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UniProtKB - P68363 (TBA1B_HUMAN)

Entry version 168 (13 Nov 2019)
Sequence version 1 (13 Aug 1987)
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Protein

Tubulin alpha-1B chain

Gene

TUBA1B

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>Sitei451Involved in polymerization1

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-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-389960 Formation of tubulin folding intermediates by CCT/TriC
R-HSA-389977 Post-chaperonin tubulin folding pathway
R-HSA-437239 Recycling pathway of L1
R-HSA-5610787 Hedgehog 'off' state
R-HSA-5617833 Cilium Assembly
R-HSA-5620924 Intraflagellar transport
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-6807878 COPI-mediated anterograde transport
R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-HSA-68877 Mitotic Prometaphase
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8955332 Carboxyterminal post-translational modifications of tubulin
R-HSA-9609736 Assembly and cell surface presentation of NMDA receptors
R-HSA-9619483 Activation of AMPK downstream of NMDARs
R-HSA-983189 Kinesins

SIGNOR Signaling Network Open Resource

More...SIGNORi		P68363

<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 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:TUBA1B
<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 12

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:18809 TUBA1B

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		602530 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P68363

<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		10376

Open Targets

More...OpenTargetsi		ENSG00000123416

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA162407332

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P68363

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3797010

Drug and drug target database

More...DrugBanki		DB07574 2-MERCAPTO-N-[1,2,3,10-TETRAMETHOXY-9-OXO-5,6,7,9-TETRAHYDRO-BENZO[A]HEPTALEN-7-YL]ACETAMIDE
DB05147 CYT997
DB01873 Epothilone D
DB03010 Patupilone

DrugCentral

More...DrugCentrali		P68363

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		TUBA1B

Domain mapping of disease mutations (DMDM)

More...DMDMi		55977474

<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_00000481081 – 451Tubulin alpha-1B chainAdd BLAST451
ChainiPRO_00004373841 – 450Detyrosinated tubulin alpha-1B chain2 PublicationsAdd 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; alternate1 Publication1
Modified residuei40N6-acetyllysine; alternate1 Publication1
Modified residuei48Phosphoserine1 Publication1
Modified residuei232Phosphoserine1 Publication1
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)
Modified residuei339Omega-N-methylarginine1 Publication1
Cross-linki370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei439PhosphoserineBy similarity1
Modified residuei4455-glutamyl polyglutamateBy similarity1
Modified residuei4513'-nitrotyrosine1 Publication1

<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
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.1 Publication
Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution.1 Publication
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
Tubulin alpha-1B chain: 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
Detyrosinated tubulin alpha-1B chain: 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, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P68363

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P68363

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P68363

MaxQB - The MaxQuant DataBase

More...MaxQBi		P68363

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

More...PaxDbi		P68363

PeptideAtlas

More...PeptideAtlasi		P68363

PRoteomics IDEntifications database

More...PRIDEi		P68363

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		57533 [P68363-1]

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P68363-1 [P68363-1]

2D gel databases

USC-OGP 2-DE database

More...OGPi		P68363

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P68363

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P68363

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P68363

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

More...PhosphoSitePlusi		P68363

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P68363

<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		ENSG00000123416 Expressed in 123 organ(s), highest expression level in anterior cingulate cortex

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P68363 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P68363 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB011513
HPA039247
HPA043684
HPA063394

<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.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		115651, 178 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P68363

Protein interaction database and analysis system

More...IntActi		P68363, 65 interactors

Molecular INTeraction database

More...MINTi		P68363

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000336799

<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		P68363

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		P68363

<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

Ensembl GeneTree

More...GeneTreei		ENSGT00950000182825

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000165711

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P68363

KEGG Orthology (KO)

More...KOi		K07374

Identification of Orthologs from Complete Genome Data

More...OMAi		VDNEACY

Database of Orthologous Groups

More...OrthoDBi		514396at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P68363

TreeFam database of animal gene trees

More...TreeFami		TF300314

Family and domain databases

Database of protein disorder

More...DisProti		DP02251

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>Sequences (2+)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.

<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.

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.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P68363-1) [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 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:August 13, 1987 - 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:i94355B4EC2086429
GO
Isoform 2 (identifier: P68363-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     108-223: Missing.

Note: No experimental confirmation available.
Show »
Length:335
Mass (Da):37,218
Checksum:iCEC8DAFE68516D27
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
F8VVB9F8VVB9_HUMAN
Tubulin alpha-1B chain
TUBA1B
246Annotation 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>
F8VX09F8VX09_HUMAN
Tubulin alpha-1B chain
TUBA1B
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>
F8VWV9F8VWV9_HUMAN
Tubulin alpha-1B chain
TUBA1B
81Annotation 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>
F8VRK0F8VRK0_HUMAN
Tubulin alpha-1B chain
TUBA1B
49Annotation 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>
F8VU66F8VU66_HUMAN
Tubulin alpha-1B chain
TUBA1B
49Annotation 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>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti131G → R in AAA91576 (PubMed:6646120).Curated1
Sequence conflicti290E → D in AAA91576 (PubMed:6646120).Curated1
Sequence conflicti308R → G in AAA91576 (PubMed:6646120).Curated1
Sequence conflicti340S → T in AAA91576 (PubMed:6646120).Curated1

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_055764108 – 223Missing in isoform 2. 1 PublicationAdd BLAST116

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
K00558 mRNA Translation: AAA91576.1
AF081484 mRNA Translation: AAC31959.1
DQ400107 mRNA Translation: ABD60581.1
BC000696 mRNA Translation: AAH00696.1
BC001128 mRNA Translation: AAH01128.1
BC006379 mRNA Translation: AAH06379.1
BC006481 mRNA Translation: AAH06481.1
BC008659 mRNA Translation: AAH08659.1
BC009314 mRNA Translation: AAH09314.1
BC009509 mRNA Translation: AAH09509.1
BC009512 mRNA Translation: AAH09512.1
BC009513 mRNA Translation: AAH09513.1
BC010494 mRNA Translation: AAH10494.1
BC011572 mRNA Translation: AAH11572.1
BC015883 mRNA Translation: AAH15883.1
BC017004 mRNA Translation: AAH17004.1
BC021564 mRNA Translation: AAH21564.1
BC030820 mRNA Translation: AAH30820.1
BC071904 mRNA Translation: AAH71904.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS31792.1 [P68363-1]

Protein sequence database of the Protein Information Resource

More...PIRi		I77403

NCBI Reference Sequences

More...RefSeqi		NP_006073.2, NM_006082.2 [P68363-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000336023; ENSP00000336799; ENSG00000123416 [P68363-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		10376

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:10376

UCSC genome browser

More...UCSCi		uc001rtm.4 human [P68363-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
K00558 mRNA Translation: AAA91576.1
AF081484 mRNA Translation: AAC31959.1
DQ400107 mRNA Translation: ABD60581.1
BC000696 mRNA Translation: AAH00696.1
BC001128 mRNA Translation: AAH01128.1
BC006379 mRNA Translation: AAH06379.1
BC006481 mRNA Translation: AAH06481.1
BC008659 mRNA Translation: AAH08659.1
BC009314 mRNA Translation: AAH09314.1
BC009509 mRNA Translation: AAH09509.1
BC009512 mRNA Translation: AAH09512.1
BC009513 mRNA Translation: AAH09513.1
BC010494 mRNA Translation: AAH10494.1
BC011572 mRNA Translation: AAH11572.1
BC015883 mRNA Translation: AAH15883.1
BC017004 mRNA Translation: AAH17004.1
BC021564 mRNA Translation: AAH21564.1
BC030820 mRNA Translation: AAH30820.1
BC071904 mRNA Translation: AAH71904.1
CCDSiCCDS31792.1 [P68363-1]
PIRiI77403
RefSeqiNP_006073.2, NM_006082.2 [P68363-1]

