Search Results

Overview

Uniprot IDQ8TCT9
Protein NameSignal peptide peptidase
Gene NameHM13
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
361 PAAVTESKEGTEASA
370 GTEASASKGLEKKEK
61 SVRCARGKNASDMPE

Function

Catalyzes intramembrane proteolysis of signal peptides that have been removed from precursors of secretory and membrane proteins, resulting in the release of the fragment from the ER membrane into the cytoplasm (PubMed:12077416, PubMed:15716490, PubMed:17517891). Required to generate lymphocyte cell surface (HLA-E) epitopes derived from MHC class I signal peptides (PubMed:11714810). May be necessary for the removal of the signal peptide that remains attached to the hepatitis C virus core protein after the initial proteolytic processing of the polyprotein (PubMed:12145199). Involved in the intramembrane cleavage of the integral membrane protein PSEN1 (PubMed:11714810, PubMed:12077416, PubMed:14741365). Cleaves the integral membrane protein XBP1 isoform 1 in a DERL1/RNF139-dependent manner (PubMed:25239945). May play a role in graft rejection (By similarity)

Protein Sequence

10 MDSALSDPHN 20 GSAEAGGPTN 30 STTRPPSTPE 40 GIALAYGSLL 50 LMALLPIFFG 60 ALRSVRCARG 70 KNASDMPETI 80 TSRDAARFPI 90 IASCTLLGLY 100 LFFKIFSQEY 110 INLLLSMYFF 120 VLGILALSHT 130 ISPFMNKFFP 140 ASFPNRQYQL 150 LFTQGSGENK 160 EEIINYEFDT 170 KDLVCLGLSS 180 IVGVWYLLRK 190 HWIANNLFGL 200 AFSLNGVELL 210 HLNNVSTGCI 220 LLGGLFIYDV 230 FWVFGTNVMV 240 TVAKSFEAPI 250 KLVFPQDLLE 260 KGLEANNFAM 270 LGLGDVVIPG 280 IFIALLLRFD 290 ISLKKNTHTY 300 FYTSFAAYIF 310 GLGLTIFIMH 320 IFKHAQPALL 330 YLVPACIGFP 340 VLVALAKGEV 350 TEMFSYEESN 360 PKDPAAVTES 370 KEGTEASASK GLEKKEK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0009986 cell surface
Cellular Component GO:0098554 cytoplasmic side of endoplasmic reticulum membrane
Cellular Component GO:0036513 Derlin-1 retrotranslocation complex
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0098553 lumenal side of endoplasmic reticulum membrane
Cellular Component GO:0016020 membrane
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0005791 rough endoplasmic reticulum
Molecular Function GO:0042500 aspartic endopeptidase activity, intramembrane cleaving
Molecular Function GO:0008233 peptidase activity
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0031625 ubiquitin protein ligase binding
Biological Process GO:0034599 cellular response to oxidative stress
Biological Process GO:0033619 membrane protein proteolysis
Biological Process GO:1904211 membrane protein proteolysis involved in retrograde protein transport, ER to cytosol
Biological Process GO:0006465 signal peptide processing

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] 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.

[3] 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.

[4] 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.