EST1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EST1_HUMAN
• UniProt AC: P23141
• Protein Name: Liver carboxylesterase 1
• Gene Name: CES1
• Organism: Homo sapiens (Human).
• Sequence Length: 567
• Subcellular Localization: Endoplasmic reticulum lumen .
• Protein Description: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. Hydrolyzes the methyl ester group of cocaine to form benzoylecgonine. Catalyzes the transesterification of cocaine to form cocaethylene. Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate..
• Protein Sequence: MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSELFTNRKENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFSTGDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGDVKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLKMKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERNFHTVPYMVGINKQEFGWLIPMQLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDLIADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLKDKEVAFWTNLFAKKAVEKPPQTEHIEL

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
28	Phosphorylation	SSPPVVDTVHGKVLG CCCCEEEECCCEEEC	11.64	33259812
79	N-linked_Glycosylation	EPWSFVKNATSYPPM CCCCCCCCCCCCCCC	43.05	12022871
83	Phosphorylation	FVKNATSYPPMCTQD CCCCCCCCCCCCCCC	13.65	-
88	Phosphorylation	TSYPPMCTQDPKAGQ CCCCCCCCCCCCHHH	29.74	-
245	Phosphorylation	NLFHRAISESGVALT HHHHHHHHHCCCEEE	25.40	25072903
247	Phosphorylation	FHRAISESGVALTSV HHHHHHHCCCEEEEE	31.60	25072903
302	Acetylation	LETTLKMKFLSLDLQ HHHHHHHHHHHCCCC	41.38	27178108
380	Phosphorylation	LDQKTAMSLLWKSYP CCHHHHHHHHHHHHH	20.18	8218228
393	Ubiquitination	YPLVCIAKELIPEAT HHHHHHHHHHCHHHH	32.89	-
402	Ubiquitination	LIPEATEKYLGGTDD HCHHHHHHHCCCCCC	41.23	-
402	Acetylation	LIPEATEKYLGGTDD HCHHHHHHHCCCCCC	41.23	20167786
403	Phosphorylation	IPEATEKYLGGTDDT CHHHHHHHCCCCCCH	12.35	-
407	Phosphorylation	TEKYLGGTDDTVKKK HHHHCCCCCCHHCHH	28.98	-
444	Phosphorylation	HRDAGAPTYMYEFQY CCCCCCCEEEEEEEC	22.01	-
493	Phosphorylation	SEEEIRLSKMVMKFW CHHHHHHHHHHHHHH	14.62	21712546
538	Acetylation	ANTQAAQKLKDKEVA CCHHHHHHHCHHHHH	53.42	30587635
558	Acetylation	FAKKAVEKPPQTEHI HHHHHCCCCCCCCCC	56.23	20167786

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

Oops, there are no upstream regulatory protein records of EST1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EST1_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 EST1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EST1_HUMAN	CES1	physical	12679808

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
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Structure-function analysis of human triacylglycerol hydrolase bysite-directed mutagenesis: identification of the catalytic triad and aglycosylation site.";
Alam M., Vance D.E., Lehner R.;
Biochemistry 41:6679-6687(2002).
Cited for: PROTEIN SEQUENCE OF 19-28, ACTIVE SITES, GLYCOSYLATION AT ASN-79, ANDMUTAGENESIS OF ASN-79; SER-221; GLU-354; HIS-468 AND 564-HIS--LEU-567.
PubMed: 12022871