dbPTM

ENTP5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ENTP5_HUMAN
UniProt AC	O75356
Protein Name	Ectonucleoside triphosphate diphosphohydrolase 5
Gene Name	ENTPD5
Organism	Homo sapiens (Human).
Sequence Length	428
Subcellular Localization	Endoplasmic reticulum. Secreted .
Protein Description	Uridine diphosphatase (UDPase) that promotes protein N-glycosylation and ATP level regulation. UDP hydrolysis promotes protein N-glycosylation and folding in the endoplasmic reticulum, as well as elevated ATP consumption in the cytosol via an ATP hydrolysis cycle. Together with CMPK1 and AK1, constitutes an ATP hydrolysis cycle that converts ATP to AMP and results in a compensatory increase in aerobic glycolysis. The nucleotide hydrolyzing preference is GDP > IDP > UDP, but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. Plays a key role in the AKT1-PTEN signaling pathway by promoting glycolysis in proliferating cells in response to phosphoinositide 3-kinase (PI3K) signaling..
Protein Sequence	MATSWGTVFFMLVVSCVCSAVSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGTRIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGVKYQYGGNQEGEVGFEPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAREVCDNLENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHLLQSLGISH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
98	Acetylation	SAFVDQPKQGAETVQ HHHCCCCCCCHHHHH	56.59	19814715
227	Phosphorylation	TPRGYLTSFEMFNST CCCCEEEEHHHCCCC	19.33	-
232	N-linked_Glycosylation	LTSFEMFNSTYKLYT EEEHHHCCCCEEEEC	31.93	16335952
234	Phosphorylation	SFEMFNSTYKLYTHS EHHHCCCCEEEECCC	26.27	-
239	Phosphorylation	NSTYKLYTHSYLGFG CCCEEEECCCHHCCC	18.12	22210691
263	Phosphorylation	GALETEGTDGHTFRS HCCCCCCCCCCCCCC	32.35	22210691
267	Phosphorylation	TEGTDGHTFRSACLP CCCCCCCCCCCCHHC	26.69	22210691
330	Phosphorylation	RGSFYAFSYYYDRAV CCCEEEEEEEECCCC	12.21	24275569
331	Phosphorylation	GSFYAFSYYYDRAVD CCEEEEEEEECCCCC	10.29	24275569
332	Phosphorylation	SFYAFSYYYDRAVDT CEEEEEEEECCCCCC	9.55	24275569
333	Phosphorylation	FYAFSYYYDRAVDTD EEEEEEEECCCCCCC	7.24	24275569
339	Phosphorylation	YYDRAVDTDMIDYEK EECCCCCCCEECCCC	22.37	24275569
368	N-linked_Glycosylation	EVCDNLENFTSGSPF HHHHCHHHCCCCCCE	48.97	UniProtKB CARBOHYD

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
Oops, there are no upstream regulatory protein records of ENTP5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ENTP5_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 ENTP5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
MXI1_HUMAN	MXI1	physical	25416956

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.

Regulatory Network of ENTP5_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-232, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-232, AND MASSSPECTROMETRY.	16335952 [Abstract]