Q71U36 (TBA1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin alpha-1A chain

Alternative name(s):
Alpha-tubulin 3
Tubulin B-alpha-1
Tubulin alpha-3 chain

Gene names

Name:	TUBA1A
Synonyms:	TUBA3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	451 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Subcellular location	Cytoplasm › cytoskeleton.
Tissue specificity	Expressed at a high level in fetal brain. Ref.8
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 polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation 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 glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules Probable. 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.
Involvement in disease	Lissencephaly 3 (LIS3) [MIM:611603]: A classic type lissencephaly associated with psychomotor retardation and seizures. Features include agyria or pachygyria or laminar heterotopia, severe mental retardation, motor delay, variable presence of seizures, and abnormalities of corpus callosum, hippocampus, cerebellar vermis and brainstem. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8
Sequence similarities	Belongs to the tubulin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Polymorphism
Disease	Disease mutation Lissencephaly
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' posttranslational protein folding Traceable author statement. Source: Reactome G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome cell division Traceable author statement PubMed 12090300. Source: BHF-UCL cytoskeleton-dependent intracellular transport Traceable author statement PubMed 12090300. Source: BHF-UCL microtubule-based process Traceable author statement PubMed 12090300. Source: BHF-UCL protein polymerization Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasmic microtubule Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome microtubule Inferred from direct assay PubMed 21525035. Source: UniProtKB
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 structural molecule activity Traceable author statement PubMed 12090300. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 451	451	Tubulin alpha-1A chain		PRO_0000048111
Regions
	Nucleotide binding	142 – 148	7	GTP Potential
Sites
	Site	451	1	Involved in polymerization By similarity
Amino acid modifications
	Modified residue	6	1	Phosphoserine By similarity
Natural variations
	Natural variant	188	1	I → L in LIS3. Ref.8		VAR_039332
	Natural variant	263	1	P → T in LIS3. Ref.8		VAR_039333
	Natural variant	264	1	R → C in LIS3. Ref.8		VAR_039334
	Natural variant	286	1	L → F in LIS3. Ref.8		VAR_039335
	Natural variant	402	1	R → C in LIS3. Ref.8		VAR_039336
	Natural variant	402	1	R → H in LIS3. Ref.8		VAR_039337
	Natural variant	419	1	S → L in LIS3. Ref.8		VAR_039338
	Natural variant	447	1	E → K. Corresponds to variant rs1065730 [ dbSNP | Ensembl ].		VAR_034540
Experimental info
	Sequence conflict	131	1	G → R in CAA25855. Ref.1
	Sequence conflict	131	1	G → R in AAA91575. Ref.7
	Sequence conflict	290	1	E → D in AAA91575. Ref.7
	Sequence conflict	308	1	R → G in CAA25855. Ref.1
	Sequence conflict	308	1	R → G in AAA91575. Ref.7
	Sequence conflict	438	1	D → H in CAA25855. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q71U36 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 00F8429A4A10E5FE	FASTA	451	50,136
	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 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 DYEEVGVDSV EGEGEEEGEE Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural features and restricted expression of a human alpha-tubulin gene." Hall J.L., Cowan N.J. Nucleic Acids Res. 13:207-223(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Tubulins in the primate retina: evidence that xanthophylls may be endogenous ligands for the paclitaxel-binding site." Crabtree D.V., Ojima I., Geng X., Adler A.J. Bioorg. Med. Chem. 9:1967-1976(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: Muscle and Skin.
[6]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 41-60; 65-79; 85-105; 113-121; 157-163; 216-304; 312-320; 327-336; 340-352; 374-390; 395-401 AND 403-430, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[7]	"Expression of human alpha-tubulin genes: interspecies conservation of 3' untranslated regions." Cowan N.J., Dobner P., Fuchs E.V., Cleveland D.W. Mol. Cell. Biol. 3:1738-1745(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 110-451. Tissue: Fetal brain.
[8]	"Large spectrum of lissencephaly and pachygyria phenotypes resulting from de novo missense mutations in tubulin alpha 1A (TUBA1A)." Poirier K., Keays D.A., Francis F., Saillour Y., Bahi N., Manouvrier S., Fallet-Bianco C., Pasquier L., Toutain A., Tuy F.P., Bienvenu T., Joriot S., Odent S., Ville D., Desguerre I., Goldenberg A., Moutard M.L., Fryns J.-P. , van Esch H., Harvey R.J., Siebold C., Flint J., Beldjord C., Chelly J. Hum. Mutat. 28:1055-1064(2007) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, VARIANTS LIS3 LEU-188; THR-263; CYS-264; PHE-286; HIS-402; CYS-402 AND LEU-419.
[9]	"Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation." Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C. Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X01703 Genomic DNA. Translation: CAA25855.1. AF141347 mRNA. Translation: AAD33871.1. AK289483 mRNA. Translation: BAF82172.1. CH471111 Genomic DNA. Translation: EAW58052.1. CH471111 Genomic DNA. Translation: EAW58055.1. BC006468 mRNA. Translation: AAH06468.1. BC050637 mRNA. Translation: AAH50637.1. K00557 mRNA. Translation: AAA91575.1.
IPI	IPI00180675.
RefSeq	NP_001257328.1. NM_001270399.1. NP_001257329.1. NM_001270400.1. NP_006000.2. NM_006009.3.
UniGene	Hs.654422.
3D structure databases
DisProt	DP00178.
ProteinModelPortal	Q71U36.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q71U36. 43 interactions.
MINT	MINT-156132.
STRING	9606.ENSP00000301071.
PTM databases
PhosphoSite	Q71U36.
Polymorphism databases
DMDM	55977864.
Proteomic databases
PaxDb	Q71U36.
PRIDE	Q71U36.
Protocols and materials databases
DNASU	7846.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000295766; ENSP00000439020; ENSG00000167552. ENST00000301071; ENSP00000301071; ENSG00000167552.
GeneID	7846.
KEGG	hsa:7846.
UCSC	uc001rtp.3. human.
Organism-specific databases
CTD	7846.
GeneCards	GC12M049578.
HGNC	HGNC:20766. TUBA1A.
HPA	CAB008686. HPA039247. HPA043684.
MIM	602529. gene. 611603. phenotype.
neXtProt	NX_Q71U36.
Orphanet	171680. Lissencephaly due to TUBA1A mutation.
PharmGKB	PA162407319.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5023.
HOGENOM	HOG000165711.
HOVERGEN	HBG000089.
InParanoid	Q71U36.
KO	K07374.
OMA	ASDDAFN.
OrthoDB	EOG44J2HZ.
PhylomeDB	Q71U36.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_11123. Membrane Trafficking. REACT_115566. Cell Cycle. REACT_17015. Metabolism of proteins. REACT_21300. Mitotic M-M/G1 phases. REACT_604. Hemostasis. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q71U36.
Bgee	Q71U36.
CleanEx	HS_TUBA1A.
Genevestigator	Q71U36.
GermOnline	ENSG00000167552. Homo sapiens.
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...
Other
BindingDB	Q71U36.
ChEMBL	CHEMBL3661.
ChiTaRS	TUBA1A. human.
GenomeRNAi	7846.
NextBio	30260.
PMAP-CutDB	Q71U36.
SOURCE	Search...

Entry information

Entry name

TBA1A_HUMAN

Accession

Primary (citable) accession number: Q71U36
Secondary accession number(s): A8K0B8, P04687, P05209

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.