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UniProtKB - P56480 (ATPB_MOUSE)

Entry version 193 (16 Oct 2019)
Sequence version 2 (02 May 2002)
Previous versions | rss
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Protein

ATP synthase subunit beta, mitochondrial

Gene

Atp5f1b

Organism
Mus musculus (Mouse)
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.

<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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei239ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi207 – 214ATPBy 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

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

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-1268020 Mitochondrial protein import
R-MMU-163210 Formation of ATP by chemiosmotic coupling
R-MMU-8949613 Cristae formation

<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, mitochondrialCurated (EC:7.1.2.2)
Alternative name(s):
ATP synthase F1 subunit betaBy similarity
<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:Atp5f1bBy similarity
Synonyms:Atp5b
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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 10

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:107801 Atp5b

<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

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

<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 – 46MitochondrionBy similarityAdd BLAST46
<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_000000244447 – 529ATP synthase subunit beta, mitochondrialAdd BLAST483

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi106O-linked (GlcNAc) serineBy similarity1
<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 residuei124N6-acetyllysine; alternateCombined sources1
Modified residuei124N6-succinyllysine; alternateCombined sources1
Modified residuei133N6-acetyllysine; alternateCombined sources1
Modified residuei133N6-succinyllysine; alternateCombined sources1
Modified residuei161N6-acetyllysine; alternateCombined sources1
Modified residuei161N6-succinyllysine; alternateCombined sources1
Modified residuei198N6-acetyllysineCombined sources1
Modified residuei259N6-acetyllysine; alternateCombined sources1
Modified residuei259N6-succinyllysine; alternateCombined sources1
Modified residuei264N6-acetyllysine; alternateCombined sources1
Modified residuei264N6-succinyllysine; alternateCombined sources1
Modified residuei312PhosphothreonineCombined sources1
Modified residuei426N6-acetyllysineCombined sources1
Modified residuei433PhosphoserineBy similarity1
Modified residuei480N6-acetyllysineCombined sources1
Modified residuei485N6-acetyllysineCombined sources1
Modified residuei522N6-acetyllysine; alternateCombined sources1
Modified residuei522N6-succinyllysine; alternateCombined sources1
Modified residuei529PhosphoserineCombined sources1

<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

Acetylation of Lys-133 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...CPTACi		non-CPTAC-3766

Encyclopedia of Proteome Dynamics

More...EPDi		P56480

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P56480

MaxQB - The MaxQuant DataBase

More...MaxQBi		P56480

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

More...PaxDbi		P56480

PeptideAtlas

More...PeptideAtlasi		P56480

PRoteomics IDEntifications database

More...PRIDEi		P56480

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P56480

2D gel databases

2-DE database at Universidad Complutense de Madrid

More...COMPLUYEAST-2DPAGEi		P56480

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00468481
P56480

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

More...SWISS-2DPAGEi		P56480

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		P56480

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P56480

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P56480

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

More...PhosphoSitePlusi		P56480

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P56480

<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		ENSMUSG00000025393 Expressed in 308 organ(s), highest expression level in central gray substance of midbrain

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P56480 MM

<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.

Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and ATP5MPL (By similarity).

Interacts with PPIF (PubMed:21281446).

Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F1F0 ATP synthase and enhances neurons metabolic efficiency (By similarity).

Interacts with CLN5 and PPT1 (PubMed:19941651).

By similarity2 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		198254, 13 interactors

Protein interaction database and analysis system

More...IntActi		P56480, 36 interactors

Molecular INTeraction database

More...MINTi		P56480

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000026459

<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		P56480

Database of comparative protein structure models

More...ModBasei		Search...

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

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

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1350 Eukaryota
COG0055 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00550000074800

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P56480

KEGG Orthology (KO)

More...KOi		K02133

Identification of Orthologs from Complete Genome Data

More...OMAi		FNMIMDG

Database of Orthologous Groups

More...OrthoDBi		495235at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P56480

