ENTP7_HUMAN - dbPTM
ENTP7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENTP7_HUMAN
UniProt AC Q9NQZ7
Protein Name Ectonucleoside triphosphate diphosphohydrolase 7
Gene Name ENTPD7
Organism Homo sapiens (Human).
Sequence Length 604
Subcellular Localization Cytoplasmic vesicle membrane
Multi-pass membrane protein . Localizes to intracellular vesicular compartments.
Protein Description Preferentially hydrolyzes nucleoside 5'-triphosphates. The order of activity with respect to possible substrates is UTP > GTP > CTP..
Protein Sequence MARISFSYLCPASWYFTVPTVSPFLRQRVAFLGLFFISCLLLLMLIIDFRHWSASLPRDRQYERYLARVGELEATDTEDPNLNYGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDIKQMRDRNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPVKKHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDESDAEATQELAAGRRRTVGILDMGGASLQIAYEVPTSTSVLPAKQEEAAKILLAEFNLGCDVQHTEHVYRVYVTTFLGFGGNFARQRYEDLVLNETLNKNRLLGQKTGLSPDNPFLDPCLPVGLTDVVERNSQVLHVRGRGDWVSCGAMLSPLLARSNTSQASLNGIYQSPIDFNNSEFYGFSEFFYCTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQRFKNGLFSSHADEHRLKYQCFKSAWMYQVLHEGFHFPYDYPNLRTAQLVYDREVQWTLGAILYKTRFLPLRDLRQEGVRQAHGSWFRLSFVYNHYLFFACILVVLLAIFLYLLRLRRIHHRQTRASAPLDLLWLEEVVPMMGVQVGP
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 Orthologous
Protein Cluster
5Phosphorylation---MARISFSYLCPA
---CCCEEEEEECCC
11.5525002506
7Phosphorylation-MARISFSYLCPASW
-CCCEEEEEECCCEE
15.4825002506
8PhosphorylationMARISFSYLCPASWY
CCCEEEEEECCCEEE
15.4325002506
13PhosphorylationFSYLCPASWYFTVPT
EEEECCCEEEEECCC
13.8825002506
15PhosphorylationYLCPASWYFTVPTVS
EECCCEEEEECCCCC
6.2025002506
17PhosphorylationCPASWYFTVPTVSPF
CCCEEEEECCCCCHH
15.1825002506
20PhosphorylationSWYFTVPTVSPFLRQ
EEEEECCCCCHHHHH
29.3125002506
22PhosphorylationYFTVPTVSPFLRQRV
EEECCCCCHHHHHHH
16.6525002506
55PhosphorylationDFRHWSASLPRDRQY
HHHHHHHCCCCHHHH
33.1324719451
128UbiquitinationRNSQPVVKKIKPGIS
CCCCCCHHHCCCCCC
49.3627667366
140O-linked_GlycosylationGISAMADTPEHASDY
CCCCCCCCHHHHHHH
22.4930379171
167PhosphorylationPVKKHKETPLYILCT
CCCCCCCCCEEEEEC
24.32-
170PhosphorylationKHKETPLYILCTAGM
CCCCCCEEEEECCCC
7.95-
174PhosphorylationTPLYILCTAGMRLLP
CCEEEEECCCCCCCH
23.85-
253PhosphorylationLAAGRRRTVGILDMG
HHHHCCCEEEEEECC
22.6724425749
274PhosphorylationAYEVPTSTSVLPAKQ
EEECCCCCCCCCCCH
25.9024425749
275O-linked_GlycosylationYEVPTSTSVLPAKQE
EECCCCCCCCCCCHH
22.79OGP
330N-linked_GlycosylationRYEDLVLNETLNKNR
HHHHHHHHHHCCCCC
32.50UniProtKB CARBOHYD
342UbiquitinationKNRLLGQKTGLSPDN
CCCCCCCCCCCCCCC
42.64-

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 ENTP7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ENTP7_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 ENTP7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPP2B_HUMANSPPL2Bphysical
28514442
UBP32_HUMANUSP32physical
28514442
AT2B2_HUMANATP2B2physical
28514442
LAP4B_HUMANLAPTM4Bphysical
28514442
JMJD8_HUMANJMJD8physical
28514442
NMU_HUMANNMUphysical
28514442
GLP3L_HUMANGOLPH3Lphysical
28514442
NFIP1_HUMANNDFIP1physical
28514442
DGLB_HUMANDAGLBphysical
28514442
PGK2_HUMANPGK2physical
28514442
C43BP_HUMANCOL4A3BPphysical
28514442
GOLP3_HUMANGOLPH3physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ENTP7_HUMAN

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Related Literatures of Post-Translational Modification

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