SubmitCancel

Skip Header

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

P36542

- ATPG_HUMAN

UniProt

P36542 - ATPG_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
ATP synthase subunit gamma, mitochondrial
Gene
ATP5C1, ATP5C, ATP5CL1
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 F1 domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha3beta3. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
  3. proton-transporting ATPase activity, rotational mechanism Source: InterPro
  4. transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  1. ATP biosynthetic process Source: UniProtKB
  2. ATP catabolic process Source: GOC
  3. cellular metabolic process Source: Reactome
  4. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
  5. oxidative phosphorylation 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 gamma, mitochondrial
Alternative name(s):
F-ATPase gamma subunit
Gene namesi
Name:ATP5C1
Synonyms:ATP5C, ATP5CL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:833. ATP5C1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrial inner membrane Source: UniProtKB
  3. mitochondrial matrix Source: Reactome
  4. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  5. mitochondrial proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB
  6. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25125.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525Mitochondrion
Add
BLAST
Chaini26 – 298273ATP synthase subunit gamma, mitochondrial
PRO_0000002685Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391N6-acetyllysine By similarity
Modified residuei49 – 491N6-succinyllysine By similarity
Modified residuei55 – 551N6-acetyllysine1 Publication
Modified residuei115 – 1151N6-acetyllysine; alternate By similarity
Modified residuei115 – 1151N6-succinyllysine; alternate By similarity
Modified residuei154 – 1541N6-acetyllysine; alternate1 Publication
Modified residuei154 – 1541N6-succinyllysine; alternate By similarity
Modified residuei197 – 1971N6-acetyllysine1 Publication
Modified residuei270 – 2701N6-succinyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP36542.
PaxDbiP36542.
PRIDEiP36542.

2D gel databases

UCD-2DPAGEP36542.

PTM databases

PhosphoSiteiP36542.

Expressioni

Tissue specificityi

Isoform Heart is expressed specifically in the heart and skeletal muscle, which require rapid energy supply. Isoform Liver is expressed in the brain, liver and kidney. Isoform Heart and Isoform Liver are expressed in the skin, intestine, stomach and aorta.

Gene expression databases

ArrayExpressiP36542.
BgeeiP36542.
CleanExiHS_ATP5C1.
GenevestigatoriP36542.

Organism-specific databases

HPAiHPA060949.

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.

Protein-protein interaction databases

BioGridi106997. 46 interactions.
IntActiP36542. 35 interactions.
MINTiMINT-1378900.
STRINGi9606.ENSP00000349142.

Structurei

3D structure databases

ProteinModelPortaliP36542.
SMRiP36542. Positions 26-297.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0224.
HOGENOMiHOG000215911.
HOVERGENiHBG000933.
InParanoidiP36542.
KOiK02136.
OMAiMATLKDX.
OrthoDBiEOG7QK0D3.
PhylomeDBiP36542.
TreeFamiTF105765.

Family and domain databases

InterProiIPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view]
PANTHERiPTHR11693. PTHR11693. 1 hit.
PfamiPF00231. ATP-synt. 1 hit.
[Graphical view]
PRINTSiPR00126. ATPASEGAMMA.
SUPFAMiSSF52943. SSF52943. 1 hit.
TIGRFAMsiTIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEiPS00153. ATPASE_GAMMA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Liver (identifier: P36542-1) [UniParc]FASTAAdd to Basket

Also known as: L

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

MFSRAGVAGL SAWTLQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM    50
VAAAKYARAE RELKPARIYG LGSLALYEKA DIKGPEDKKK HLLIGVSSDR 100
GLCGAIHSSI AKQMKSEVAT LTAAGKEVML VGIGDKIRGI LYRTHSDQFL 150
VAFKEVGRKP PTFGDASVIA LELLNSGYEF DEGSIIFNKF RSVISYKTEE 200
KPIFSLNTVA SADSMSIYDD IDADVLQNYQ EYNLANIIYY SLKESTTSEQ 250
SARMTAMDNA SKNASEMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD 298
Length:298
Mass (Da):32,996
Last modified:June 1, 1994 - v1
Checksum:i021A95168FD53E04
GO
Isoform Heart (identifier: P36542-2) [UniParc]FASTAAdd to Basket

Also known as: H

The sequence of this isoform differs from the canonical sequence as follows:
     298-298: Missing.

Show »
Length:297
Mass (Da):32,881
Checksum:iCA95168FD53E0447
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei298 – 2981Missing in isoform Heart.
VSP_000439

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451T → A in AAH16812. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16561 Genomic DNA. Translation: BAA03994.1.
D16561 Genomic DNA. Translation: BAA03995.1.
D16562 mRNA. Translation: BAA03996.1.
D16563 mRNA. Translation: BAA03997.1.
AK292896 mRNA. Translation: BAF85585.1.
CR457403 mRNA. Translation: CAG33684.1.
AL353754, AL158044 Genomic DNA. Translation: CAH73453.1.
AL353754, AL158044 Genomic DNA. Translation: CAH73454.1.
AL158044, AL353754 Genomic DNA. Translation: CAI12960.1.
AL158044, AL353754 Genomic DNA. Translation: CAI12961.1.
CH471072 Genomic DNA. Translation: EAW86372.1.
CH471072 Genomic DNA. Translation: EAW86373.1.
BC000470 mRNA. Translation: AAH00470.1.
BC000931 mRNA. Translation: AAH00931.1.
BC013394 mRNA. Translation: AAH13394.1.
BC016812 mRNA. Translation: AAH16812.1.
BC020824 mRNA. Translation: AAH20824.1.
CCDSiCCDS31142.1. [P36542-1]
CCDS7081.1. [P36542-2]
PIRiA49108.
RefSeqiNP_001001973.1. NM_001001973.1. [P36542-1]
NP_005165.1. NM_005174.2. [P36542-2]
UniGeneiHs.271135.

