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Protein

ATP synthase subunit beta, mitochondrial

Gene

ATP5F1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei239ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi207 – 214ATPBy similarity8

GO - Molecular functioni

  • angiostatin binding Source: CAFA
  • ATP binding Source: UniProtKB-KW
  • MHC class I protein binding Source: UniProtKB
  • proton-transporting ATPase activity, rotational mechanism Source: UniProtKB
  • proton-transporting ATP synthase activity, rotational mechanism Source: CAFA
  • transmembrane transporter activity Source: UniProtKB
  • transporter activity Source: UniProtKB

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-HSA-1268020 Mitochondrial protein import
R-HSA-163210 Formation of ATP by chemiosmotic coupling
R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-8949613 Cristae formation

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit beta, mitochondrialCurated (EC:3.6.3.14)
Alternative name(s):
ATP synthase F1 subunit betaImported
Gene namesi
Name:ATP5F1BImported
Synonyms:ATP5BImported, ATPMB, ATPSBImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000110955.8
HGNCiHGNC:830 ATP5F1B
MIMi102910 gene
neXtProtiNX_P06576

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; Source: COMPARTMENTS

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi506
OpenTargetsiENSG00000110955
PharmGKBiPA25122

Chemistry databases

ChEMBLiCHEMBL2062350
DrugBankiDB07384 1-ACETYL-2-CARBOXYPIPERIDINE
DB07394 AUROVERTIN B
DB08399 PICEATANNOL
DB04216 Quercetin

Polymorphism and mutation databases

BioMutaiATP5B
DMDMi114549

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 47Mitochondrion1 PublicationAdd BLAST47
ChainiPRO_000000244348 – 529ATP synthase subunit beta, mitochondrialAdd BLAST482

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi106O-linked (GlcNAc) serineBy similarity1
Modified residuei124N6-acetyllysine; alternateBy similarity1
Modified residuei124N6-succinyllysine; alternateBy similarity1
Modified residuei133N6-acetyllysine; alternateCombined sources1
Modified residuei133N6-succinyllysine; alternateBy similarity1
Modified residuei161N6-acetyllysine; alternateBy similarity1
Modified residuei161N6-succinyllysine; alternateBy similarity1
Modified residuei198N6-acetyllysineCombined sources1
Modified residuei259N6-acetyllysine; alternateBy similarity1
Modified residuei259N6-succinyllysine; alternateBy similarity1
Modified residuei264N6-acetyllysine; alternateBy similarity1
Modified residuei264N6-succinyllysine; alternateBy similarity1
Modified residuei312PhosphothreonineBy similarity1
Modified residuei415PhosphoserineCombined sources1
Modified residuei426N6-acetyllysineCombined sources1
Modified residuei433PhosphoserineBy similarity1
Modified residuei480N6-acetyllysineBy similarity1
Modified residuei485N6-acetyllysineBy similarity1
Modified residuei522N6-acetyllysine; alternateBy similarity1
Modified residuei522N6-succinyllysine; alternateBy similarity1
Modified residuei529PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP06576
PaxDbiP06576
PeptideAtlasiP06576
PRIDEiP06576
ProteomicsDBi51907
TopDownProteomicsiP06576

2D gel databases

DOSAC-COBS-2DPAGEiP06576
OGPiP06576
REPRODUCTION-2DPAGEiIPI00303476
P06576
SWISS-2DPAGEiP06576
UCD-2DPAGEiP06576

PTM databases

CarbonylDBiP06576
iPTMnetiP06576
PhosphoSitePlusiP06576
SwissPalmiP06576

Expressioni

Gene expression databases

BgeeiENSG00000110955 Expressed in 228 organ(s), highest expression level in apex of heart
CleanExiHS_ATP5B
ExpressionAtlasiP06576 baseline and differential
GenevisibleiP06576 HS

Organism-specific databases

HPAiCAB017527
HPA001520
HPA001528

Interactioni

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 MP68. Interacts with PPIF. 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 efficency. Interacts with CLN5 and PPT1.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
YWHAZP631042EBI-356231,EBI-347088

GO - Molecular functioni

Protein-protein interaction databases

BioGridi106994, 187 interactors
CORUMiP06576
IntActiP06576, 73 interactors
MINTiP06576
STRINGi9606.ENSP00000262030

Structurei

3D structure databases

ProteinModelPortaliP06576
SMRiP06576
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1350 Eukaryota
COG0055 LUCA
GeneTreeiENSGT00550000074800
HOGENOMiHOG000009605
HOVERGENiHBG004307
InParanoidiP06576
KOiK02133
OMAiFNMIMDG
OrthoDBiEOG091G0KVV
PhylomeDBiP06576
TreeFamiTF105640

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

Sequence (1+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

P06576-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLGFVGRVAA APASGALRRL TPSASLPPAQ LLLRAAPTAV HPVRDYAAQT
60 70 80 90 100
SPSPKAGAAT GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA
110 120 130 140 150
QHLGESTVRT IAMDGTEGLV RGQKVLDSGA PIKIPVGPET LGRIMNVIGE
160 170 180 190 200
PIDERGPIKT KQFAPIHAEA PEFMEMSVEQ 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 NIVGSEHYDV ARGVQKILQD YKSLQDIIAI LGMDELSEED
460 470 480 490 500
KLTVSRARKI QRFLSQPFQV AEVFTGHMGK LVPLKETIKG FQQILAGEYD
510 520
HLPEQAFYMV GPIEEAVAKA DKLAEEHSS
Length:529
Mass (Da):56,560
Last modified:April 1, 1990 - v3
Checksum:i960C616A2252B91A
GO

Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YH81H0YH81_HUMAN
ATP synthase subunit beta
ATP5F1B
362Annotation score:
F8W0P7F8W0P7_HUMAN
ATP synthase subunit beta, mitochon...
ATP5F1B
270Annotation score:
F8W079F8W079_HUMAN
ATP synthase subunit beta, mitochon...
ATP5F1B
284Annotation score:
H0YI37H0YI37_HUMAN
ATP synthase subunit beta, mitochon...
ATP5F1B
133Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1 – 6MLGFVG → MTSLWGKGTGCKLFKF in BAA00016 (PubMed:2870059).Curated6
Sequence conflicti1 – 6MLGFVG → MTSLWGKGTGCKLFKF in CAA27246 (PubMed:2870059).Curated6
Sequence conflicti36 – 40APTAV → VRRRF in AAA51808 (PubMed:2900241).Curated5
Sequence conflicti36 – 40APTAV → VRRRS in BAA00016 (PubMed:2870059).Curated5
Sequence conflicti36 – 40APTAV → VRRRS in CAA27246 (PubMed:2870059).Curated5
Sequence conflicti130 – 132API → DQL in AAA51808 (PubMed:2900241).Curated3
Sequence conflicti378H → D in AAA51808 (PubMed:2900241).Curated1
Sequence conflicti435Q → H in AAA51808 (PubMed:2900241).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_074188130A → V1 Publication1
Natural variantiVAR_048371274E → Q2 PublicationsCorresponds to variant dbSNP:rs1042001Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27132 Genomic DNA Translation: AAA51809.1
M19483, M19482 Genomic DNA Translation: AAA51808.1
X03559 mRNA Translation: CAA27246.1
D00022 mRNA Translation: BAA00016.1
AK291085 mRNA Translation: BAF83774.1
CH471054 Genomic DNA Translation: EAW96952.1
BC016512 mRNA Translation: AAH16512.1
X05606 mRNA Translation: CAA29095.1
CCDSiCCDS8924.1
PIRiA33370
RefSeqiNP_001677.2, NM_001686.3
UniGeneiHs.406510

Genome annotation databases

EnsembliENST00000262030; ENSP00000262030; ENSG00000110955
GeneIDi506
KEGGihsa:506

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27132 Genomic DNA Translation: AAA51809.1
M19483, M19482 Genomic DNA Translation: AAA51808.1
X03559 mRNA Translation: CAA27246.1
D00022 mRNA Translation: BAA00016.1
AK291085 mRNA Translation: BAF83774.1
CH471054 Genomic DNA Translation: EAW96952.1
BC016512 mRNA Translation: AAH16512.1
X05606 mRNA Translation: CAA29095.1
CCDSiCCDS8924.1
PIRiA33370
RefSeqiNP_001677.2, NM_001686.3
UniGeneiHs.406510

3D structure databases

ProteinModelPortaliP06576
SMRiP06576
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106994, 187 interactors
CORUMiP06576
IntActiP06576, 73 interactors
MINTiP06576
STRINGi9606.ENSP00000262030

Chemistry databases

ChEMBLiCHEMBL2062350
DrugBankiDB07384 1-ACETYL-2-CARBOXYPIPERIDINE
DB07394 AUROVERTIN B
DB08399 PICEATANNOL
DB04216 Quercetin

PTM databases

CarbonylDBiP06576
iPTMnetiP06576
PhosphoSitePlusiP06576
SwissPalmiP06576

Polymorphism and mutation databases

BioMutaiATP5B
DMDMi114549

2D gel databases

DOSAC-COBS-2DPAGEiP06576
OGPiP06576
REPRODUCTION-2DPAGEiIPI00303476
P06576
SWISS-2DPAGEiP06576
UCD-2DPAGEiP06576

Proteomic databases

EPDiP06576
PaxDbiP06576
PeptideAtlasiP06576
PRIDEiP06576
ProteomicsDBi51907
TopDownProteomicsiP06576

Protocols and materials databases

DNASUi506
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262030; ENSP00000262030; ENSG00000110955
GeneIDi506
KEGGihsa:506

Organism-specific databases

CTDi506
DisGeNETi506
EuPathDBiHostDB:ENSG00000110955.8
GeneCardsiATP5F1B
HGNCiHGNC:830 ATP5F1B
HPAiCAB017527
HPA001520
HPA001528
MIMi102910 gene
neXtProtiNX_P06576
OpenTargetsiENSG00000110955
PharmGKBiPA25122
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1350 Eukaryota
COG0055 LUCA
GeneTreeiENSGT00550000074800
HOGENOMiHOG000009605
HOVERGENiHBG004307
InParanoidiP06576
KOiK02133
OMAiFNMIMDG
OrthoDBiEOG091G0KVV
PhylomeDBiP06576
TreeFamiTF105640

Enzyme and pathway databases

ReactomeiR-HSA-1268020 Mitochondrial protein import
R-HSA-163210 Formation of ATP by chemiosmotic coupling
R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-8949613 Cristae formation

Miscellaneous databases

ChiTaRSiATP5B human
GeneWikiiATP5B
GenomeRNAii506
PROiPR:P06576
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000110955 Expressed in 228 organ(s), highest expression level in apex of heart
CleanExiHS_ATP5B
ExpressionAtlasiP06576 baseline and differential
GenevisibleiP06576 HS

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
ProtoNetiSearch...

Entry informationi

Entry nameiATPB_HUMAN
AccessioniPrimary (citable) accession number: P06576
Secondary accession number(s): A8K4X0, Q14283
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: April 1, 1990
Last modified: October 10, 2018
This is version 220 of the entry and version 3 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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