Search Results

Overview

Uniprot IDP06576
Protein NameATP synthase F(1) complex subunit beta, mitochondrial
Gene NameATP5F1B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
124 EGLVRGQKVLDSGAP
133 LDSGAPIKIPVGPET
161 ERGPIKTKQFAPIHA
198 DLLAPYAKGGKIGLF
201 APYAKGGKIGLFGGA
259 ESGVINLKDATSKVA
264 NLKDATSKVALVYGQ
426 DVARGVQKILQDYKS
480 VFTGHMGKLVPLKET
485 MGKLVPLKETIKGFQ
522 EAVAKADKLAEEHSS

Function

Catalytic subunit beta, 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) (PubMed:37244256). 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 subunit alpha (ATP5F1A), forms the catalytic core in the F(1) domain (PubMed:37244256)

Protein Sequence

10 MLGFVGRVAA 20 APASGALRRL 30 TPSASLPPAQ 40 LLLRAAPTAV 50 HPVRDYAAQT 60 SPSPKAGAAT 70 GRIVAVIGAV 80 VDVQFDEGLP 90 PILNALEVQG 100 RETRLVLEVA 110 QHLGESTVRT 120 IAMDGTEGLV 130 RGQKVLDSGA 140 PIKIPVGPET 150 LGRIMNVIGE 160 PIDERGPIKT 170 KQFAPIHAEA 180 PEFMEMSVEQ 190 EILVTGIKVV 200 DLLAPYAKGG 210 KIGLFGGAGV 220 GKTVLIMELI 230 NNVAKAHGGY 240 SVFAGVGERT 250 REGNDLYHEM 260 IESGVINLKD 270 ATSKVALVYG 280 QMNEPPGARA 290 RVALTGLTVA 300 EYFRDQEGQD 310 VLLFIDNIFR 320 FTQAGSEVSA 330 LLGRIPSAVG 340 YQPTLATDMG 350 TMQERITTTK 360 KGSITSVQAI 370 YVPADDLTDP 380 APATTFAHLD 390 ATTVLSRAIA 400 ELGIYPAVDP 410 LDSTSRIMDP 420 NIVGSEHYDV 430 ARGVQKILQD 440 YKSLQDIIAI 450 LGMDELSEED 460 KLTVSRARKI 470 QRFLSQPFQV 480 AEVFTGHMGK 490 LVPLKETIKG 500 FQQILAGEYD 510 HLPEQAFYMV 520 GPIEEAVAKA DKLAEEHSS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0009986 cell surface
Molecular Function GO:0042288 MHC class I protein binding
Molecular Function GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
Molecular Function GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process GO:0001525 angiogenesis
Biological Process GO:0006754 ATP biosynthetic process
Biological Process GO:0006091 generation of precursor metabolites and energy
Biological Process GO:0001649 osteoblast differentiation
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:1902600 proton transmembrane transport
Biological Process GO:0051453 regulation of intracellular pH
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0005743 mitochondrial inner membrane
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0031966 mitochondrial membrane
Cellular Component GO:0042645 mitochondrial nucleoid
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0045259 proton-transporting ATP synthase complex
Molecular Function GO:0043532 angiostatin binding
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0046872 metal ion binding

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] 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.

[6] 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.

[7] 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.

[8] 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.

[9] 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.