TreeFam database of animal gene trees

More...TreeFami		TF105640

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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P56480-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLSLVGRVAS ASASGALRGL SPSAALPQAQ LLLRAAPAGV HPARDYAAQA 
        60         70         80         90        100
SAAPKAGTAT GRIVAVIGAV VDVQFDEGLP PILNALEVQG RDSRLVLEVA 
       110        120        130        140        150
QHLGESTVRT IAMDGTEGLV RGQKVLDSGA PIKIPVGPET LGRIMNVIGE 
       160        170        180        190        200
PIDERGPIKT KQFAPIHAEA PEFIEMSVEQ EILVTGIKVV DLLAPYAKGG 
       210        220        230        240        250
KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT REGNDLYHEM 
       260        270        280        290        300
IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD 
       310        320        330        340        350
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK 
       360        370        380        390        400
KGSITSVQAI YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP 
       410        420        430        440        450
LDSTSRIMDP NIVGNEHYDV ARGVQKILQD YKSLQDIIAI LGMDELSEED 
       460        470        480        490        500
KLTVSRARKI QRFLSQPFQV AEVFTGHMGK LVPLKETIKG FQQILAGEYD 
       510        520 
HLPEQAFYMV GPIEEAVAKA DKLAEEHGS
Length:529
Mass (Da):56,300
Last modified:May 2, 2002 - 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:iF3E1100C390A78A7
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH37127 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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 conflicti25A → V in AAB86421 (PubMed:10657236).Curated1
Sequence conflicti43A → V in BAE35088 (PubMed:16141072).Curated1
Sequence conflicti76D → G in BAE40961 (PubMed:16141072).Curated1
Sequence conflicti92D → E in AAB86421 (PubMed:10657236).Curated1
Sequence conflicti134I → V in BAE31497 (PubMed:16141072).Curated1
Sequence conflicti239R → K in AAB86421 (PubMed:10657236).Curated1
Sequence conflicti271Q → R in BAE38888 (PubMed:16141072).Curated1
Sequence conflicti271Q → R in BAE39301 (PubMed:16141072).Curated1
Sequence conflicti279 – 280RA → PT in AAB86421 (PubMed:10657236).Curated2
Sequence conflicti288T → A in BAE31497 (PubMed:16141072).Curated1
Sequence conflicti288T → A in BAE31630 (PubMed:16141072).Curated1
Sequence conflicti375T → N in BAE30095 (PubMed:16141072).Curated1
Sequence conflicti383T → S in BAB22802 (PubMed:16141072).Curated1
Sequence conflicti433 – 434SL → FF in AAB86421 (PubMed:10657236).Curated2
Sequence conflicti466Q → H in BAB22802 (PubMed:16141072).Curated1
Sequence conflicti469Q → R in BAE39797 (PubMed:16141072).Curated1
Sequence conflicti518A → V in BAE35331 (PubMed:16141072).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
AF030559 mRNA Translation: AAB86421.1
AK003460 mRNA Translation: BAB22802.1
AK010314 mRNA Translation: BAB26846.1
AK084009 mRNA Translation: BAC39095.1
AK145684 mRNA Translation: BAE26587.1
AK148891 mRNA Translation: BAE28692.1
AK150599 mRNA Translation: BAE29691.1
AK151081 mRNA Translation: BAE30095.1
AK151600 mRNA Translation: BAE30540.1
AK152788 mRNA Translation: BAE31497.1
AK152976 mRNA Translation: BAE31630.1
AK153099 mRNA Translation: BAE31720.1
AK159444 mRNA Translation: BAE35088.1
AK159737 mRNA Translation: BAE35331.1
AK159978 mRNA Translation: BAE35529.1
AK160199 mRNA Translation: BAE35689.1
AK160608 mRNA Translation: BAE35911.1
AK164383 mRNA Translation: BAE37764.1
AK166525 mRNA Translation: BAE38829.1
AK166603 mRNA Translation: BAE38888.1
AK166979 mRNA Translation: BAE39161.1
AK167119 mRNA Translation: BAE39267.1
AK167160 mRNA Translation: BAE39301.1
AK167728 mRNA Translation: BAE39769.1
AK167764 mRNA Translation: BAE39797.1
AK168692 mRNA Translation: BAE40537.1
AK168941 mRNA Translation: BAE40749.1
AK169184 mRNA Translation: BAE40961.1
BC018392 mRNA Translation: AAH18392.1
BC037127 mRNA Translation: AAH37127.1 Different initiation.
BC046616 mRNA Translation: AAH46616.1
DQ403100 mRNA Translation: ABD77233.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS24259.1

NCBI Reference Sequences

More...RefSeqi		NP_058054.2, NM_016774.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000026459; ENSMUSP00000026459; ENSMUSG00000025393

