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Entry version 225 (31 Jul 2019)
Sequence version 2 (21 Dec 2004)
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Protein

Tubulin beta chain

Gene

TUBB

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.

Regions

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

GO - Biological processi

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

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition
R-HSA-380259 Loss of Nlp from mitotic centrosomes
R-HSA-380270 Recruitment of mitotic centrosome proteins and complexes
R-HSA-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
R-HSA-5620912 Anchoring of the basal body to the plasma membrane
R-HSA-6798695 Neutrophil degranulation
R-HSA-8854518 AURKA Activation by TPX2

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P07437

<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 chain
Alternative name(s):
Tubulin beta-5 chain
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TUBB
Synonyms:TUBB5
ORF Names:OK/SW-cl.56
<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 6

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:20778 TUBB

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
191130 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P07437

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

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

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

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

Cortical dysplasia, complex, with other brain malformations 6 (CDCBM6)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 microcephaly, ataxia, and severe delayed psychomotor development. Brain imaging shows variable malformations of cortical development, including white matter streaks, dysmorphic basal ganglia, corpus callosum abnormalities, brainstem and cerebellar hypoplasia, cortical dysplasia, polymicrogyria.
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_071763299M → V in CDCBM6; decreases the ability of the protein to assemble into tubulin heterodimers. 1 PublicationCorresponds to variant dbSNP:rs587777355EnsemblClinVar.1
Natural variantiVAR_071764353V → I in CDCBM6; does not affect the ability of the mutant polypeptides to assemble into heterodimers and incorporate into microtubules. 1 PublicationCorresponds to variant dbSNP:rs587777356EnsemblClinVar.1
Natural variantiVAR_071765401E → K in CDCBM6; arrests the assembly pathway of alpha/beta-tubulin; the mutant protein is unable to coassemble into a tubulin heterodimer but is instead distributed throughout the cytoplasm. 1 PublicationCorresponds to variant dbSNP:rs587777357EnsemblClinVar.1
Skin creases, congenital symmetric circumferential, 1 (CSCSC1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disease characterized by multiple, symmetric, circumferential rings of folded skin, affecting primarily the limbs. Affected individuals also exhibit intellectual disability, cleft palate, and dysmorphic features.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07654315Q → K in CSCSC1; disrupts heterodimer assembly and microtubule dynamics. 1 PublicationCorresponds to variant dbSNP:rs864321676EnsemblClinVar.1
Natural variantiVAR_076544222Y → F in CSCSC1; disrupts heterodimer assembly and microtubule dynamics. 1 PublicationCorresponds to variant dbSNP:rs864321677EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
203068

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

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GeneReviewsi
TUBB

MalaCards human disease database

More...
MalaCardsi
TUBB
MIMi156610 phenotype
615771 phenotype

Open Targets

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OpenTargetsi
ENSG00000196230

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

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Orphaneti
2505 Multiple benign circumferential skin creases on limbs

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA358

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5444

Drug and drug target database

More...
DrugBanki
DB05284 CA4P
DB01394 Colchicine
DB05147 CYT997
DB03010 Epothilone B
DB01873 Epothilone D
DB01179 Podofilox
DB00570 Vinblastine
DB00541 Vincristine
DB00361 Vinorelbine
DB06042 ZEN-012

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2640

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TUBB

Domain mapping of disease mutations (DMDM)

More...
DMDMi
56757569

<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_00000482431 – 444Tubulin beta chainAdd BLAST444

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 residuei40PhosphoserineBy similarity1
Modified residuei55PhosphothreonineCombined sources1
Modified residuei58N6-acetyllysine; alternateCombined sources1
Modified residuei58N6-succinyllysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei172Phosphoserine; by CDK11 Publication1
Modified residuei285PhosphothreonineCombined sources1
Modified residuei290PhosphothreonineCombined sources1
Modified residuei318Omega-N-methylarginine1 Publication1
Cross-linki324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei4385-glutamyl polyglutamateBy 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

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P07437

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P07437

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

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PaxDbi
P07437

PeptideAtlas

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PeptideAtlasi
P07437

PRoteomics IDEntifications database

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PRIDEi
P07437

ProteomicsDB human proteome resource

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ProteomicsDBi
52002

Consortium for Top Down Proteomics

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TopDownProteomicsi
P07437

2D gel databases

USC-OGP 2-DE database

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OGPi
P07437

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
P07437

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P07437

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P07437

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P07437

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

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PhosphoSitePlusi
P07437

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P07437

<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

Ubiquitously expressed with highest levels in spleen, thymus and immature brain.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000196230 Expressed in 234 organ(s), highest expression level in cerebral cortex

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P07437 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P07437 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB005417
CAB012406
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

Heterodimer of alpha and beta chains (PubMed:26637975). 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 PIFO (PubMed:20643351).

Interacts with DIAPH1 (PubMed:23325789).

Interacts with MX1 (By similarity). May interact with RNABP10 (By similarity).

Interacts with CFAP157 (By similarity).

By similarity3 Publications

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
128444, 335 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P07437

Database of interacting proteins

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DIPi
DIP-32772N

Protein interaction database and analysis system

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IntActi
P07437, 121 interactors

Molecular INTeraction database

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MINTi
P07437

STRING: functional protein association networks

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STRINGi
9606.ENSP00000339001

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

3D structure databases

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

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SMRi
P07437

Database of comparative protein structure models

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ModBasei
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
ENSGT00940000154370

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P07437

KEGG Orthology (KO)

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KOi
K07375

Identification of Orthologs from Complete Genome Data

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OMAi
YYSEASD

Database of Orthologous Groups

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OrthoDBi
962471at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P07437

TreeFam database of animal gene trees

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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

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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

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

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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P07437-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY
60 70 80 90 100
YNEATGGKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEEDFGEEA EEEA
Length:444
Mass (Da):49,671
Last modified:December 21, 2004 - 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:i1E6CD0A36773A103
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5ST81Q5ST81_HUMAN
Tubulin beta chain
TUBB
372Annotation 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>
Q5JP53Q5JP53_HUMAN
Tubulin beta chain
TUBB
426Annotation 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>

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 conflicti216K → R no nucleotide entry (PubMed:6688039).Curated1
Sequence conflicti216K → R in AAB59507 (PubMed:6865944).Curated1
Sequence conflicti231A → G no nucleotide entry (PubMed:6688039).Curated1
Sequence conflicti231A → G in AAB59507 (PubMed:6865944).Curated1
Sequence conflicti234 – 235SG → EC no nucleotide entry (PubMed:6688039).Curated2
Sequence conflicti234 – 235SG → EC in AAB59507 (PubMed:6865944).Curated2
Sequence conflicti288E → D no nucleotide entry (PubMed:6688039).Curated1
Sequence conflicti288E → D in AAB59507 (PubMed:6865944).Curated1
Sequence conflicti298N → D in AAH20946 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07654315Q → K in CSCSC1; disrupts heterodimer assembly and microtubule dynamics. 1 PublicationCorresponds to variant dbSNP:rs864321676EnsemblClinVar.1
Natural variantiVAR_076544222Y → F in CSCSC1; disrupts heterodimer assembly and microtubule dynamics. 1 PublicationCorresponds to variant dbSNP:rs864321677EnsemblClinVar.1
Natural variantiVAR_071763299M → V in CDCBM6; decreases the ability of the protein to assemble into tubulin heterodimers. 1 PublicationCorresponds to variant dbSNP:rs587777355EnsemblClinVar.1
Natural variantiVAR_071764353V → I in CDCBM6; does not affect the ability of the mutant polypeptides to assemble into heterodimers and incorporate into microtubules. 1 PublicationCorresponds to variant dbSNP:rs587777356EnsemblClinVar.1
Natural variantiVAR_071765401E → K in CDCBM6; arrests the assembly pathway of alpha/beta-tubulin; the mutant protein is unable to coassemble into a tubulin heterodimer but is instead distributed throughout the cytoplasm. 1 PublicationCorresponds to variant dbSNP:rs587777357EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
J00314 Genomic DNA Translation: AAB59507.1
AF141349 mRNA Translation: AAD33873.1
AF070561 mRNA Translation: AAC28642.1
AF070593 mRNA Translation: AAC28650.1
AF070600 mRNA Translation: AAC28654.1
BA000025 Genomic DNA Translation: BAB63321.1
AB088100 Genomic DNA Translation: BAC54932.1
AB062393 mRNA Translation: BAB93480.1
BC001938 mRNA Translation: AAH01938.1
BC002347 mRNA Translation: AAH02347.1
BC005838 mRNA Translation: AAH05838.1
BC007605 mRNA Translation: AAH07605.1
BC013374 mRNA Translation: AAH13374.1
BC019924 mRNA Translation: AAH19924.1
BC020946 mRNA Translation: AAH20946.1
BC021909 mRNA Translation: AAH21909.1
BC070326 mRNA Translation: AAH70326.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS4687.1

Protein sequence database of the Protein Information Resource

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PIRi
A26561

NCBI Reference Sequences

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RefSeqi
NP_001280141.1, NM_001293212.1
NP_001280142.1, NM_001293213.1
NP_001280143.1, NM_001293214.1
NP_001280144.1, NM_001293215.1
NP_001280145.1, NM_001293216.1
NP_821133.1, NM_178014.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000327892; ENSP00000339001; ENSG00000196230
ENST00000383564; ENSP00000373058; ENSG00000183311
ENST00000419792; ENSP00000401317; ENSG00000235067
ENST00000421473; ENSP00000399155; ENSG00000224156
ENST00000422650; ENSP00000400663; ENSG00000229684
ENST00000422674; ENSP00000406811; ENSG00000227739
ENST00000432462; ENSP00000410829; ENSG00000232421
ENST00000436628; ENSP00000410071; ENSG00000232575

