Q9NY65 (TBA8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulin alpha-8 chain

Alternative name(s):
Alpha-tubulin 8
Tubulin alpha chain-like 2

Gene names

Name:	TUBA8
Synonyms:	TUBAL2

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	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	Preferentially expressed in heart, skeletal muscle and testis. Expressed at low levels in the developing brain. Ref.9
Post-translational modification	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.
Involvement in disease	Defects in TUBA8 are the cause of polymicrogyria with optic nerve hypoplasia (PMGONH) [MIM:613180]. It is a disease characterized by extensive polymicrogyria, optic nerve hypoplasia, severe developmental delay, hypotonia, seizures, a dysplastic or absent corpus callosum and colpocephaly. Polymicrogyria is a malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. Ref.6
Miscellaneous	This tubulin does not have a C-terminal tyrosine.
Sequence similarities	Belongs to the tubulin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome 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	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW
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 – 449	449	Tubulin alpha-8 chain		PRO_0000048113
Regions
	Nucleotide binding	142 – 148	7	GTP Potential
Amino acid modifications
	Modified residue	103	1	Phosphotyrosine By similarity
	Modified residue	357	1	Phosphotyrosine By similarity
	Modified residue	370	1	N6-acetyllysine Ref.8
Natural variations
	Natural variant	128	1	A → V. Corresponds to variant rs2234331 [ dbSNP | Ensembl ].		VAR_052670
	Natural variant	301	1	Q → R. Corresponds to variant rs2234333 [ dbSNP | Ensembl ].		VAR_024680

Sequences

	Sequence		Length	Mass (Da)
	Q9NY65 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 8D1AFB9D131529BD	FASTA	449	50,094
	10 20 30 40 50 60 MRECISVHVG QAGVQIGNAC WELFCLEHGI QADGTFDAQA SKINDDDSFT TFFSETGNGK 70 80 90 100 110 120 HVPRAVMIDL 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: 10772959] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle.
[2]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Caudate nucleus.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	"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: 19896110] [Abstract] Cited for: INVOLVEMENT IN PMGONH.
[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]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-370, MASS SPECTROMETRY.
[9]	"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: 20466094] [Abstract] Cited for: TISSUE SPECIFICITY.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ245922 mRNA. Translation: CAB88036.1. CR456600 mRNA. Translation: CAG30486.1. AK315316 mRNA. Translation: BAG37719.1. CH471193 Genomic DNA. Translation: EAW57788.1. BC074827 mRNA. Translation: AAH74827.1. BC104845 mRNA. Translation: AAI04846.1.
IPI	IPI00646909.
RefSeq	NP_001180343.1. NM_001193414.1. NP_061816.1. NM_018943.2.
UniGene	Hs.137400.
3D structure databases
ProteinModelPortal	Q9NY65.
SMR	Q9NY65. Positions 1-439.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NY65. 1 interaction.
MINT	MINT-134532.
STRING	Q9NY65.
PTM databases
PhosphoSite	Q9NY65.
Polymorphism databases
DMDM	12585376.
Proteomic databases
PRIDE	Q9NY65.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000330423; ENSP00000333326; ENSG00000183785.
GeneID	51807.
KEGG	hsa:51807.
UCSC	uc002znv.1. human.
Organism-specific databases
CTD	51807.
GeneCards	GC22P018593.
H-InvDB	HIX0041378. HIX0080241.
HGNC	HGNC:12410. TUBA8.
HPA	CAB046031.
MIM	605742. gene. 613180. phenotype.
neXtProt	NX_Q9NY65.
Orphanet	250972. Polymicrogyria with optic nerve hypoplasia.
PharmGKB	PA37074.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18016.
GeneTree	ENSGT00600000084279.
HOVERGEN	HBG000089.
InParanoid	Q9NY65.
OrthoDB	EOG4QC158.
PhylomeDB	Q9NY65.
Gene expression databases
ArrayExpress	Q9NY65.
CleanEx	HS_TUBA8.
Genevestigator	Q9NY65.
GermOnline	ENSG00000183785. 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.
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	55932.
PMAP-CutDB	Q9NY65.
SOURCE	Search...

Entry information

Entry name

TBA8_HUMAN

Accession

Primary (citable) accession number: Q9NY65
Secondary accession number(s): B2RCX2, Q2M3N4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
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

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.