ID ATPMK_HUMAN Reviewed; 58 AA. AC Q96IX5; B2R4N2; D3DR92; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 04-NOV-2026, entry version 172. DE RecName: Full=ATP synthase F(0) complex subunit k, mitochondrial {ECO:0000305}; DE AltName: Full=ATP synthase membrane subunit DAPIT, mitochondrial {ECO:0000305}; DE AltName: Full=Diabetes-associated protein in insulin-sensitive tissues; DE AltName: Full=HCV F-transactivated protein 2; DE AltName: Full=Up-regulated during skeletal muscle growth protein 5 {ECO:0000305}; GN Name=ATP5MK {ECO:0000312|HGNC:HGNC:30889}; GN Synonyms=ATP5MD, DAPIT, HCVFTP2, USMG5; ORFNames=PD04912; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY SBP1. RX PubMed=16222733; DOI=10.3748/wjg.v11.i35.5438; RA Ji D., Cheng J., Chen G.-F., Liu Y., Wang L., Guo J.; RT "Study of transactivating effect of pre-S2 protein of hepatitis B virus and RT cloning of genes transactivated by pre-S2 protein with suppression RT subtractive hybridization."; RL World J. Gastroenterol. 11:5438-5443(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; RA Frigimelica E., Lanfranchi G.; RT "Study of 100 skeletal muscle full length mRNA."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Blood, Lung, and Skeletal muscle; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [8] 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., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21345788; DOI=10.1074/jbc.m110.198523; RA Ohsakaya S., Fujikawa M., Hisabori T., Yoshida M.; RT "Knockdown of DAPIT (diabetes-associated protein in insulin-sensitive RT tissue) results in loss of ATP synthase in mitochondria."; RL J. Biol. Chem. 286:20292-20296(2011). RN [10] RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [11] RP INVOLVEMENT IN MC5DN6, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=29917077; DOI=10.1093/hmg/ddy231; RA Barca E., Ganetzky R.D., Potluri P., Juanola-Falgarona M., Gai X., Li D., RA Jalas C., Hirsch Y., Emmanuele V., Tadesse S., Ziosi M., Akman H.O., RA Chung W.K., Tanji K., McCormick E.M., Place E., Consugar M., Pierce E.A., RA Hakonarson H., Wallace D.C., Hirano M., Falk M.J.; RT "USMG5 Ashkenazi Jewish founder mutation impairs mitochondrial complex V RT dimerization and ATP synthesis."; RL Hum. Mol. Genet. 27:3305-3312(2018). CC -!- FUNCTION: Subunit k, of the mitochondrial membrane ATP synthase complex CC (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the CC presence of a proton gradient across the membrane which is generated by CC electron transport complexes of the respiratory chain (Probable). ATP CC synthase complex consist of a soluble F(1) head domain - the catalytic CC core - and a membrane F(1) domain - the membrane proton channel (By CC similarity). These two domains are linked by a central stalk rotating CC inside the F(1) region and a stationary peripheral stalk (By CC similarity). During catalysis, ATP synthesis in the catalytic domain of CC F(1) is coupled via a rotary mechanism of the central stalk subunits to CC proton translocation (Probable). In vivo, can only synthesize ATP CC although its ATP hydrolase activity can be activated artificially in CC vitro (By similarity). Part of the complex F(0) domain (By similarity). CC Required for dimerization of the ATP synthase complex and as such CC regulates ATP synthesis in the mitochondria (PubMed:21345788, CC PubMed:29917077). {ECO:0000250|UniProtKB:P19483, CC ECO:0000250|UniProtKB:Q3ZBI7, ECO:0000269|PubMed:21345788, CC ECO:0000269|PubMed:29917077, ECO:0000305|PubMed:29917077}. CC -!