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Entry version 171 (08 May 2019)
Sequence version 1 (01 Jun 2001)
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Protein

Tubulin beta-2B chain

Gene

TUBB2B

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 (PubMed:23001566, PubMed:28013290, PubMed:26732629). 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 (By similarity). Plays a critical role in proper axon guidance in both central and peripheral axon tracts (PubMed:23001566). Implicated in neuronal migration (PubMed:19465910).By similarity4 Publications

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

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

Biological processNeurogenesis
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-HSA-190861 Gap junction assembly
R-HSA-2132295 MHC class II antigen presentation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-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-9609736 Assembly and cell surface presentation of NMDA receptors
R-HSA-9619483 Activation of AMPK downstream of NMDARs
R-HSA-983189 Kinesins

<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-2B 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:TUBB2B
<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:30829 TUBB2B

Online Mendelian Inheritance in Man (OMIM)

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MIMi
612850 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q9BVA1

<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 7 (CDCBM7)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. Polymicrogyria is a heterogeneous disorder, considered to be the result of postmigratory abnormal cortical organization.
See also OMIM:610031
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_078186117L → P in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs397514569EnsemblClinVar.1
Natural variantiVAR_063389172S → P in CDCBM7; affects microtubules assembly. 1 PublicationCorresponds to variant dbSNP:rs137853194EnsemblClinVar.1
Natural variantiVAR_063391210I → T in CDCBM7. 1 Publication1
Natural variantiVAR_063392228L → P in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs137853195EnsemblClinVar.1
Natural variantiVAR_078188256N → S in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs397514568EnsemblClinVar.1
Natural variantiVAR_063393265F → L in CDCBM7; affects microtubules assembly. 1 PublicationCorresponds to variant dbSNP:rs137853196EnsemblClinVar.1
Natural variantiVAR_063394312T → M in CDCBM7. 1 Publication1
Natural variantiVAR_078190417D → N in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs397514567EnsemblClinVar.1
Natural variantiVAR_078191421E → K in CDCBM7; decreased protein expression; decreased tubulin heterodimer formation; no effect on integration into the microtubule lattice; no effect on microtubule cytoskeleton subcellular location; loss of axon guidance. 1 PublicationCorresponds to variant dbSNP:rs398122369EnsemblClinVar.1
Fetal akinesia deformation sequence (FADS)1 Publication
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionA clinically and genetically heterogeneous group of disorders with congenital malformations related to impaired fetal movement. Clinical features include fetal akinesia, intrauterine growth retardation, polyhydramnios, arthrogryposis, pulmonary hypoplasia, craniofacial abnormalities, and cryptorchidism.
See also OMIM:208150
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078187239C → F in FADS; decreased tubulin heterodimer formation; decreased ability to incorporate into the cytoskeleton; no effect on microtubules disintegration; increased ability to repolymerize. 1 PublicationCorresponds to variant dbSNP:rs878853284EnsemblClinVar.1
Defects in TUBB2B may be involved in cerebellar ataxia, mental retardation, and dysequilibrium syndrome (CAMRQ).1 Publication

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

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DisGeNETi
347733

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

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GeneReviewsi
TUBB2B

MalaCards human disease database

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MalaCardsi
TUBB2B
MIMi208150 phenotype
610031 phenotype

Open Targets

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OpenTargetsi
ENSG00000137285

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

More...
Orphaneti
45358 Congenital fibrosis of extraocular muscles
1766 Dysequilibrium syndrome
300573 Polymicrogyria due to TUBB2B mutation
467166 Tubulinopathy-associated dysgyria

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA142670671

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2095182

Drug and drug target database

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DrugBanki
DB05147 CYT997

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TUBB2B

Domain mapping of disease mutations (DMDM)

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DMDMi
74761283

<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_00002626511 – 445Tubulin beta-2B chainAdd BLAST445