Genome annotation databases

EnsembliENST00000335698; ENSP00000338568; ENSG00000165629. [P36542-2]
ENST00000356708; ENSP00000349142; ENSG00000165629. [P36542-1]
GeneIDi509.
KEGGihsa:509.
UCSCiuc001iju.3. human. [P36542-1]

Polymorphism databases

DMDMi543875.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16561 Genomic DNA. Translation: BAA03994.1 .
D16561 Genomic DNA. Translation: BAA03995.1 .
D16562 mRNA. Translation: BAA03996.1 .
D16563 mRNA. Translation: BAA03997.1 .
AK292896 mRNA. Translation: BAF85585.1 .
CR457403 mRNA. Translation: CAG33684.1 .
AL353754 , AL158044 Genomic DNA. Translation: CAH73453.1 .
AL353754 , AL158044 Genomic DNA. Translation: CAH73454.1 .
AL158044 , AL353754 Genomic DNA. Translation: CAI12960.1 .
AL158044 , AL353754 Genomic DNA. Translation: CAI12961.1 .
CH471072 Genomic DNA. Translation: EAW86372.1 .
CH471072 Genomic DNA. Translation: EAW86373.1 .
BC000470 mRNA. Translation: AAH00470.1 .
BC000931 mRNA. Translation: AAH00931.1 .
BC013394 mRNA. Translation: AAH13394.1 .
BC016812 mRNA. Translation: AAH16812.1 .
BC020824 mRNA. Translation: AAH20824.1 .
CCDSi CCDS31142.1. [P36542-1 ]
CCDS7081.1. [P36542-2 ]
PIRi A49108.
RefSeqi NP_001001973.1. NM_001001973.1. [P36542-1 ]
NP_005165.1. NM_005174.2. [P36542-2 ]
UniGenei Hs.271135.

3D structure databases

ProteinModelPortali P36542.
SMRi P36542. Positions 26-297.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106997. 46 interactions.
IntActi P36542. 35 interactions.
MINTi MINT-1378900.
STRINGi 9606.ENSP00000349142.

PTM databases

PhosphoSitei P36542.

Polymorphism databases

DMDMi 543875.

2D gel databases

UCD-2DPAGE P36542.

Proteomic databases

MaxQBi P36542.
PaxDbi P36542.
PRIDEi P36542.

Protocols and materials databases

DNASUi 509.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000335698 ; ENSP00000338568 ; ENSG00000165629 . [P36542-2 ]
ENST00000356708 ; ENSP00000349142 ; ENSG00000165629 . [P36542-1 ]
GeneIDi 509.
KEGGi hsa:509.
UCSCi uc001iju.3. human. [P36542-1 ]

Organism-specific databases

CTDi 509.
GeneCardsi GC10P007830.
HGNCi HGNC:833. ATP5C1.
HPAi HPA060949.
MIMi 108729. gene.
neXtProti NX_P36542.
PharmGKBi PA25125.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0224.
HOGENOMi HOG000215911.
HOVERGENi HBG000933.
InParanoidi P36542.
KOi K02136.
OMAi MATLKDX.
OrthoDBi EOG7QK0D3.
PhylomeDBi P36542.
TreeFami TF105765.

Enzyme and pathway databases

Reactomei REACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSi ATP5C1. human.
GeneWikii ATP5C1.
GenomeRNAii 509.
NextBioi 2117.
PROi P36542.
SOURCEi Search...

Gene expression databases

ArrayExpressi P36542.
Bgeei P36542.
CleanExi HS_ATP5C1.
Genevestigatori P36542.

Family and domain databases

InterProi IPR000131. ATPase_F1-cplx_gsu.
IPR023632. ATPase_F1_gsu_CS.
IPR023633. ATPase_F1_gsu_dom.
[Graphical view ]
PANTHERi PTHR11693. PTHR11693. 1 hit.
Pfami PF00231. ATP-synt. 1 hit.
[Graphical view ]
PRINTSi PR00126. ATPASEGAMMA.
SUPFAMi SSF52943. SSF52943. 1 hit.
TIGRFAMsi TIGR01146. ATPsyn_F1gamma. 1 hit.
PROSITEi PS00153. ATPASE_GAMMA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Gene structure of human mitochondrial ATP synthase gamma-subunit. Tissue specificity produced by alternative RNA splicing."
    Matsuda C., Endo H., Ohta S., Kagawa Y.
    J. Biol. Chem. 268:24950-24958(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS HEART AND LIVER).
    Tissue: Heart and Liver.
  2. "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] (ISOFORM HEART).
    Tissue: Trachea.
  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] (ISOFORM LIVER).
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 LIVER).
    Tissue: Liver, Muscle, Placenta and Urinary bladder.
  7. Bienvenut W.V., Glen H., Frame M.C.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 68-79; 116-126; 144-154; 263-277 AND 286-298, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Osteosarcoma.
  8. "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-55; LYS-154 AND LYS-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATPG_HUMAN
AccessioniPrimary (citable) accession number: P36542
Secondary accession number(s): A8KA31
, Q5VYP3, Q6I9V2, Q96AS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: September 3, 2014
This is version 147 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 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi