RAP1B_MOUSE - dbPTM
RAP1B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAP1B_MOUSE
UniProt AC Q99JI6
Protein Name Ras-related protein Rap-1b
Gene Name Rap1b
Organism Mus musculus (Mouse).
Sequence Length 184
Subcellular Localization Cell membrane. Cytoplasm, cytosol. Cell junction. May shuttle between plasma membrane and cytosol. Presence of KRIT1 and CDH5 is required for its localization to the cell junction (By similarity)..
Protein Description GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function (By similarity)..
Protein Sequence MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKARKKSSCQLL
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
39ADP-ribosylationYDPTIEDSYRKQVEV
CCCCCCHHHHHHHEE
17.66-
39PhosphorylationYDPTIEDSYRKQVEV
CCCCCCHHHHHHHEE
17.6630635358
40PhosphorylationDPTIEDSYRKQVEVD
CCCCCHHHHHHHEEC
33.8627717184
51GlutathionylationVEVDAQQCMLEILDT
HEECHHHHHHHHHHH
1.9224333276
106PhosphorylationQILRVKDTDDVPMIL
HHHCCCCCCCCCEEE
28.5120469934
117UbiquitinationPMILVGNKCDLEDER
CEEEECCCCCCCCCE
24.17-
118S-nitrosocysteineMILVGNKCDLEDERV
EEEECCCCCCCCCEE
9.29-
118S-nitrosylationMILVGNKCDLEDERV
EEEECCCCCCCCCEE
9.2921278135
118GlutathionylationMILVGNKCDLEDERV
EEEECCCCCCCCCEE
9.2924333276
128UbiquitinationEDERVVGKEQGQNLA
CCCEECCHHHHHHHH
34.94-
128MalonylationEDERVVGKEQGQNLA
CCCEECCHHHHHHHH
34.9426320211
141S-nitrosylationLARQWNNCAFLESSA
HHHHHHCCHHHHHHC
2.2724895380
141S-nitrosocysteineLARQWNNCAFLESSA
HHHHHHCCHHHHHHC
2.27-
149UbiquitinationAFLESSAKSKINVNE
HHHHHHCCCCCCHHH
54.98-
150PhosphorylationFLESSAKSKINVNEI
HHHHHCCCCCCHHHH
38.1821082442
151UbiquitinationLESSAKSKINVNEIF
HHHHCCCCCCHHHHH
37.28-
159PhosphorylationINVNEIFYDLVRQIN
CCHHHHHHHHHHHHC
17.6522817900
174MalonylationRKTPVPGKARKKSSC
CCCCCCCCCCCCCCC
38.6626320211
179PhosphorylationPGKARKKSSCQLL--
CCCCCCCCCCCCC--
39.1124759943
180PhosphorylationGKARKKSSCQLL---
CCCCCCCCCCCC---
18.1124759943
181MethylationKARKKSSCQLL----
CCCCCCCCCCC----
4.22-
181GeranylgeranylationKARKKSSCQLL----
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
179SPhosphorylationKinasePKA-Uniprot
-KUbiquitinationE3 ubiquitin ligaseSmurf2A2A5Z6
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAP1B_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 RAP1B_MOUSE !!

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

Oops, there are no PPI records of RAP1B_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAP1B_MOUSE

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Related Literatures of Post-Translational Modification

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