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Q06055

- AT5G2_HUMAN

UniProt

Q06055 - AT5G2_HUMAN

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Protein

ATP synthase F(0) complex subunit C2, mitochondrial

Gene

ATP5G2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei124 – 1241Reversibly protonated during proton transportBy similarity

GO - Molecular functioni

  1. hydrogen ion transmembrane transporter activity Source: InterPro
  2. lipid binding Source: UniProtKB-KW
  3. transporter activity Source: ProtInc

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. ATP synthesis coupled proton transport Source: InterPro
  3. response to ethanol Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase F(0) complex subunit C2, mitochondrial
Alternative name(s):
ATP synthase lipid-binding protein
ATP synthase proteolipid P2
ATP synthase proton-transporting mitochondrial F(0) complex subunit C2
ATPase protein 9
ATPase subunit c
Gene namesi
Name:ATP5G2
ORF Names:PSEC0033
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:842. ATP5G2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei82 – 10221HelicalSequence AnalysisAdd
BLAST
Transmembranei117 – 13721HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial proton-transporting ATP synthase complex Source: ProtInc
  3. proton-transporting ATP synthase complex, coupling factor F(o) Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25132.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6666MitochondrionBy similarityAdd
BLAST
Chaini67 – 14175ATP synthase F(0) complex subunit C2, mitochondrialPRO_0000002562Add
BLAST

Proteomic databases

PaxDbiQ06055.
PRIDEiQ06055.

PTM databases

PhosphoSiteiQ06055.

Expressioni

Gene expression databases

BgeeiQ06055.
CleanExiHS_ATP5G2.
GenevestigatoriQ06055.

Organism-specific databases

HPAiHPA051469.

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.

Protein-protein interaction databases

BioGridi107002. 5 interactions.
IntActiQ06055. 3 interactions.
STRINGi9606.ENSP00000377878.

Structurei

3D structure databases

ProteinModelPortaliQ06055.
SMRiQ06055. Positions 68-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase C chain family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0636.
GeneTreeiENSGT00390000006210.
HOGENOMiHOG000235246.
HOVERGENiHBG050605.
InParanoidiQ06055.
KOiK02128.
OMAiHPLKMYT.
OrthoDBiEOG7VHT0K.
PhylomeDBiQ06055.
TreeFamiTF300140.

Family and domain databases

Gene3Di1.20.20.10. 1 hit.
HAMAPiMF_01396. ATP_synth_c_bact.
InterProiIPR000454. ATPase_F0-cplx_csu.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c_like_dom.
[Graphical view]
PfamiPF00137. ATP-synt_C. 1 hit.
[Graphical view]
PRINTSiPR00124. ATPASEC.
SUPFAMiSSF81333. SSF81333. 1 hit.
PROSITEiPS00605. ATPASE_C. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q06055-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MFACSKFVST PSLVKSTSQL LSRPLSAVVL KRPEILTDES LSSLAVSCPL
60 70 80 90 100
TSLVSSRSFQ TSAISRDIDT AAKFIGAGAA TVGVAGSGAG IGTVFGSLII
110 120 130 140
GYARNPSLKQ QLFSYAILGF ALSEAMGLFC LMVAFLILFA M
Length:141
Mass (Da):14,637
Last modified:February 1, 1994 - v1
Checksum:i6E627A504A7AE52D
GO
Isoform 2 (identifier: Q06055-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPELILYVAITLSVAERLVGPGHACAEPSFRSSRCSAPLCLLCSGSSSPATAPHPLKM

Note: Derived from EST data.

Show »
Length:198
Mass (Da):20,513
Checksum:i6ACCBD405F313CC8
GO
Isoform 3 (identifier: Q06055-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPELILSPATAPHPLKM

Note: Derived from EST data.

Show »
Length:157
Mass (Da):16,334
Checksum:i84032DCC16E10CED
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631A → T in BAG52118. (PubMed:16303743)Curated
Sequence conflicti107 – 1071S → F in BAG52118. (PubMed:16303743)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti58 – 581S → I.
Corresponds to variant rs13819 [ dbSNP | Ensembl ].
VAR_011920
Natural varianti141 – 1411M → K.
Corresponds to variant rs1803177 [ dbSNP | Ensembl ].
VAR_011921

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MPELILYVAITLSVAERLVG PGHACAEPSFRSSRCSAPLC LLCSGSSSPATAPHPLKM in isoform 2. CuratedVSP_037348
Alternative sequencei1 – 11M → MPELILSPATAPHPLKM in isoform 3. CuratedVSP_037349

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69908 Genomic DNA. Translation: CAA49533.1.
D13119 mRNA. Translation: BAA02421.1.
AK075351 mRNA. Translation: BAG52118.1.
AC073594 Genomic DNA. No translation available.
BC020826 mRNA. Translation: AAH20826.1.
CCDSiCCDS31812.1. [Q06055-3]
CCDS8863.2. [Q06055-2]
PIRiS34067.
RefSeqiNP_001002031.1. NM_001002031.2. [Q06055-3]
NP_005167.2. NM_005176.5. [Q06055-2]
UniGeneiHs.524464.