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 residuei55PhosphothreonineBy similarity1
Modified residuei58N6-acetyllysine; alternateBy similarity1
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); alternateBy similarity
Modified residuei172Phosphoserine; by CDK11 Publication1
Modified residuei285PhosphothreonineBy similarity1
Modified residuei290PhosphothreonineBy similarity1
Modified residuei318Omega-N-methylarginineBy similarity1
Cross-linki324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
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
Q9BVA1

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9BVA1

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9BVA1

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

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PaxDbi
Q9BVA1

PeptideAtlas

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PeptideAtlasi
Q9BVA1

PRoteomics IDEntifications database

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PRIDEi
Q9BVA1

ProteomicsDB human proteome resource

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ProteomicsDBi
79190

Consortium for Top Down Proteomics

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TopDownProteomicsi
Q9BVA1

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9BVA1

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

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PhosphoSitePlusi
Q9BVA1

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q9BVA1

<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

High expression in brain.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000137285 Expressed in 206 organ(s), highest expression level in brain

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9BVA1 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 (PubMed:23001566, PubMed:28013290, PubMed:26732629). 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.3 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

WithEntry#Exp.IntActNotes
CACNA1AO005552EBI-355665,EBI-766279

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
131483, 81 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9BVA1

Protein interaction database and analysis system

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IntActi
Q9BVA1, 33 interactors

Molecular INTeraction database

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MINTi
Q9BVA1

STRING: functional protein association networks

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STRINGi
9606.ENSP00000259818

<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

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
6E7Celectron microscopy3.65B1-426[»]

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

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SMRi
Q9BVA1

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 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
ENSGT00940000154150

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000165710

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9BVA1

KEGG Orthology (KO)

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KOi
K07375

Identification of Orthologs from Complete Genome Data

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OMAi
EMHKVQT

Database of Orthologous Groups

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OrthoDBi
962471at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9BVA1

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

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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<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.

Q9BVA1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY
60 70 80 90 100
YNEATGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEYP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM
310 320 330 340 350
AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEE GEDEA
Length:445
Mass (Da):49,953
Last modified:June 1, 2001 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4DC3956EFF880746
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078186117L → P in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs397514569EnsemblClinVar.1
Natural variantiVAR_063389172S → P in CDCBM7; affects microtubules assembly. 1 PublicationCorresponds to variant dbSNP:rs137853194EnsemblClinVar.1
Natural variantiVAR_063390201C → S1 PublicationCorresponds to variant dbSNP:rs1054331Ensembl.1
Natural variantiVAR_063391210I → T in CDCBM7. 1 Publication1
Natural variantiVAR_063392228L → P in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs137853195EnsemblClinVar.1
Natural variantiVAR_078187239C → F in FADS; decreased tubulin heterodimer formation; decreased ability to incorporate into the cytoskeleton; no effect on microtubules disintegration; increased ability to repolymerize. 1 PublicationCorresponds to variant dbSNP:rs878853284EnsemblClinVar.1
Natural variantiVAR_078188256N → S in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs397514568EnsemblClinVar.1
Natural variantiVAR_063393265F → L in CDCBM7; affects microtubules assembly. 1 PublicationCorresponds to variant dbSNP:rs137853196EnsemblClinVar.1
Natural variantiVAR_063394312T → M in CDCBM7. 1 Publication1
Natural variantiVAR_078189390R → Q Probable disease-associated mutation found in a patient with cerebellar ataxia mental retardation and dysequilibrium syndrome; unknown pathological significance; no effect on protein folding; no effect on tubulin heterodimer formation; no effect on integration into the microtubule lattice; no effect on cytoskeleton subcellular location. 1 Publication1
Natural variantiVAR_078190417D → N in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs397514567EnsemblClinVar.1
Natural variantiVAR_078191421E → K in CDCBM7; decreased protein expression; decreased tubulin heterodimer formation; no effect on integration into the microtubule lattice; no effect on microtubule cytoskeleton subcellular location; loss of axon guidance. 1 PublicationCorresponds to variant dbSNP:rs398122369EnsemblClinVar.1

