Q13748 (TBA3C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin alpha-3C/D chain

Alternative name(s):
Alpha-tubulin 2
Alpha-tubulin 3C/D
Tubulin alpha-2 chain

Gene names

Name:	TUBA3C
Synonyms:	TUBA2
AND
Name:	TUBA3D

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	450 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	Testis specific. Ref.5
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-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.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	'de novo' posttranslational protein folding Traceable author statement. Source: Reactome microtubule-based movement 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 Non-traceable author statement. Source: UniProtKB
Molecular function	GTP binding Non-traceable author statement. Source: UniProtKB GTPase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NMI	Q13287	2	EBI-355068,EBI-372942

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13748-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q13748-2)

The sequence of this isoform differs from the canonical sequence as follows:
     393-424: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 450	450	Tubulin alpha-3C/D chain		PRO_0000048110
Regions
	Nucleotide binding	142 – 148	7	GTP Potential
Sites
	Site	450	1	Involved in polymerization
Amino acid modifications
	Modified residue	40	1	N6-acetyllysine By similarity
	Modified residue	48	1	Phosphoserine Ref.6 Ref.8
	Modified residue	51	1	Phosphothreonine Ref.8
Natural variations
	Alternative sequence	393 – 424	32	Missing in isoform 2.		VSP_006678
	Natural variant	75	1	V → L. Corresponds to variant rs36215077 [ dbSNP | Ensembl ].		VAR_034541
	Natural variant	392	1	D → V. Corresponds to variant rs17076703 [ dbSNP | Ensembl ].		VAR_052666
	Natural variant	440	1	V → M. Corresponds to variant rs1803092 [ dbSNP | Ensembl ].		VAR_022068
Experimental info
	Sequence conflict	305	1	C → Y in AAH57810. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 2, 2002. Version 3. Checksum: 2A78714CBA782D55	FASTA	450	49,960
	10 20 30 40 50 60 MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK 70 80 90 100 110 120 HVPRAVFVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIVDLVLD 130 140 150 160 170 180 RIRKLADLCT GLQGFLIFHS FGGGTGSGFA SLLMERLSVD YGKKSKLEFA 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 KYMACCMLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP 370 380 390 400 410 420 TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE 430 440 450 AREDLAALEK DYEEVGVDSV EAEAEEGEEY
	Isoform 2 [UniParc]. Checksum: B103B8C73F95D81B	FASTA	418	46,112
	10 20 30 40 50 60 MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK 70 80 90 100 110 120 HVPRAVFVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIVDLVLD 130 140 150 160 170 180 RIRKLADLCT GLQGFLIFHS FGGGTGSGFA SLLMERLSVD YGKKSKLEFA 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 KYMACCMLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP 370 380 390 400 410 TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDLAALEKDY EEVGVDSVEA EAEEGEEY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence characterization of a newly identified human alpha-tubulin gene (TUBA2)." Dode C., Weil D., Levilliers J., Crozet F., Chaib H., Levi-Acobas F., Guilford P., Petit C. Genomics 47:125-130(1998) [PubMed: 9465305] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[2]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed: 15057823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Skin and Testis.
[5]	"The alpha-tubulin gene on chromosome 13 (TUBA2) encodes a testis-specific isotype." Bonaldo M., Su L., Lawton L.N., Soares M.B. Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 352-449 (ISOFORM 1), TISSUE SPECIFICITY.
[6]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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: 19524510] [Abstract] Cited for: GLYCYLATION.
[8]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND THR-51, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Web resources

Wikipedia

Tubulin entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF005392 Genomic DNA. Translation: AAC39578.1. AL139327 Genomic DNA. Translation: CAH73534.1. CH471075 Genomic DNA. Translation: EAX08210.1. BC011721 mRNA. Translation: AAH11721.1. BC057810 mRNA. Translation: AAH57810.1. L11645 mRNA. Translation: AAA35521.1.
IPI	IPI00179709. IPI00218345.
RefSeq	NP_005992.1. NM_006001.2. NP_525125.2. NM_080386.3.
UniGene	Hs.349695. Hs.503749.
3D structure databases
ProteinModelPortal	Q13748.
SMR	Q13748. Positions 1-438.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13748. 6 interactions.
MINT	MINT-1157262.
STRING	Q13748.
PTM databases
PhosphoSite	Q13748.
Proteomic databases
PRIDE	Q13748.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000321253; ENSP00000326042; ENSG00000075886. ENST00000400113; ENSP00000382982; ENSG00000198033.
GeneID	113457. 7278.
KEGG	hsa:113457. hsa:7278.
UCSC	uc002tsu.2. human.
Organism-specific databases
CTD	113457. 7278.
H-InvDB	HIX0002464.
HGNC	HGNC:12408. TUBA3C. HGNC:24071. TUBA3D.
HPA	CAB004972.
MIM	602528. gene.
neXtProt	NX_Q13748.
PharmGKB	PA162407346.
GenAtlas	Search...
Phylogenomic databases
eggNOG	veNOG08633.
HOGENOM	HBG750007.
HOVERGEN	HBG000089.
InParanoid	Q13748.
OMA	KRATHES.
OrthoDB	EOG44J2HZ.
PhylomeDB	Q13748.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_11123. Membrane Trafficking. REACT_152. Cell Cycle, Mitotic. REACT_17015. Metabolism of proteins. REACT_383. DNA Replication. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	Q13748.
Bgee	Q13748.
CleanEx	HS_TUBA3C. HS_TUBA3D.
Genevestigator	Q13748.
GermOnline	ENSG00000075886. Homo sapiens. ENSG00000198033. Homo sapiens.
Family and domain databases
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]
Gene3D	G3DSA: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.
KO	K07374.
PANTHER	PTHR11588. Tubulin. 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
NextBio	78848.
PMAP-CutDB	Q13748.
SOURCE	Search...

Entry information

Entry name

TBA3C_HUMAN

Accession

Primary (citable) accession number: Q13748
Secondary accession number(s): A6NJQ0 , Q5W099, Q6PEY3, Q96F18

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	May 2, 2002
Last modified:	January 25, 2012
This is version 119 of the entry and version 3 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.