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Entry version 117 (12 Aug 2020)
Sequence version 1 (05 Jul 2004)
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Protein

Tubulin beta-4B chain

Gene

Tubb4b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:4 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).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi140 – 146GTPSequence analysis7

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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-RNO-190840, Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-RNO-2132295, MHC class II antigen presentation
R-RNO-2467813, Separation of Sister Chromatids
R-RNO-2500257, Resolution of Sister Chromatid Cohesion
R-RNO-2565942, Regulation of PLK1 Activity at G2/M Transition
R-RNO-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-RNO-380259, Loss of Nlp from mitotic centrosomes
R-RNO-380270, Recruitment of mitotic centrosome proteins and complexes
R-RNO-380284, Loss of proteins required for interphase microtubule organization from the centrosome
R-RNO-380320, Recruitment of NuMA to mitotic centrosomes
R-RNO-437239, Recycling pathway of L1
R-RNO-5610787, Hedgehog 'off' state
R-RNO-5617833, Cilium Assembly
R-RNO-5620912, Anchoring of the basal body to the plasma membrane
R-RNO-5620924, Intraflagellar transport
R-RNO-5626467, RHO GTPases activate IQGAPs
R-RNO-5663220, RHO GTPases Activate Formins
R-RNO-6798695, Neutrophil degranulation
R-RNO-6807878, COPI-mediated anterograde transport
R-RNO-6811434, COPI-dependent Golgi-to-ER retrograde traffic
R-RNO-6811436, COPI-independent Golgi-to-ER retrograde traffic
R-RNO-68877, Mitotic Prometaphase
R-RNO-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-RNO-8854518, AURKA Activation by TPX2
R-RNO-8955332, Carboxyterminal post-translational modifications of tubulin
R-RNO-9646399, Aggrephagy
R-RNO-9648025, EML4 and NUDC in mitotic spindle formation
R-RNO-9668328, Sealing of the nuclear envelope (NE) by ESCRT-III
R-RNO-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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Tubulin beta-4B chain
Alternative name(s):
Tubulin beta-2C chain
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Tubb4b
Synonyms:Tubb2c
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
735101, Tubb4b

<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 describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002707551 – 445Tubulin beta-4B 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 residuei55PhosphothreonineCombined sources1
Modified residuei58N6-acetyllysineBy similarity1
Modified residuei172Phosphoserine; by CDK1By similarity1
Modified residuei4385-glutamyl polyglutamateBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear.By similarity
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity). 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 (By similarity).By similarity
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.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q6P9T8

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

More...
PaxDbi
Q6P9T8

PRoteomics IDEntifications database

More...
PRIDEi
Q6P9T8

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6P9T8

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

More...
PhosphoSitePlusi
Q6P9T8

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
255395, 12 interactors

Protein interaction database and analysis system

More...
IntActi
Q6P9T8, 4 interactors

Molecular INTeraction database

More...
MINTi
Q6P9T8

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000013863

<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

More...
SMRi
Q6P9T8

Database of comparative protein structure models

More...
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.By similarity

<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

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q6P9T8

KEGG Orthology (KO)

More...
KOi
K07375

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q6P9T8

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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

Integrated resource of protein families, domains and functional sites

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

The PANTHER Classification System

More...
PANTHERi
PTHR11588, PTHR11588, 1 hit

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01163, BETATUBULIN
PR01161, TUBULIN

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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

PROSITE; a protein domain and family database

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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q6P9T8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY
60 70 80 90 100
YNEATGGKYV PRAVLVDLEP 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 ATMSGVTACL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEGEFEEEA EEEVA
Length:445
Mass (Da):49,801
Last modified:July 5, 2004 - 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:i4BA931832C5B0B78
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V7C6G3V7C6_RAT
Tubulin beta chain
Tubb4b
548Annotation 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>

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
BC060597 mRNA Translation: AAH60597.1

NCBI Reference Sequences

More...
RefSeqi
NP_954525.1, NM_199094.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
296554

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:296554

UCSC genome browser

More...
UCSCi
RGD:735101, rat

<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
BC060597 mRNA Translation: AAH60597.1
RefSeqiNP_954525.1, NM_199094.2

