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Entry version 166 (16 Oct 2019)
Sequence version 1 (05 Jul 2004)
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Protein

Tubulin alpha-1A chain

Gene

TUBA1A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei451Involved in polymerizationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi142 – 148GTPSequence analysis7

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-HSA-190861 Gap junction assembly
R-HSA-2132295 MHC class II antigen presentation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition
R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-380259 Loss of Nlp from mitotic centrosomes
R-HSA-380270 Recruitment of mitotic centrosome proteins and complexes
R-HSA-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
R-HSA-389957 Prefoldin mediated transfer of substrate to CCT/TriC
R-HSA-389960 Formation of tubulin folding intermediates by CCT/TriC
R-HSA-389977 Post-chaperonin tubulin folding pathway
R-HSA-437239 Recycling pathway of L1
R-HSA-5610787 Hedgehog 'off' state
R-HSA-5617833 Cilium Assembly
R-HSA-5620912 Anchoring of the basal body to the plasma membrane
R-HSA-5620924 Intraflagellar transport
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-6807878 COPI-mediated anterograde transport
R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-HSA-68877 Mitotic Prometaphase
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854518 AURKA Activation by TPX2
R-HSA-8955332 Carboxyterminal post-translational modifications of tubulin
R-HSA-9609736 Assembly and cell surface presentation of NMDA receptors
R-HSA-9619483 Activation of AMPK downstream of NMDARs
R-HSA-983189 Kinesins

SIGNOR Signaling Network Open Resource

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SIGNORi
Q71U36

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Tubulin alpha-1A chain
Alternative name(s):
Alpha-tubulin 3
Tubulin B-alpha-1
Tubulin alpha-3 chain
Cleaved into the following chain:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TUBA1A
Synonyms:TUBA3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:20766 TUBA1A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602529 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q71U36

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Lissencephaly 3 (LIS3)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA classic type lissencephaly associated with psychomotor retardation and seizures. Features include agyria or pachygyria or laminar heterotopia, severe mental retardation, motor delay, variable presence of seizures, and abnormalities of corpus callosum, hippocampus, cerebellar vermis and brainstem.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_039332188I → L in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853045EnsemblClinVar.1
Natural variantiVAR_039333263P → T in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853046EnsemblClinVar.1
Natural variantiVAR_039334264R → C in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853043EnsemblClinVar.1
Natural variantiVAR_039335286L → F in LIS3. 1 Publication1
Natural variantiVAR_039336402R → C in LIS3. 1 PublicationCorresponds to variant dbSNP:rs587784483EnsemblClinVar.1
Natural variantiVAR_039337402R → H in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853044EnsemblClinVar.1
Natural variantiVAR_078711402R → L in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853044EnsemblClinVar.1
Natural variantiVAR_039338419S → L in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853047EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Lissencephaly

Organism-specific databases

DisGeNET

More...
DisGeNETi
7846

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
TUBA1A

MalaCards human disease database

More...
MalaCardsi
TUBA1A
MIMi611603 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000167552

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
171680 Lissencephaly due to TUBA1A mutation
467166 Tubulinopathy-associated dysgyria

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA162407319

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q71U36

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3661

Drug and drug target database

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DrugBanki
DB07574 2-MERCAPTO-N-[1,2,3,10-TETRAMETHOXY-9-OXO-5,6,7,9-TETRAHYDRO-BENZO[A]HEPTALEN-7-YL]ACETAMIDE
DB00518 Albendazole
DB11638 Artenimol
DB05147 CYT997
DB01873 Epothilone D
DB00643 Mebendazole
DB03010 Patupilone
DB12695 Phenethyl Isothiocyanate
DB00570 Vinblastine

DrugCentral

More...
DrugCentrali
Q71U36

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TUBA1A

Domain mapping of disease mutations (DMDM)

More...
DMDMi
55977864

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000481111 – 451Tubulin alpha-1A chainAdd BLAST451
ChainiPRO_00004373781 – 450Detyrosinated tubulin alpha-1A chain2 PublicationsAdd BLAST450

