Search Results

Overview

Uniprot IDP24539
Protein NameATP synthase peripheral stalk subunit b, mitochondrial
Gene NameATP5PB
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
131 ADKLNEQKLAQLEEA
139 LAQLEEAKQASIQHI
154 QNAIDTEKSQQALVQ
162 SQQALVQKRHYLFDV
221 HMINWVEKHVVQSIS
233 SISTQQEKETIAKCI
238 QEKETIAKCIADLKL
249 DLKLLAKKAQAQPVM

Function

Subunit b, 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 (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). Part of the complex F(0) domain (PubMed:37244256). Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity)

Protein Sequence

10 MLSRVVLSAA 20 ATAAPSLKNA 30 AFLGPGVLQA 40 TRTFHTGQPH 50 LVPVPPLPEY 60 GGKVRYGLIP 70 EEFFQFLYPK 80 TGVTGPYVLG 90 TGLILYALSK 100 EIYVISAETF 110 TALSVLGVMV 120 YGIKKYGPFV 130 ADFADKLNEQ 140 KLAQLEEAKQ 150 ASIQHIQNAI 160 DTEKSQQALV 170 QKRHYLFDVQ 180 RNNIAMALEV 190 TYRERLYRVY 200 KEVKNRLDYH 210 ISVQNMMRRK 220 EQEHMINWVE 230 KHVVQSISTQ 240 QEKETIAKCI 250 ADLKLLAKKA QAQPVM

Gene Ontology

Classification GO ID Description
Cellular Component GO:0016020 membrane
Cellular Component GO:0005743 mitochondrial inner membrane
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005634 nucleus
Cellular Component GO:0045259 proton-transporting ATP synthase complex
Molecular Function GO:0015078 proton transmembrane transporter activity
Biological Process GO:0015986 proton motive force-driven ATP synthesis
Biological Process GO:0042776 proton motive force-driven mitochondrial ATP synthesis
Biological Process GO:0021762 substantia nigra development

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] 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.

[5] 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.

[6] 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.