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UniProtKB - P81947 (TBA1B_BOVIN)

Entry version 138 (11 Dec 2019)
Sequence version 2 (10 Feb 2009)
Previous versions | rss
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Protein

Tubulin alpha-1B chain

Gene
N/A
Organism
Bos taurus (Bovine)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei451Involved in polymerizationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi142 – 148GTPSequence 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

Complete GO annotation on QuickGO ...

GO - Biological processi

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-BTA-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-BTA-2467813 Separation of Sister Chromatids
R-BTA-2500257 Resolution of Sister Chromatid Cohesion
R-BTA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-BTA-380320 Recruitment of NuMA to mitotic centrosomes
R-BTA-5610787 Hedgehog 'off' state
R-BTA-5617833 Cilium Assembly
R-BTA-5620924 Intraflagellar transport
R-BTA-5626467 RHO GTPases activate IQGAPs
R-BTA-5663220 RHO GTPases Activate Formins
R-BTA-6807878 COPI-mediated anterograde transport
R-BTA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-BTA-68877 Mitotic Prometaphase
R-BTA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-BTA-8955332 Carboxyterminal post-translational modifications of tubulin
R-BTA-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 alpha-1B chain
Alternative name(s):
Alpha-tubulin ubiquitous
Tubulin K-alpha-1
Tubulin alpha-ubiquitous chain
Cleaved into the following chain:
Detyrosinated tubulin alpha-1B chain
<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>OrganismiBos taurus (Bovine)Curated
<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 identifieri9913 [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 › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<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
  • UP000009136 <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: Unplaced

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000481141 – 451Tubulin alpha-1B chainAdd BLAST451
ChainiPRO_00004373971 – 450Detyrosinated tubulin alpha-1B chainBy similarityAdd BLAST450

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei40N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei40N6-acetyllysine; alternateBy similarity1
Modified residuei48PhosphoserineBy similarity1
Modified residuei232PhosphoserineBy similarity1
Modified residuei282Nitrated tyrosineBy 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-linki326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei339Omega-N-methylarginineBy similarity1
Cross-linki370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei439PhosphoserineBy similarity1
Modified residuei4455-glutamyl polyglutamateBy similarity1
Modified residuei4513'-nitrotyrosineBy 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 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
Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly.By similarity
Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.By similarity
Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution.By similarity
Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively.By similarity
Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules. In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity).By similarity
Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (By similarity). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle. In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		P81947

PeptideAtlas

More...PeptideAtlasi		P81947

PRoteomics IDEntifications database

More...PRIDEi		P81947

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P81947

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P81947

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSBTAG00000012244 Expressed in 9 organ(s), highest expression level in prefrontal cortex

<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

Database of interacting proteins

More...DIPi		DIP-41283N

Protein interaction database and analysis system

More...IntActi		P81947, 1 interactor

Molecular INTeraction database

More...MINTi		P81947

STRING: functional protein association networks

More...STRINGi		9913.ENSBTAP00000016242

<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

Secondary structure

1451
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P81947

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P81947

<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		KOG1376 Eukaryota
COG5023 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000165711

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P81947

KEGG Orthology (KO)

More...KOi		K07374

Identification of Orthologs from Complete Genome Data

More...OMAi		VDNEACY

Database of Orthologous Groups

More...OrthoDBi		514396at2759

TreeFam database of animal gene trees

More...TreeFami		TF300314

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
IPR002452 Alpha_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		PR01162 ALPHATUBULIN
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

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

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P81947-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN 
        60         70         80         90        100
TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA 
       110        120        130        140        150
NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT 
       160        170        180        190        200
SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC 
       210        220        230        240        250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV 
       260        270        280        290        300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 
       310        320        330        340        350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG 
       360        370        380        390        400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA 
       410        420        430        440        450
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE 

Y
Length:451
Mass (Da):50,152
Last modified:February 10, 2009 - 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:i94355B4EC2086429
GO

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
BC146060 mRNA Translation: AAI46061.1

NCBI Reference Sequences

More...RefSeqi		NP_001108328.1, NM_001114856.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		539882

