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P48047

- ATPO_HUMAN

UniProt

P48047 - ATPO_HUMAN

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Protein

ATP synthase subunit O, mitochondrial

Gene

ATP5O

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- 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. Part of the complex F0 domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha3beta3 subcomplex and subunit a/ATP6 static relative to the rotary elements.

GO - Molecular functioni

  1. drug binding Source: UniProtKB
  2. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
  3. transmembrane transporter activity Source: UniProtKB
  4. transporter activity Source: ProtInc

GO - Biological processi

  1. ATP biosynthetic process Source: UniProtKB
  2. ATP catabolic process Source: UniProtKB
  3. cellular metabolic process Source: Reactome
  4. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
  5. proton transport Source: UniProtKB
  6. respiratory electron transport chain Source: Reactome
  7. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit O, mitochondrial
Alternative name(s):
Oligomycin sensitivity conferral protein
Short name:
OSCP
Gene namesi
Name:ATP5O
Synonyms:ATPO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:850. ATP5O.

Subcellular locationi

Mitochondrion By similarity. Mitochondrion inner membrane By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrial inner membrane Source: Reactome
  3. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  4. mitochondrion Source: UniProtKB
  5. nucleus Source: UniProt
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi162 – 1621K → R: Increased ATP levels. 1 Publication

Organism-specific databases

PharmGKBiPA25144.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323Mitochondrion1 PublicationAdd
BLAST
Chaini24 – 213190ATP synthase subunit O, mitochondrialPRO_0000002646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541N6-acetyllysine1 Publication
Modified residuei60 – 601N6-acetyllysineBy similarity
Modified residuei70 – 701N6-acetyllysineBy similarity
Modified residuei73 – 731N6-acetyllysineBy similarity
Modified residuei90 – 901N6-succinyllysineBy similarity
Modified residuei158 – 1581N6-acetyllysine; alternateBy similarity
Modified residuei158 – 1581N6-succinyllysine; alternateBy similarity
Modified residuei162 – 1621N6-acetyllysine; alternate2 Publications
Modified residuei162 – 1621N6-succinyllysine; alternateBy similarity
Modified residuei172 – 1721N6-acetyllysine1 Publication
Modified residuei176 – 1761N6-acetyllysineBy similarity
Modified residuei192 – 1921N6-acetyllysine1 Publication
Modified residuei199 – 1991N6-succinyllysineBy similarity

Post-translational modificationi

Acetylation at Lys-162 decreases ATP production. Deacetylated by SIRT3.2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP48047.
PaxDbiP48047.
PeptideAtlasiP48047.
PRIDEiP48047.

2D gel databases

OGPiP48047.
UCD-2DPAGEP48047.

PTM databases

PhosphoSiteiP48047.

Expressioni

Gene expression databases

BgeeiP48047.
CleanExiHS_ATP5O.
ExpressionAtlasiP48047. baseline.
GenevestigatoriP48047.

Organism-specific databases

HPAiCAB016209.
HPA041394.

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 ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 By similarity.By similarity

Protein-protein interaction databases

BioGridi107021. 26 interactions.
IntActiP48047. 13 interactions.
MINTiMINT-5002594.
STRINGi9606.ENSP00000290299.

Structurei

3D structure databases

ProteinModelPortaliP48047.
SMRiP48047. Positions 24-212.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase delta chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0712.
GeneTreeiENSGT00390000015060.
HOGENOMiHOG000075825.
HOVERGENiHBG004309.
InParanoidiP48047.
KOiK02137.
OMAiTKNFLAV.
PhylomeDBiP48047.
TreeFamiTF106241.

Family and domain databases

Gene3Di1.10.520.20. 1 hit.
HAMAPiMF_01416. ATP_synth_delta_bact.
InterProiIPR020781. ATPase_OSCP/d_CS.
IPR026015. ATPase_OSCP/delta_N.
IPR000711. ATPase_OSCP/dsu.
[Graphical view]
PANTHERiPTHR11910. PTHR11910. 1 hit.
PfamiPF00213. OSCP. 1 hit.
[Graphical view]
PRINTSiPR00125. ATPASEDELTA.
SUPFAMiSSF47928. SSF47928. 1 hit.
TIGRFAMsiTIGR01145. ATP_synt_delta. 1 hit.
PROSITEiPS00389. ATPASE_DELTA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P48047-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAPAVSGLS RQVRCFSTSV VRPFAKLVRP PVQVYGIEGR YATALYSAAS
60 70 80 90 100
KQNKLEQVEK ELLRVAQILK EPKVAASVLN PYVKRSIKVK SLNDITAKER
110 120 130 140 150
FSPLTTNLIN LLAENGRLSN TQGVVSAFST MMSVHRGEVP CTVTSASPLE
160 170 180 190 200
EATLSELKTV LKSFLSQGQV LKLEAKTDPS ILGGMIVRIG EKYVDMSVKT
210
KIQKLGRAMR EIV
Length:213
Mass (Da):23,277
Last modified:February 1, 1996 - v1
Checksum:i311F53576A31FC93
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti98 – 981K → R.2 Publications
Corresponds to variant rs4842 [ dbSNP | Ensembl ].
VAR_011930

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83218 mRNA. Translation: CAA58219.1.
BT019836 mRNA. Translation: AAV38639.1.
CR456822 mRNA. Translation: CAG33103.1.
AK222962 mRNA. Translation: BAD96682.1.
AK311796 mRNA. Translation: BAG34739.1.
CH471079 Genomic DNA. Translation: EAX09802.1.
BC021233 mRNA. Translation: AAH21233.1.
BC022865 mRNA. Translation: AAH22865.1.
CCDSiCCDS13634.1.
RefSeqiNP_001688.1. NM_001697.2.
UniGeneiHs.409140.