Sequence databases

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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
BT019930 mRNA Translation: AAV38733.1
CR456788 mRNA Translation: CAG33069.1
AK289433 mRNA Translation: BAF82122.1
AL445309 Genomic DNA No translation available.
CH471087 Genomic DNA Translation: EAW55125.1
BC001352 mRNA Translation: AAH01352.1
BC063610 mRNA Translation: AAH63610.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS4485.1

NCBI Reference Sequences

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RefSeqi
NP_821080.1, NM_178012.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000259818; ENSP00000259818; ENSG00000137285

Database of genes from NCBI RefSeq genomes

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GeneIDi
347733

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:347733

UCSC genome browser

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UCSCi
uc003mvg.4 human

Keywords - Coding sequence diversityi

Polymorphism

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT019930 mRNA Translation: AAV38733.1
CR456788 mRNA Translation: CAG33069.1
AK289433 mRNA Translation: BAF82122.1
AL445309 Genomic DNA No translation available.
CH471087 Genomic DNA Translation: EAW55125.1
BC001352 mRNA Translation: AAH01352.1
BC063610 mRNA Translation: AAH63610.1
CCDSiCCDS4485.1
RefSeqiNP_821080.1, NM_178012.4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6E7Celectron microscopy3.65B1-426[»]
SMRiQ9BVA1
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131483, 81 interactors
CORUMiQ9BVA1
IntActiQ9BVA1, 33 interactors
MINTiQ9BVA1
STRINGi9606.ENSP00000259818

Chemistry databases

ChEMBLiCHEMBL2095182
DrugBankiDB05147 CYT997

PTM databases

iPTMnetiQ9BVA1
PhosphoSitePlusiQ9BVA1
SwissPalmiQ9BVA1

Polymorphism and mutation databases

BioMutaiTUBB2B
DMDMi74761283

Proteomic databases

EPDiQ9BVA1
jPOSTiQ9BVA1
MaxQBiQ9BVA1
PaxDbiQ9BVA1
PeptideAtlasiQ9BVA1
PRIDEiQ9BVA1
ProteomicsDBi79190
TopDownProteomicsiQ9BVA1

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
347733
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000259818; ENSP00000259818; ENSG00000137285
GeneIDi347733
KEGGihsa:347733
UCSCiuc003mvg.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
347733
DisGeNETi347733

GeneCards: human genes, protein and diseases

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GeneCardsi
TUBB2B
GeneReviewsiTUBB2B
HGNCiHGNC:30829 TUBB2B
HPAiHPA043640
HPA046280
MalaCardsiTUBB2B
MIMi208150 phenotype
610031 phenotype
612850 gene
neXtProtiNX_Q9BVA1
OpenTargetsiENSG00000137285
Orphaneti45358 Congenital fibrosis of extraocular muscles
1766 Dysequilibrium syndrome
300573 Polymicrogyria due to TUBB2B mutation
467166 Tubulinopathy-associated dysgyria
PharmGKBiPA142670671

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG1375 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00940000154150
HOGENOMiHOG000165710
InParanoidiQ9BVA1
KOiK07375
OMAiEMHKVQT
OrthoDBi962471at2759
PhylomeDBiQ9BVA1
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-9609736 Assembly and cell surface presentation of NMDA receptors
R-HSA-9619483 Activation of AMPK downstream of NMDARs
R-HSA-983189 Kinesins

Miscellaneous databases

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

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ChiTaRSi
TUBB2B human

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

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GenomeRNAii
347733

Protein Ontology

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PROi
PR:Q9BVA1

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000137285 Expressed in 206 organ(s), highest expression level in brain
GenevisibleiQ9BVA1 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
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<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 nameiTBB2B_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: Q9BVA1
Secondary accession number(s): A8K068
<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: November 28, 2006
Last sequence update: June 1, 2001
Last modified: May 8, 2019
This is version 171 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

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

Documents

  1. 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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