Search Results

Overview

Uniprot IDQ9BZZ5
Protein NameApoptosis inhibitor 5
Gene NameAPI5
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
158 AIKFLSTKLKTLPDE
160 KFLSTKLKTLPDEVL
202 MKILSGLKSLQTVSG
398 LRLALQGKTGEALKT
404 GKTGEALKTEENKIK
448 LSWKPVQKVEIGQKR
454 QKVEIGQKRASEDTT
467 TTSGSPPKKSSAGPK

Function

Antiapoptotic factor that may have a role in protein assembly. Negatively regulates ACIN1. By binding to ACIN1, it suppresses ACIN1 cleavage from CASP3 and ACIN1-mediated DNA fragmentation. Also known to efficiently suppress E2F1-induced apoptosis. Its depletion enhances the cytotoxic action of the chemotherapeutic drugs

Protein Sequence

10 MPTVEELYRN 20 YGILADATEQ 30 VGQHKDAYQV 40 ILDGVKGGTK 50 EKRLAAQFIP 60 KFFKHFPELA 70 DSAINAQLDL 80 CEDEDVSIRR 90 QAIKELPQFA 100 TGENLPRVAD 110 ILTQLLQTDD 120 SAEFNLVNNA 130 LLSIFKMDAK 140 GTLGGLFSQI 150 LQGEDIVRER 160 AIKFLSTKLK 170 TLPDEVLTKE 180 VEELILTESK 190 KVLEDVTGEE 200 FVLFMKILSG 210 LKSLQTVSGR 220 QQLVELVAEQ 230 ADLEQTFNPS 240 DPDCVDRLLQ 250 CTRQAVPLFS 260 KNVHSTRFVT 270 YFCEQVLPNL 280 GTLTTPVEGL 290 DIQLEVLKLL 300 AEMSSFCGDM 310 EKLETNLRKL 320 FDKLLEYMPL 330 PPEEAENGEN 340 AGNEEPKLQF 350 SYVECLLYSF 360 HQLGRKLPDF 370 LTAKLNAEKL 380 KDFKIRLQYF 390 ARGLQVYIRQ 400 LRLALQGKTG 410 EALKTEENKI 420 KVVALKITNN 430 INVLIKDLFH 440 IPPSYKSTVT 450 LSWKPVQKVE 460 IGQKRASEDT 470 TSGSPPKKSS 480 AGPKRDARQI 490 YNPPSGKYSS 500 NLGNFNYEQR 510 GAFRGSRGGR 520 GWGTRGNRSR GRLY

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0016020 membrane
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005681 spliceosomal complex
Molecular Function GO:0017134 fibroblast growth factor binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0006915 apoptotic process
Biological Process GO:0043066 negative regulation of apoptotic 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] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] 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.

[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.