P08537 (TBA_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin alpha chain

Gene names

Name:	tuba
Synonyms:	tuba1

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	449 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
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. 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.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation
Gene Ontology (GO)
Biological_process	microtubule-based process Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro structural constituent of cytoskeleton Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 449	449	Tubulin alpha chain		PRO_0000048238
Regions
	Nucleotide binding	142 – 148	7	GTP Potential
Sites
	Site	449	1	Involved in polymerization
Amino acid modifications
	Modified residue	40	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	154	1	M → L in CAA30094. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P08537 [UniParc]. Last modified November 14, 2006. Version 2. Checksum: 9A5B8497FA27FF8C	FASTA	449	49,879
	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 YGKKSKLEFA IYPAPQVSTA 190 200 210 220 230 240 VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA 250 260 270 280 290 300 SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLTVAD 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 AREDMAALEK DYEEVGADSA DAEDEGEEY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X07046 mRNA. Translation: CAA30094.1. X07045 Genomic DNA. Translation: CAA30093.1. BC097546 mRNA. Translation: AAH97546.1. BC106207 mRNA. Translation: AAI06208.1.
PIR	S00253.
RefSeq	NP_001095253.1. NM_001101783.1. NP_001165669.1. NM_001172198.1.
UniGene	Xl.13561. Xl.66058.
3D structure databases
ProteinModelPortal	P08537.
SMR	P08537. Positions 1-439.
ModBase	Search...
Protein-protein interaction databases
IntAct	P08537. 1 interaction.
Proteomic databases
PRIDE	P08537.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100337592. 399313.
KEGG	xla:100337592. xla:399313.
Organism-specific databases
CTD	10376. 112714.
Xenbase	XB-GENE-6464328. tuba3e.
Phylogenomic databases
HOVERGEN	HBG000089.
KO	K07374.
Family and domain databases
Gene3D	1.10.287.600. 1 hit. 3.30.1330.20. 1 hit. 3.40.50.1440. 1 hit.
InterPro	IPR002452. 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]
PANTHER	PTHR11588. PTHR11588. 1 hit.
Pfam	PF00091. Tubulin. 1 hit. PF03953. Tubulin_C. 1 hit. [Graphical view]
PRINTS	PR01162. ALPHATUBULIN. PR01161. TUBULIN.
SMART	SM00864. Tubulin. 1 hit. SM00865. Tubulin_C. 1 hit. [Graphical view]
SUPFAM	SSF55307. Tub_FtsZ_C. 1 hit. SSF52490. Tubulin_FtsZ. 1 hit.
PROSITE	PS00227. TUBULIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TBA_XENLA

Accession

Primary (citable) accession number: P08537
Secondary accession number(s): Q4V850

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	November 14, 2006
Last modified:	May 1, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program