Search Results

Overview

Uniprot IDP83111
Protein NameSerine beta-lactamase-like protein LACTB, mitochondrial
Gene NameLACTB
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
240 EKAYKALKMMKENVA
243 YKALKMMKENVAFEQ
252 NVAFEQEKEGKSNEK
255 FEQEKEGKSNEKNDF
259 KEGKSNEKNDFTKFK
264 NEKNDFTKFKTEQEN
266 KNDFTKFKTEQENEA
274 TEQENEAKCRNSKPG
283 RNSKPGKKKNDFEQG
284 NSKPGKKKNDFEQGE
379 ARFYVYNKKKRLVNT

Function

Mitochondrial serine protease that acts as a regulator of mitochondrial lipid metabolism (PubMed:28329758). Acts by decreasing protein levels of PISD, a mitochondrial enzyme that converts phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn), thereby affecting mitochondrial lipid metabolism (PubMed:28329758). It is unclear whether it acts directly by mediating proteolysis of PISD or by mediating proteolysis of another lipid metabolism protein (PubMed:28329758). Acts as a tumor suppressor that has the ability to inhibit proliferation of multiple types of breast cancer cells: probably by promoting decreased levels of PISD, thereby affecting mitochondrial lipid metabolism (PubMed:28329758)

Protein Sequence

10 MYRLMSAVTA 20 RAAAPGGLAS 30 SCGRRGVHQR 40 AGLPPLGHGW 50 VGGLGLGLGL 60 ALGVKLAGGL 70 RGAAPAQSPA 80 APDPEASPLA 90 EPPQEQSLAP 100 WSPQTPAPPC 110 SRCFARAIES 120 SRDLLHRIKD 130 EVGAPGIVVG 140 VSVDGKEVWS 150 EGLGYADVEN 160 RVPCKPETVM 170 RIASISKSLT 180 MVALAKLWEA 190 GKLDLDIPVQ 200 HYVPEFPEKE 210 YEGEKVSVTT 220 RLLISHLSGI 230 RHYEKDIKKV 240 KEEKAYKALK 250 MMKENVAFEQ 260 EKEGKSNEKN 270 DFTKFKTEQE 280 NEAKCRNSKP 290 GKKKNDFEQG 300 ELYLREKFEN 310 SIESLRLFKN 320 DPLFFKPGSQ 330 FLYSTFGYTL 340 LAAIVERASG 350 CKYLDYMQKI 360 FHDLDMLTTV 370 QEENEPVIYN 380 RARFYVYNKK 390 KRLVNTPYVD 400 NSYKWAGGGF 410 LSTVGDLLKF 420 GNAMLYGYQV 430 GLFKNSNENL 440 LPGYLKPETM 450 VMMWTPVPNT 460 EMSWDKEGKY 470 AMAWGVVERK 480 QTYGSCRKQR 490 HYASHTGGAV 500 GASSVLLVLP 510 EELDTETINN 520 KVPPRGIIVS 530 IICNMQSVGL 540 NSTALKIALE FDKDRSD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005739 mitochondrion
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0008233 peptidase activity
Biological Process GO:0006629 lipid metabolic process
Biological Process GO:0006508 proteolysis
Biological Process GO:0019216 regulation of lipid metabolic process

Reference

[1] 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.

[2] 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.

[3] 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.

[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] 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.

[6] 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.