Search Results

Overview

Uniprot IDQ9CQQ7
Protein NameATP synthase peripheral stalk subunit b, mitochondrial
Gene NameAtp5pb
OrganismMus musculus

Kla Sites from experimental identification

Position Flanking peptide
115 LIVYVIKKYGASFGE
131 IDKLNEEKIAQLEEV
139 IAQLEEVKQSSMKQI
144 EVKQSSMKQIQDAID
162 AQQALVQKRHYLFDV
210 VQNMMRRKEEEHMID
221 HMIDWVEKHVVKSIS
225 WVEKHVVKSISVQQE
233 SISVQQEKETIAKCI
238 QEKETIAKCIEDLKL
244 AKCIEDLKLLAKKAQ
249 DLKLLAKKAQAQPIM

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. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. 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 (By similarity). 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 (By similarity). 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 ATAAPCLKNA 30 AALGPGVLQA 40 TRAFHTGQPR 50 LAPLPPLPEY 60 GGKVRLGLIP 70 EEFFQFLYPK 80 TGVTGPYVLG 90 TGLSLYFLSK 100 EIYVITPETF 110 STISVVGLIV 120 YVIKKYGASF 130 GEFIDKLNEE 140 KIAQLEEVKQ 150 SSMKQIQDAI 160 DMEKAQQALV 170 QKRHYLFDVQ 180 RNNIALALEV 190 TYRERLHKAY 200 KEVKNRLDYH 210 ISVQNMMRRK 220 EEEHMIDWVE 230 KHVVKSISVQ 240 QEKETIAKCI 250 EDLKLLAKKA QAQPIM

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005743 mitochondrial inner membrane
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0043209 myelin sheath
Cellular Component GO:0045259 proton-transporting ATP synthase complex
Molecular Function GO:0044877 protein-containing complex binding
Molecular Function GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
Biological Process GO:0015986 proton motive force-driven ATP synthesis
Biological Process GO:0042776 proton motive force-driven mitochondrial ATP synthesis

Reference

[1] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.

[2] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.

[3] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.