- SUBUNIT: Component of the ATP synthase complex composed at least of CC ATP5F1A/subunit alpha, ATP5F1B/subunit beta, ATP5MC1/subunit c CC (homooctamer), MT-ATP6/subunit a, MT-ATP8/subunit 8, ATP5ME/subunit e, CC ATP5MF/subunit f, ATP5MG/subunit g, ATP5MK/subunit k, ATP5MJ/subunit j, CC ATP5F1C/subunit gamma, ATP5F1D/subunit delta, ATP5F1E/subunit epsilon, CC ATP5PF/subunit F6, ATP5PB/subunit b, ATP5PD/subunit d, ATP5PO/subunit CC OSCP (By similarity). ATP synthase complex consists of a soluble F(1) CC head domain (subunits alpha(3) and beta(3)) - the catalytic core - and CC a membrane F(0) domain - the membrane proton channel (subunits c, a, 8, CC e, f, g, k and j) (By similarity). These two domains are linked by a CC central stalk (subunits gamma, delta, and epsilon) rotating inside the CC F1 region and a stationary peripheral stalk (subunits F6, b, d, and CC OSCP) (By similarity). The ATP synthase complex/complex V exists as a CC monomeric and a dimeric supercomplex that helps shape mitochondrial CC cristae to optimize proton flow (PubMed:29917077). CC {ECO:0000250|UniProtKB:Q3ZBI7, ECO:0000269|PubMed:29917077}. CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane CC {ECO:0000269|PubMed:21345788, ECO:0000269|PubMed:29917077}; Single-pass CC membrane protein {ECO:0000255}. CC -!- INDUCTION: Transactivated by SBP1. {ECO:0000269|PubMed:16222733}. CC -!- DISEASE: Mitochondrial complex V deficiency, nuclear type 6 (MC5DN6) CC [MIM:618683]: An autosomal recessive mitochondrial disorder CC characterized by gross motor developmental delay manifesting in the CC first years of life, and subsequent episodic developmental regression. CC The episodes are associated with metabolic stress, including fever, CC illness, and general anesthesia. Patients develop gait difficulties or CC loss of ambulation, as well as other variable abnormalities, including CC abnormal movements, hemiplegia, and persistent lethargy. Brain imaging CC shows degenerative features in the basal ganglia and brainstem CC consistent with a diagnosis of Leigh syndrome. CC {ECO:0000269|PubMed:29917077}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY740522; AAU89079.1; -; mRNA. DR EMBL; AJ272056; CAC81243.1; -; mRNA. DR EMBL; AK311888; BAG34829.1; -; mRNA. DR EMBL; AL591408; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW49642.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49643.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49644.1; -; Genomic_DNA. DR EMBL; BC007087; AAH07087.1; -; mRNA. DR EMBL; BC072683; AAH72683.1; -; mRNA. DR EMBL; BC091507; AAH91507.1; -; mRNA. DR CCDS; CCDS7548.1; -. DR RefSeq; NP_001193355.1; NM_001206426.2. DR RefSeq; NP_001193356.1; NM_001206427.2. DR RefSeq; NP_116136.1; NM_032747.4. DR RefSeq; XP_024304005.1; XM_024448237.2. DR RefSeq; XP_054222974.1; XM_054366999.1. DR AlphaFoldDB; Q96IX5; -. DR SMR; Q96IX5; -. DR BioGRID; 124287; 148. DR ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex. DR FunCoup; Q96IX5; 1120. DR IntAct; Q96IX5; 97. DR STRING; 9606.ENSP00000358840; -. DR BindingDB; Q96IX5; -. DR ChEMBL; CHEMBL6066304; -. DR GlyGen; Q96IX5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96IX5; -. DR PhosphoSitePlus; Q96IX5; -. DR SwissPalm; Q96IX5; -. DR BioMuta; USMG5; -. DR jPOST; Q96IX5; -. DR MassIVE; Q96IX5; -. DR PaxDb; 9606-ENSP00000358840; -. DR PeptideAtlas; Q96IX5; -. DR ProteomicsDB; 76865; -. DR Pumba; Q96IX5; -. DR TopDownProteomics; Q96IX5; -. DR Antibodypedia; 46057; 82 antibodies from 16 providers. DR DNASU; 84833; -. DR Ensembl; ENST00000309579.7; ENSP00000311245.3; ENSG00000173915.17. DR Ensembl; ENST00000337003.4; ENSP00000337705.4; ENSG00000173915.17. DR Ensembl; ENST00000369811.5; ENSP00000358826.1; ENSG00000173915.17. DR Ensembl; ENST00000369815.6; ENSP00000358830.1; ENSG00000173915.17. DR Ensembl; ENST00000369825.6; ENSP00000358840.1; ENSG00000173915.17. DR Ensembl; ENST00000876173.1; ENSP00000546232.1; ENSG00000173915.17. DR Ensembl; ENST00000876174.1; ENSP00000546233.1; ENSG00000173915.17. DR Ensembl; ENST00000876175.1; ENSP00000546234.1; ENSG00000173915.17. DR Ensembl; ENST00000876176.1; ENSP00000546235.1; ENSG00000173915.17. DR Ensembl; ENST00000876177.1; ENSP00000546236.1; ENSG00000173915.17. DR Ensembl; ENST00000876178.1; ENSP00000546237.1; ENSG00000173915.17. DR