Full text data of ATP5H
ATP5H
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
ATP synthase subunit d, mitochondrial; ATPase subunit d
ATP synthase subunit d, mitochondrial; ATPase subunit d
UniProt
O75947
ID ATP5H_HUMAN Reviewed; 161 AA.
AC O75947; B2R5L6; Q9H3J4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=ATP synthase subunit d, mitochondrial;
DE Short=ATPase subunit d;
GN Name=ATP5H; ORFNames=My032;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
RA Lee H.C., Park D.S., Lee C.M., Cho W.K., Ahn H.J., Lee M.Y.,
RA Hwang M.Y., Jin S.W., Sohn U.I.K.;
RT "cDNA cloning, and chromosomal localization of a human F1F0-type
RT ATPase subunit d.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Ying K.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 10-25; 33-58; 64-72; 79-109 AND 124-144.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-85; LYS-95; LYS-117 AND
RP LYS-149, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC synthase or Complex V) produces ATP from ADP in the presence of a
CC proton gradient across the membrane which is generated by electron
CC transport complexes of the respiratory chain. F-type ATPases
CC consist of two structural domains, F(1) - containing the
CC extramembraneous catalytic core, and F(0) - containing the
CC membrane proton channel, linked together by a central stalk and a
CC peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC domain of F(1) is coupled via a rotary mechanism of the central
CC stalk subunits to proton translocation. Part of the complex F(0)
CC domain and the peripheric stalk, which acts as a stator to hold
CC the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC core - and CF(0) - the membrane proton channel. CF(0) seems to
CC have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L).
CC Component of an ATP synthase complex composed of ATP5F1, ATP5G1,
CC ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1,
CC ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75947-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75947-2; Sequence=VSP_000436;
CC -!- SIMILARITY: Belongs to the ATPase d subunit family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF087135; AAC36338.1; -; mRNA.
DR EMBL; AF070650; AAD20956.1; -; mRNA.
DR EMBL; AF061735; AAG43146.1; -; mRNA.
DR EMBL; AK312230; BAG35163.1; -; mRNA.
DR EMBL; CH471099; EAW89228.1; -; Genomic_DNA.
DR EMBL; BC032245; AAH32245.1; -; mRNA.
DR EMBL; BC038092; AAH38092.1; -; mRNA.
DR RefSeq; NP_001003785.1; NM_001003785.1.
DR RefSeq; NP_006347.1; NM_006356.2.
DR UniGene; Hs.514465; -.
DR ProteinModelPortal; O75947; -.
DR SMR; O75947; 4-124.
DR IntAct; O75947; 6.
DR MINT; MINT-1407327; -.
DR STRING; 9606.ENSP00000301587; -.
DR PhosphoSite; O75947; -.
DR OGP; O75947; -.
DR REPRODUCTION-2DPAGE; IPI00456049; -.
DR UCD-2DPAGE; O75947; -.
DR PaxDb; O75947; -.
DR PeptideAtlas; O75947; -.
DR PRIDE; O75947; -.
DR Ensembl; ENST00000301587; ENSP00000301587; ENSG00000167863.
DR Ensembl; ENST00000344546; ENSP00000344230; ENSG00000167863.
DR GeneID; 10476; -.
DR KEGG; hsa:10476; -.
DR UCSC; uc002jmn.1; human.
DR CTD; 10476; -.
DR GeneCards; GC17M073034; -.
DR HGNC; HGNC:845; ATP5H.
DR HPA; HPA042777; -.
DR HPA; HPA048459; -.
DR neXtProt; NX_O75947; -.
DR PharmGKB; PA25135; -.
DR eggNOG; NOG307464; -.
DR HOGENOM; HOG000267023; -.
DR HOVERGEN; HBG050612; -.
DR InParanoid; O75947; -.
DR KO; K02138; -.
DR OMA; MEDYRDA; -.
DR PhylomeDB; O75947; -.
DR Reactome; REACT_111217; Metabolism.
DR GeneWiki; ATP5H; -.
DR GenomeRNAi; 10476; -.
DR NextBio; 39734; -.
DR PRO; PR:O75947; -.
DR ArrayExpress; O75947; -.
DR Bgee; O75947; -.
DR CleanEx; HS_ATP5H; -.
DR Genevestigator; O75947; -.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
DR GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IC:UniProtKB.
DR GO; GO:0006200; P:ATP catabolic process; IDA:GOC.
DR GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome.
DR InterPro; IPR008689; ATPase_F0-cplx_dsu_mt.
DR Pfam; PF05873; Mt_ATP-synt_D; 1.
DR PIRSF; PIRSF005514; ATPase_F0_D_mt; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; CF(0); Complete proteome;
KW Direct protein sequencing; Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transport.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 161 ATP synthase subunit d, mitochondrial.
FT /FTId=PRO_0000071673.
FT MOD_RES 2 2 N-acetylalanine (By similarity).
FT MOD_RES 85 85 N6-acetyllysine.
FT MOD_RES 95 95 N6-acetyllysine.
FT MOD_RES 117 117 N6-acetyllysine.
FT MOD_RES 149 149 N6-acetyllysine.
FT VAR_SEQ 74 97 Missing (in isoform 2).
FT /FTId=VSP_000436.
SQ SEQUENCE 161 AA; 18491 MW; E93020ADA1BA1694 CRC64;
MAGRKLALKT IDWVAFAEII PQNQKAIASS LKSWNETLTS RLAALPENPP AIDWAYYKAN
VAKAGLVDDF EKKFNALKVP VPEDKYTAQV DAEEKEDVKS CAEWVSLSKA RIVEYEKEME
KMKNLIPFDQ MTIEDLNEAF PETKLDKKKY PYWPHQPIEN L
//
ID ATP5H_HUMAN Reviewed; 161 AA.
