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UniProtKB - P02557 (TBB_YEAST)

Entry version 186 (13 Feb 2019)
Sequence version 2 (01 Nov 1995)
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Protein

Tubulin beta chain

Gene

TUB2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 (PubMed:28013290). 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.1 Publication

Miscellaneous

Rhizoxin, an antibiotic that exhibits potent anti-mitotic activity against most eukaryotic cells except for yeasts, binds to beta tubulin.

Regions

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

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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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

Biological processAntibiotic resistance
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		YEAST:G3O-30425-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-5610787 Hedgehog 'off' state
R-SCE-5617833 Cilium Assembly
R-SCE-5626467 RHO GTPases activate IQGAPs
R-SCE-6798695 Neutrophil degranulation
R-SCE-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-SCE-8955332 Carboxyterminal post-translational modifications of tubulin
R-SCE-983189 Kinesins

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Tubulin beta chain
Alternative name(s):
Beta-tubulin
<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:TUB2
Ordered Locus Names:YFL037W
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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
  • UP000002311 <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 VI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:YFL037W

Saccharomyces Genome Database

More...SGDi		S000001857 TUB2

<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 Cell wall Cytoskeleton Vacuole 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi100V → N: Becomes sensitive to rhizoxin. 1
Mutagenesisi390K → Q: Decreased microtubule stability. 1 Publication1
Mutagenesisi421E → K: Increased microtubule polymerization and depolymerization rates. Increased microtubule stability. Decreased kinesin KIP3 subcellular location at microtubule plus ends. 1 Publication1

<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_00000484431 – 457Tubulin beta chainAdd BLAST457

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 residuei278PhosphoserineCombined sources1
Modified residuei280PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P02557

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

More...PaxDbi		P02557

PRoteomics IDEntifications database

More...PRIDEi		P02557

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P02557

<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.

<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

WithEntry#Exp.IntActNotes
RBL2P486062EBI-18986,EBI-18991

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		31109, 441 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1424 Tubulin alpha-beta heterodimeric complex, TUB1 variant
CPX-1425 Tubulin alpha-beta heterodimeric complex, TUB3 variant

Database of interacting proteins

More...DIPi		DIP-2340N

Protein interaction database and analysis system

More...IntActi		P02557, 339 interactors

Molecular INTeraction database

More...MINTi		P02557

STRING: functional protein association networks

More...STRINGi		4932.YFL037W

<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

1457
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
4FFBX-ray2.88B1-457[»]
4U3JX-ray2.81B1-457[»]
5W3Felectron microscopy3.70B1-457[»]
5W3Helectron microscopy4.00B1-457[»]
5W3Jelectron microscopy4.00B1-457[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P02557

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

More...SMRi		P02557

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154394

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000165710

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P02557

KEGG Orthology (KO)

More...KOi		K07375

Identification of Orthologs from Complete Genome Data

More...OMAi		DMSATFI

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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

Integrated resource of protein families, domains and functional sites

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

The PANTHER Classification System

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

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01163 BETATUBULIN
PR01161 TUBULIN

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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

PROSITE; a protein domain and family database

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

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

P02557-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MREIIHISTG QCGNQIGAAF WETICGEHGL DFNGTYHGHD DIQKERLNVY 
        60         70         80         90        100
FNEASSGKWV PRSINVDLEP GTIDAVRNSA IGNLFRPDNY IFGQSSAGNV 
       110        120        130        140        150
WAKGHYTEGA ELVDSVMDVI RREAEGCDSL QGFQITHSLG GGTGSGMGTL 
       160        170        180        190        200
LISKIREEFP DRMMATFSVL PSPKTSDTVV EPYNATLSVH QLVEHSDETF 
       210        220        230        240        250
CIDNEALYDI CQRTLKLNQP SYGDLNNLVS SVMSGVTTSL RYPGQLNSDL 
       260        270        280        290        300
RKLAVNLVPF PRLHFFMVGY APLTAIGSQS FRSLTVPELT QQMFDAKNMM 
       310        320        330        340        350
AAADPRNGRY LTVAAFFRGK VSVKEVEDEM HKVQSKNSDY FVEWIPNNVQ 
       360        370        380        390        400
TAVCSVAPQG LDMAATFIAN STSIQELFKR VGDQFSAMFK RKAFLHWYTS 
       410        420        430        440        450
EGMDELEFSE AESNMNDLVS EYQQYQEATV EDDEEVDENG DFGAPQNQDE 

