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O75947 (ATP5H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit d, mitochondrial

Short name=ATPase subunit d
Gene names
Name:ATP5H
ORF Names:My032
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length161 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Mitochondrion. Mitochondrion inner membrane.

Sequence similarities

Belongs to the ATPase d subunit family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75947-1)

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.
Isoform 2 (identifier: O75947-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 161160ATP synthase subunit d, mitochondrial
PRO_0000071673

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue851N6-acetyllysine Ref.8
Modified residue951N6-acetyllysine Ref.8
Modified residue1171N6-acetyllysine Ref.8
Modified residue1491N6-acetyllysine Ref.8

Natural variations

Alternative sequence74 – 9724Missing in isoform 2.
VSP_000436

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E93020ADA1BA1694

FASTA16118,491
        10         20         30         40         50         60 
MAGRKLALKT IDWVAFAEII PQNQKAIASS LKSWNETLTS RLAALPENPP AIDWAYYKAN 

        70         80         90        100        110        120 
VAKAGLVDDF EKKFNALKVP VPEDKYTAQV DAEEKEDVKS CAEWVSLSKA RIVEYEKEME 

       130        140        150        160 
KMKNLIPFDQ MTIEDLNEAF PETKLDKKKY PYWPHQPIEN L 

« Hide

Isoform 2 [UniParc].

Checksum: 0796685CD2CC605E
Show »

FASTA13715,773

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11712.1. [O75947-1]
CCDS32727.1. [O75947-2]
RefSeqNP_001003785.1. NM_001003785.1. [O75947-2]
NP_006347.1. NM_006356.2. [O75947-1]
UniGeneHs.514465.

3D structure databases

ProteinModelPortalO75947.
SMRO75947. Positions 4-124.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115739. 10 interactions.
IntActO75947. 6 interactions.
MINTMINT-1407327.
STRING9606.ENSP00000301587.

PTM databases

PhosphoSiteO75947.

2D gel databases

OGPO75947.
REPRODUCTION-2DPAGEIPI00456049.
UCD-2DPAGEO75947.

Proteomic databases

MaxQBO75947.
PaxDbO75947.
PeptideAtlasO75947.
PRIDEO75947.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301587; ENSP00000301587; ENSG00000167863. [O75947-1]
ENST00000344546; ENSP00000344230; ENSG00000167863. [O75947-2]
GeneID10476.
KEGGhsa:10476.
UCSCuc002jmn.1. human. [O75947-1]
uc002jmo.1. human. [O75947-2]

Organism-specific databases

CTD10476.
GeneCardsGC17M073034.
HGNCHGNC:845. ATP5H.
HPAHPA042777.
HPA048459.
neXtProtNX_O75947.
PharmGKBPA25135.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG307464.
HOGENOMHOG000267023.
HOVERGENHBG050612.
InParanoidO75947.
KOK02138.
OMAMEDYRDA.
PhylomeDBO75947.
TreeFamTF314031.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO75947.
BgeeO75947.
CleanExHS_ATP5H.
GenevestigatorO75947.

Family and domain databases

InterProIPR008689. ATPase_F0-cplx_dsu_mt.
[Graphical view]
PfamPF05873. Mt_ATP-synt_D. 1 hit.
[Graphical view]
PIRSFPIRSF005514. ATPase_F0_D_mt. 1 hit.
ProtoNetSearch...

Other

GeneWikiATP5H.
GenomeRNAi10476.
NextBio39734.
PROO75947.

Entry information

Entry nameATP5H_HUMAN
AccessionPrimary (citable) accession number: O75947
Secondary accession number(s): B2R5L6, Q9H3J4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM