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O75947

- ATP5H_HUMAN

UniProt

O75947 - ATP5H_HUMAN

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Protein

ATP synthase subunit d, mitochondrial

Gene

ATP5H

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

GO - Biological processi

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

Keywords - Biological processi

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 d, mitochondrial
Short name:
ATPase subunit d
Gene namesi
Name:ATP5H
ORF Names:My032
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:845. ATP5H.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrial inner membrane Source: UniProtKB
  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: UniProt
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25135.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 161160ATP synthase subunit d, mitochondrialPRO_0000071673Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei85 – 851N6-acetyllysine1 Publication
Modified residuei95 – 951N6-acetyllysine1 Publication
Modified residuei117 – 1171N6-acetyllysine1 Publication
Modified residuei149 – 1491N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO75947.
PaxDbiO75947.
PeptideAtlasiO75947.
PRIDEiO75947.

2D gel databases

OGPiO75947.
REPRODUCTION-2DPAGEIPI00456049.
UCD-2DPAGEO75947.

PTM databases

PhosphoSiteiO75947.

Expressioni

Gene expression databases

BgeeiO75947.
CleanExiHS_ATP5H.
ExpressionAtlasiO75947. baseline and differential.
GenevestigatoriO75947.

Organism-specific databases

HPAiHPA042777.
HPA048459.

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

BioGridi115739. 12 interactions.
IntActiO75947. 6 interactions.
MINTiMINT-1407327.
STRINGi9606.ENSP00000301587.

Structurei

3D structure databases

ProteinModelPortaliO75947.
SMRiO75947. Positions 4-124.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase d subunit family.Curated

Phylogenomic databases

eggNOGiNOG307464.
GeneTreeiENSGT00390000003582.
HOGENOMiHOG000267023.
HOVERGENiHBG050612.
InParanoidiO75947.
KOiK02138.
OMAiMEDYRDA.
PhylomeDBiO75947.
TreeFamiTF314031.

Family and domain databases

InterProiIPR008689. ATPase_F0-cplx_dsu_mt.
[Graphical view]
PfamiPF05873. Mt_ATP-synt_D. 1 hit.
[Graphical view]
PIRSFiPIRSF005514. ATPase_F0_D_mt. 1 hit.

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 1 (identifier: O75947-1) [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
MAGRKLALKT IDWVAFAEII PQNQKAIASS LKSWNETLTS RLAALPENPP
60 70 80 90 100
AIDWAYYKAN VAKAGLVDDF EKKFNALKVP VPEDKYTAQV DAEEKEDVKS
110 120 130 140 150
CAEWVSLSKA RIVEYEKEME KMKNLIPFDQ MTIEDLNEAF PETKLDKKKY
160
PYWPHQPIEN L
Length:161
Mass (Da):18,491
Last modified:January 23, 2007 - v3
Checksum:iE93020ADA1BA1694
GO
Isoform 2 (identifier: O75947-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-97: Missing.

Show »
Length:137
Mass (Da):15,773
Checksum:i0796685CD2CC605E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei74 – 9724Missing in isoform 2. 2 PublicationsVSP_000436Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF087135 mRNA. Translation: AAC36338.1.
AF070650 mRNA. Translation: AAD20956.1.
AF061735 mRNA. Translation: AAG43146.1.
AK312230 mRNA. Translation: BAG35163.1.
CH471099 Genomic DNA. Translation: EAW89228.1.
BC032245 mRNA. Translation: AAH32245.1.
BC038092 mRNA. Translation: AAH38092.1.
CCDSiCCDS11712.1. [O75947-1]
CCDS32727.1. [O75947-2]
RefSeqiNP_001003785.1. NM_001003785.1. [O75947-2]
NP_006347.1. NM_006356.2. [O75947-1]
UniGeneiHs.514465.

