RRAS_HUMAN - dbPTM
RRAS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRAS_HUMAN
UniProt AC P10301
Protein Name Ras-related protein R-Ras
Gene Name RRAS
Organism Homo sapiens (Human).
Sequence Length 218
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side. Inner surface of plasma membrane possibly with attachment requiring acylation of the C-terminal cysteine (By similarity with RAS).
Protein Description Regulates the organization of the actin cytoskeleton. [PubMed: 16537651]
Protein Sequence MSSGAASGTGRGRPRGGGPGPGDPPPSETHKLVVVGGGGVGKSALTIQFIQSYFVSDYDPTIEDSYTKICSVDGIPARLDILDTAGQEEFGAMREQYMRAGHGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPVVLVGNKADLESQRQVPRSEASAFGASHHVAYFEASAKLRLNVDEAFEQLVRAVRKYQEQELPPSPPSAPRKKGGGCPCVLL
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
2Phosphorylation------MSSGAASGT
------CCCCCCCCC
37.1628857561
3Phosphorylation-----MSSGAASGTG
-----CCCCCCCCCC
31.0228857561
9PhosphorylationSSGAASGTGRGRPRG
CCCCCCCCCCCCCCC
22.62-
11MethylationGAASGTGRGRPRGGG
CCCCCCCCCCCCCCC
37.47115492893
31UbiquitinationPPPSETHKLVVVGGG
CCCCCCCEEEEECCC
50.85-
52PhosphorylationLTIQFIQSYFVSDYD
HHHHHHHHHHCCCCC
18.7422210691
56PhosphorylationFIQSYFVSDYDPTIE
HHHHHHCCCCCCCCC
22.1322210691
58PhosphorylationQSYFVSDYDPTIEDS
HHHHCCCCCCCCCCC
19.13-
66PhosphorylationDPTIEDSYTKICSVD
CCCCCCCCCEEECCC
25.1110570155
67PhosphorylationPTIEDSYTKICSVDG
CCCCCCCCEEECCCC
20.2022210691
93SulfoxidationGQEEFGAMREQYMRA
CHHHHHHHHHHHHHC
5.0521406390
121UbiquitinationQSFNEVGKLFTQILR
CHHHHHHHHHHHHHC
45.67-
143UbiquitinationPVVLVGNKADLESQR
CEEEECCHHHHHHHC
37.03-
192UbiquitinationQLVRAVRKYQEQELP
HHHHHHHHHHHHCCC
44.6921906983
193PhosphorylationLVRAVRKYQEQELPP
HHHHHHHHHHHCCCC
13.5025072903
201PhosphorylationQEQELPPSPPSAPRK
HHHCCCCCCCCCCCC
47.7230266825
204PhosphorylationELPPSPPSAPRKKGG
CCCCCCCCCCCCCCC
55.0521815630
213S-palmitoylationPRKKGGGCPCVLL--
CCCCCCCCCCEEC--
2.3912890755
215MethylationKKGGGCPCVLL----
CCCCCCCCEEC----
3.81-
215GeranylgeranylationKKGGGCPCVLL----
CCCCCCCCEEC----
3.81-

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
66YPhosphorylationKinaseEPHB2P29323
PSP
66YPhosphorylationKinaseSRCP12931
PSP
66YPhosphorylationKinaseSRC64-PhosphoELM
201SPhosphorylationKinaseMAPK1P63085
GPS
201SPhosphorylationKinaseMAPK3P27361
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRAS_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 RRAS_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GNDS_HUMANRALGDSphysical
7809086
EF1A1_HUMANEEF1A1physical
18624398
RM36_HUMANMRPL36physical
18624398

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 RRAS_HUMAN

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Related Literatures of Post-Translational Modification

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