Genome annotation databases

EnsembliENST00000290299; ENSP00000290299; ENSG00000241837.
GeneIDi539.
KEGGihsa:539.
UCSCiuc002ytl.3. human.

Polymorphism databases

DMDMi1352049.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83218 mRNA. Translation: CAA58219.1 .
BT019836 mRNA. Translation: AAV38639.1 .
CR456822 mRNA. Translation: CAG33103.1 .
AK222962 mRNA. Translation: BAD96682.1 .
AK311796 mRNA. Translation: BAG34739.1 .
CH471079 Genomic DNA. Translation: EAX09802.1 .
BC021233 mRNA. Translation: AAH21233.1 .
BC022865 mRNA. Translation: AAH22865.1 .
CCDSi CCDS13634.1.
RefSeqi NP_001688.1. NM_001697.2.
UniGenei Hs.409140.

3D structure databases

ProteinModelPortali P48047.
SMRi P48047. Positions 24-212.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107021. 26 interactions.
IntActi P48047. 13 interactions.
MINTi MINT-5002594.
STRINGi 9606.ENSP00000290299.

PTM databases

PhosphoSitei P48047.

Polymorphism databases

DMDMi 1352049.

2D gel databases

OGPi P48047.
UCD-2DPAGE P48047.

Proteomic databases

MaxQBi P48047.
PaxDbi P48047.
PeptideAtlasi P48047.
PRIDEi P48047.

Protocols and materials databases

DNASUi 539.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000290299 ; ENSP00000290299 ; ENSG00000241837 .
GeneIDi 539.
KEGGi hsa:539.
UCSCi uc002ytl.3. human.

Organism-specific databases

CTDi 539.
GeneCardsi GC21M035275.
H-InvDB HIX0158705.
HGNCi HGNC:850. ATP5O.
HPAi CAB016209.
HPA041394.
MIMi 600828. gene.
neXtProti NX_P48047.
PharmGKBi PA25144.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0712.
GeneTreei ENSGT00390000015060.
HOGENOMi HOG000075825.
HOVERGENi HBG004309.
InParanoidi P48047.
KOi K02137.
OMAi TKNFLAV.
PhylomeDBi P48047.
TreeFami TF106241.

Enzyme and pathway databases

Reactomei REACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSi ATP5O. human.
GeneWikii ATP5O.
GenomeRNAii 539.
NextBioi 2235.
PROi P48047.
SOURCEi Search...

Gene expression databases

Bgeei P48047.
CleanExi HS_ATP5O.
ExpressionAtlasi P48047. baseline.
Genevestigatori P48047.

Family and domain databases

Gene3Di 1.10.520.20. 1 hit.
HAMAPi MF_01416. ATP_synth_delta_bact.
InterProi IPR020781. ATPase_OSCP/d_CS.
IPR026015. ATPase_OSCP/delta_N.
IPR000711. ATPase_OSCP/dsu.
[Graphical view ]
PANTHERi PTHR11910. PTHR11910. 1 hit.
Pfami PF00213. OSCP. 1 hit.
[Graphical view ]
PRINTSi PR00125. ATPASEDELTA.
SUPFAMi SSF47928. SSF47928. 1 hit.
TIGRFAMsi TIGR01145. ATP_synt_delta. 1 hit.
PROSITEi PS00389. ATPASE_DELTA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the cDNA for the human ATP synthase OSCP subunit (ATP5O) by exon trapping and mapping to chromosome 21q22.1-q22.2."
    Chen H.M., Morris M.A., Rossier C., Blouin J.-L., Antonarakis S.E.
    Genomics 28:470-476(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain and Muscle.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-98.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-98.
    Tissue: Heart.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-40.
    Tissue: Platelet.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-162; LYS-172 AND LYS-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "SIRT3 deacetylates ATP synthase F1 complex proteins in response to nutrient and exercise-induced stress."
    Vassilopoulos A., Pennington D.J., Andresson T., Rees D., Fearnley I., Ham A., Yan Y., Flynn C.R., Jones K., Kim H.S., Deng C., Walker J., Gius D.
    Antioxid. Redox Signal. 0:0-0(2013)
    Cited for: ACETYLATION AT LYS-162, DEACETYLATION BY SIRT3, MUTAGENESIS OF LYS-162.

Entry informationi

Entry nameiATPO_HUMAN
AccessioniPrimary (citable) accession number: P48047
Secondary accession number(s): B2R4E2, Q5U042, Q6IBI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 146 of the entry and version 1 of the sequence. [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 chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3