dbPTM

CHKB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CHKB_HUMAN
UniProt AC	Q9Y259
Protein Name	Choline/ethanolamine kinase
Gene Name	CHKB
Organism	Homo sapiens (Human).
Sequence Length	395
Subcellular Localization
Protein Description	Has a key role in phospholipid biosynthesis. Catalyzes the first step in phosphatidylethanolamine biosynthesis. Phosphorylates ethanolamine, and can also act on choline (in vitro). Has higher activity with ethanolamine. May not significantly contribute to in vivo phosphatidylcholine biosynthesis..
Protein Sequence	MAAEATAVAGSGAVGGCLAKDGLQQSKCPDTTPKRRRASSLSRDAERRAYQWCREYLGGAWRRVQPEELRVYPVSGGLSNLLFRCSLPDHLPSVGEEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYIPSRPLKTQELREPVLSAAIATKMAQFHGMEMPFTKEPHWLFGTMERYLKQIQDLPPTGLPEMNLLEMYSLKDEMGNLRKLLESTPSPVVFCHNDIQEGNILLLSEPENADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTHEEWPFYKARPTDYPTQEQQLHFIRHYLAEAKKGETLSQEEQRKLEEDLLVEVSRYALASHFFWGLWSILQASMSTIEFGYLDYAQSRFQFYFQQKGQLTSVHSSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAEATAVA ------CCCCCEEHH	17.63	22223895
39	Phosphorylation	TPKRRRASSLSRDAE CCHHHHHHHCCHHHH	29.96	26055452
40	Phosphorylation	PKRRRASSLSRDAER CHHHHHHHCCHHHHH	29.40	26055452
42	Phosphorylation	RRRASSLSRDAERRA HHHHHHCCHHHHHHH	30.02	17924679
56	Phosphorylation	AYQWCREYLGGAWRR HHHHHHHHCCCCHHH	7.41	22985185
72	Phosphorylation	QPEELRVYPVSGGLS CHHHEEEEECCCCHH	7.47	-
75	Phosphorylation	ELRVYPVSGGLSNLL HEEEEECCCCHHHHH	23.73	-
79	Phosphorylation	YPVSGGLSNLLFRCS EECCCCHHHHHHHCC	28.80	-
97 (in isoform 2)	Phosphorylation	-	43.67	28450419
100 (in isoform 2)	Phosphorylation	-	48.51	28450419
103 (in isoform 2)	Phosphorylation	-	4.24	28450419
106 (in isoform 2)	Phosphorylation	-	9.70	28450419
217	Phosphorylation	MNLLEMYSLKDEMGN CCHHHHHCCCCCHHH	27.86	24719451
321	Ubiquitination	RHYLAEAKKGETLSQ HHHHHHHHCCCCCCH	53.46	-
327	Phosphorylation	AKKGETLSQEEQRKL HHCCCCCCHHHHHHH	42.86	28348404
381	Phosphorylation	AQSRFQFYFQQKGQL HHHHEEEEEEECCCE	6.95	22461510
394	Phosphorylation	QLTSVHSSS------ CEEECCCCC------	25.78	22461510

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
39	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
40	S	Phosphorylation	Kinase	PRKACA	P17612	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CHKB_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of CHKB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CHKB_HUMAN !!

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

Regulatory Network of CHKB_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-42, AND MASSSPECTROMETRY.	17924679 [Abstract]