RAP1A_MOUSE - dbPTM
RAP1A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAP1A_MOUSE
UniProt AC P62835
Protein Name Ras-related protein Rap-1A
Gene Name Rap1a
Organism Mus musculus (Mouse).
Sequence Length 184
Subcellular Localization Cell membrane
Lipid-anchor. Cell junction . Cytoplasm. Cytoplasm, perinuclear region. Early endosome. Late endosome. Recruited from early endosome to late endosome compartment after nerve growth factor (NGF) stimulation. Colocalized with RAPGEF2 in
Protein Description Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes (By similarity). Plays a role in nerve growth factor (NGF)-induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions..
Protein Sequence MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINRKTPVEKKKPKKKSCLLL
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
5Ubiquitination---MREYKLVVLGSG
---CCEEEEEEECCC
30.01-
11PhosphorylationYKLVVLGSGGVGKSA
EEEEEECCCCCCCHH
28.3628066266
31UbiquitinationVQGIFVEKYDPTIED
EEEEEEEECCCCCCH
50.04-
32PhosphorylationQGIFVEKYDPTIEDS
EEEEEEECCCCCCHH
17.4129514104
39PhosphorylationYDPTIEDSYRKQVEV
CCCCCCHHHHHHCEE
17.6623684622
40PhosphorylationDPTIEDSYRKQVEVD
CCCCCHHHHHHCEEH
33.8627717184
48GlutathionylationRKQVEVDCQQCMLEI
HHHCEEHHHHHHHHH
3.4824333276
51GlutathionylationVEVDCQQCMLEILDT
CEEHHHHHHHHHHHH
1.0724333276
117UbiquitinationPMILVGNKCDLEDER
CEEEECCCCCCCCCE
24.17-
118S-nitrosocysteineMILVGNKCDLEDERV
EEEECCCCCCCCCEE
9.29-
118S-nitrosylationMILVGNKCDLEDERV
EEEECCCCCCCCCEE
9.2921278135
128UbiquitinationEDERVVGKEQGQNLA
CCCEECCHHHHHHHH
34.94-
128MalonylationEDERVVGKEQGQNLA
CCCEECCHHHHHHHH
34.9426320211
141GlutathionylationLARQWCNCAFLESSA
HHHHHHCHHHHHHHC
2.2824333276
149UbiquitinationAFLESSAKSKINVNE
HHHHHHCCCCCCHHH
54.98-
150PhosphorylationFLESSAKSKINVNEI
HHHHHCCCCCCHHHH
38.1821082442
151UbiquitinationLESSAKSKINVNEIF
HHHHCCCCCCHHHHH
37.28-
159PhosphorylationINVNEIFYDLVRQIN
CCHHHHHHHHHHHHH
17.6522817900
181GeranylgeranylationKKPKKKSCLLL----
CCCCCCCCCCC----
4.22-
181MethylationKKPKKKSCLLL----
CCCCCCCCCCC----
4.22-

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 RAP1A_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAP1A_MOUSE !!

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 RAP1A_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RAP1A_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAP1A_MOUSE

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Related Literatures of Post-Translational Modification

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