Q9JJZ2 (TBA8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin alpha-8 chain

Alternative name(s):
Alpha-tubulin 8

Gene names

Name:

Tuba8

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	Expressed at highest levels in the testis, followed by skeletal and heart muscle. Expressed at low levels in the developing brain. Ref.2
Developmental stage	At embryonic day (E) 13.5, expressed in the cortical preplate and cingulate cortex. By E15. 5, the strongest expression is seen in the cortical plate. By E18.5, cortical expression is most intense in the upper layers and subplate. There is strong expression in the areas CA1-3 of the hippocampus. At P0, cortical expression is strongest in the dense cortical plate and subplate. Hippocampal expression is more intense in areas CA1-3 than in the dentate gyrus. At P8, lamination is almost complete and cortical expression is strongest in layers II-III and V and the subplate. There is also expression in the mediodorsal nuclei of the thalamus, the mitral cell layer of the olfactory bulb, and the external granular layer, molecular layer, and internal granular cell layer of the cerebellum. Ref.2 Ref.8
Post-translational modification	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.
Miscellaneous	This tubulin does not have a C-terminal tyrosine.
Sequence similarities	Belongs to the tubulin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	microtubule cytoskeleton organization Inferred from sequence alignment Ref.1. Source: MGI protein polymerization Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from sequence alignment Ref.1. 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 sequence alignment Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 449	449	Tubulin alpha-8 chain		PRO_0000048125
Regions
	Nucleotide binding	142 – 148	7	GTP Potential
Amino acid modifications
	Modified residue	103	1	Phosphotyrosine Ref.7
	Modified residue	357	1	Phosphotyrosine Ref.7
Experimental info
	Sequence conflict	447	1	E → G in BAB26288. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9JJZ2 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: AA979E2DB21FC5DD	FASTA	449	50,052
	10 20 30 40 50 60 MRECISVHVG QAGVQIGNAC WELFCLEHGI QADGTFGTQA SKINDDDSFT TFFSETGNGK 70 80 90 100 110 120 HVPRAVMVDL EPTVVDEVRA GTYRQLFHPE QLITGKEDAA NNYARGHYTV GKESIDLVLD 130 140 150 160 170 180 RIRKLTDACS GLQGFLIFHS FGGGTGSGFT SLLMERLSLD YGKKSKLEFA IYPAPQVSTA 190 200 210 220 230 240 VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA 250 260 270 280 290 300 SLRFDGALNV DLTEFQTNLV PYPRIHFPLV TYAPIISAEK AYHEQLSVAE ITSSCFEPNS 310 320 330 340 350 360 QMVKCDPRHG KYMACCMLYR GDVVPKDVNV AIAAIKTKRT IQFVDWCPTG FKVGINYQPP 370 380 390 400 410 420 TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE 430 440 AREDLAALEK DYEEVGTDSF EEENEGEEF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"TUBA8: a new tissue-specific isoform of alpha-tubulin that is highly conserved in human and mouse." Stanchi F., Corso V., Scannapieco P., Ievolella C., Negrisolo E., Tiso N., Lanfranchi G., Valle G. Biochem. Biophys. Res. Commun. 270:1111-1118(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle.
[2]	"Tuba8 is expressed at low levels in the developing mouse and human brain." Braun A., Breuss M., Salzer M.C., Flint J., Cowan N.J., Keays D.A. Am. J. Hum. Genet. 86:819-822(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6. Tissue: Olfactory bulb.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Eye.
[5]	"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 118-449. Strain: C57BL/6J. Tissue: Tongue.
[6]	"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.
[7]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-103 AND TYR-357, MASS SPECTROMETRY. Tissue: Brain.
[8]	"Mutation of the variant alpha-tubulin TUBA8 results in polymicrogyria with optic nerve hypoplasia." Abdollahi M.R., Morrison E., Sirey T., Molnar Z., Hayward B.E., Carr I.M., Springell K., Woods C.G., Ahmed M., Hattingh L., Corry P., Pilz D.T., Stoodley N., Crow Y., Taylor G.R., Bonthron D.T., Sheridan E. Am. J. Hum. Genet. 85:737-744(2009) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[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: POLYGLYCYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ245923 mRNA. Translation: CAB88033.1. GU591980 mRNA. Translation: ADD82895.1. CH466523 Genomic DNA. Translation: EDK99659.1. BC017631 mRNA. Translation: AAH17631.1. AK009439 mRNA. Translation: BAB26288.1.
IPI	IPI00311175.
RefSeq	NP_059075.1. NM_017379.1.
UniGene	Mm.32884.
3D structure databases
ProteinModelPortal	Q9JJZ2.
SMR	Q9JJZ2. Positions 1-438.
ModBase	Search...
PTM databases
PhosphoSite	Q9JJZ2.
Proteomic databases
PRIDE	Q9JJZ2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000032233; ENSMUSP00000032233; ENSMUSG00000030137.
GeneID	53857.
KEGG	mmu:53857.
Organism-specific databases
CTD	51807.
MGI	MGI:1858225. Tuba8.
Phylogenomic databases
GeneTree	ENSGT00700000104224.
HOGENOM	HOG000165711.
HOVERGEN	HBG000089.
InParanoid	Q9JJZ2.
KO	K07374.
OMA	DGTFGAQ.
OrthoDB	EOG4QC158.
Enzyme and pathway databases
Reactome	REACT_147847. Translocation of Glut4 to the Plasma Membrane. REACT_88307. Membrane Trafficking.
Gene expression databases
Bgee	Q9JJZ2.
CleanEx	MM_TUBA8.
Genevestigator	Q9JJZ2.
GermOnline	ENSMUSG00000030137. 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	310689.
SOURCE	Search...

Entry information

Entry name

TBA8_MOUSE

Accession

Primary (citable) accession number: Q9JJZ2
Secondary accession number(s): D4P911, Q9CV57

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program