Ensembl; ENST00000876179.1; ENSP00000546238.1; ENSG00000173915.17. DR Ensembl; ENST00000876180.1; ENSP00000546239.1; ENSG00000173915.17. DR Ensembl; ENST00000876181.1; ENSP00000546240.1; ENSG00000173915.17. DR Ensembl; ENST00000940566.1; ENSP00000610625.1; ENSG00000173915.17. DR Ensembl; ENST00000940567.1; ENSP00000610626.1; ENSG00000173915.17. DR Ensembl; ENST00000940568.1; ENSP00000610627.1; ENSG00000173915.17. DR Ensembl; ENST00000940569.1; ENSP00000610628.1; ENSG00000173915.17. DR Ensembl; ENST00000940570.1; ENSP00000610629.1; ENSG00000173915.17. DR Ensembl; ENST00000940571.1; ENSP00000610630.1; ENSG00000173915.17. DR Ensembl; ENST00000940572.1; ENSP00000610631.1; ENSG00000173915.17. DR Ensembl; ENST00000940573.1; ENSP00000610632.1; ENSG00000173915.17. DR Ensembl; ENST00000940575.1; ENSP00000610634.1; ENSG00000173915.17. DR Ensembl; ENST00000940576.1; ENSP00000610635.1; ENSG00000173915.17. DR Ensembl; ENST00000940577.1; ENSP00000610636.1; ENSG00000173915.17. DR Ensembl; ENST00000940578.1; ENSP00000610637.1; ENSG00000173915.17. DR Ensembl; ENST00000940579.1; ENSP00000610638.1; ENSG00000173915.17. DR Ensembl; ENST00000940580.1; ENSP00000610639.1; ENSG00000173915.17. DR Ensembl; ENST00000940581.1; ENSP00000610640.1; ENSG00000173915.17. DR Ensembl; ENST00000951950.1; ENSP00000622009.1; ENSG00000173915.17. DR Ensembl; ENST00000951951.1; ENSP00000622010.1; ENSG00000173915.17. DR GeneID; 84833; -. DR KEGG; hsa:84833; -. DR MANE-Select; ENST00000369815.6; ENSP00000358830.1; NM_001206427.2; NP_001193356.1. DR UCSC; uc001kww.4; human. DR AGR; HGNC:30889; -. DR ClinPGx; PA134968209; -. DR CTD; 84833; -. DR DisGeNET; 84833; -. DR GeneCards; ATP5MK; -. DR HGNC; HGNC:30889; ATP5MK. DR HPA; ENSG00000173915; Low tissue specificity. DR MalaCards; ATP5MK; -. DR MIM; 615204; gene. DR MIM; 618683; phenotype. DR OpenTargets; ENSG00000173915; -. DR Orphanet; 254913; Isolated ATP synthase deficiency. DR VEuPathDB; HostDB:ENSG00000173915; -. DR eggNOG; ENOG502S82X; Eukaryota. DR GeneTree; ENSGT00390000015489; -. DR HOGENOM; CLU_209345_1_0_1; -. DR InParanoid; Q96IX5; -. DR OMA; ADEQFHF; -. DR OrthoDB; 9435504at2759; -. DR PAN-GO; Q96IX5; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q96IX5; -. DR PathwayCommons; Q96IX5; -. DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling. DR Reactome; R-HSA-8949613; Cristae formation. DR SignaLink; Q96IX5; -. DR Agora; ENSG00000173915; -. DR BioGRID-ORCS; 84833; 28 hits in 1009 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; USMG5; human. DR GenomeRNAi; 84833; -. DR Pharos; Q96IX5; Tbio. DR PRO; PR:Q96IX5; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q96IX5; protein. DR Bgee; ENSG00000173915; Expressed in quadriceps femoris and 104 other cell types or tissues. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0031966; C:mitochondrial membrane; EXP:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IMP:UniProtKB. DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; NAS:ComplexPortal. DR InterPro; IPR009125; ATPMK. DR PANTHER; PTHR34038; ATP SYNTHASE MEMBRANE SUBUNIT DAPIT, MITOCHONDRIAL; 1. DR PANTHER; PTHR34038:SF1; ATP SYNTHASE MEMBRANE SUBUNIT K, MITOCHONDRIAL; 1. DR Pfam; PF14960; ATP_synth_reg; 1. DR PRINTS; PR01821; DAPIT. PE 1: Evidence at protein level; KW Acetylation; Membrane; Mitochondrion; Primary mitochondrial disease; KW Proteomics identification; Reference proteome; Transmembrane; KW Transmembrane helix. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:25944712" FT CHAIN 2..58 FT /note="ATP synthase F(0) complex subunit k, mitochondrial" FT /id="PRO_0000231578" FT TRANSMEM 23..45 FT /note="Helical" FT /evidence="ECO:0000255" FT MOD_RES 16 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q78IK2" FT MOD_RES 17 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q78IK2" SQ SEQUENCE 58 AA; 6458 MW; 3BFC4C9E2920B126 CRC64; MAGPESDAQY QFTGIKKYFN SYTLTGRMNC VLATYGSIAL IVLYFKLRSK KTPAVKAT //