Search Results

Overview

Uniprot ID	P25705
Protein Name	ATP synthase F(1) complex subunit alpha, mitochondrial
Gene Name	ATP5F1A
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
123	VVVFGNDKLIKEGDI
126	FGNDKLIKEGDIVKR
161	LGNAIDGKGPIGSKT
167	GKGPIGSKTRRRVGL
175	TRRRVGLKAPGIIPR
194	EPMQTGIKAVDSLVP
218	IGDRQTGKTSIAIDT
230	IDTIINQKRFNDGSD
239	FNDGSDEKKKLYCIY
261	STVAQLVKRLTDADA
305	EYFRDNGKHALIIYD
316	IIYDDLSKQAVAYRQ
427	AAQTRAMKQVAGTMK
434	KQVAGTMKLELAQYR
498	GVRGYLDKLEPSKIT
503	LDKLEPSKITKFENA
506	LEPSKITKFENAFLS
531	GTIRADGKISEQSDA
539	ISEQSDAKLKEIVTN

Function

Subunit alpha, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that 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 (Probable). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the catalytic subunit beta (ATP5F1B), forms the catalytic core in the F(1) domain (PubMed:37244256). Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (Probable). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (PubMed:30146159)

Protein Sequence

10 MLSVRVAAAV 20 VRALPRRAGL 30 VSRNALGSSF 40 IAARNFHASN 50 THLQKTGTAE 60 MSSILEERIL 70 GADTSVDLEE 80 TGRVLSIGDG 90 IARVHGLRNV 100 QAEEMVEFSS 110 GLKGMSLNLE 120 PDNVGVVVFG 130 NDKLIKEGDI 140 VKRTGAIVDV 150 PVGEELLGRV 160 VDALGNAIDG 170 KGPIGSKTRR 180 RVGLKAPGII 190 PRISVREPMQ 200 TGIKAVDSLV 210 PIGRGQRELI 220 IGDRQTGKTS 230 IAIDTIINQK 240 RFNDGSDEKK 250 KLYCIYVAIG 260 QKRSTVAQLV 270 KRLTDADAMK 280 YTIVVSATAS 290 DAAPLQYLAP 300 YSGCSMGEYF 310 RDNGKHALII 320 YDDLSKQAVA 330 YRQMSLLLRR 340 PPGREAYPGD 350 VFYLHSRLLE 360 RAAKMNDAFG 370 GGSLTALPVI 380 ETQAGDVSAY 390 IPTNVISITD 400 GQIFLETELF 410 YKGIRPAINV 420 GLSVSRVGSA 430 AQTRAMKQVA 440 GTMKLELAQY 450 REVAAFAQFG 460 SDLDAATQQL 470 LSRGVRLTEL 480 LKQGQYSPMA 490 IEEQVAVIYA 500 GVRGYLDKLE 510 PSKITKFENA 520 FLSHVVSQHQ 530 ALLGTIRADG 540 KISEQSDAKL 550 KEIVTNFLAG FEA

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0009986	cell surface
Cellular Component	GO:0070062	extracellular exosome
Cellular Component	GO:0016020	membrane
Cellular Component	GO:0045121	membrane raft
Cellular Component	GO:0005743	mitochondrial inner membrane
Cellular Component	GO:0005759	mitochondrial matrix
Cellular Component	GO:0005739	mitochondrion
Cellular Component	GO:0005886	plasma membrane
Cellular Component	GO:0045259	proton-transporting ATP synthase complex
Molecular Function	GO:0043531	ADP binding
Molecular Function	GO:0043532	angiostatin binding
Molecular Function	GO:0005524	ATP binding
Molecular Function	GO:0016887	ATP hydrolysis activity
Molecular Function	GO:0042288	MHC class I protein binding
Molecular Function	GO:0002020	protease binding
Molecular Function	GO:0046933	proton-transporting ATP synthase activity, rotational mechanism
Molecular Function	GO:0003723	RNA binding
Biological Process	GO:0006754	ATP biosynthetic process
Biological Process	GO:0071549	cellular response to dexamethasone stimulus
Biological Process	GO:0071732	cellular response to nitric oxide
Biological Process	GO:0006629	lipid metabolic process
Biological Process	GO:0001937	negative regulation of endothelial cell proliferation
Biological Process	GO:0043536	positive regulation of blood vessel endothelial cell migration
Biological Process	GO:0015986	proton motive force-driven ATP synthesis
Biological Process	GO:0042776	proton motive force-driven mitochondrial ATP synthesis
Biological Process	GO:0045471	response to ethanol
Biological Process	GO:0014850	response to muscle activity

Reference

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[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[6] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[7] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[8] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[9] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[10] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[11] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[12] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.