Q9NY65 (TBA8_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 103.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Tubulin alpha-8 chain Alternative name(s): Alpha-tubulin 8 Tubulin alpha chain-like 2 | ||||
| Gene names |
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| 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 | |
| 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 polymerizationInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubuleInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activityInferred from electronic annotation. Source: InterPro structural molecule activityInferred 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
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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 |
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| 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. | ||||||||
Relevant documents
| Human chromosome 22 Human chromosome 22: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with