Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P00830 (ATPB_YEAST)

Entry version 204 (13 Feb 2019)
Sequence version 2 (20 Dec 2005)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

ATP synthase subunit beta, mitochondrial

Gene

ATP2

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

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

Miscellaneous

Present with 164000 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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 bindingi190 – 197ATPBy similarity8

<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

  • ATP synthesis coupled proton transport Source: SGD
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

Molecular functionTranslocase
Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		YEAST:G3O-31742-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.6.3.14 984

Protein family/group databases

Transport Classification Database

More...TCDBi		3.A.2.1.3 the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily

<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:
ATP synthase subunit beta, mitochondrial (EC:7.1.2.2)
<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:ATP2
Ordered Locus Names:YJR121W
ORF Names:J2041
<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 X

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:YJR121W

Saccharomyces Genome Database

More...SGDi		S000003882 ATP2

<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

CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1075103

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 33MitochondrionAdd BLAST33
<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_000000245434 – 511ATP synthase subunit beta, mitochondrialAdd BLAST478

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 residuei112PhosphothreonineCombined sources1
Modified residuei237PhosphothreonineCombined sources1
Modified residuei373PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P00830

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

More...PaxDbi		P00830

PRoteomics IDEntifications database

More...PRIDEi		P00830

2D gel databases

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

More...SWISS-2DPAGEi		P00830

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P00830

<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

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c.

<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
INA17Q028882EBI-3242,EBI-7668387

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		33877, 200 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3281 Mitochondrial proton-transporting ATP synthase complex

Database of interacting proteins

More...DIPi		DIP-3028N

Protein interaction database and analysis system

More...IntActi		P00830, 176 interactors

Molecular INTeraction database

More...MINTi		P00830

STRING: functional protein association networks

More...STRINGi		4932.YJR121W

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P00830

<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

1511
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
2HLDX-ray2.80D/E/F/M/N/O/V/W/X34-511[»]
2WPDX-ray3.43D/E/F34-511[»]
2XOKX-ray3.01D/E/F1-507[»]
3FKSX-ray3.59D/E/F/M/N/O/V/W/X36-511[»]
3OE7X-ray3.19D/E/F/M/N/O/V/W/X36-511[»]
3OEEX-ray2.74D/E/F/M/N/O/V/W/X36-511[»]
3OEHX-ray3.00D/E/F/M/N/O/V/W/X36-511[»]
3OFNX-ray3.20D/E/F/M/N/O/V/W/X36-511[»]
3ZIAX-ray2.50D/E/F/N/O/P34-511[»]
3ZRYX-ray6.50D/E/F34-511[»]
4B2Qelectron microscopy37.00D/d39-508[»]
E/F/e/f39-511[»]
6B8Helectron microscopy3.60D/E/F/Y/Z/c34-511[»]
6CP3electron microscopy3.80D/E/F34-511[»]
6CP6electron microscopy3.60D/E/F34-511[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P00830

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

More...SMRi		P00830

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P00830

<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 ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

Ensembl GeneTree

More...GeneTreei		ENSGT00550000074800

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000009605

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P00830

KEGG Orthology (KO)

More...KOi		K02133

Identification of Orthologs from Complete Genome Data

More...OMAi		FNMIMDG

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1140.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01347 ATP_synth_beta_bact, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003593 AAA+_ATPase
IPR005722 ATP_synth_F1_bsu
IPR020003 ATPase_a/bsu_AS
IPR004100 ATPase_F1/V1/A1_a/bsu_N
IPR036121 ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR024034 ATPase_F1/V1_b/a_C
IPR027417 P-loop_NTPase

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00006 ATP-synt_ab, 1 hit
PF02874 ATP-synt_ab_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00382 AAA, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50615 SSF50615, 1 hit
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01039 atpD, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00152 ATPASE_ALPHA_BETA, 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.

<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.

P00830-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVLPRLYTAT SRAAFKAAKQ SAPLLSTSWK RCMASAAQST PITGKVTAVI 
        60         70         80         90        100
GAIVDVHFEQ SELPAILNAL EIKTPQGKLV LEVAQHLGEN TVRTIAMDGT 
       110        120        130        140        150
EGLVRGEKVL DTGGPISVPV GRETLGRIIN VIGEPIDERG PIKSKLRKPI 
       160        170        180        190        200
HADPPSFAEQ STSAEILETG IKVVDLLAPY ARGGKIGLFG GAGVGKTVFI 
       210        220        230        240        250
QELINNIAKA HGGFSVFTGV GERTREGNDL YREMKETGVI NLEGESKVAL 
       260        270        280        290        300
VFGQMNEPPG ARARVALTGL TIAEYFRDEE GQDVLLFIDN IFRFTQAGSE 
       310        320        330        340        350
VSALLGRIPS AVGYQPTLAT DMGLLQERIT TTKKGSVTSV QAVYVPADDL 
       360        370        380        390        400
TDPAPATTFA HLDATTVLSR GISELGIYPA VDPLDSKSRL LDAAVVGQEH 
       410        420        430        440        450
YDVASKVQET LQTYKSLQDI IAILGMDELS EQDKLTVERA RKIQRFLSQP 
       460        470        480        490        500
FAVAEVFTGI PGKLVRLKDT VASFKAVLEG KYDNIPEHAF YMVGGIEDVV 
       510 
AKAEKLAAEA N
Length:511
Mass (Da):54,794
Last modified:December 20, 2005 - 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:iEDFF256826F68F0C
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 conflicti201Q → M in AAA34443 (PubMed:6225776).Curated1
Sequence conflicti218T → A in AAA34444 (PubMed:2866186).Curated1
Sequence conflicti218T → A in AAA34443 (PubMed:6225776).Curated1
Sequence conflicti232 – 237REMKET → HEMEDS in AAA34443 (PubMed:6225776).Curated6
Sequence conflicti260G → E in AAA34443 (PubMed:6225776).Curated1
Sequence conflicti287 – 288FI → Y in AAA34443 (PubMed:6225776).Curated2
Sequence conflicti354 – 358APATT → SPSTS in AAA34444 (PubMed:2866186).Curated5
Sequence conflicti365 – 366TT → SS in AAA34444 (PubMed:2866186).Curated2
Sequence conflicti365 – 366TT → SS in AAA34443 (PubMed:6225776).Curated2
Sequence conflicti469 – 473DTVAS → RTRCL in AAA34443 (PubMed:6225776).Curated5
Sequence conflicti489A → R in AAA34443 (PubMed:6225776).Curated1
Sequence conflicti501A → R in AAA34444 (PubMed:2866186).Curated1
Sequence conflicti508A → R in AAA34444 (PubMed:2866186).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
M12082 Genomic DNA Translation: AAA34444.1
U46215 Genomic DNA Translation: AAC49475.1
Z49621 Genomic DNA Translation: CAA89652.1
X52004 Genomic DNA Translation: CAA36255.1
K00560 Genomic DNA Translation: AAA34443.1
BK006943 Genomic DNA Translation: DAA08906.1

