P68373 (TBA1C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin alpha-1C chain

Alternative name(s):
Alpha-tubulin 6
Alpha-tubulin isotype M-alpha-6
Tubulin alpha-6 chain

Gene names

Name:	Tuba1c
Synonyms:	Tuba6

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	449 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	Minor alpha-tubulin expressed in all tissues. 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 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 Nitration Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	microtubule-based process Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasmic microtubule Inferred from direct assay PubMed 19103752. Source: MGI
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-1C chain		PRO_0000048124
Regions
	Nucleotide binding	142 – 148	7	GTP Potential
Sites
	Site	449	1	Involved in polymerization
Amino acid modifications
	Modified residue	282	1	Nitrated tyrosine Ref.6
	Modified residue	432	1	Phosphotyrosine By similarity
	Modified residue	439	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	167	1	L → P in BAB28608. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P68373 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 0DA9F082D9DC8549	FASTA	449	49,909
	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 ISQIVSSITA 250 260 270 280 290 300 SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLTVAE 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 AREDMAALEK DYEEVGADSA EGDDEGEEY

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"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]. Strain: FVB/N. Tissue: Liver and Mammary tumor.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-449. Strain: C57BL/6J. Tissue: Embryo.
[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; 374-390; 395-401 AND 403-430, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[5]	"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] [Europe PMC] [Abstract] Cited for: POLYGLUTAMYLATION.
[6]	"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease." Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J. Biochemistry 45:8009-8022(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-282, MASS SPECTROMETRY. Tissue: Brain.
[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] [Europe PMC] [Abstract] Cited for: POLYGLYCYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M13441 mRNA. Translation: AAA40503.1. BC004745 mRNA. Translation: AAH04745.1. BC022182 mRNA. Translation: AAH22182.1. BC026753 mRNA. Translation: AAH26753.1. AK013029 mRNA. Translation: BAB28608.1.
IPI	IPI00403810.
PIR	I77428. PH0108.
RefSeq	NP_033474.1. NM_009448.4.
UniGene	Mm.88212.
3D structure databases
ProteinModelPortal	P68373.
SMR	P68373. Positions 1-436.
ModBase	Search...
Protein-protein interaction databases
IntAct	P68373. 7 interactions.
PTM databases
PhosphoSite	P68373.
2D gel databases
REPRODUCTION-2DPAGE	P68373.
SWISS-2DPAGE	P99040.
Proteomic databases
PaxDb	P68373.
PRIDE	P68373.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000058914; ENSMUSP00000051033; ENSMUSG00000043091.
GeneID	22146.
KEGG	mmu:22146.
Organism-specific databases
CTD	84790.
MGI	MGI:1095409. Tuba1c.
Phylogenomic databases
eggNOG	COG5023.
HOGENOM	HOG000165711.
HOVERGEN	HBG000089.
InParanoid	P68373.
KO	K07374.
OMA	CDSKREC.
OrthoDB	EOG44J2HZ.
Enzyme and pathway databases
Reactome	REACT_147847. Translocation of Glut4 to the Plasma Membrane. REACT_88307. Membrane Trafficking.
Gene expression databases
ArrayExpress	P68373.
Bgee	P68373.
CleanEx	MM_TUBA1C.
Genevestigator	P68373.
GermOnline	ENSMUSG00000043091. Mus musculus.
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
NextBio	302054.
SOURCE	Search...

Entry information

Entry name

TBA1C_MOUSE

Accession

Primary (citable) accession number: P68373
Secondary accession number(s): P05216, Q9CSE9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program