Genome annotation databases

EnsembliENST00000301587; ENSP00000301587; ENSG00000167863. [O75947-1]
ENST00000344546; ENSP00000344230; ENSG00000167863. [O75947-2]
GeneIDi10476.
KEGGihsa:10476.
UCSCiuc002jmn.1. human. [O75947-1]
uc002jmo.1. human. [O75947-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF087135 mRNA. Translation: AAC36338.1 .
AF070650 mRNA. Translation: AAD20956.1 .
AF061735 mRNA. Translation: AAG43146.1 .
AK312230 mRNA. Translation: BAG35163.1 .
CH471099 Genomic DNA. Translation: EAW89228.1 .
BC032245 mRNA. Translation: AAH32245.1 .
BC038092 mRNA. Translation: AAH38092.1 .
CCDSi CCDS11712.1. [O75947-1 ]
CCDS32727.1. [O75947-2 ]
RefSeqi NP_001003785.1. NM_001003785.1. [O75947-2 ]
NP_006347.1. NM_006356.2. [O75947-1 ]
UniGenei Hs.514465.

3D structure databases

ProteinModelPortali O75947.
SMRi O75947. Positions 4-124.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115739. 12 interactions.
IntActi O75947. 6 interactions.
MINTi MINT-1407327.
STRINGi 9606.ENSP00000301587.

PTM databases

PhosphoSitei O75947.

2D gel databases

OGPi O75947.
REPRODUCTION-2DPAGE IPI00456049.
UCD-2DPAGE O75947.

Proteomic databases

MaxQBi O75947.
PaxDbi O75947.
PeptideAtlasi O75947.
PRIDEi O75947.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301587 ; ENSP00000301587 ; ENSG00000167863 . [O75947-1 ]
ENST00000344546 ; ENSP00000344230 ; ENSG00000167863 . [O75947-2 ]
GeneIDi 10476.
KEGGi hsa:10476.
UCSCi uc002jmn.1. human. [O75947-1 ]
uc002jmo.1. human. [O75947-2 ]

Organism-specific databases

CTDi 10476.
GeneCardsi GC17M073034.
HGNCi HGNC:845. ATP5H.
HPAi HPA042777.
HPA048459.
neXtProti NX_O75947.
PharmGKBi PA25135.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG307464.
GeneTreei ENSGT00390000003582.
HOGENOMi HOG000267023.
HOVERGENi HBG050612.
InParanoidi O75947.
KOi K02138.
OMAi MEDYRDA.
PhylomeDBi O75947.
TreeFami TF314031.

Enzyme and pathway databases

Reactomei REACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

GeneWikii ATP5H.
GenomeRNAii 10476.
NextBioi 39734.
PROi O75947.

Gene expression databases

Bgeei O75947.
CleanExi HS_ATP5H.
ExpressionAtlasi O75947. baseline and differential.
Genevestigatori O75947.

Family and domain databases

InterProi IPR008689. ATPase_F0-cplx_dsu_mt.
[Graphical view ]
Pfami PF05873. Mt_ATP-synt_D. 1 hit.
[Graphical view ]
PIRSFi PIRSF005514. ATPase_F0_D_mt. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning, and chromosomal localization of a human F1F0-type ATPase subunit d."
    Lee H.C., Park D.S., Lee C.M., Cho W.K., Ahn H.J., Lee M.Y., Hwang M.Y., Jin S.W., Sohn U.I.K.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Thymus.
  2. "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] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  3. Mao Y.M., Xie Y., Ying K.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal brain.
  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] (ISOFORM 1).
    Tissue: Uterus.
  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] (ISOFORMS 1 AND 2).
    Tissue: Brain and Pancreas.
  7. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 10-25; 33-58; 64-72; 79-109 AND 124-144.
    Tissue: Fetal brain cortex.
  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-85; LYS-95; LYS-117 AND LYS-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATP5H_HUMAN
AccessioniPrimary (citable) accession number: O75947
Secondary accession number(s): B2R5L6, Q9H3J4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 138 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3