Protein sequence database of the Protein Information Resource

More...PIRi		S57144 PWBYB

NCBI Reference Sequences

More...RefSeqi		NP_012655.3, NM_001181779.3

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YJR121W_mRNA; YJR121W_mRNA; YJR121W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		853585

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YJR121W

<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
M12082 Genomic DNA Translation: AAA34444.1
U46215 Genomic DNA Translation: AAC49475.1
Z49621 Genomic DNA Translation: CAA89652.1
X52004 Genomic DNA Translation: CAA36255.1
K00560 Genomic DNA Translation: AAA34443.1
BK006943 Genomic DNA Translation: DAA08906.1
PIRiS57144 PWBYB
RefSeqiNP_012655.3, NM_001181779.3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HLDX-ray2.80D/E/F/M/N/O/V/W/X34-511[»]
2WPDX-ray3.43D/E/F34-511[»]
2XOKX-ray3.01D/E/F1-507[»]
3FKSX-ray3.59D/E/F/M/N/O/V/W/X36-511[»]
3OE7X-ray3.19D/E/F/M/N/O/V/W/X36-511[»]
3OEEX-ray2.74D/E/F/M/N/O/V/W/X36-511[»]
3OEHX-ray3.00D/E/F/M/N/O/V/W/X36-511[»]
3OFNX-ray3.20D/E/F/M/N/O/V/W/X36-511[»]
3ZIAX-ray2.50D/E/F/N/O/P34-511[»]
3ZRYX-ray6.50D/E/F34-511[»]
4B2Qelectron microscopy37.00D/d39-508[»]
E/F/e/f39-511[»]
6B8Helectron microscopy3.60D/E/F/Y/Z/c34-511[»]
6CP3electron microscopy3.80D/E/F34-511[»]
6CP6electron microscopy3.60D/E/F34-511[»]
ProteinModelPortaliP00830
SMRiP00830
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33877, 200 interactors
ComplexPortaliCPX-3281 Mitochondrial proton-transporting ATP synthase complex
DIPiDIP-3028N
IntActiP00830, 176 interactors
MINTiP00830
STRINGi4932.YJR121W

Chemistry databases

BindingDBiP00830
ChEMBLiCHEMBL1075103

Protein family/group databases

TCDBi3.A.2.1.3 the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily

PTM databases

iPTMnetiP00830

2D gel databases

SWISS-2DPAGEiP00830

Proteomic databases

MaxQBiP00830
PaxDbiP00830
PRIDEiP00830

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR121W_mRNA; YJR121W_mRNA; YJR121W
GeneIDi853585
KEGGisce:YJR121W

Organism-specific databases

EuPathDBiFungiDB:YJR121W
SGDiS000003882 ATP2

Phylogenomic databases

GeneTreeiENSGT00550000074800
HOGENOMiHOG000009605
InParanoidiP00830
KOiK02133
OMAiFNMIMDG

Enzyme and pathway databases

BioCyciYEAST:G3O-31742-MONOMER
BRENDAi3.6.3.14 984

Miscellaneous databases

EvolutionaryTraceiP00830

Protein Ontology

More...PROi		PR:P00830

Family and domain databases

Gene3Di1.10.1140.10, 1 hit
HAMAPiMF_01347 ATP_synth_beta_bact, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR005722 ATP_synth_F1_bsu
IPR020003 ATPase_a/bsu_AS
IPR004100 ATPase_F1/V1/A1_a/bsu_N
IPR036121 ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR024034 ATPase_F1/V1_b/a_C
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00006 ATP-synt_ab, 1 hit
PF02874 ATP-synt_ab_N, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF50615 SSF50615, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01039 atpD, 1 hit
PROSITEiView protein in PROSITE
PS00152 ATPASE_ALPHA_BETA, 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 nameiATPB_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: P00830
Secondary accession number(s): D6VWU0
<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: December 20, 2005
Last modified: February 13, 2019
This is version 204 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, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again