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bta:539882

<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
BC146060 mRNA Translation: AAI46061.1
RefSeqiNP_001108328.1, NM_001114856.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DCOelectron microscopy1.90A1-451[»]
3EDLelectron microscopy28.00A/F1-451[»]
3IZ0electron microscopy8.60A1-451[»]
3J1Telectron microscopy9.70B1-451[»]
3J1Uelectron microscopy9.70B1-451[»]
3J2Uelectron microscopy10.80A/C1-451[»]
4I4TX-ray1.80A/C1-450[»]
4I50X-ray2.30A/C1-451[»]
4I55X-ray2.20A/C1-450[»]
4IHJX-ray2.00A/C1-450[»]
4IIJX-ray2.60A/C1-451[»]
4O2AX-ray2.50A/C1-451[»]
4O2BX-ray2.30A/C1-451[»]
4O4HX-ray2.10A/C1-451[»]
4O4IX-ray2.40A/C1-451[»]
4O4JX-ray2.20A/C1-451[»]
4O4LX-ray2.20A/C1-451[»]
4TUYX-ray2.10A/C1-451[»]
4TV8X-ray2.10A/C1-451[»]
4TV9X-ray2.00A/C1-451[»]
4UXOelectron microscopy6.30A1-451[»]
4UXPelectron microscopy6.30A1-451[»]
4UXRelectron microscopy7.00A1-451[»]
4UXSelectron microscopy7.00A1-451[»]
4UXTelectron microscopy7.40A1-451[»]
4UXYelectron microscopy6.50A1-451[»]
4UY0electron microscopy7.70A1-451[»]
4YJ2X-ray2.60A/C1-451[»]
4YJ3X-ray3.75A/C1-451[»]
5BMVX-ray2.50A/C1-451[»]
5EIBX-ray2.10C1-451[»]
5GONX-ray2.48A/C1-440[»]
5HNWelectron microscopy6.60A2-451[»]
5HNXelectron microscopy6.60A1-451[»]
5HNYelectron microscopy6.30A2-439[»]
5HNZelectron microscopy5.80A1-451[»]
5ITZX-ray2.20A1-451[»]
5IYZX-ray1.80A/C1-451[»]
5J2TX-ray2.20A/C1-451[»]
5J2UX-ray2.50A/C1-451[»]
5JH7X-ray2.25A/C1-450[»]
5JVDX-ray2.39A/C1-451[»]
5LA6X-ray2.10A/C1-451[»]
5LOVX-ray2.40A/C1-451[»]
5LP6X-ray2.90A1-439[»]
C1-440[»]
5LXSX-ray2.20A/C1-451[»]
5LXTX-ray1.90A/C1-451[»]
5LYJX-ray2.40A/C1-451[»]
5M50electron microscopy5.30A/D1-439[»]
5M54electron microscopy8.00A/D2-439[»]
5M5Celectron microscopy4.80A/D2-439[»]
5M7EX-ray2.05A/C1-451[»]
5M7GX-ray2.25A/C1-451[»]
5M8DX-ray2.25A/C1-451[»]
5M8GX-ray2.15A/C1-451[»]
5MF4X-ray2.30A/C1-451[»]
5MIOX-ray3.19A1-451[»]
5ND2electron microscopy5.80A1-451[»]
5ND3electron microscopy6.10A1-451[»]
5ND4electron microscopy4.40A2-439[»]
5ND7electron microscopy7.90A1-451[»]
5NFZX-ray2.10A/C1-451[»]
5NG1X-ray2.20A/C1-451[»]
5NJHX-ray2.39A/C1-450[»]
5NM5X-ray2.05A1-451[»]
5NQTX-ray2.15A1-451[»]
5NQUX-ray1.80A1-451[»]
5O7AX-ray2.50A/C1-451[»]
5OAMelectron microscopy5.50A1-451[»]
5OCUelectron microscopy5.20A1-451[»]
5OGCelectron microscopy4.80A1-451[»]
5OSKX-ray2.11A/C1-451[»]
5OV7X-ray2.40A/C1-451[»]
5XAFX-ray2.55A/C1-451[»]
5XAGX-ray2.56A/C1-451[»]
5XLTX-ray2.81A/C1-450[»]
5XLZX-ray2.30A/C1-450[»]
5YZ3X-ray2.54A/C1-450[»]
5Z4PX-ray2.50A1-438[»]
C1-440[»]
6BBNX-ray3.51A/C1-451[»]
6F7CX-ray2.00A/C1-451[»]
6FIIX-ray2.40A/C1-451[»]
6FJFX-ray2.40A/C1-451[»]
6FJMX-ray2.10A/C1-451[»]
6FKJX-ray2.15A/C1-451[»]
6FKLX-ray2.10A/C1-451[»]
6GF3X-ray2.40A/C1-451[»]
6GJ4X-ray2.40A/C1-451[»]
6HX8X-ray2.40A/C1-451[»]
6I5CX-ray2.95A/C1-451[»]
6K9VX-ray2.54A/C1-450[»]
6QQNX-ray2.30A/C1-451[»]
6QTNX-ray1.90A/C1-451[»]
SMRiP81947
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-41283N
IntActiP81947, 1 interactor
MINTiP81947
STRINGi9913.ENSBTAP00000016242

PTM databases

iPTMnetiP81947
SwissPalmiP81947

Proteomic databases

PaxDbiP81947
PeptideAtlasiP81947
PRIDEiP81947

Genome annotation databases

GeneIDi539882
KEGGibta:539882

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		10376

Phylogenomic databases

eggNOGiKOG1376 Eukaryota
COG5023 LUCA
HOGENOMiHOG000165711
InParanoidiP81947
KOiK07374
OMAiVDNEACY
OrthoDBi514396at2759
TreeFamiTF300314

Enzyme and pathway databases

ReactomeiR-BTA-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-BTA-2467813 Separation of Sister Chromatids
R-BTA-2500257 Resolution of Sister Chromatid Cohesion
R-BTA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-BTA-380320 Recruitment of NuMA to mitotic centrosomes
R-BTA-5610787 Hedgehog 'off' state
R-BTA-5617833 Cilium Assembly
R-BTA-5620924 Intraflagellar transport
R-BTA-5626467 RHO GTPases activate IQGAPs
R-BTA-5663220 RHO GTPases Activate Formins
R-BTA-6807878 COPI-mediated anterograde transport
R-BTA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-BTA-68877 Mitotic Prometaphase
R-BTA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-BTA-8955332 Carboxyterminal post-translational modifications of tubulin
R-BTA-983189 Kinesins

Miscellaneous databases

EvolutionaryTraceiP81947

Gene expression databases

BgeeiENSBTAG00000012244 Expressed in 9 organ(s), highest expression level in prefrontal cortex

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
IPR002452 Alpha_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
PRINTSiPR01162 ALPHATUBULIN
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

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 nameiTBA1B_BOVIN
<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: P81947
Secondary accession number(s): A6H700
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: February 10, 2009
Last modified: December 11, 2019
This is version 138 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

<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, 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
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