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Protein

ATP synthase subunit g, mitochondrial

Gene

ATP5L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Minor subunit located with subunit a in the membrane.

GO - Molecular functioni

  1. hydrogen ion transmembrane transporter activity Source: InterPro
  2. transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  1. cellular metabolic process Source: Reactome
  2. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
  3. respiratory electron transport chain Source: Reactome
  4. 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 g, mitochondrial
Short name:
ATPase subunit g
Gene namesi
Name:ATP5L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:14247. ATP5L.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. mitochondrial inner membrane Source: Reactome
  3. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  4. mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: InterPro
  5. mitochondrion Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25143.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 103102ATP synthase subunit g, mitochondrialPRO_0000071691Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei11 – 111N6-acetyllysineBy similarity
Modified residuei24 – 241N6-acetyllysine1 Publication
Modified residuei35 – 351N6-acetyllysineBy similarity
Modified residuei54 – 541N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO75964.
PaxDbiO75964.
PeptideAtlasiO75964.
PRIDEiO75964.

PTM databases

PhosphoSiteiO75964.

Expressioni

Gene expression databases

BgeeiO75964.
CleanExiHS_ATP5L.
ExpressionAtlasiO75964. baseline and differential.
GenevestigatoriO75964.

Organism-specific databases

HPAiHPA044629.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF0 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). 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

BioGridi115876. 10 interactions.
IntActiO75964. 7 interactions.
MINTiMINT-3002124.
STRINGi9606.ENSP00000300688.

Structurei

3D structure databases

ProteinModelPortaliO75964.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase g subunit family.Curated

Phylogenomic databases

eggNOGiNOG323765.
GeneTreeiENSGT00390000009724.
HOGENOMiHOG000007506.
HOVERGENiHBG050614.
InParanoidiO75964.
KOiK02140.
OMAiWQYAKVE.
PhylomeDBiO75964.
TreeFamiTF313978.

Family and domain databases

InterProiIPR016702. ATP-Synthase_su_G_mt_met.
IPR006808. ATPase_F0-cplx_gsu_mt.
[Graphical view]
PfamiPF04718. ATP-synt_G. 1 hit.
[Graphical view]
PIRSFiPIRSF017835. ATP-synth_g_mitoch_animal. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O75964-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQFVRNLVE KTPALVNAAV TYSKPRLATF WYYAKVELVP PTPAEIPRAI
60 70 80 90 100
QSLKKIVNSA QTGSFKQLTV KEAVLNGLVA TEVLMWFYVG EIIGKRGIIG

YDV
Length:103
Mass (Da):11,428
Last modified:April 26, 2005 - v3
Checksum:i03D484BCF836E6C2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → G in AAC61597 (Ref. 1) Curated
Sequence conflicti48 – 481R → K in AAC61597 (Ref. 1) Curated
Sequence conflicti57 – 571V → A in AAH15128 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092124 mRNA. Translation: AAC61597.1.
AF087846 mRNA. Translation: AAP97159.1.
AF070655 mRNA. Translation: AAD20961.1.
AL050277 mRNA. Translation: CAB43378.1.
CR533494 mRNA. Translation: CAG38525.1.
CR542211 mRNA. Translation: CAG47007.1.
AK289568 mRNA. Translation: BAF82257.1.
CH471065 Genomic DNA. Translation: EAW67376.1.
BC015128 mRNA. Translation: AAH15128.1.
BC070165 mRNA. Translation: AAH70165.1.
CCDSiCCDS8397.1.
PIRiT08727.
RefSeqiNP_006467.4. NM_006476.4.
UniGeneiHs.486360.

Genome annotation databases

EnsembliENST00000300688; ENSP00000300688; ENSG00000167283.
GeneIDi10632.
KEGGihsa:10632.
UCSCiuc001psx.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092124 mRNA. Translation: AAC61597.1.
AF087846 mRNA. Translation: AAP97159.1.
AF070655 mRNA. Translation: AAD20961.1.
AL050277 mRNA. Translation: CAB43378.1.
CR533494 mRNA. Translation: CAG38525.1.
CR542211 mRNA. Translation: CAG47007.1.
AK289568 mRNA. Translation: BAF82257.1.
CH471065 Genomic DNA. Translation: EAW67376.1.
BC015128 mRNA. Translation: AAH15128.1.
BC070165 mRNA. Translation: AAH70165.1.
CCDSiCCDS8397.1.
PIRiT08727.
RefSeqiNP_006467.4. NM_006476.4.
UniGeneiHs.486360.

3D structure databases

ProteinModelPortaliO75964.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115876. 10 interactions.
IntActiO75964. 7 interactions.
MINTiMINT-3002124.
STRINGi9606.ENSP00000300688.

PTM databases

PhosphoSiteiO75964.

Proteomic databases

MaxQBiO75964.
PaxDbiO75964.
PeptideAtlasiO75964.
PRIDEiO75964.

Protocols and materials databases

DNASUi10632.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300688; ENSP00000300688; ENSG00000167283.
GeneIDi10632.
KEGGihsa:10632.
UCSCiuc001psx.3. human.

Organism-specific databases

CTDi10632.
GeneCardsiGC11P118271.
HGNCiHGNC:14247. ATP5L.
HPAiHPA044629.
neXtProtiNX_O75964.
PharmGKBiPA25143.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG323765.
GeneTreeiENSGT00390000009724.
HOGENOMiHOG000007506.
HOVERGENiHBG050614.
InParanoidiO75964.
KOiK02140.
OMAiWQYAKVE.
PhylomeDBiO75964.
TreeFamiTF313978.

Enzyme and pathway databases

ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSiATP5L. human.
GeneWikiiATP5L.
GenomeRNAii10632.
NextBioi40403.
PROiO75964.

Gene expression databases

BgeeiO75964.
CleanExiHS_ATP5L.
ExpressionAtlasiO75964. baseline and differential.
GenevestigatoriO75964.

Family and domain databases

InterProiIPR016702. ATP-Synthase_su_G_mt_met.
IPR006808. ATPase_F0-cplx_gsu_mt.
[Graphical view]
PfamiPF04718. ATP-synt_G. 1 hit.
[Graphical view]
PIRSFiPIRSF017835. ATP-synth_g_mitoch_animal. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and chromosomal assignment of F1F0-type ATP synthase subunit g from human infant thymus."
    Kang Y.J., Hwang M.Y., Lee M.Y., Lee H.C., Sohn U.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Thymus.
  2. "Cloning and characterization of a novel human cDNA homologous to Bos taurus F1Fo-ATP synthase complex Fo membrane domain g subunit mRNA."
    Zhang M., Yu L., Zhou Y., Hu P.R., Xin Y.R., Zhao S.Y.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "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: Cerebellum.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Lung.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "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-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiATP5L_HUMAN
AccessioniPrimary (citable) accession number: O75964
Secondary accession number(s): A8K0K3, Q96BV6, Q9UBZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 26, 2005
Last modified: March 4, 2015
This is version 130 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.