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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.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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

  • GTPase activity Source: InterPro
  • GTP binding Source: GO_Central
  • structural constituent of cytoskeleton Source: GO_Central

GO - Biological processi

  • axon guidance Source: UniProtKB
  • microtubule-based process Source: GO_Central
  • microtubule cytoskeleton organization Source: GO_Central
  • mitotic cell cycle Source: GO_Central
  • neuron differentiation Source: GO_Central

<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

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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-983189 Kinesins

SIGNOR Signaling Network Open Resource

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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_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 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_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:TUBB3
Synonyms:TUBB4
<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 16

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000258947.6

Human Gene Nomenclature Database

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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; 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

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.
See also OMIM:600638
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.
See also OMIM:614039
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:rs878853258Ensembl.1
Natural variantiVAR_066209323M → V in CDCBM1; reduced heterodimers formation. 1 PublicationCorresponds to variant dbSNP:rs878853256Ensembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
10381

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

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GeneReviewsi
TUBB3

MalaCards human disease database

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MalaCardsi
TUBB3
MIMi600638 phenotype
614039 phenotype

Open Targets

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OpenTargetsi
ENSG00000258947

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

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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

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PharmGKBi
PA134953867

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2597

Drug and drug target database

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DrugBanki
DB05147 CYT997
DB03010 Epothilone B
DB01873 Epothilone D
DB04845 Ixabepilone
DB06042 ZEN-012

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2752

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TUBB3

Domain mapping of disease mutations (DMDM)

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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.<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_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
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

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EPDi
Q13509

MaxQB - The MaxQuant DataBase

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MaxQBi
Q13509

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

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PaxDbi
Q13509

PeptideAtlas

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PeptideAtlasi
Q13509

PRoteomics IDEntifications database

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PRIDEi
Q13509

ProteomicsDB human proteome resource

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ProteomicsDBi
59510

Consortium for Top Down Proteomics

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TopDownProteomicsi
Q13509-1 [Q13509-1]

2D gel databases

USC-OGP 2-DE database

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OGPi
Q13509

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q13509

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

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PhosphoSitePlusi
Q13509

SwissPalm database of S-palmitoylation events

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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

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Bgeei
ENSG00000258947 Expressed in 87 organ(s), highest expression level in hypothalamus

CleanEx database of gene expression profiles

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CleanExi
HS_TUBB3
HS_TUBB4

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q13509 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q13509 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA043640
HPA046280

<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.

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
115654, 267 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q13509

Database of interacting proteins

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DIPi
DIP-31505N

Protein interaction database and analysis system

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IntActi
Q13509, 147 interactors

Molecular INTeraction database

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MINTi
Q13509

STRING: functional protein association networks

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STRINGi
9606.ENSP00000320295

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q13509

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

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SMRi
Q13509

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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

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eggNOGi
KOG1375 Eukaryota
COG5023 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159115

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000165710

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000089

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q13509

KEGG Orthology (KO)

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KOi
K07375

Database of Orthologous Groups

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OrthoDBi
EOG091G06U2

Database for complete collections of gene phylogenies

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PhylomeDBi
Q13509

TreeFam database of animal gene trees

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TreeFami
TF300298

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
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

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PANTHERi
PTHR11588 PTHR11588, 1 hit
PTHR11588:SF256 PTHR11588:SF256, 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
PR01163 BETATUBULIN
PR01161 TUBULIN

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit

PROSITE; a protein domain and family database

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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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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.

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 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 'canonical' 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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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.

Note: No experimental confirmation available.
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>
G3V5W4G3V5W4_HUMAN
Tubulin beta-3 chain
TUBB3
97Annotation 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>
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>
G3V3R4G3V3R4_HUMAN
HCG1983504, isoform CRA_c
TUBB3 hCG_1983504
148Annotation 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>
G3V2R8G3V2R8_HUMAN
HCG1983504, isoform CRA_e
TUBB3 hCG_1983504
118Annotation 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>
G3V2N6G3V2N6_HUMAN
HCG1983504, isoform CRA_d
TUBB3 hCG_1983504
164Annotation 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:rs878853258Ensembl.1
Natural variantiVAR_066209323M → V in CDCBM1; reduced heterodimers formation. 1 PublicationCorresponds to variant dbSNP:rs878853256Ensembl.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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<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]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.511743

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]
UniGeneiHs.511743

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[»]
ProteinModelPortaliQ13509
SMRiQ13509
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115654, 267 interactors
CORUMiQ13509
DIPiDIP-31505N
IntActiQ13509, 147 interactors
MINTiQ13509
STRINGi9606.ENSP00000320295

Chemistry databases

ChEMBLiCHEMBL2597
DrugBankiDB05147 CYT997
DB03010 Epothilone B
DB01873 Epothilone D
DB04845 Ixabepilone
DB06042 ZEN-012
GuidetoPHARMACOLOGYi2752

PTM databases

iPTMnetiQ13509
PhosphoSitePlusiQ13509
SwissPalmiQ13509

Polymorphism and mutation databases

BioMutaiTUBB3
DMDMi20455526

2D gel databases

OGPiQ13509

Proteomic databases

EPDiQ13509
MaxQBiQ13509
PaxDbiQ13509
PeptideAtlasiQ13509
PRIDEiQ13509
ProteomicsDBi59510
TopDownProteomicsiQ13509-1 [Q13509-1]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
10381
Structural Biology KnowledgebaseSearch...

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
HPAiHPA043640
HPA046280
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
COG5023 LUCA
GeneTreeiENSGT00940000159115
HOGENOMiHOG000165710
HOVERGENiHBG000089
InParanoidiQ13509
KOiK07375
OrthoDBiEOG091G06U2
PhylomeDBiQ13509
TreeFamiTF300298

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-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-983189 Kinesins
SIGNORiQ13509

Miscellaneous databases

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

Protein Ontology

More...
PROi
PR:Q13509

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000258947 Expressed in 87 organ(s), highest expression level in hypothalamus
CleanExiHS_TUBB3
HS_TUBB4
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
PTHR11588:SF256 PTHR11588:SF256, 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...

<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_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: July 15, 1998
Last sequence update: May 2, 2002
Last modified: December 5, 2018
This is version 184 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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