AC O75947; B2R5L6; Q9H3J4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=ATP synthase subunit d, mitochondrial;
DE Short=ATPase subunit d;
GN Name=ATP5H; ORFNames=My032;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
RA Lee H.C., Park D.S., Lee C.M., Cho W.K., Ahn H.J., Lee M.Y.,
RA Hwang M.Y., Jin S.W., Sohn U.I.K.;
RT "cDNA cloning, and chromosomal localization of a human F1F0-type
RT ATPase subunit d.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Ying K.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 10-25; 33-58; 64-72; 79-109 AND 124-144.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-85; LYS-95; LYS-117 AND
RP LYS-149, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC synthase or Complex V) produces ATP from ADP in the presence of a
CC proton gradient across the membrane which is generated by electron
CC transport complexes of the respiratory chain. F-type ATPases
CC consist of two structural domains, F(1) - containing the
CC extramembraneous catalytic core, and F(0) - containing the
CC membrane proton channel, linked together by a central stalk and a
CC peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC domain of F(1) is coupled via a rotary mechanism of the central
CC stalk subunits to proton translocation. Part of the complex F(0)
CC domain and the peripheric stalk, which acts as a stator to hold
CC the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC core - and CF(0) - the membrane proton channel. CF(0) seems to
CC have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L).
CC Component of an ATP synthase complex composed of ATP5F1, ATP5G1,
CC ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1,
CC ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75947-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75947-2; Sequence=VSP_000436;
CC -!- SIMILARITY: Belongs to the ATPase d subunit family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF087135; AAC36338.1; -; mRNA.
DR EMBL; AF070650; AAD20956.1; -; mRNA.
DR EMBL; AF061735; AAG43146.1; -; mRNA.
DR EMBL; AK312230; BAG35163.1; -; mRNA.
DR EMBL; CH471099; EAW89228.1; -; Genomic_DNA.
DR EMBL; BC032245; AAH32245.1; -; mRNA.
DR EMBL; BC038092; AAH38092.1; -; mRNA.
DR RefSeq; NP_001003785.1; NM_001003785.1.
DR RefSeq; NP_006347.1; NM_006356.2.
DR UniGene; Hs.514465; -.
DR ProteinModelPortal; O75947; -.
DR SMR; O75947; 4-124.
DR IntAct; O75947; 6.
DR MINT; MINT-1407327; -.
DR STRING; 9606.ENSP00000301587; -.
DR PhosphoSite; O75947; -.
DR OGP; O75947; -.
DR REPRODUCTION-2DPAGE; IPI00456049; -.
DR UCD-2DPAGE; O75947; -.
DR PaxDb; O75947; -.
DR PeptideAtlas; O75947; -.
DR PRIDE; O75947; -.
DR Ensembl; ENST00000301587; ENSP00000301587; ENSG00000167863.
DR Ensembl; ENST00000344546; ENSP00000344230; ENSG00000167863.
DR GeneID; 10476; -.
DR KEGG; hsa:10476; -.
DR UCSC; uc002jmn.1; human.
DR CTD; 10476; -.
DR GeneCards; GC17M073034; -.
DR HGNC; HGNC:845; ATP5H.
DR HPA; HPA042777; -.
DR HPA; HPA048459; -.
DR neXtProt; NX_O75947; -.
DR PharmGKB; PA25135; -.
DR eggNOG; NOG307464; -.
DR HOGENOM; HOG000267023; -.
DR HOVERGEN; HBG050612; -.
DR InParanoid; O75947; -.
DR KO; K02138; -.
DR OMA; MEDYRDA; -.
DR PhylomeDB; O75947; -.
DR Reactome; REACT_111217; Metabolism.
DR GeneWiki; ATP5H; -.
DR GenomeRNAi; 10476; -.
DR NextBio; 39734; -.
DR PRO; PR:O75947; -.
DR ArrayExpress; O75947; -.
DR Bgee; O75947; -.
DR CleanEx; HS_ATP5H; -.
DR Genevestigator; O75947; -.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
DR GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IC:UniProtKB.
DR GO; GO:0006200; P:ATP catabolic process; IDA:GOC.
DR GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; TAS:Reactome.
DR InterPro; IPR008689; ATPase_F0-cplx_dsu_mt.
DR Pfam; PF05873; Mt_ATP-synt_D; 1.
DR PIRSF; PIRSF005514; ATPase_F0_D_mt; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; CF(0); Complete proteome;
KW Direct protein sequencing; Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transport.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 161 ATP synthase subunit d, mitochondrial.
FT /FTId=PRO_0000071673.
FT MOD_RES 2 2 N-acetylalanine (By similarity).
FT MOD_RES 85 85 N6-acetyllysine.
FT MOD_RES 95 95 N6-acetyllysine.
FT MOD_RES 117 117 N6-acetyllysine.
FT MOD_RES 149 149 N6-acetyllysine.
FT VAR_SEQ 74 97 Missing (in isoform 2).
FT /FTId=VSP_000436.
SQ SEQUENCE 161 AA; 18491 MW; E93020ADA1BA1694 CRC64;
MAGRKLALKT IDWVAFAEII PQNQKAIASS LKSWNETLTS RLAALPENPP AIDWAYYKAN
VAKAGLVDDF EKKFNALKVP VPEDKYTAQV DAEEKEDVKS CAEWVSLSKA RIVEYEKEME
KMKNLIPFDQ MTIEDLNEAF PETKLDKKKY PYWPHQPIEN L
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