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UniProtKB - Q13509 (TBB3_HUMAN)

Entry version 201 (02 Dec 2020)
Sequence version 2 (02 May 2002)
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Protein

Tubulin beta-3 chain

Gene

TUBB3

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. TUBB3 plays a critical role in proper axon guidance and mantainance. Binding of NTN1/Netrin-1 to its receptor UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion (PubMed:28483977). Plays a role in dorsal root ganglion axon projection towards the spinal cord (PubMed:28483977).2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi140 – 146GTPSequence 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q13509

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-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR)
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-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-8955332, Carboxyterminal post-translational modifications of tubulin
R-HSA-9609690, HCMV Early Events
R-HSA-9609736, Assembly and cell surface presentation of NMDA receptors
R-HSA-9619483, Activation of AMPK downstream of NMDARs
R-HSA-9646399, Aggrephagy
R-HSA-9648025, EML4 and NUDC in mitotic spindle formation
R-HSA-9668328, Sealing of the nuclear envelope (NE) by ESCRT-III
R-HSA-983189, Kinesins

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q13509

<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%5Fand%5Ftaxonomy%5Fsection">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 beta-3 chain
Alternative name(s):
Tubulin beta-4 chain
Tubulin beta-III
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:TUBB3
Synonyms:TUBB4
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 16

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...EuPathDBi		HostDB:ENSG00000258947.6

Human Gene Nomenclature Database

More...HGNCi		HGNC:20772, TUBB3

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		602661, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q13509

<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

Cell projection, 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

Fibrosis of extraocular muscles, congenital, 3A (CFEOM3A)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA congenital ocular motility disorder marked by restrictive ophthalmoplegia affecting extraocular muscles innervated by the oculomotor and/or trochlear nerves. It is clinically characterized by anchoring of the eyes in downward gaze, ptosis, and backward tilt of the head. Congenital fibrosis of extraocular muscles type 3 presents as a non-progressive, autosomal dominant disorder with variable expression. Patients may be bilaterally or unilaterally affected, and their oculo-motility defects range from complete ophthalmoplegia (with the eyes fixed in a hypo- and exotropic position), to mild asymptomatic restrictions of ocular movement. Ptosis, refractive error, amblyopia, and compensatory head positions are associated with the more severe forms of the disorder. In some cases, the ocular phenotype is accompanied by additional features including developmental delay, corpus callosum agenesis, basal ganglia dysmorphism, facial weakness, polyneuropathy.
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_06275862R → Q in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 PublicationCorresponds to variant dbSNP:rs864321714EnsemblClinVar.1
Natural variantiVAR_062759262R → C in CFEOM3A; affects heterodimers formation; affects microtubules polymerization and depolymerization rates. 1 PublicationCorresponds to variant dbSNP:rs267607162EnsemblClinVar.1
Natural variantiVAR_062760262R → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures; affects microtubules polymerization and depolymerization rates. 1 PublicationCorresponds to variant dbSNP:rs864321716EnsemblClinVar.1
Natural variantiVAR_062761302A → T in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 PublicationCorresponds to variant dbSNP:rs267607163EnsemblClinVar.1
Natural variantiVAR_062762380R → C in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 PublicationCorresponds to variant dbSNP:rs864321717EnsemblClinVar.1
Natural variantiVAR_062763410E → K in CFEOM3A; severe phenotype with congenital facial weakness; lower extremity weakness and sensory loss in the second to third decade of life in one patient; affects microtubules polymerization and depolymerization rates. 1 PublicationCorresponds to variant dbSNP:rs267607165EnsemblClinVar.1
Natural variantiVAR_062764417D → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures. 1 PublicationCorresponds to variant dbSNP:rs267607164EnsemblClinVar.1
Natural variantiVAR_062765417D → N in CFEOM3A; some patients with lower extremity weakness and sensory loss in the second to third decade of life; also found in patients without CFEOM3A who developed polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs267607164EnsemblClinVar.1
Cortical dysplasia, complex, with other brain malformations 1 (CDCBM1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of aberrant neuronal migration and disturbed axonal guidance. Affected individuals have mild to severe mental retardation, strabismus, axial hypotonia, and spasticity. Brain imaging shows variable malformations of cortical development, including polymicrogyria, gyral disorganization, and fusion of the basal ganglia, as well as thin corpus callosum, hypoplastic brainstem, and dysplastic cerebellar vermis. Extraocular muscles are not involved.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_066206178T → M in CDCBM1; can form tubulin heterodimers that are properly incorporated into microtubules; the microtubules are less stable than wild-type. 1 PublicationCorresponds to variant dbSNP:rs747480526EnsemblClinVar.1
Natural variantiVAR_066207205E → K in CDCBM1; does not form tubulin heterodimers; patient fibroblasts show no major alterations in the microtubule network, but the microtubules are less stable than wild-type. 1 PublicationCorresponds to variant dbSNP:rs878853257EnsemblClinVar.1
Natural variantiVAR_066208302A → V in CDCBM1; does not form tubulin heterodimers. 1 PublicationCorresponds to variant dbSNP:rs878853258EnsemblClinVar.1
Natural variantiVAR_066209323M → V in CDCBM1; reduced heterodimers formation. 1 PublicationCorresponds to variant dbSNP:rs878853256EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		10381

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

More...GeneReviewsi		TUBB3

MalaCards human disease database

More...MalaCardsi		TUBB3
MIMi600638, phenotype
614039, phenotype

Open Targets

More...OpenTargetsi		ENSG00000258947

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

More...Orphaneti		45358, Congenital fibrosis of extraocular muscles
300570, Cortical dysgenesis with pontocerebellar hypoplasia due to TUBB3 mutation
467166, Tubulinopathy-associated dysgyria

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA134953867

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q13509, Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2597

Drug and drug target database

More...DrugBanki		DB05147, CYT997
DB01873, Epothilone D
DB04845, Ixabepilone
DB03010, Patupilone
DB12695, Phenethyl Isothiocyanate
DB06042, ZEN-012

DrugCentral

More...DrugCentrali		Q13509

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2752

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		TUBB3

Domain mapping of disease mutations (DMDM)

More...DMDMi		20455526

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000482501 – 450Tubulin beta-3 chainAdd 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 residuei172Phosphoserine; by CDK11 Publication1
Modified residuei4385-glutamyl polyglutamateBy similarity1
Modified residuei444PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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
Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q13509

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q13509

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q13509

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q13509

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

More...PaxDbi		Q13509

PeptideAtlas

More...PeptideAtlasi		Q13509

PRoteomics IDEntifications database

More...PRIDEi		Q13509

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		1874
59510 [Q13509-1]

Consortium for Top Down Proteomics

More...TopDownProteomicsi		Q13509-1 [Q13509-1]

2D gel databases

USC-OGP 2-DE database

More...OGPi		Q13509

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q13509

MetOSite database of methionine sulfoxide sites

More...MetOSitei		Q13509

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

More...PhosphoSitePlusi		Q13509

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q13509

<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

Expression is primarily restricted to central and peripheral nervous system. Greatly increased expression in most cancerous tissues.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000258947, Expressed in cortical plate and 112 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q13509, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q13509, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000258947, Tissue enriched (brain)

<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%5Fsection">'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%5Fsection">'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 UNC5C (via cytoplasmic domain); this interaction is decreased by NTN1/Netrin-1 (PubMed:28483977).

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		115654, 320 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q13509

Database of interacting proteins

More...DIPi		DIP-31505N

Protein interaction database and analysis system

More...IntActi		Q13509, 263 interactors

Molecular INTeraction database

More...MINTi		Q13509

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000320295

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q13509, protein

<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

Secondary structure

1450
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		Q13509

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...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 general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The highly acidic C-terminal region may bind cations such as calcium.

<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

More...eggNOGi		KOG1375, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159115

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_015718_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q13509

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q13509

TreeFam database of animal gene trees

More...TreeFami		TF300298

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...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

More...InterProi		View protein in InterPro
IPR013838, Beta-tubulin_BS
IPR002453, Beta_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

More...PANTHERi		PTHR11588, PTHR11588, 1 hit

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01163, BETATUBULIN
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
PS00228, TUBULIN_B_AUTOREG, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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 9 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q13509-1) [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.

« Hide
        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY 
        60         70         80         90        100
YNEASSHKYV PRAILVDLEP GTMDSVRSGA FGHLFRPDNF IFGQSGAGNN 
       110        120        130        140        150
WAKGHYTEGA ELVDSVLDVV RKECENCDCL QGFQLTHSLG GGTGSGMGTL 
       160        170        180        190        200
LISKVREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSIH QLVENTDETY 
       210        220        230        240        250
CIDNEALYDI CFRTLKLATP TYGDLNHLVS ATMSGVTTSL RFPGQLNADL 
       260        270        280        290        300
RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM 
       310        320        330        340        350
AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK 
       360        370        380        390        400
VAVCDIPPRG LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 
       410        420        430        440        450
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEGEMYEDD EEESEAQGPK
Length:450
Mass (Da):50,433
Last modified:May 2, 2002 - v2
<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:i4B9CDE7DBA102949
GO
Isoform 2 (identifier: Q13509-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Show »
Length:378
Mass (Da):42,433
Checksum:iA190AB5B6264F2AB
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 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V2A3G3V2A3_HUMAN
Tubulin beta chain
TUBB3
189Annotation 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>
G3V2N6G3V2N6_HUMAN
HCG1983504, isoform CRA_d
TUBB3 hCG_1983504
164Annotation 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>
G3V3R4G3V3R4_HUMAN
HCG1983504, isoform CRA_c
TUBB3 hCG_1983504
148Annotation 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>
G3V5W4G3V5W4_HUMAN
Tubulin beta-3 chain
TUBB3
97Annotation 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>
G3V2R8G3V2R8_HUMAN
HCG1983504, isoform CRA_e
TUBB3 hCG_1983504
118Annotation 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>
G3V542G3V542_HUMAN
Tubulin beta-3 chain
TUBB3
46Annotation 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>
G3V3W7G3V3W7_HUMAN
Tubulin beta-3 chain
TUBB3
87Annotation 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>
G3V3J6G3V3J6_HUMAN
HCG1983504, isoform CRA_b
TUBB3 hCG_1983504
55Annotation 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>
G3V4U2G3V4U2_HUMAN
Tubulin beta-3 chain
TUBB3
51Annotation 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 conflicti275A → R in AAC52035 (PubMed:9473684).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06275862R → Q in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 PublicationCorresponds to variant dbSNP:rs864321714EnsemblClinVar.1
Natural variantiVAR_066206178T → M in CDCBM1; can form tubulin heterodimers that are properly incorporated into microtubules; the microtubules are less stable than wild-type. 1 PublicationCorresponds to variant dbSNP:rs747480526EnsemblClinVar.1
Natural variantiVAR_066207205E → K in CDCBM1; does not form tubulin heterodimers; patient fibroblasts show no major alterations in the microtubule network, but the microtubules are less stable than wild-type. 1 PublicationCorresponds to variant dbSNP:rs878853257EnsemblClinVar.1
Natural variantiVAR_062759262R → C in CFEOM3A; affects heterodimers formation; affects microtubules polymerization and depolymerization rates. 1 PublicationCorresponds to variant dbSNP:rs267607162EnsemblClinVar.1
Natural variantiVAR_062760262R → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures; affects microtubules polymerization and depolymerization rates. 1 PublicationCorresponds to variant dbSNP:rs864321716EnsemblClinVar.1
Natural variantiVAR_062761302A → T in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 PublicationCorresponds to variant dbSNP:rs267607163EnsemblClinVar.1
Natural variantiVAR_066208302A → V in CDCBM1; does not form tubulin heterodimers. 1 PublicationCorresponds to variant dbSNP:rs878853258EnsemblClinVar.1
Natural variantiVAR_066209323M → V in CDCBM1; reduced heterodimers formation. 1 PublicationCorresponds to variant dbSNP:rs878853256EnsemblClinVar.1
Natural variantiVAR_062762380R → C in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 PublicationCorresponds to variant dbSNP:rs864321717EnsemblClinVar.1
Natural variantiVAR_062763410E → K in CFEOM3A; severe phenotype with congenital facial weakness; lower extremity weakness and sensory loss in the second to third decade of life in one patient; affects microtubules polymerization and depolymerization rates. 1 PublicationCorresponds to variant dbSNP:rs267607165EnsemblClinVar.1
Natural variantiVAR_062764417D → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures. 1 PublicationCorresponds to variant dbSNP:rs267607164EnsemblClinVar.1
Natural variantiVAR_062765417D → N in CFEOM3A; some patients with lower extremity weakness and sensory loss in the second to third decade of life; also found in patients without CFEOM3A who developed polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs267607164EnsemblClinVar.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_0546591 – 72Missing in isoform 2. 1 PublicationAdd BLAST72

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
U47634 mRNA Translation: AAC52035.1
AF427491 mRNA Translation: AAL28094.1
AK122757 mRNA Translation: BAG53710.1
AK292219 mRNA Translation: BAF84908.1
AC092143 Genomic DNA No translation available.
CH471184 Genomic DNA Translation: EAW66674.1
BC000748 mRNA Translation: AAH00748.1
BC003021 mRNA Translation: AAH03021.2

The Consensus CDS (CCDS) project

More...CCDSi		CCDS10988.1 [Q13509-1]
CCDS56012.1 [Q13509-2]

NCBI Reference Sequences

More...RefSeqi		NP_001184110.1, NM_001197181.1 [Q13509-2]
NP_006077.2, NM_006086.3 [Q13509-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000315491; ENSP00000320295; ENSG00000258947 [Q13509-1]
ENST00000554444; ENSP00000451617; ENSG00000258947 [Q13509-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		10381