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei40N6-acetyllysine1 Publication1
Modified residuei282Nitrated tyrosineBy similarity1
Modified residuei439PhosphoserineBy similarity1
Modified residuei4455-glutamyl polyglutamateBy similarity1
Modified residuei4513'-nitrotyrosine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866).1 Publication
Some glutamate residues at the C-terminus are 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). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear (Probable).1 Publication
Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly.1 Publication
Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.By similarity
Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution.1 Publication
Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively.4 Publications
Tubulin alpha-1A chain: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1. Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules (PubMed:26972003, PubMed:26968983). In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (PubMed:26968983).2 Publications
Detyrosinated tubulin alpha-1A chain: Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (PubMed:25908662). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle. In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (By similarity).By similarity1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q71U36

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q71U36

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q71U36

MaxQB - The MaxQuant DataBase

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MaxQBi
Q71U36

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q71U36

PeptideAtlas

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PeptideAtlasi
Q71U36

PRoteomics IDEntifications database

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PRIDEi
Q71U36

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
32448
68631 [Q71U36-1]

Consortium for Top Down Proteomics

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TopDownProteomicsi
Q71U36-1 [Q71U36-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q71U36

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q71U36

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q71U36

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
Q71U36

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed at a high level in fetal brain.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000167552 Expressed in 237 organ(s), highest expression level in endothelial cell

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q71U36 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q71U36 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB008686
HPA039247
HPA043684
HPA063394

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Interacts with SETD2; the interaction is independent on alpha-tubulin acetylation on Lys-40.

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
113603, 428 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q71U36

Database of interacting proteins

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DIPi
DIP-32773N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q71U36

Protein interaction database and analysis system

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IntActi
Q71U36, 390 interactors

Molecular INTeraction database

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MINTi
Q71U36

STRING: functional protein association networks

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STRINGi
9606.ENSP00000301071

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q71U36

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1376 Eukaryota
COG5023 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000182825

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000165711

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q71U36

KEGG Orthology (KO)

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KOi
K07374

Identification of Orthologs from Complete Genome Data

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OMAi
CKISTAV

Database of Orthologous Groups

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OrthoDBi
514396at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q71U36

TreeFam database of animal gene trees

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TreeFami
TF300314

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.287.600, 1 hit
3.30.1330.20, 1 hit
3.40.50.1440, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002452 Alpha_tubulin
IPR008280 Tub_FtsZ_C
IPR000217 Tubulin
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR023123 Tubulin_C
IPR017975 Tubulin_CS
IPR003008 Tubulin_FtsZ_GTPase

The PANTHER Classification System

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PANTHERi
PTHR11588 PTHR11588, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01162 ALPHATUBULIN
PR01161 TUBULIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00227 TUBULIN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q71U36-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN
60 70 80 90 100
TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440 450
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE

Y
Length:451
Mass (Da):50,136
Last modified:July 5, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i00F8429A4A10E5FE
GO
Isoform 2 (identifier: Q71U36-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Note: No experimental confirmation available.
Show »
Length:416
Mass (Da):46,297
Checksum:iBF1E2C9AC0754A68
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8VQQ4F8VQQ4_HUMAN
Tubulin alpha chain
TUBA1A
219Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8W0F6F8W0F6_HUMAN
Tubulin alpha-1A chain
TUBA1A
231Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8VRZ4F8VRZ4_HUMAN
Tubulin alpha-1A chain
TUBA1A
112Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8VXZ7F8VXZ7_HUMAN
Tubulin alpha-1A chain
TUBA1A
26Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti131G → R in CAA25855 (PubMed:3839072).Curated1
Sequence conflicti131G → R in AAA91575 (PubMed:6646120).Curated1
Sequence conflicti290E → D in AAA91575 (PubMed:6646120).Curated1
Sequence conflicti308R → G in CAA25855 (PubMed:3839072).Curated1
Sequence conflicti308R → G in AAA91575 (PubMed:6646120).Curated1
Sequence conflicti438D → H in CAA25855 (PubMed:3839072).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_039332188I → L in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853045EnsemblClinVar.1
Natural variantiVAR_039333263P → T in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853046EnsemblClinVar.1
Natural variantiVAR_039334264R → C in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853043EnsemblClinVar.1
Natural variantiVAR_039335286L → F in LIS3. 1 Publication1
Natural variantiVAR_039336402R → C in LIS3. 1 PublicationCorresponds to variant dbSNP:rs587784483EnsemblClinVar.1
Natural variantiVAR_039337402R → H in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853044EnsemblClinVar.1
Natural variantiVAR_078711402R → L in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853044EnsemblClinVar.1
Natural variantiVAR_039338419S → L in LIS3. 1 PublicationCorresponds to variant dbSNP:rs137853047EnsemblClinVar.1
Natural variantiVAR_034540447E → K. Corresponds to variant dbSNP:rs1065730Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0467821 – 35Missing in isoform 2. CuratedAdd BLAST35