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
2E4HNMR-B416-451[»]
5IJ0electron microscopy3.80A1-437[»]
5IJ9electron microscopy3.70A1-437[»]
5N5Nelectron microscopy4.00G/H/I/J/K/L1-437[»]
6E7Belectron microscopy3.50A1-437[»]
6E7Celectron microscopy3.65A1-437[»]
6I2Ielectron microscopy3.60A1-451[»]
6J4VX-ray2.10C431-451[»]
SMRiP68363
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi115651, 178 interactors
CORUMiP68363
IntActiP68363, 65 interactors
MINTiP68363
STRINGi9606.ENSP00000336799

Chemistry databases

ChEMBLiCHEMBL3797010
DrugBankiDB07574 2-MERCAPTO-N-[1,2,3,10-TETRAMETHOXY-9-OXO-5,6,7,9-TETRAHYDRO-BENZO[A]HEPTALEN-7-YL]ACETAMIDE
DB05147 CYT997
DB01873 Epothilone D
DB03010 Patupilone
DrugCentraliP68363

PTM databases

CarbonylDBiP68363
iPTMnetiP68363
PhosphoSitePlusiP68363
SwissPalmiP68363

Polymorphism and mutation databases

BioMutaiTUBA1B
DMDMi55977474

2D gel databases

OGPiP68363
SWISS-2DPAGEiP68363

Proteomic databases

EPDiP68363
jPOSTiP68363
MassIVEiP68363
MaxQBiP68363
PaxDbiP68363
PeptideAtlasiP68363
PRIDEiP68363
ProteomicsDBi57533 [P68363-1]
TopDownProteomicsiP68363-1 [P68363-1]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P68363

The DNASU plasmid repository

More...DNASUi		10376

Genome annotation databases

EnsembliENST00000336023; ENSP00000336799; ENSG00000123416 [P68363-1]
GeneIDi10376
KEGGihsa:10376
UCSCiuc001rtm.4 human [P68363-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		10376
DisGeNETi10376

GeneCards: human genes, protein and diseases

More...GeneCardsi		TUBA1B
HGNCiHGNC:18809 TUBA1B
HPAiCAB011513
HPA039247
HPA043684
HPA063394
MIMi602530 gene
neXtProtiNX_P68363
OpenTargetsiENSG00000123416
PharmGKBiPA162407332

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1376 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00950000182825
HOGENOMiHOG000165711
InParanoidiP68363
KOiK07374
OMAiVDNEACY
OrthoDBi514396at2759
PhylomeDBiP68363
TreeFamiTF300314

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-389960 Formation of tubulin folding intermediates by CCT/TriC
R-HSA-389977 Post-chaperonin tubulin folding pathway
R-HSA-437239 Recycling pathway of L1
R-HSA-5610787 Hedgehog 'off' state
R-HSA-5617833 Cilium Assembly
R-HSA-5620924 Intraflagellar transport
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-6807878 COPI-mediated anterograde transport
R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-HSA-68877 Mitotic Prometaphase
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8955332 Carboxyterminal post-translational modifications of tubulin
R-HSA-9609736 Assembly and cell surface presentation of NMDA receptors
R-HSA-9619483 Activation of AMPK downstream of NMDARs
R-HSA-983189 Kinesins
SIGNORiP68363

Miscellaneous databases

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

More...ChiTaRSi		TUBA1B human
EvolutionaryTraceiP68363

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		TUBA1B

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

More...GenomeRNAii		10376
PharosiP68363

Protein Ontology

More...PROi		PR:P68363

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000123416 Expressed in 123 organ(s), highest expression level in anterior cingulate cortex
ExpressionAtlasiP68363 baseline and differential
GenevisibleiP68363 HS

Family and domain databases

DisProtiDP02251
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_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: P68363
Secondary accession number(s): P04687
, P05209, Q27I68, Q8WU19
<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 13, 1987
Last sequence update: August 13, 1987
Last modified: November 13, 2019
This is version 168 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

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

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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