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Entry version 17 (07 Oct 2020)
Sequence version 1 (18 Jul 2018)
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Protein

Tubulin alpha-3C chain

Gene

TUBA3C

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.

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>Sitei450Involved in polymerization1

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 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

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

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
P0DPH7

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1445148, Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-190840, Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-HSA-190861, Gap junction assembly
R-HSA-2132295, MHC class II antigen presentation
R-HSA-2467813, Separation of Sister Chromatids
R-HSA-2500257, Resolution of Sister Chromatid Cohesion
R-HSA-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-380320, Recruitment of NuMA to mitotic centrosomes
R-HSA-389957, Prefoldin mediated transfer of substrate to CCT/TriC
R-HSA-389960, Formation of tubulin folding intermediates by CCT/TriC
R-HSA-389977, Post-chaperonin tubulin folding pathway
R-HSA-437239, Recycling pathway of L1
R-HSA-5610787, Hedgehog 'off' state
R-HSA-5617833, Cilium Assembly
R-HSA-5620924, Intraflagellar transport
R-HSA-5626467, RHO GTPases activate IQGAPs
R-HSA-5663220, RHO GTPases Activate Formins
R-HSA-6807878, COPI-mediated anterograde transport
R-HSA-6811434, COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-6811436, COPI-independent Golgi-to-ER retrograde traffic
R-HSA-68877, Mitotic Prometaphase
R-HSA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8955332, Carboxyterminal post-translational modifications of tubulin
R-HSA-9609690, HCMV Early Events
R-HSA-9609736, Assembly and cell surface presentation of NMDA receptors
R-HSA-9619483, Activation of AMPK downstream of NMDARs
R-HSA-9646399, Aggrephagy
R-HSA-9648025, EML4 and NUDC in mitotic spindle formation
R-HSA-9668328, Sealing of the nuclear envelope (NE) by ESCRT-III
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%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 alpha-3C chain
Alternative name(s):
Alpha-tubulin 2
Alpha-tubulin 3C
Tubulin alpha-2 chain
Cleaved into the following 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:TUBA3C
Synonyms:TUBA2
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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: Chromosome 13

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:12408, TUBA3C

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
602528, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P0DPH7

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

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

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

Organism-specific databases

DisGeNET

More...
DisGeNETi
113457
7278

Open Targets

More...
OpenTargetsi
ENSG00000075886
ENSG00000198033

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2095182

<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_00000481101 – 450Tubulin alpha-3C chainAdd BLAST450
ChainiPRO_00004373991 – 449Detyrosinated tubulin alpha-3C chain2 PublicationsAdd BLAST449

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-acetyllysine1 Publication1
Modified residuei2823'-nitrotyrosineBy similarity1
Modified residuei439PhosphoserineBy similarity1
Modified residuei4503'-nitrotyrosineBy 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 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
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.1 Publication
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-450 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.3 Publications
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 (PubMed:26972003). In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity).By similarity1 Publication
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 (PubMed:25908662). 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 similarity1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0DPH7

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P0DPH7

PeptideAtlas

More...
PeptideAtlasi
P0DPH7

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P0DPH7

<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 in testis.1 Publication

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P0DPH7, baseline and differential

<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.

<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
P0DPH7

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 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

Ensembl GeneTree

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GeneTreei
ENSGT00950000182825

KEGG Orthology (KO)

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KOi
K07374

Identification of Orthologs from Complete Genome Data

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OMAi
QMVPNGD

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

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PANTHERi
PTHR11588, PTHR11588, 1 hit

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
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%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>Sequences (2)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.

<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 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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P0DPH7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN
60 70 80 90 100
TFFSETGAGK HVPRAVFVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKEIVDLVLD RIRKLADLCT GLQGFLIFHS FGGGTGSGFA
160 170 180 190 200
SLLMERLSVD YGKKSKLEFA IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCMLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440 450
KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGVDSV EAEAEEGEEY
Length:450
Mass (Da):49,960
Last modified:July 18, 2018 - 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:i2A78714CBA782D55
GO
Isoform 2 (identifier: P0DPH7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     393-424: Missing.