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X01703 Genomic DNA Translation: CAA25855.1
AF141347 mRNA Translation: AAD33871.1
AK289483 mRNA Translation: BAF82172.1
AC010173 Genomic DNA No translation available.
CH471111 Genomic DNA Translation: EAW58052.1
CH471111 Genomic DNA Translation: EAW58054.1
CH471111 Genomic DNA Translation: EAW58055.1
BC006468 mRNA Translation: AAH06468.1
BC050637 mRNA Translation: AAH50637.1
K00557 mRNA Translation: AAA91575.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS58226.1 [Q71U36-2]
CCDS58227.1 [Q71U36-1]
CCDS8781.1 [Q71U36-1]

NCBI Reference Sequences

More...
RefSeqi
NP_001257328.1, NM_001270399.1 [Q71U36-1]
NP_001257329.1, NM_001270400.1 [Q71U36-2]
NP_006000.2, NM_006009.3 [Q71U36-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000295766; ENSP00000439020; ENSG00000167552 [Q71U36-1]
ENST00000301071; ENSP00000301071; ENSG00000167552 [Q71U36-1]
ENST00000550767; ENSP00000446637; ENSG00000167552 [Q71U36-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7846

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7846

UCSC genome browser

More...
UCSCi
uc001rtp.5 human [Q71U36-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01703 Genomic DNA Translation: CAA25855.1
AF141347 mRNA Translation: AAD33871.1
AK289483 mRNA Translation: BAF82172.1
AC010173 Genomic DNA No translation available.
CH471111 Genomic DNA Translation: EAW58052.1
CH471111 Genomic DNA Translation: EAW58054.1
CH471111 Genomic DNA Translation: EAW58055.1
BC006468 mRNA Translation: AAH06468.1
BC050637 mRNA Translation: AAH50637.1
K00557 mRNA Translation: AAA91575.1
CCDSiCCDS58226.1 [Q71U36-2]
CCDS58227.1 [Q71U36-1]
CCDS8781.1 [Q71U36-1]
RefSeqiNP_001257328.1, NM_001270399.1 [Q71U36-1]
NP_001257329.1, NM_001270400.1 [Q71U36-2]
NP_006000.2, NM_006009.3 [Q71U36-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5JCOelectron microscopy4.00A/B/E/F/G/H1-437[»]
SMRiQ71U36
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi113603, 428 interactors
CORUMiQ71U36
DIPiDIP-32773N
ELMiQ71U36
IntActiQ71U36, 390 interactors
MINTiQ71U36
STRINGi9606.ENSP00000301071

Chemistry databases

ChEMBLiCHEMBL3661
DrugBankiDB07574 2-MERCAPTO-N-[1,2,3,10-TETRAMETHOXY-9-OXO-5,6,7,9-TETRAHYDRO-BENZO[A]HEPTALEN-7-YL]ACETAMIDE
DB00518 Albendazole
DB11638 Artenimol
DB05147 CYT997
DB01873 Epothilone D
DB00643 Mebendazole
DB03010 Patupilone
DB12695 Phenethyl Isothiocyanate
DB00570 Vinblastine
DrugCentraliQ71U36

