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UniProtKB - Q3ZCM7 (TBB8_HUMAN)

Entry version 127 (13 Feb 2019)
Sequence version 2 (26 Feb 2008)
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Protein

Tubulin beta-8 chain

Gene

TUBB8

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 (By similarity). TUBB8 has a key role in meiotic spindle assembly and oocyte maturation (PubMed:26789871).By similarity1 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
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

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-437239 Recycling pathway of L1
R-HSA-5617833 Cilium Assembly
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-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-8 chainCurated
Alternative name(s):
Tubulin beta 8 class VIIIImported
<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:TUBB8Imported
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_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 10

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000261456.5

Human Gene Nomenclature Database

More...HGNCi		HGNC:20773 TUBB8

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		616768 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q3ZCM7

<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

Oocyte maturation defect 2 (OOMD2)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant infertility disorder caused by defective oocyte maturation. Oocytes are arrested at metaphase I, and have an abnormal or no detectable spindle on polarization microscopy.
See also OMIM:616780
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_0768982R → K in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025273EnsemblClinVar.1
Natural variantiVAR_07689927 – 33Missing in OOMD2; loss of alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly. 1 Publication7
Natural variantiVAR_076900176S → L in OOMD2; loss of function in oocyte maturation; loss of function in meiotic spindle assembly; decreased alpha/beta-tubulin heterodimer assembly. 2 PublicationsCorresponds to variant dbSNP:rs869025609EnsemblClinVar.1
Natural variantiVAR_076901210I → V in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs781853492Ensembl.1
Natural variantiVAR_076902229V → A in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025271EnsemblClinVar.1
Natural variantiVAR_076903238T → M in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs1057520306Ensembl.1
Natural variantiVAR_076904255V → M in OOMD2; loss of function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs782269374Ensembl.1
Natural variantiVAR_076905262R → Q in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025610EnsemblClinVar.1
Natural variantiVAR_076906262R → W in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; does not affect function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs782486119Ensembl.1
Natural variantiVAR_076907285T → P in OOMD2; loss of function in meiotic spindle assembly. 1 Publication1
Natural variantiVAR_076908300M → I in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025612EnsemblClinVar.1
Natural variantiVAR_076909348N → S in OOMD2; loss of function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs1270068662Ensembl.1
Natural variantiVAR_076910363M → T in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025611EnsemblClinVar.1
Natural variantiVAR_076911417D → N in OOMD2; loss of function in oocyte maturation; loss of function in meiotic spindle assembly; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025272EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		347688

MalaCards human disease database

More...MalaCardsi		TUBB8
MIMi616780 phenotype

Open Targets

More...OpenTargetsi		ENSG00000261456

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

More...Orphaneti		488191 Female infertility due to oocyte meiotic arrest

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2095182

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		TUBB8

Domain mapping of disease mutations (DMDM)

More...DMDMi		182705285

<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_00003206311 – 444Tubulin beta-8 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 residuei172Phosphoserine; by CDK11 Publication1
Modified residuei4365-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

Isopeptide bond, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q3ZCM7

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q3ZCM7

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q3ZCM7

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

More...PaxDbi		Q3ZCM7

PeptideAtlas

More...PeptideAtlasi		Q3ZCM7

PRoteomics IDEntifications database

More...PRIDEi		Q3ZCM7

ProteomicsDB human proteome resource

More...ProteomicsDBi		61904

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q3ZCM7

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

More...PhosphoSitePlusi		Q3ZCM7

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q3ZCM7

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

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

Expressed at a high level in oocytes, at different stages of development.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000261456 Expressed in 60 organ(s), highest expression level in testis

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q3ZCM7 baseline and differential

Organism-specific databases

Human Protein Atlas

More...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.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		131462, 204 interactors

Protein interaction database and analysis system

More...IntActi		Q3ZCM7, 15 interactors

Molecular INTeraction database

More...MINTi		Q3ZCM7

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000328808

<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

More...ProteinModelPortali		Q3ZCM7

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

More...SMRi		Q3ZCM7

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...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

More...eggNOGi		KOG1375 Eukaryota
COG5023 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000161436