3D structure databases

SMRiQ6P9T8
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi255395, 12 interactors
IntActiQ6P9T8, 4 interactors
MINTiQ6P9T8
STRINGi10116.ENSRNOP00000013863

PTM databases

iPTMnetiQ6P9T8
PhosphoSitePlusiQ6P9T8

Proteomic databases

jPOSTiQ6P9T8
PaxDbiQ6P9T8
PRIDEiQ6P9T8

Genome annotation databases

GeneIDi296554
KEGGirno:296554
UCSCiRGD:735101, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10383
RGDi735101, Tubb4b

Phylogenomic databases

eggNOGiKOG1375, Eukaryota
InParanoidiQ6P9T8
KOiK07375
PhylomeDBiQ6P9T8

Enzyme and pathway databases

ReactomeiR-RNO-190840, Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-RNO-2132295, MHC class II antigen presentation
R-RNO-2467813, Separation of Sister Chromatids
R-RNO-2500257, Resolution of Sister Chromatid Cohesion
R-RNO-2565942, Regulation of PLK1 Activity at G2/M Transition
R-RNO-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-RNO-380259, Loss of Nlp from mitotic centrosomes
R-RNO-380270, Recruitment of mitotic centrosome proteins and complexes
R-RNO-380284, Loss of proteins required for interphase microtubule organization from the centrosome
R-RNO-380320, Recruitment of NuMA to mitotic centrosomes
R-RNO-437239, Recycling pathway of L1
R-RNO-5610787, Hedgehog 'off' state
R-RNO-5617833, Cilium Assembly
R-RNO-5620912, Anchoring of the basal body to the plasma membrane
R-RNO-5620924, Intraflagellar transport
R-RNO-5626467, RHO GTPases activate IQGAPs
R-RNO-5663220, RHO GTPases Activate Formins
R-RNO-6798695, Neutrophil degranulation
R-RNO-6807878, COPI-mediated anterograde transport
R-RNO-6811434, COPI-dependent Golgi-to-ER retrograde traffic
R-RNO-6811436, COPI-independent Golgi-to-ER retrograde traffic
R-RNO-68877, Mitotic Prometaphase
R-RNO-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-RNO-8854518, AURKA Activation by TPX2
R-RNO-8955332, Carboxyterminal post-translational modifications of tubulin
R-RNO-9646399, Aggrephagy
R-RNO-9648025, EML4 and NUDC in mitotic spindle formation
R-RNO-9668328, Sealing of the nuclear envelope (NE) by ESCRT-III
R-RNO-983189, Kinesins

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q6P9T8

Family and domain databases

Gene3Di1.10.287.600, 1 hit
3.30.1330.20, 1 hit
3.40.50.1440, 1 hit
InterProiView protein in InterPro
IPR013838, Beta-tubulin_BS
IPR002453, Beta_tubulin
IPR008280, Tub_FtsZ_C
IPR000217, Tubulin
IPR018316, Tubulin/FtsZ_2-layer-sand-dom
IPR037103, Tubulin/FtsZ_C_sf
IPR036525, Tubulin/FtsZ_GTPase_sf
IPR023123, Tubulin_C
IPR017975, Tubulin_CS
IPR003008, Tubulin_FtsZ_GTPase
PANTHERiPTHR11588, PTHR11588, 1 hit
PfamiView protein in Pfam
PF00091, Tubulin, 1 hit
PF03953, Tubulin_C, 1 hit
PRINTSiPR01163, BETATUBULIN
PR01161, TUBULIN
SMARTiView protein in SMART
SM00864, Tubulin, 1 hit
SM00865, Tubulin_C, 1 hit
SUPFAMiSSF52490, SSF52490, 1 hit
SSF55307, SSF55307, 1 hit
PROSITEiView protein in PROSITE
PS00227, TUBULIN, 1 hit
PS00228, TUBULIN_B_AUTOREG, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTBB4B_RAT
<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: Q6P9T8
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: July 5, 2004
Last modified: August 12, 2020
This is version 117 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

<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

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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