Search Results

Overview

Uniprot IDP22234
Protein NameBifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
Gene NamePAICS
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
11 AEVLNIGKKLYEGKT
110 IATGSFLKRNPGVKE
19 KLYEGKTKEVYELLD
228 DRSQQKDKQSYRDLK
235 KQSYRDLKEVTPEGL
246 PEGLQMVKKNFEWVA
247 EGLQMVKKNFEWVAE
283 SDLGHCEKIKKACGN
286 GHCEKIKKACGNFGI
304 LRVTSAHKGPDETLR
36 GKVLLQSKDQITAGN
53 RKNHLEGKAAISNKI

Function

Bifunctional phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazole succinocarboxamide synthetase catalyzing two reactions of the de novo purine biosynthetic pathway

Protein Sequence

10 MATAEVLNIG 20 KKLYEGKTKE 30 VYELLDSPGK 40 VLLQSKDQIT 50 AGNAARKNHL 60 EGKAAISNKI 70 TSCIFQLLQE 80 AGIKTAFTRK 90 CGETAFIAPQ 100 CEMIPIEWVC 110 RRIATGSFLK 120 RNPGVKEGYK 130 FYPPKVELFF 140 KDDANNDPQW 150 SEEQLIAAKF 160 CFAGLLIGQT 170 EVDIMSHATQ 180 AIFEILEKSW 190 LPQNCTLVDM 200 KIEFGVDVTT 210 KEIVLADVID 220 NDSWRLWPSG 230 DRSQQKDKQS 240 YRDLKEVTPE 250 GLQMVKKNFE 260 WVAERVELLL 270 KSESQCRVVV 280 LMGSTSDLGH 290 CEKIKKACGN 300 FGIPCELRVT 310 SAHKGPDETL 320 RIKAEYEGDG 330 IPTVFVAVAG 340 RSNGLGPVMS 350 GNTAYPVISC 360 PPLTPDWGVQ 370 DVWSSLRLPS 380 GLGCSTVLSP 390 EGSAQFAAQI 400 FGLSNHLVWS 410 KLRASILNTW 420 ISLKQADKKI RECNL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0016020 membrane
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0004638 phosphoribosylaminoimidazole carboxylase activity
Molecular Function GO:0004639 phosphoribosylaminoimidazolesuccinocarboxamide synthase activity
Biological Process GO:0044208 'de novo' AMP biosynthetic process
Biological Process GO:0006189 'de novo' IMP biosynthetic process
Biological Process GO:0097294 'de novo' XMP biosynthetic process
Biological Process GO:0006177 GMP biosynthetic process
Biological Process GO:0009113 purine nucleobase biosynthetic process

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] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[4] 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.

[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] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[7] 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.

[8] 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.