ENTP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ENTP1_HUMAN
• UniProt AC: P49961
• Protein Name: Ectonucleoside triphosphate diphosphohydrolase 1
• Gene Name: ENTPD1
• Organism: Homo sapiens (Human).
• Sequence Length: 510
• Subcellular Localization: Membrane ; Multi-pass membrane protein .
• Protein Description: In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well..
• Protein Sequence: MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWITINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFRLYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTPCTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAFSAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYILSLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFLMVLFSLVLFTVAIIGLLIFHKPSYFWKDMV

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
4 (in isoform 2)	Phosphorylation	-	24.33	-
4 (in isoform 3)	Phosphorylation	-	24.33	-
13	S-palmitoylation	ESNVKTFCSKNILAI HHHHHHHHHHHHHHH	7.38	10636909
49	Phosphorylation	ALPENVKYGIVLDAG CCCCCCCEEEEEECC	14.06	17053785
65	Phosphorylation	SHTSLYIYKWPAEKE CCCEEEEEEECCCCC	8.08	17053785
73	N-linked_Glycosylation	KWPAEKENDTGVVHQ EECCCCCCCCCCEEE	64.31	19159218
227	N-linked_Glycosylation	QVTFVPQNQTIESPD EEEEECCCCCCCCCC	34.59	UniProtKB CARBOHYD
284 (in isoform 3)	Phosphorylation	-	22.92	27732954
292	N-linked_Glycosylation	PGYKKVVNVSDLYKT CCCCEEEEHHHHCCC	30.48	19159218
334	N-linked_Glycosylation	QSILELFNTSYCPYS HHHHHHHCCCCCCCC	40.51	UniProtKB CARBOHYD
371	N-linked_Glycosylation	YFVMKFLNLTSEKVS HHHHHHHCCCCCCCC	44.39	UniProtKB CARBOHYD
457	N-linked_Glycosylation	WTLGYMLNLTNMIPA HHHHHHHHCCCCCCC	28.43	UniProtKB CARBOHYD

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

Oops, there are no upstream regulatory protein records of ENTP1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ENTP1_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 ENTP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RANB9_HUMAN	RANBP9	physical	16478441

Drug and Disease Associations

• Kegg Disease
• H00627: Premature ovarian failure
• OMIM Disease
• 615683: Spastic paraplegia 64, autosomal recessive (SPG64)
• 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

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-73 AND ASN-292, AND MASSSPECTROMETRY.
PubMed: 19159218

Phosphorylation

"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-49 AND TYR-65, AND MASSSPECTROMETRY.
PubMed: 17053785