ATRAP_HUMAN - dbPTM
ATRAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATRAP_HUMAN
UniProt AC Q6RW13
Protein Name Type-1 angiotensin II receptor-associated protein
Gene Name AGTRAP
Organism Homo sapiens (Human).
Sequence Length 159
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Golgi apparatus membrane
Multi-pass membrane protein . Cytoplasmic vesicle membrane
Multi-pass membrane protein . Present in perinuclear vesicular membranes, Endoplasmic reticulum, Go
Protein Description Appears to be a negative regulator of type-1 angiotensin II receptor-mediated signaling by regulating receptor internalisation as well as mechanism of receptor desensitization such as phosphorylation. Induces also a decrease in cell proliferation and angiotensin II-stimulated transcriptional activity..
Protein Sequence MELPAVNLKVILLGHWLLTTWGCIVFSGSYAWANFTILALGVWAVAQRDSIDAISMFLGGLLATIFLDIVHISIFYPRVSLTDTGRFGVGMAILSLLLKPLSCCFVYHMYRERGGELLVHTGFLGSSQDRSAYQTIDSAEAPADPFAVPEGRSQDARGY
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
113MethylationVYHMYRERGGELLVH
HHHHHHHCCCEEEEE
49.79-
119 (in isoform 2)Phosphorylation-6.2425262027
120 (in isoform 2)Phosphorylation-21.9025262027
121PhosphorylationGGELLVHTGFLGSSQ
CCEEEEEECCCCCCC
23.3428060719
126PhosphorylationVHTGFLGSSQDRSAY
EEECCCCCCCCCHHH
27.2920873877
127PhosphorylationHTGFLGSSQDRSAYQ
EECCCCCCCCCHHHH
34.0121712546
131PhosphorylationLGSSQDRSAYQTIDS
CCCCCCCHHHHHCCC
39.3521945579
133PhosphorylationSSQDRSAYQTIDSAE
CCCCCHHHHHCCCCC
13.8721945579
135PhosphorylationQDRSAYQTIDSAEAP
CCCHHHHHCCCCCCC
17.6721945579
138PhosphorylationSAYQTIDSAEAPADP
HHHHHCCCCCCCCCC
24.9421945579
153PhosphorylationFAVPEGRSQDARGY-
CCCCCCCCCCCCCC-
43.1828450419

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 ATRAP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATRAP_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 ATRAP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATRAP_HUMANAGTRAPphysical
16189514
RACK1_HUMANGNB2L1physical
11733189
ATRAP_HUMANAGTRAPphysical
25416956
DDX55_HUMANDDX55physical
25416956
PPCT_HUMANPCTPphysical
25416956
SENP2_HUMANSENP2physical
25416956
NDRG4_HUMANNDRG4physical
25416956
DDA1_HUMANDDA1physical
25416956
ZFY21_HUMANZFYVE21physical
25416956
FAKD3_HUMANFASTKD3physical
25416956
MRM1_HUMANMRM1physical
25416956
ACSF2_HUMANACSF2physical
25416956
SYT16_HUMANSYT16physical
25416956
F16A2_HUMANFAM160A2physical
25416956
MCEE_HUMANMCEEphysical
25416956
LNX1_HUMANLNX1physical
25416956
TPD55_HUMANTPD52L3physical
25416956
FATE1_HUMANFATE1physical
25416956
NXP20_HUMANFAM114A1physical
25416956
MID49_HUMANMIEF2physical
25416956
TEAN2_HUMANTCEANC2physical
25416956
BPIA2_HUMANBPIFA2physical
25416956
HSC20_HUMANHSCBphysical
25416956
RMD2_HUMANRMDN2physical
25416956
ZN391_HUMANZNF391physical
25416956
PTN9_HUMANPTPN9physical
21516116
UBC9_HUMANUBE2Iphysical
21516116
ODPX_HUMANPDHXphysical
21516116
TM14B_HUMANTMEM14Bphysical
21516116
FA96A_HUMANFAM96Aphysical
21516116

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 ATRAP_HUMAN

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Related Literatures of Post-Translational Modification

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