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:10381

UCSC genome browser

More...UCSCi		uc002fph.2, human [Q13509-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
U47634 mRNA Translation: AAC52035.1
AF427491 mRNA Translation: AAL28094.1
AK122757 mRNA Translation: BAG53710.1
AK292219 mRNA Translation: BAF84908.1
AC092143 Genomic DNA No translation available.
CH471184 Genomic DNA Translation: EAW66674.1
BC000748 mRNA Translation: AAH00748.1
BC003021 mRNA Translation: AAH03021.2
CCDSiCCDS10988.1 [Q13509-1]
CCDS56012.1 [Q13509-2]
RefSeqiNP_001184110.1, NM_001197181.1 [Q13509-2]
NP_006077.2, NM_006086.3 [Q13509-1]

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
5IJ0electron microscopy3.80B1-426[»]
5IJ9electron microscopy3.70B1-426[»]
5JCOelectron microscopy4.00C/D/I/J/K/L1-426[»]
6E7Belectron microscopy3.50B1-426[»]
6S8LX-ray1.80B1-450[»]
6WSLelectron microscopy3.10B/F1-450[»]
SMRiQ13509
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi115654, 320 interactors
CORUMiQ13509
DIPiDIP-31505N
IntActiQ13509, 263 interactors
MINTiQ13509
STRINGi9606.ENSP00000320295

Chemistry databases

ChEMBLiCHEMBL2597
DrugBankiDB05147, CYT997
DB01873, Epothilone D
DB04845, Ixabepilone
DB03010, Patupilone
DB12695, Phenethyl Isothiocyanate
DB06042, ZEN-012
DrugCentraliQ13509
GuidetoPHARMACOLOGYi2752

PTM databases

iPTMnetiQ13509
MetOSiteiQ13509
PhosphoSitePlusiQ13509
SwissPalmiQ13509

Polymorphism and mutation databases

BioMutaiTUBB3
DMDMi20455526

2D gel databases

OGPiQ13509

Proteomic databases

EPDiQ13509
jPOSTiQ13509
MassIVEiQ13509
MaxQBiQ13509
PaxDbiQ13509
PeptideAtlasiQ13509
PRIDEiQ13509
ProteomicsDBi1874
59510 [Q13509-1]
TopDownProteomicsiQ13509-1 [Q13509-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		54822, 1034 antibodies

The DNASU plasmid repository

More...DNASUi		10381

Genome annotation databases

EnsembliENST00000315491; ENSP00000320295; ENSG00000258947 [Q13509-1]
ENST00000554444; ENSP00000451617; ENSG00000258947 [Q13509-2]
GeneIDi10381
KEGGihsa:10381
UCSCiuc002fph.2, human [Q13509-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		10381
DisGeNETi10381
EuPathDBiHostDB:ENSG00000258947.6

GeneCards: human genes, protein and diseases

More...GeneCardsi		TUBB3
GeneReviewsiTUBB3
HGNCiHGNC:20772, TUBB3
HPAiENSG00000258947, Tissue enriched (brain)
MalaCardsiTUBB3
MIMi600638, phenotype
602661, gene
614039, phenotype
neXtProtiNX_Q13509
OpenTargetsiENSG00000258947
Orphaneti45358, Congenital fibrosis of extraocular muscles
300570, Cortical dysgenesis with pontocerebellar hypoplasia due to TUBB3 mutation
467166, Tubulinopathy-associated dysgyria
PharmGKBiPA134953867

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1375, Eukaryota
GeneTreeiENSGT00940000159115
HOGENOMiCLU_015718_0_0_1
InParanoidiQ13509
PhylomeDBiQ13509
TreeFamiTF300298

Enzyme and pathway databases

PathwayCommonsiQ13509
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-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR)
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-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-8955332, Carboxyterminal post-translational modifications of tubulin
R-HSA-9609690, HCMV Early Events
R-HSA-9609736, Assembly and cell surface presentation of NMDA receptors
R-HSA-9619483, Activation of AMPK downstream of NMDARs
R-HSA-9646399, Aggrephagy
R-HSA-9648025, EML4 and NUDC in mitotic spindle formation
R-HSA-9668328, Sealing of the nuclear envelope (NE) by ESCRT-III
R-HSA-983189, Kinesins
SIGNORiQ13509

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		10381, 86 hits in 846 CRISPR screens

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

More...ChiTaRSi		TUBB3, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		TUBB3

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

More...GenomeRNAii		10381
PharosiQ13509, Tclin

Protein Ontology

More...PROi		PR:Q13509
RNActiQ13509, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000258947, Expressed in cortical plate and 112 other tissues
ExpressionAtlasiQ13509, baseline and differential
GenevisibleiQ13509, 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
IPR013838, Beta-tubulin_BS
IPR002453, Beta_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
PRINTSiPR01163, BETATUBULIN
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
PS00228, TUBULIN_B_AUTOREG, 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 nameiTBB3_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: Q13509
Secondary accession number(s): A8K854, Q9BTZ0, Q9BW10
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 2, 2002
Last modified: December 2, 2020
This is version 201 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
  5. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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