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000165710

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG000089

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q3ZCM7

KEGG Orthology (KO)

More...KOi		K07375

Identification of Orthologs from Complete Genome Data

More...OMAi		WEAVCDE

Database of Orthologous Groups

More...OrthoDBi		962471at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q3ZCM7

TreeFam database of animal gene trees

More...TreeFami		TF300298

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.287.600, 1 hit
3.30.1330.20, 1 hit
3.40.50.1440, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013838 Beta-tubulin_BS
IPR002453 Beta_tubulin
IPR008280 Tub_FtsZ_C
IPR000217 Tubulin
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR023123 Tubulin_C
IPR017975 Tubulin_CS
IPR003008 Tubulin_FtsZ_GTPase

The PANTHER Classification System

More...PANTHERi		PTHR11588 PTHR11588, 1 hit
PTHR11588:SF256 PTHR11588:SF256, 1 hit

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01163 BETATUBULIN
PR01161 TUBULIN

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00227 TUBULIN, 1 hit
PS00228 TUBULIN_B_AUTOREG, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_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>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 5 potential isoforms that are computationally mapped.Show allAlign All

Q3ZCM7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MREIVLTQIG QCGNQIGAKF WEVISDEHAI DSAGTYHGDS HLQLERINVY 
        60         70         80         90        100
YNEASGGRYV PRAVLVDLEP GTMDSVRSGP FGQVFRPDNF IFGQCGAGNN 
       110        120        130        140        150
WAKGHYTEGA ELMESVMDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL 
       160        170        180        190        200
LLSKIREEYP DRIINTFSIL PSPKVSDTVV EPYNATLSVH QLIENADETF 
       210        220        230        240        250
CIDNEALYDI CSKTLKLPTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL 
       260        270        280        290        300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVAELT QQMFDAKNMM 
       310        320        330        340        350
AACDPRHGRY LTAAAIFRGR MPMREVDEQM FNIQDKNSSY FADWLPNNVK 
       360        370        380        390        400
TAVCDIPPRG LKMSATFIGN NTAIQELFKR VSEQFTAMFR RKAFLHWYTG 
       410        420        430        440 
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEEDEEYAE EEVA
Length:444
Mass (Da):49,776
Last modified:February 26, 2008 - 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:i3EC4AC10946BF590
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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5SQY0Q5SQY0_HUMAN
Tubulin beta chain
TUBB8 hCG_2017862
410Annotation 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>
A0A075B736A0A075B736_HUMAN
Tubulin beta chain
TUBB8
407Annotation 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>
A0A075B724A0A075B724_HUMAN
Tubulin beta-8 chain
TUBB8
119Annotation 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>
A0A075B735A0A075B735_HUMAN
Tubulin beta-8 chain
TUBB8
75Annotation 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>
A0A075B725A0A075B725_HUMAN
Tubulin beta-8 chain
TUBB8
89Annotation 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0768982R → K in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025273EnsemblClinVar.1
Natural variantiVAR_07689927 – 33Missing in OOMD2; loss of alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly. 1 Publication7
Natural variantiVAR_076900176S → L in OOMD2; loss of function in oocyte maturation; loss of function in meiotic spindle assembly; decreased alpha/beta-tubulin heterodimer assembly. 2 PublicationsCorresponds to variant dbSNP:rs869025609EnsemblClinVar.1
Natural variantiVAR_076901210I → V in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs781853492Ensembl.1
Natural variantiVAR_076902229V → A in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025271EnsemblClinVar.1
Natural variantiVAR_076903238T → M in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs1057520306Ensembl.1
Natural variantiVAR_076904255V → M in OOMD2; loss of function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs782269374Ensembl.1
Natural variantiVAR_076905262R → Q in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025610EnsemblClinVar.1
Natural variantiVAR_076906262R → W in OOMD2; decreased alpha/beta-tubulin heterodimer assembly; does not affect function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs782486119Ensembl.1
Natural variantiVAR_076907285T → P in OOMD2; loss of function in meiotic spindle assembly. 1 Publication1
Natural variantiVAR_076908300M → I in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025612EnsemblClinVar.1
Natural variantiVAR_039240345L → F. Corresponds to variant dbSNP:rs4880608Ensembl.1
Natural variantiVAR_076909348N → S in OOMD2; loss of function in meiotic spindle assembly. 1 PublicationCorresponds to variant dbSNP:rs1270068662Ensembl.1
Natural variantiVAR_076910363M → T in OOMD2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025611EnsemblClinVar.1
Natural variantiVAR_076911417D → N in OOMD2; loss of function in oocyte maturation; loss of function in meiotic spindle assembly; decreased alpha/beta-tubulin heterodimer assembly. 1 PublicationCorresponds to variant dbSNP:rs869025272EnsemblClinVar.1