Database of genes from NCBI RefSeq genomes

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GeneIDi
203068

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:203068

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Tubulin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00314 Genomic DNA Translation: AAB59507.1
AF141349 mRNA Translation: AAD33873.1
AF070561 mRNA Translation: AAC28642.1
AF070593 mRNA Translation: AAC28650.1
AF070600 mRNA Translation: AAC28654.1
BA000025 Genomic DNA Translation: BAB63321.1
AB088100 Genomic DNA Translation: BAC54932.1
AB062393 mRNA Translation: BAB93480.1
BC001938 mRNA Translation: AAH01938.1
BC002347 mRNA Translation: AAH02347.1
BC005838 mRNA Translation: AAH05838.1
BC007605 mRNA Translation: AAH07605.1
BC013374 mRNA Translation: AAH13374.1
BC019924 mRNA Translation: AAH19924.1
BC020946 mRNA Translation: AAH20946.1
BC021909 mRNA Translation: AAH21909.1
BC070326 mRNA Translation: AAH70326.1
CCDSiCCDS4687.1
PIRiA26561
RefSeqiNP_001280141.1, NM_001293212.1
NP_001280142.1, NM_001293213.1
NP_001280143.1, NM_001293214.1
NP_001280144.1, NM_001293215.1
NP_001280145.1, NM_001293216.1
NP_821133.1, NM_178014.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QNZX-ray2.20C429-438[»]
3QO0X-ray2.30C422-441[»]
5N5Nelectron microscopy4.00A/B/C/D/E/F1-426[»]
SMRiP07437
ModBaseiSearch...

Protein-protein interaction databases

BioGridi128444, 335 interactors
CORUMiP07437
DIPiDIP-32772N
IntActiP07437, 121 interactors
MINTiP07437
STRINGi9606.ENSP00000339001

Chemistry databases

ChEMBLiCHEMBL5444
DrugBankiDB05284 CA4P
DB01394 Colchicine
DB05147 CYT997
DB03010 Epothilone B
DB01873 Epothilone D
DB01179 Podofilox
DB00570 Vinblastine
DB00541 Vincristine
DB00361 Vinorelbine
DB06042 ZEN-012
GuidetoPHARMACOLOGYi2640

PTM databases

iPTMnetiP07437
PhosphoSitePlusiP07437
SwissPalmiP07437

Polymorphism and mutation databases

BioMutaiTUBB
DMDMi56757569

2D gel databases

OGPiP07437
REPRODUCTION-2DPAGEiP07437
SWISS-2DPAGEiP07437
UCD-2DPAGEiP07437

Proteomic databases

EPDiP07437
jPOSTiP07437
PaxDbiP07437
PeptideAtlasiP07437
PRIDEiP07437
ProteomicsDBi52002
TopDownProteomicsiP07437

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P07437
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327892; ENSP00000339001; ENSG00000196230
ENST00000383564; ENSP00000373058; ENSG00000183311
ENST00000419792; ENSP00000401317; ENSG00000235067
ENST00000421473; ENSP00000399155; ENSG00000224156
ENST00000422650; ENSP00000400663; ENSG00000229684
ENST00000422674; ENSP00000406811; ENSG00000227739
ENST00000432462; ENSP00000410829; ENSG00000232421
ENST00000436628; ENSP00000410071; ENSG00000232575
GeneIDi203068
KEGGihsa:203068

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
203068
DisGeNETi203068

GeneCards: human genes, protein and diseases

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GeneCardsi
TUBB
GeneReviewsiTUBB
HGNCiHGNC:20778 TUBB
HPAiCAB005417
CAB012406
HPA043640
HPA046280
MalaCardsiTUBB
MIMi156610 phenotype
191130 gene
615771 phenotype
neXtProtiNX_P07437
OpenTargetsiENSG00000196230
Orphaneti2505 Multiple benign circumferential skin creases on limbs
PharmGKBiPA358

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1375 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00940000154370
InParanoidiP07437
KOiK07375
OMAiYYSEASD
OrthoDBi962471at2759
PhylomeDBiP07437
TreeFamiTF300298

Enzyme and pathway databases

ReactomeiR-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition
R-HSA-380259 Loss of Nlp from mitotic centrosomes
R-HSA-380270 Recruitment of mitotic centrosome proteins and complexes
R-HSA-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
R-HSA-5620912 Anchoring of the basal body to the plasma membrane
R-HSA-6798695 Neutrophil degranulation
R-HSA-8854518 AURKA Activation by TPX2
SIGNORiP07437

Miscellaneous databases

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

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ChiTaRSi
TUBB human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
TUBB

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

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GenomeRNAii
203068

Protein Ontology

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PROi
PR:P07437

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000196230 Expressed in 234 organ(s), highest expression level in cerebral cortex
ExpressionAtlasiP07437 baseline and differential
GenevisibleiP07437 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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiTBB5_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: P07437
Secondary accession number(s): P05218, Q8WUC1, Q9CY33
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: December 21, 2004
Last modified: July 31, 2019
This is version 225 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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