P68369 (TBA1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin alpha-1A chain

Alternative name(s):
Alpha-tubulin 1
Alpha-tubulin isotype M-alpha-1
Tubulin alpha-1 chain

Gene names

Name:	Tuba1a
Synonyms:	Tuba1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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	Ubiquitously expressed, although primarily in lung and brain. Ref.1
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 either polyglutamylated or polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or 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 such modifications is still unclear but they are regulate the assembly and dynamics of axonemal microtubules. 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
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	microtubule-based movement Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasmic microtubule Inferred from direct assay. Source: MGI
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro structural molecule activity 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 – 451	451	Tubulin alpha-1A chain		PRO_0000048120
Regions
	Nucleotide binding	142 – 148	7	GTP Potential
Sites
	Site	451	1	Involved in polymerization
Amino acid modifications
	Modified residue	6	1	Phosphoserine Ref.6
	Modified residue	40	1	N6-acetyllysine By similarity
	Modified residue	48	1	Phosphoserine By similarity
	Modified residue	272	1	Phosphotyrosine By similarity
	Modified residue	439	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	124	1	K → E in BAE40598. Ref.2
	Sequence conflict	132	1	L → P in BAE26417. Ref.2
	Sequence conflict	257	1	T → I in BAE37745. Ref.2
	Sequence conflict	273	1	A → S in AAH83344. Ref.3
	Sequence conflict	328	1	V → G in BAE26417. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P68369 [UniParc]. Last modified July 21, 1986. 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]	"Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis-specific expression of two sister genes." Villasante A., Wang D., Dobner P., Dolph P., Lewis S.A., Cowan N.J. Mol. Cell. Biol. 6:2409-2419(1986) [PubMed: 3785200] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Heart, Kidney, Placenta, Spinal ganglion and Thymus.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain and Olfactory epithelium.
[4]	Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 41-60; 65-79; 85-121; 157-163; 216-280; 312-320; 327-336; 340-370; 374-401 AND 403-440, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[5]	"Five mouse tubulin isotypes and their regulated expression during development." Lewis S.A., Lee M.G.-S., Cowan N.J. J. Cell Biol. 101:852-861(1985) [PubMed: 3839797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 254-451.
[6]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed: 15345747] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, MASS SPECTROMETRY. Tissue: Embryonic brain.
[7]	"Tubulin polyglutamylase enzymes are members of the TTL domain protein family." Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M., Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S., Gaertig J., Edde B. Science 308:1758-1762(2005) [PubMed: 15890843] [Abstract] Cited for: POLYGLUTAMYLATION.
[8]	"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: POLYGLYCYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M13445 mRNA. Translation: AAA40499.1. AK077529 mRNA. Translation: BAC36848.1. AK145404 mRNA. Translation: BAE26417.1. AK146983 mRNA. Translation: BAE27586.1. AK164335 mRNA. Translation: BAE37745.1. AK167687 mRNA. Translation: BAE39734.1. AK168762 mRNA. Translation: BAE40598.1. AK169610 mRNA. Translation: BAE41258.1. BC056169 mRNA. Translation: AAH56169.1. BC083343 mRNA. Translation: AAH83343.1. BC083345 mRNA. Translation: AAH83345.1. BC085256 mRNA. Translation: AAH85256.1. M28729 mRNA. Translation: AAA40506.1. BC083344 mRNA. Translation: AAH83344.1.
IPI	IPI00110753.
PIR	I77424.
RefSeq	NP_035783.1. NM_011653.2.
UniGene	Mm.439690.
3D structure databases
ProteinModelPortal	P68369.
SMR	P68369. Positions 1-438.
ModBase	Search...
Protein-protein interaction databases
IntAct	P68369. 9 interactions.
MINT	MINT-3288915.
STRING	P68369.
PTM databases
PhosphoSite	P68369.
2D gel databases
SWISS-2DPAGE	P68369.
Proteomic databases
PRIDE	P68369.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000097014; ENSMUSP00000094778; ENSMUSG00000072235.
GeneID	22142.
KEGG	mmu:22142.
Organism-specific databases
CTD	7846.
MGI	MGI:98869. Tuba1a.
Phylogenomic databases
GeneTree	ENSGT00600000084100.
HOVERGEN	HBG000089.
InParanoid	P68369.
OMA	ANHEANS.
OrthoDB	EOG44J2HZ.
PhylomeDB	P68369.
Gene expression databases
ArrayExpress	P68369.
Bgee	P68369.
CleanEx	MM_TUBA1A.
Genevestigator	P68369.
GermOnline	ENSMUSG00000072235. Mus musculus.
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	302038.
PMAP-CutDB	P68369.
SOURCE	Search...

Entry information

Entry name

TBA1A_MOUSE

Accession

Primary (citable) accession number: P68369
Secondary accession number(s): P02551 , P05210, P05212, Q3TGF0, Q3TIW2, Q3TPJ1, Q3ULN1, Q5XJF8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 25, 2012
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program