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
AF355127 Genomic DNA Translation: AAL32434.1
CR590375 mRNA No translation available.
AL713922 Genomic DNA No translation available.
CH471072 Genomic DNA Translation: EAW86545.1
BC101270 mRNA Translation: AAI01271.1
BC101271 mRNA Translation: AAI01272.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS7051.1

NCBI Reference Sequences

More...RefSeqi		NP_817124.1, NM_177987.2

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.532659

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000568584; ENSP00000456206; ENSG00000261456

Database of genes from NCBI RefSeq genomes

More...GeneIDi		347688

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:347688

UCSC genome browser

More...UCSCi		uc001ifi.3 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
AF355127 Genomic DNA Translation: AAL32434.1
CR590375 mRNA No translation available.
AL713922 Genomic DNA No translation available.
CH471072 Genomic DNA Translation: EAW86545.1
BC101270 mRNA Translation: AAI01271.1
BC101271 mRNA Translation: AAI01272.1
CCDSiCCDS7051.1
RefSeqiNP_817124.1, NM_177987.2
UniGeneiHs.532659

3D structure databases

ProteinModelPortaliQ3ZCM7
SMRiQ3ZCM7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131462, 204 interactors
IntActiQ3ZCM7, 15 interactors
MINTiQ3ZCM7
STRINGi9606.ENSP00000328808

Chemistry databases

ChEMBLiCHEMBL2095182

PTM databases

iPTMnetiQ3ZCM7
PhosphoSitePlusiQ3ZCM7
SwissPalmiQ3ZCM7

Polymorphism and mutation databases

BioMutaiTUBB8
DMDMi182705285

Proteomic databases

EPDiQ3ZCM7
jPOSTiQ3ZCM7
MaxQBiQ3ZCM7
PaxDbiQ3ZCM7
PeptideAtlasiQ3ZCM7
PRIDEiQ3ZCM7
ProteomicsDBi61904

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		347688
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000568584; ENSP00000456206; ENSG00000261456
GeneIDi347688
KEGGihsa:347688
UCSCiuc001ifi.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		347688
DisGeNETi347688
EuPathDBiHostDB:ENSG00000261456.5

GeneCards: human genes, protein and diseases

More...GeneCardsi		TUBB8

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0029368
HGNCiHGNC:20773 TUBB8
HPAiHPA043640
HPA046280
MalaCardsiTUBB8
MIMi616768 gene
616780 phenotype
neXtProtiNX_Q3ZCM7
OpenTargetsiENSG00000261456
Orphaneti488191 Female infertility due to oocyte meiotic arrest

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1375 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00940000161436
HOGENOMiHOG000165710
HOVERGENiHBG000089
InParanoidiQ3ZCM7
KOiK07375
OMAiWEAVCDE
OrthoDBi962471at2759
PhylomeDBiQ3ZCM7
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-437239 Recycling pathway of L1
R-HSA-5617833 Cilium Assembly
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-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

More...ChiTaRSi		TUBB8 human

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

More...GenomeRNAii		347688

Protein Ontology

More...PROi		PR:Q3ZCM7

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000261456 Expressed in 60 organ(s), highest expression level in testis
ExpressionAtlasiQ3ZCM7 baseline and differential

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 nameiTBB8_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: Q3ZCM7
Secondary accession number(s): Q5SQX9, Q8WZ78
<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: February 26, 2008
Last sequence update: February 26, 2008
Last modified: February 13, 2019
This is version 127 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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