PTM databases

iPTMnetiQ71U36
PhosphoSitePlusiQ71U36
SwissPalmiQ71U36

Polymorphism and mutation databases

BioMutaiTUBA1A
DMDMi55977864

Proteomic databases

EPDiQ71U36
jPOSTiQ71U36
MassIVEiQ71U36
MaxQBiQ71U36
PaxDbiQ71U36
PeptideAtlasiQ71U36
PRIDEiQ71U36
ProteomicsDBi32448
68631 [Q71U36-1]
TopDownProteomicsiQ71U36-1 [Q71U36-1]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
7846

Genome annotation databases

EnsembliENST00000295766; ENSP00000439020; ENSG00000167552 [Q71U36-1]
ENST00000301071; ENSP00000301071; ENSG00000167552 [Q71U36-1]
ENST00000550767; ENSP00000446637; ENSG00000167552 [Q71U36-2]
GeneIDi7846
KEGGihsa:7846
UCSCiuc001rtp.5 human [Q71U36-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7846
DisGeNETi7846

GeneCards: human genes, protein and diseases

More...
GeneCardsi
TUBA1A
GeneReviewsiTUBA1A
HGNCiHGNC:20766 TUBA1A
HPAiCAB008686
HPA039247
HPA043684
HPA063394
MalaCardsiTUBA1A
MIMi602529 gene
611603 phenotype
neXtProtiNX_Q71U36
OpenTargetsiENSG00000167552
Orphaneti171680 Lissencephaly due to TUBA1A mutation
467166 Tubulinopathy-associated dysgyria
PharmGKBiPA162407319

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1376 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00950000182825
HOGENOMiHOG000165711
InParanoidiQ71U36
KOiK07374
OMAiCKISTAV
OrthoDBi514396at2759
PhylomeDBiQ71U36
TreeFamiTF300314

Enzyme and pathway databases

ReactomeiR-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-HSA-190861 Gap junction assembly
R-HSA-2132295 MHC class II antigen presentation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition
R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-380259 Loss of Nlp from mitotic centrosomes
R-HSA-380270 Recruitment of mitotic centrosome proteins and complexes
R-HSA-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
R-HSA-389957 Prefoldin mediated transfer of substrate to CCT/TriC
R-HSA-389960 Formation of tubulin folding intermediates by CCT/TriC
R-HSA-389977 Post-chaperonin tubulin folding pathway
R-HSA-437239 Recycling pathway of L1
R-HSA-5610787 Hedgehog 'off' state
R-HSA-5617833 Cilium Assembly
R-HSA-5620912 Anchoring of the basal body to the plasma membrane
R-HSA-5620924 Intraflagellar transport
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-6807878 COPI-mediated anterograde transport
R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-HSA-68877 Mitotic Prometaphase
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854518 AURKA Activation by TPX2
R-HSA-8955332 Carboxyterminal post-translational modifications of tubulin
R-HSA-9609736 Assembly and cell surface presentation of NMDA receptors
R-HSA-9619483 Activation of AMPK downstream of NMDARs
R-HSA-983189 Kinesins
SIGNORiQ71U36

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
TUBA1A human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
TUBA1A

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
7846
PharosiQ71U36
PMAP-CutDBiQ71U36

Protein Ontology

More...
PROi
PR:Q71U36

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000167552 Expressed in 237 organ(s), highest expression level in endothelial cell
ExpressionAtlasiQ71U36 baseline and differential
GenevisibleiQ71U36 HS

Family and domain databases

Gene3Di1.10.287.600, 1 hit
3.30.1330.20, 1 hit
3.40.50.1440, 1 hit
InterProiView protein in InterPro
IPR002452 Alpha_tubulin
IPR008280 Tub_FtsZ_C
IPR000217 Tubulin
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR023123 Tubulin_C
IPR017975 Tubulin_CS
IPR003008 Tubulin_FtsZ_GTPase
PANTHERiPTHR11588 PTHR11588, 1 hit
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01162 ALPHATUBULIN
PR01161 TUBULIN
SMARTiView protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit
SUPFAMiSSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit
PROSITEiView protein in PROSITE
PS00227 TUBULIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTBA1A_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q71U36
Secondary accession number(s): A8K0B8
, G3V1U9, P04687, P05209
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: July 5, 2004
Last modified: October 16, 2019
This is version 166 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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