O75947 (ATP5H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit d, mitochondrial
Short name=ATPase subunit d

Gene names

Name:	ATP5H
ORF Names:	My032

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	161 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from direct assay PubMed 12110673. Source: GOC mitochondrial ATP synthesis coupled proton transport Inferred by curator PubMed 12110673. Source: UniProtKB respiratory electron transport chain Traceable author statement. Source: Reactome
Cellular_component	mitochondrial proton-transporting ATP synthase complex Inferred from direct assay PubMed 12110673. Source: UniProtKB mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: InterPro
Molecular_function	hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro transmembrane transporter activity Inferred by curator PubMed 12110673. Source: UniProtKB
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 161	160	ATP synthase subunit d, mitochondrial		PRO_0000071673
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	63	1	N6-acetyllysine By similarity
	Modified residue	78	1	N6-acetyllysine By similarity
	Modified residue	85	1	N6-acetyllysine Ref.8
	Modified residue	95	1	N6-acetyllysine Ref.8
	Modified residue	99	1	N6-acetyllysine By similarity
	Modified residue	117	1	N6-acetyllysine Ref.8
	Modified residue	149	1	N6-acetyllysine Ref.8
Natural variations
	Alternative sequence	74 – 97	24	Missing in isoform 2.		VSP_000436

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E93020ADA1BA1694	FASTA	161	18,491
	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
	Isoform 2 [UniParc]. Checksum: 0796685CD2CC605E	FASTA	137	15,773
	10 20 30 40 50 60 MAGRKLALKT IDWVAFAEII PQNQKAIASS LKSWNETLTS RLAALPENPP AIDWAYYKAN 70 80 90 100 110 120 VAKAGLVDDF EKKVKSCAEW VSLSKARIVE YEKEMEKMKN LIPFDQMTIE DLNEAFPETK 130 LDKKKYPYWP HQPIENL

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY.
[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.
IPI	IPI00220487. IPI00456049.
RefSeq	NP_001003785.1. NM_001003785.1. NP_006347.1. NM_006356.2.
UniGene	Hs.514465.
3D structure databases
ProteinModelPortal	O75947.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75947. 4 interactions.
MINT	MINT-1407327.
STRING	9606.ENSP00000301587.
PTM databases
PhosphoSite	O75947.
2D gel databases
OGP	O75947.
REPRODUCTION-2DPAGE	IPI00456049.
UCD-2DPAGE	O75947.
Proteomic databases
PaxDb	O75947.
PeptideAtlas	O75947.
PRIDE	O75947.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000301587; ENSP00000301587; ENSG00000167863. ENST00000344546; ENSP00000344230; ENSG00000167863.
GeneID	10476.
KEGG	hsa:10476.
UCSC	uc002jmn.1. human. uc002jmo.1. human.
Organism-specific databases
CTD	10476.
GeneCards	GC17M073034.
HGNC	HGNC:845. ATP5H.
HPA	HPA042777. HPA048459.
neXtProt	NX_O75947.
PharmGKB	PA25135.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG307464.
HOGENOM	HOG000267023.
HOVERGEN	HBG050612.
InParanoid	O75947.
KO	K02138.
OMA	MEDYRDA.
OrthoDB	EOG4XWG04.
PhylomeDB	O75947.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
Bgee	O75947.
CleanEx	HS_ATP5H.
Genevestigator	O75947.
GermOnline	ENSG00000167863. Homo sapiens.
Family and domain databases
InterPro	IPR008689. ATPase_F0-cplx_dsu_mt. [Graphical view]
Pfam	PF05873. Mt_ATP-synt_D. 1 hit. [Graphical view]
PIRSF	PIRSF005514. ATPase_F0_D_mt. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	10476.
NextBio	39734.

Entry information

Entry name

ATP5H_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 125 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.