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Overview

Uniprot IDP49585
Protein NameCholine-phosphate cytidylyltransferase A
Gene NamePCYT1A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
16 VNARKRRKEAPGPNG
228 LQRGYTAKELNVSFI
238 NVSFINEKKYHLQER
239 VSFINEKKYHLQERV
254 DKVKKKVKDVEEKSK
261 KDVEEKSKEFVQKVE
266 KSKEFVQKVEEKSID
355 PANLSRHKAAAYDIS
8 MDAQCSAKVNARKRR

Function

Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis

Protein Sequence

10 MDAQCSAKVN 20 ARKRRKEAPG 30 PNGATEEDGV 40 PSKVQRCAVG 50 LRQPAPFSDE 60 IEVDFSKPYV 70 RVTMEEASRG 80 TPCERPVRVY 90 ADGIFDLFHS 100 GHARALMQAK 110 NLFPNTYLIV 120 GVCSDELTHN 130 FKGFTVMNEN 140 ERYDAVQHCR 150 YVDEVVRNAP 160 WTLTPEFLAE 170 HRIDFVAHDD 180 IPYSSAGSDD 190 VYKHIKEAGM 200 FAPTQRTEGI 210 STSDIITRIV 220 RDYDVYARRN 230 LQRGYTAKEL 240 NVSFINEKKY 250 HLQERVDKVK 260 KKVKDVEEKS 270 KEFVQKVEEK 280 SIDLIQKWEE 290 KSREFIGSFL 300 EMFGPEGALK 310 HMLKEGKGRM 320 LQAISPKQSP 330 SSSPTRERSP 340 SPSFRWPFSG 350 KTSPPCSPAN 360 LSRHKAAAYD ISEDEED

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0042587 glycogen granule
Cellular Component GO:0005635 nuclear envelope
Cellular Component GO:0005634 nucleus
Molecular Function GO:0005516 calmodulin binding
Molecular Function GO:0004105 choline-phosphate cytidylyltransferase activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0140678 molecular function inhibitor activity
Molecular Function GO:0031210 phosphatidylcholine binding
Molecular Function GO:0042803 protein homodimerization activity
Biological Process GO:0042100 B cell proliferation
Biological Process GO:0006657 CDP-choline pathway
Biological Process GO:0045190 isotype switching
Biological Process GO:0006656 phosphatidylcholine 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] 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] 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.

[5] 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.

[6] 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.

[7] 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.