Show »
Length:418
Mass (Da):46,112
Checksum:iB103B8C73F95D81B
GO

Natural variant

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_03454175V → L. Corresponds to variant dbSNP:rs36215077Ensembl.1
Natural variantiVAR_052666392D → V. Corresponds to variant dbSNP:rs17076703Ensembl.1
Natural variantiVAR_022068440V → M. Corresponds to variant dbSNP:rs1803092Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_006678393 – 424Missing in isoform 2. 1 PublicationAdd BLAST32

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF005392 Genomic DNA Translation: AAC39578.1
AL139327 Genomic DNA No translation available.
CH471075 Genomic DNA Translation: EAX08210.1
BC011721 mRNA Translation: AAH11721.1
L11645 mRNA Translation: AAA35521.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS9284.1 [P0DPH7-1]

NCBI Reference Sequences

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RefSeqi
NP_005992.1, NM_006001.2 [P0DPH7-1]
NP_525125.2, NM_080386.3 [P0DPH7-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000400113; ENSP00000382982; ENSG00000198033 [P0DPH7-1]
ENST00000618094; ENSP00000482878; ENSG00000198033 [P0DPH7-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
113457
7278

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:113457
hsa:7278

Keywords - Coding sequence diversityi

Alternative splicing, 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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Tubulin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005392 Genomic DNA Translation: AAC39578.1
AL139327 Genomic DNA No translation available.
CH471075 Genomic DNA Translation: EAX08210.1
BC011721 mRNA Translation: AAH11721.1
L11645 mRNA Translation: AAA35521.1
CCDSiCCDS9284.1 [P0DPH7-1]
RefSeqiNP_005992.1, NM_006001.2 [P0DPH7-1]
NP_525125.2, NM_080386.3 [P0DPH7-1]

3D structure databases

SMRiP0DPH7
ModBaseiSearch...

Chemistry databases

ChEMBLiCHEMBL2095182

PTM databases

iPTMnetiP0DPH7

Proteomic databases

jPOSTiP0DPH7
MassIVEiP0DPH7
PeptideAtlasiP0DPH7

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
22219, 156 antibodies

Genome annotation databases

EnsembliENST00000400113; ENSP00000382982; ENSG00000198033 [P0DPH7-1]
ENST00000618094; ENSP00000482878; ENSG00000198033 [P0DPH7-2]
GeneIDi113457
7278
KEGGihsa:113457
hsa:7278

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
113457
7278
DisGeNETi113457
7278

GeneCards: human genes, protein and diseases

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GeneCardsi
TUBA3C
HGNCiHGNC:12408, TUBA3C
MIMi602528, gene
neXtProtiNX_P0DPH7
OpenTargetsiENSG00000075886
ENSG00000198033

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

GeneTreeiENSGT00950000182825
KOiK07374
OMAiQMVPNGD

Enzyme and pathway databases

PathwayCommonsiP0DPH7
ReactomeiR-HSA-1445148, Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-190840, Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-HSA-190861, Gap junction assembly
R-HSA-2132295, MHC class II antigen presentation
R-HSA-2467813, Separation of Sister Chromatids
R-HSA-2500257, Resolution of Sister Chromatid Cohesion
R-HSA-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-380320, Recruitment of NuMA to mitotic centrosomes
R-HSA-389957, Prefoldin mediated transfer of substrate to CCT/TriC
R-HSA-389960, Formation of tubulin folding intermediates by CCT/TriC
R-HSA-389977, Post-chaperonin tubulin folding pathway
R-HSA-437239, Recycling pathway of L1
R-HSA-5610787, Hedgehog 'off' state
R-HSA-5617833, Cilium Assembly
R-HSA-5620924, Intraflagellar transport
R-HSA-5626467, RHO GTPases activate IQGAPs
R-HSA-5663220, RHO GTPases Activate Formins
R-HSA-6807878, COPI-mediated anterograde transport
R-HSA-6811434, COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-6811436, COPI-independent Golgi-to-ER retrograde traffic
R-HSA-68877, Mitotic Prometaphase
R-HSA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8955332, Carboxyterminal post-translational modifications of tubulin
R-HSA-9609690, HCMV Early Events
R-HSA-9609736, Assembly and cell surface presentation of NMDA receptors
R-HSA-9619483, Activation of AMPK downstream of NMDARs
R-HSA-9646399, Aggrephagy
R-HSA-9648025, EML4 and NUDC in mitotic spindle formation
R-HSA-9668328, Sealing of the nuclear envelope (NE) by ESCRT-III
R-HSA-983189, Kinesins

Miscellaneous databases

Protein Ontology

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PROi
PR:P0DPH7

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

ExpressionAtlasiP0DPH7, 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
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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTBA3C_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: P0DPH7
Secondary accession number(s): A6NJQ0
, Q13748, Q5W099, Q6PEY3, Q96F18
<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: July 18, 2018
Last sequence update: July 18, 2018
Last modified: October 7, 2020
This is version 17 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. SIMILARITY comments
    Index of protein domains and families
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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