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Overview

Uniprot ID	Q99447
Protein Name	Ethanolamine-phosphate cytidylyltransferase
Gene Name	PCYT2
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
158	GRMLLVTKAHHSSQE
179	EYADSFGKCPGGRNP
366	RNQKKEAKELAFLEA
66	DEEIAKHKGPPVFTQ
78	FTQEERYKMVQAIKW

Function

Ethanolamine-phosphate cytidylyltransferase that catalyzes the second step in the synthesis of phosphatidylethanolamine (PE) from ethanolamine via the CDP-ethanolamine pathway (PubMed:31637422, PubMed:9083101). Phosphatidylethanolamine is a dominant inner-leaflet phospholipid in cell membranes, where it plays a role in membrane function by structurally stabilizing membrane-anchored proteins, and participates in important cellular processes such as cell division, cell fusion, blood coagulation, and apoptosis (PubMed:9083101)

Protein Sequence

10 MIRNGRGAAG 20 GAEQPGPGGR 30 RAVRVWCDGC 40 YDMVHYGHSN 50 QLRQARAMGD 60 YLIVGVHTDE 70 EIAKHKGPPV 80 FTQEERYKMV 90 QAIKWVDEVV 100 PAAPYVTTLE 110 TLDKYNCDFC 120 VHGNDITLTV 130 DGRDTYEEVK 140 QAGRYRECKR 150 TQGVSTTDLV 160 GRMLLVTKAH 170 HSSQEMSSEY 180 REYADSFGKC 190 PGGRNPWTGV 200 SQFLQTSQKI 210 IQFASGKEPQ 220 PGETVIYVAG 230 AFDLFHIGHV 240 DFLEKVHRLA 250 ERPYIIAGLH 260 FDQEVNHYKG 270 KNYPIMNLHE 280 RTLSVLACRY 290 VSEVVIGAPY 300 AVTAELLSHF 310 KVDLVCHGKT 320 EIIPDRDGSD 330 PYQEPKRRGI 340 FRQIDSGSNL 350 TTDLIVQRII 360 TNRLEYEARN 370 QKKEAKELAF 380 LEAARQQAAQ PLGERDGDF

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005789	endoplasmic reticulum membrane
Molecular Function	GO:0004306	ethanolamine-phosphate cytidylyltransferase activity
Biological Process	GO:0006646	phosphatidylethanolamine biosynthetic process
Biological Process	GO:0008654	phospholipid biosynthetic 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] 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.