Database of genes from NCBI RefSeq genomes

More...GeneIDi		11947

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:11947

UCSC genome browser

More...UCSCi		uc007hle.1 mouse

<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
AF030559 mRNA Translation: AAB86421.1
AK003460 mRNA Translation: BAB22802.1
AK010314 mRNA Translation: BAB26846.1
AK084009 mRNA Translation: BAC39095.1
AK145684 mRNA Translation: BAE26587.1
AK148891 mRNA Translation: BAE28692.1
AK150599 mRNA Translation: BAE29691.1
AK151081 mRNA Translation: BAE30095.1
AK151600 mRNA Translation: BAE30540.1
AK152788 mRNA Translation: BAE31497.1
AK152976 mRNA Translation: BAE31630.1
AK153099 mRNA Translation: BAE31720.1
AK159444 mRNA Translation: BAE35088.1
AK159737 mRNA Translation: BAE35331.1
AK159978 mRNA Translation: BAE35529.1
AK160199 mRNA Translation: BAE35689.1
AK160608 mRNA Translation: BAE35911.1
AK164383 mRNA Translation: BAE37764.1
AK166525 mRNA Translation: BAE38829.1
AK166603 mRNA Translation: BAE38888.1
AK166979 mRNA Translation: BAE39161.1
AK167119 mRNA Translation: BAE39267.1
AK167160 mRNA Translation: BAE39301.1
AK167728 mRNA Translation: BAE39769.1
AK167764 mRNA Translation: BAE39797.1
AK168692 mRNA Translation: BAE40537.1
AK168941 mRNA Translation: BAE40749.1
AK169184 mRNA Translation: BAE40961.1
BC018392 mRNA Translation: AAH18392.1
BC037127 mRNA Translation: AAH37127.1 Different initiation.
BC046616 mRNA Translation: AAH46616.1
DQ403100 mRNA Translation: ABD77233.1
CCDSiCCDS24259.1
RefSeqiNP_058054.2, NM_016774.3

3D structure databases

SMRiP56480
ModBaseiSearch...

Protein-protein interaction databases

BioGridi198254, 13 interactors
IntActiP56480, 36 interactors
MINTiP56480
STRINGi10090.ENSMUSP00000026459

PTM databases

CarbonylDBiP56480
iPTMnetiP56480
PhosphoSitePlusiP56480
SwissPalmiP56480

2D gel databases

COMPLUYEAST-2DPAGEiP56480
REPRODUCTION-2DPAGEiIPI00468481
P56480
SWISS-2DPAGEiP56480
UCD-2DPAGEiP56480

Proteomic databases

CPTACinon-CPTAC-3766
EPDiP56480
jPOSTiP56480
MaxQBiP56480
PaxDbiP56480
PeptideAtlasiP56480
PRIDEiP56480
TopDownProteomicsiP56480

Genome annotation databases

EnsembliENSMUST00000026459; ENSMUSP00000026459; ENSMUSG00000025393
GeneIDi11947
KEGGimmu:11947
UCSCiuc007hle.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		11947
MGIiMGI:107801 Atp5b

Phylogenomic databases

eggNOGiKOG1350 Eukaryota
COG0055 LUCA
GeneTreeiENSGT00550000074800
InParanoidiP56480
KOiK02133
OMAiFNMIMDG
OrthoDBi495235at2759
PhylomeDBiP56480
TreeFamiTF105640

Enzyme and pathway databases

ReactomeiR-MMU-1268020 Mitochondrial protein import
R-MMU-163210 Formation of ATP by chemiosmotic coupling
R-MMU-8949613 Cristae formation

Miscellaneous databases

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

More...ChiTaRSi		Atp5b mouse

Protein Ontology

More...PROi		PR:P56480

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000025393 Expressed in 308 organ(s), highest expression level in central gray substance of midbrain
GenevisibleiP56480 MM

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...

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 nameiATPB_MOUSE
<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: P56480
Secondary accession number(s): Q0QEP4
, Q3TFD7, Q3TIP9, Q3TK44, Q3TWD5, Q3TX28, Q3U6U4, Q3U774, Q3UB69, Q3UF69, Q8CI65, Q8VEJ5, Q9CTI7, Q9CWX7
<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 15, 1998
Last sequence update: May 2, 2002
Last modified: October 16, 2019
This is version 193 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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