RRAGA_HUMAN - dbPTM
RRAGA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRAGA_HUMAN
UniProt AC Q7L523
Protein Name Ras-related GTP-binding protein A {ECO:0000305}
Gene Name RRAGA {ECO:0000312|HGNC:HGNC:16963}
Organism Homo sapiens (Human).
Sequence Length 313
Subcellular Localization Cytoplasm . Nucleus . Lysosome . Predominantly cytoplasmic. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state (PubMed:8995684, PubMed:9394008). Colocalizes in vivo with adenovirus E3-14.7K mainly to the cytoplasm
Protein Description Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade. Forms heterodimeric Rag complexes with RRAGC or RRAGD and cycles between an inactive GDP-bound and an active GTP-bound form. In its active form participates in the relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. Involved in the RCC1/Ran-GTPase pathway. May play a direct role in a TNF-alpha signaling pathway leading to induction of cell death. May alternatively act as a cellular target for adenovirus E3-14.7K, an inhibitor of TNF-alpha functions, thereby affecting cell death..
Protein Sequence MPNTAMKKKVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQRDNIFRNVEVLIYVFDVESRELEKDMHYYQSCLEAILQNSPDAKIFCLVHKMDLVQEDQRDLIFKEREEDLRRLSRPLECACFRTSIWDETLYKAWSSIVYQLIPNVQQLEMNLRNFAQIIEADEVLLFERATFLVISHYQCKEQRDVHRFEKISNIIKQFKLSCSKLAASFQSMEVRNSNFAAFIDIFTSNTYVMVVMSDPSIPSAATLINIRNARKHFEKLERVDGPKHSLLMR
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
15UbiquitinationKKVLLMGKSGSGKTS
CEEEEECCCCCCCHH
37.3627667366
16PhosphorylationKVLLMGKSGSGKTSM
EEEEECCCCCCCHHH
32.2520068231
18PhosphorylationLLMGKSGSGKTSMRS
EEECCCCCCCHHHHH
44.1820068231
21PhosphorylationGKSGSGKTSMRSIIF
CCCCCCCHHHHHHHH
31.1420068231
22PhosphorylationKSGSGKTSMRSIIFA
CCCCCCHHHHHHHHH
18.7120068231
25PhosphorylationSGKTSMRSIIFANYI
CCCHHHHHHHHHHHH
16.0520068231
31PhosphorylationRSIIFANYIARDTRR
HHHHHHHHHHCCHHC
7.7920068231
36PhosphorylationANYIARDTRRLGATI
HHHHHCCHHCCCCEE
16.4924719451
42PhosphorylationDTRRLGATIDVEHSH
CHHCCCCEEECCCHH
18.8623312004
96PhosphorylationIYVFDVESRELEKDM
EEEEECCCCHHHHHH
30.79-
128UbiquitinationKIFCLVHKMDLVQED
EEEEEEECHHHHCHH
26.9929967540
142UbiquitinationDQRDLIFKEREEDLR
HHHHHHHHHHHHHHH
49.2027667366
152PhosphorylationEEDLRRLSRPLECAC
HHHHHHHCCCHHHHH
30.0029449344
215PhosphorylationRATFLVISHYQCKEQ
HCCEEEEECCCCHHH
14.5229083192
217PhosphorylationTFLVISHYQCKEQRD
CEEEEECCCCHHHCC
14.6029083192
220UbiquitinationVISHYQCKEQRDVHR
EEECCCCHHHCCHHH
41.16PubMed
230UbiquitinationRDVHRFEKISNIIKQ
CCHHHHHHHHHHHHH
49.04PubMed
232PhosphorylationVHRFEKISNIIKQFK
HHHHHHHHHHHHHHH
32.8028060719
236UbiquitinationEKISNIIKQFKLSCS
HHHHHHHHHHHHCHH
45.9833845483
239UbiquitinationSNIIKQFKLSCSKLA
HHHHHHHHHCHHHHH
36.6823000965
244UbiquitinationQFKLSCSKLAASFQS
HHHHCHHHHHHHHHC
46.6123000965
248PhosphorylationSCSKLAASFQSMEVR
CHHHHHHHHHCCHHC
20.4321406692
251PhosphorylationKLAASFQSMEVRNSN
HHHHHHHCCHHCCCC
18.2021406692
299UbiquitinationNARKHFEKLERVDGP
HHHHHHHHHHCCCCC
55.4929967540
307UbiquitinationLERVDGPKHSLLMR-
HHCCCCCCCCCCCC-
51.8933845483
307AcetylationLERVDGPKHSLLMR-
HHCCCCCCCCCCCC-
51.8921339330
309PhosphorylationRVDGPKHSLLMR---
CCCCCCCCCCCC---
29.3529514088

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
-KUbiquitinationE3 ubiquitin ligaseRNF152Q8N8N0
PMID:25936802
-KUbiquitinationE3 ubiquitin ligaseSKP2Q13309
PMID:26051179

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRAGA_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 RRAGA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RRAGC_HUMANRRAGCphysical
16189514
NOL8_HUMANNOL8physical
14660641
RRAGC_HUMANRRAGCphysical
11073942
RRAGD_HUMANRRAGDphysical
11073942
RRAGC_HUMANRRAGCphysical
21816923
RPTOR_HUMANRPTORphysical
21816923
LTOR1_HUMANLAMTOR1physical
21816923
RPTOR_HUMANRPTORphysical
18497260
IL7RA_HUMANIL7Rphysical
23151878
RRAGC_HUMANRRAGCphysical
23184942
RPTOR_HUMANRPTORphysical
23184942
RRAGC_HUMANRRAGCphysical
24337580
RPTOR_HUMANRPTORphysical
24337580
TSC2_HUMANTSC2physical
24529380
TSC1_HUMANTSC1physical
24529380
RRAGD_HUMANRRAGDphysical
26186194
RRAGC_HUMANRRAGCphysical
26186194
NPC2_HUMANNPC2physical
26186194
CTU2_HUMANCTU2physical
26186194
PPR1A_HUMANPPP1R1Aphysical
26186194
RPTOR_HUMANRPTORphysical
26186194
S38A9_HUMANSLC38A9physical
26186194
RN152_HUMANRNF152physical
25936802
RRAGC_HUMANRRAGCphysical
25936802
NPRL2_HUMANNPRL2physical
25936802
NPRL3_HUMANNPRL3physical
25936802
DEPD5_HUMANDEPDC5physical
25936802
TSC2_HUMANTSC2physical
25936802
RRAGD_HUMANRRAGDphysical
28514442
RRAGC_HUMANRRAGCphysical
28514442
S38A9_HUMANSLC38A9physical
28514442
PPR1A_HUMANPPP1R1Aphysical
28514442
RPTOR_HUMANRPTORphysical
28514442
NPC2_HUMANNPC2physical
28514442

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 RRAGA_HUMAN

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Related Literatures of Post-Translational Modification

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