Genome annotation databases

EnsembliENST00000338662; ENSP00000340315; ENSG00000135390. [Q06055-3]
ENST00000394349; ENSP00000377878; ENSG00000135390. [Q06055-2]
ENST00000549164; ENSP00000447317; ENSG00000135390. [Q06055-1]
ENST00000552242; ENSP00000448801; ENSG00000135390. [Q06055-1]
ENST00000602871; ENSP00000473535; ENSG00000135390. [Q06055-1]
GeneIDi517.
KEGGihsa:517.
UCSCiuc001sec.3. human. [Q06055-2]
uc001sed.3. human. [Q06055-3]
uc009znc.3. human. [Q06055-1]

Polymorphism databases

DMDMi461592.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69908 Genomic DNA. Translation: CAA49533.1 .
D13119 mRNA. Translation: BAA02421.1 .
AK075351 mRNA. Translation: BAG52118.1 .
AC073594 Genomic DNA. No translation available.
BC020826 mRNA. Translation: AAH20826.1 .
CCDSi CCDS31812.1. [Q06055-3 ]
CCDS8863.2. [Q06055-2 ]
PIRi S34067.
RefSeqi NP_001002031.1. NM_001002031.2. [Q06055-3 ]
NP_005167.2. NM_005176.5. [Q06055-2 ]
UniGenei Hs.524464.

3D structure databases

ProteinModelPortali Q06055.
SMRi Q06055. Positions 68-139.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107002. 5 interactions.
IntActi Q06055. 3 interactions.
STRINGi 9606.ENSP00000377878.

PTM databases

PhosphoSitei Q06055.

Polymorphism databases

DMDMi 461592.

Proteomic databases

PaxDbi Q06055.
PRIDEi Q06055.

Protocols and materials databases

DNASUi 517.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338662 ; ENSP00000340315 ; ENSG00000135390 . [Q06055-3 ]
ENST00000394349 ; ENSP00000377878 ; ENSG00000135390 . [Q06055-2 ]
ENST00000549164 ; ENSP00000447317 ; ENSG00000135390 . [Q06055-1 ]
ENST00000552242 ; ENSP00000448801 ; ENSG00000135390 . [Q06055-1 ]
ENST00000602871 ; ENSP00000473535 ; ENSG00000135390 . [Q06055-1 ]
GeneIDi 517.
KEGGi hsa:517.
UCSCi uc001sec.3. human. [Q06055-2 ]
uc001sed.3. human. [Q06055-3 ]
uc009znc.3. human. [Q06055-1 ]

Organism-specific databases

CTDi 517.
GeneCardsi GC12M054030.
H-InvDB HIX0201895.
HGNCi HGNC:842. ATP5G2.
HPAi HPA051469.
MIMi 603193. gene.
neXtProti NX_Q06055.
PharmGKBi PA25132.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0636.
GeneTreei ENSGT00390000006210.
HOGENOMi HOG000235246.
HOVERGENi HBG050605.
InParanoidi Q06055.
KOi K02128.
OMAi HPLKMYT.
OrthoDBi EOG7VHT0K.
PhylomeDBi Q06055.
TreeFami TF300140.

Enzyme and pathway databases

Reactomei REACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSi ATP5G2. human.
GeneWikii ATP5G2.
GenomeRNAii 517.
NextBioi 2145.
PROi Q06055.
SOURCEi Search...

Gene expression databases

Bgeei Q06055.
CleanExi HS_ATP5G2.
Genevestigatori Q06055.

Family and domain databases

Gene3Di 1.20.20.10. 1 hit.
HAMAPi MF_01396. ATP_synth_c_bact.
InterProi IPR000454. ATPase_F0-cplx_csu.
IPR020537. ATPase_F0-cplx_csu_DDCD_BS.
IPR002379. ATPase_proteolipid_c_like_dom.
[Graphical view ]
Pfami PF00137. ATP-synt_C. 1 hit.
[Graphical view ]
PRINTSi PR00124. ATPASEC.
SUPFAMi SSF81333. SSF81333. 1 hit.
PROSITEi PS00605. ATPASE_C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequences of members of the human gene family for the c subunit of mitochondrial ATP synthase."
    Dyer M.R., Walker J.E.
    Biochem. J. 293:51-64(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular cloning and sequence of two cDNAs for human subunit c of H(+)-ATP synthase in mitochondria."
    Higuti T., Kawamura Y., Kuroiwa K., Miyazaki S., Tsujita H.
    Biochim. Biophys. Acta 1173:87-90(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Lung.
  6. "Human liver cDNA clones encoding proteolipid subunit 9 of the mitochondrial ATPase complex."
    Farrell L.B., Nagley P.
    Biochem. Biophys. Res. Commun. 144:1257-1264(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-141 (ISOFORMS 1/2/3).
    Tissue: Liver.

Entry informationi

Entry nameiAT5G2_HUMAN
AccessioniPrimary (citable) accession number: Q06055
Secondary accession number(s): B3KQQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 29, 2014
This is version 139 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

Miscellaneous

There are three genes which encode the mitochondrial ATP synthase proteolipid and they specify precursors with different import sequences but identical mature proteins. Is the major protein stored in the storage bodies of animals or humans affected with ceroid lipofuscinosis (Batten disease).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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