PITENFE
Length:457
Mass (Da):50,923
Last modified:November 1, 1995 - 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:i68EBEA7D7A5B8EA1
GO

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 conflicti9T → A in CAA24603 (PubMed:6380751).Curated1
Sequence conflicti12C → Y in CAA24603 (PubMed:6380751).Curated1
Sequence conflicti71G → W in CAA24603 (PubMed:6380751).Curated1
Sequence conflicti152I → F in CAA24603 (PubMed:6380751).Curated1
Sequence conflicti156R → K in CAA24603 (PubMed:6380751).Curated1
Sequence conflicti159F → L in CAA24603 (PubMed:6380751).Curated1

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
V01296 Genomic DNA Translation: CAA24603.1
D50617 Genomic DNA Translation: BAA09202.1
X00209 Genomic DNA Translation: CAA25035.1
BK006940 Genomic DNA Translation: DAA12403.1

Protein sequence database of the Protein Information Resource

More...PIRi		S56217 UBBYB

NCBI Reference Sequences

More...RefSeqi		NP_116616.1, NM_001179929.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YFL037W_mRNA; YFL037W_mRNA; YFL037W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		850506

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YFL037W

<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
V01296 Genomic DNA Translation: CAA24603.1
D50617 Genomic DNA Translation: BAA09202.1
X00209 Genomic DNA Translation: CAA25035.1
BK006940 Genomic DNA Translation: DAA12403.1
PIRiS56217 UBBYB
RefSeqiNP_116616.1, NM_001179929.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FFBX-ray2.88B1-457[»]
4U3JX-ray2.81B1-457[»]
5W3Felectron microscopy3.70B1-457[»]
5W3Helectron microscopy4.00B1-457[»]
5W3Jelectron microscopy4.00B1-457[»]
ProteinModelPortaliP02557
SMRiP02557
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31109, 441 interactors
ComplexPortaliCPX-1424 Tubulin alpha-beta heterodimeric complex, TUB1 variant
CPX-1425 Tubulin alpha-beta heterodimeric complex, TUB3 variant
DIPiDIP-2340N
IntActiP02557, 339 interactors
MINTiP02557
STRINGi4932.YFL037W

PTM databases

iPTMnetiP02557

Proteomic databases

MaxQBiP02557
PaxDbiP02557
PRIDEiP02557

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYFL037W_mRNA; YFL037W_mRNA; YFL037W
GeneIDi850506
KEGGisce:YFL037W

Organism-specific databases

EuPathDBiFungiDB:YFL037W
SGDiS000001857 TUB2

Phylogenomic databases

GeneTreeiENSGT00940000154394
HOGENOMiHOG000165710
InParanoidiP02557
KOiK07375
OMAiDMSATFI

Enzyme and pathway databases

BioCyciYEAST:G3O-30425-MONOMER
ReactomeiR-SCE-5610787 Hedgehog 'off' state
R-SCE-5617833 Cilium Assembly
R-SCE-5626467 RHO GTPases activate IQGAPs
R-SCE-6798695 Neutrophil degranulation
R-SCE-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-SCE-8955332 Carboxyterminal post-translational modifications of tubulin
R-SCE-983189 Kinesins

Miscellaneous databases

Protein Ontology

More...PROi		PR:P02557

Family and domain databases

Gene3Di1.10.287.600, 1 hit
3.30.1330.20, 1 hit
3.40.50.1440, 1 hit
InterProiView protein in InterPro
IPR013838 Beta-tubulin_BS
IPR002453 Beta_tubulin
IPR008280 Tub_FtsZ_C
IPR000217 Tubulin
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR023123 Tubulin_C
IPR017975 Tubulin_CS
IPR003008 Tubulin_FtsZ_GTPase
PANTHERiPTHR11588 PTHR11588, 1 hit
PTHR11588:SF256 PTHR11588:SF256, 1 hit
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01163 BETATUBULIN
PR01161 TUBULIN
SMARTiView protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit
SUPFAMiSSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit
PROSITEiView protein in PROSITE
PS00227 TUBULIN, 1 hit
PS00228 TUBULIN_B_AUTOREG, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTBB_YEAST
<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: P02557
Secondary accession number(s): D6VTJ3
<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: July 21, 1986
Last sequence update: November 1, 1995
Last modified: February 13, 2019
This is version 186 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 programFungal 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, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast chromosome VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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