl.66058.

3D structure databases

ProteinModelPortaliP08537.
SMRiP08537. Positions 1-439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP08537. 1 interaction.
MINTiMINT-1204896.

Proteomic databases

PRIDEiP08537.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100337592.
399313.
KEGGixla:100337592.
xla:399313.

Organism-specific databases

CTDi10376.
112714.
XenbaseiXB-GENE-6464328. tuba3e.

Phylogenomic databases

HOVERGENiHBG000089.
KOiK07374.

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. "The complete sequence of a frog alpha-tubulin gene and its regulated expression in mouse L-cells."
    Smith D.J.
    Biochem. J. 249:465-472(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.

Entry informationi

Entry nameiTBA_XENLA
AccessioniPrimary (citable) accession number: P08537
Secondary accession number(s): Q4V850
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 14, 2006
Last modified: March 4, 2015
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.