CEPT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CEPT1_HUMAN
• UniProt AC: Q9Y6K0
• Protein Name: Choline/ethanolaminephosphotransferase 1
• Gene Name: CEPT1
• Organism: Homo sapiens (Human).
• Sequence Length: 416
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein . Nucleus membrane ; Multi-pass membrane protein .
• Protein Description: Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP-ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity..
• Protein Sequence: MSGHRSTRKRCGDSHPESPVGFGHMSTTGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAGRSLLEPLMQGYWEWLVRRVPSWIAPNLITIIGLSINICTTILLVFYCPTATEQAPLWAYIACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSMIPVLNIQMKIFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLAAMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLHIHVFRIKVSTAHSNHH

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	S-palmitoylation	HRSTRKRCGDSHPES CCCCCCCCCCCCCCC	8.78	21044946
14	Phosphorylation	TRKRCGDSHPESPVG CCCCCCCCCCCCCCC	26.65	23927012
18	Phosphorylation	CGDSHPESPVGFGHM CCCCCCCCCCCCCCC	29.36	20201521
26	Phosphorylation	PVGFGHMSTTGCVLN CCCCCCCCCCCHHHH	19.69	28270605
27	Phosphorylation	VGFGHMSTTGCVLNK CCCCCCCCCCHHHHH	21.45	20068231
28	Phosphorylation	GFGHMSTTGCVLNKL CCCCCCCCCHHHHHH	22.68	19845377
30	S-palmitoylation	GHMSTTGCVLNKLFQ CCCCCCCHHHHHHHC	2.71	21044946
40	Phosphorylation	NKLFQLPTPPLSRHQ HHHHCCCCCCCCHHH	46.24	25159151
44	Phosphorylation	QLPTPPLSRHQLKRL CCCCCCCCHHHHHHH	33.23	23927012
56	Phosphorylation	KRLEEHRYQSAGRSL HHHHHHHHHHHCHHH	14.55	24719451
62	Phosphorylation	RYQSAGRSLLEPLMQ HHHHHCHHHHHHHHH	36.07	24719451
144	N-linked_Glycosylation	GKQARRTNSSSPLGE CCHHCCCCCCCCHHH	37.78	UniProtKB CARBOHYD

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CEPT1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CEPT1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CEPT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RBM6_HUMAN	RBM6	physical	28514442
AFAD_HUMAN	MLLT4	physical	28514442
ARFG2_HUMAN	ARFGAP2	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00122: Choline

Related Literatures of Post-Translational Modification

Phosphorylation

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND THR-40, AND MASSSPECTROMETRY.
PubMed: 18691976