RRAGB_HUMAN - dbPTM
RRAGB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRAGB_HUMAN
UniProt AC Q5VZM2
Protein Name Ras-related GTP-binding protein B {ECO:0000305}
Gene Name RRAGB {ECO:0000312|HGNC:HGNC:19901}
Organism Homo sapiens (Human).
Sequence Length 374
Subcellular Localization Cytoplasm . Lysosome .
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..
Protein Sequence MEESDSEKTTEKENLGPRMDPPLGEPEGSLGWVLPNTAMKKKVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATILDRIHSLQINSSLSTYSLVDSVGNTKTFDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQRDNIFRNVEVLIYVFDVESRELEKDMHYYQSCLEAILQNSPDAKIFCLVHKMDLVQEDQRDLIFKEREEDLRRLSRPLECSCFRTSIWDETLYKAWSSIVYQLIPNVQQLEMNLRNFAEIIEADEVLLFERATFLVISHYQCKEQRDAHRFEKISNIIKQFKLSCSKLAASFQSMEVRNSNFAAFIDIFTSNTYVMVVMSDPSIPSAATLINIRNARKHFEKLERVDGPKQCLLMR
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
1Acetylation-------MEESDSEK
-------CCCCCCCC
13.3922814378
4Phosphorylation----MEESDSEKTTE
----CCCCCCCCCCC
32.8823401153
6Phosphorylation--MEESDSEKTTEKE
--CCCCCCCCCCCCC
50.7229255136
9PhosphorylationEESDSEKTTEKENLG
CCCCCCCCCCCCCCC
35.8129083192
10PhosphorylationESDSEKTTEKENLGP
CCCCCCCCCCCCCCC
57.0129083192
10UbiquitinationESDSEKTTEKENLGP
CCCCCCCCCCCCCCC
57.0127667366
29PhosphorylationPLGEPEGSLGWVLPN
CCCCCCCCCCCCCCC
23.2727251275
48UbiquitinationKKVLLMGKSGSGKTS
CEEEEECCCCCCCHH
37.3627667366
49PhosphorylationKVLLMGKSGSGKTSM
EEEEECCCCCCCHHH
32.2520068231
51PhosphorylationLLMGKSGSGKTSMRS
EEECCCCCCCHHHHH
44.1820068231
54PhosphorylationGKSGSGKTSMRSIIF
CCCCCCCHHHHHHHH
31.1420068231
55PhosphorylationKSGSGKTSMRSIIFA
CCCCCCHHHHHHHHH
18.7120068231
58PhosphorylationSGKTSMRSIIFANYI
CCCHHHHHHHHHHHH
16.0520068231
64PhosphorylationRSIIFANYIARDTRR
HHHHHHHHHHHHHHH
7.7920068231
69PhosphorylationANYIARDTRRLGATI
HHHHHHHHHHHCCHH
16.4924719451
137UbiquitinationFMENYFTSQRDNIFR
HHHHHCHHCCCCHHC
17.2027667366
157PhosphorylationIYVFDVESRELEKDM
EEEEECCCCHHHHHH
30.79-
161UbiquitinationDVESRELEKDMHYYQ
ECCCCHHHHHHHHHH
42.1129967540
165UbiquitinationRELEKDMHYYQSCLE
CHHHHHHHHHHHHHH
28.4327667366
175UbiquitinationQSCLEAILQNSPDAK
HHHHHHHHHCCCCCE
5.2033845483
189UbiquitinationKIFCLVHKMDLVQED
EEEEEEECHHHHCHH
26.9929967540
203UbiquitinationDQRDLIFKEREEDLR
HHHHHHHHHHHHHHH
49.2033845483
225UbiquitinationCSCFRTSIWDETLYK
CCHHCCCCCCHHHHH
5.4821890473
234UbiquitinationDETLYKAWSSIVYQL
CHHHHHHHHHHHHHH
6.6123000965
239UbiquitinationKAWSSIVYQLIPNVQ
HHHHHHHHHHCCCHH
8.9123000965
253UbiquitinationQQLEMNLRNFAEIIE
HHHHHHHHHHHHHHH
31.0821890473
262UbiquitinationFAEIIEADEVLLFER
HHHHHHHHHEEHHHH
33.4723000965
263 (in isoform 2)Ubiquitination-41.9621890473
263UbiquitinationAEIIEADEVLLFERA
HHHHHHHHEEHHHHC
41.9621890473
267UbiquitinationEADEVLLFERATFLV
HHHHEEHHHHCCEEE
5.3723000965
272UbiquitinationLLFERATFLVISHYQ
EHHHHCCEEEEECCC
5.1123000965
276PhosphorylationRATFLVISHYQCKEQ
HCCEEEEECCCCHHH
14.5229083192
277UbiquitinationATFLVISHYQCKEQR
CCEEEEECCCCHHHH
12.9323000965
278PhosphorylationTFLVISHYQCKEQRD
CEEEEECCCCHHHHH
14.6029083192
291 (in isoform 1)Ubiquitination-49.0421890473
291UbiquitinationRDAHRFEKISNIIKQ
HHHHHHHHHHHHHHH
49.0421890473
293PhosphorylationAHRFEKISNIIKQFK
HHHHHHHHHHHHHHH
32.8028060719
297UbiquitinationEKISNIIKQFKLSCS
HHHHHHHHHHHHHHH
45.98-
297AcetylationEKISNIIKQFKLSCS
HHHHHHHHHHHHHHH
45.9819824289
300AcetylationSNIIKQFKLSCSKLA
HHHHHHHHHHHHHHH
36.6819824297
300UbiquitinationSNIIKQFKLSCSKLA
HHHHHHHHHHHHHHH
36.6823000965
305UbiquitinationQFKLSCSKLAASFQS
HHHHHHHHHHHHHHC
46.6123000965
305AcetylationQFKLSCSKLAASFQS
HHHHHHHHHHHHHHC
46.6119824305
309PhosphorylationSCSKLAASFQSMEVR
HHHHHHHHHHCCCCC
20.4321406692
312PhosphorylationKLAASFQSMEVRNSN
HHHHHHHCCCCCCCC
18.2021406692
360UbiquitinationNARKHFEKLERVDGP
HHHHHHHHHHCCCCC
55.49-
360AcetylationNARKHFEKLERVDGP
HHHHHHHHHHCCCCC
55.4925953088

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 RRAGB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRAGB_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 RRAGB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RRAGD_HUMANRRAGDphysical
11073942
RRAGC_HUMANRRAGCphysical
11073942
RPTOR_HUMANRPTORphysical
18497260
A4_HUMANAPPphysical
21832049
KCRB_HUMANCKBphysical
22863883
XPO2_HUMANCSE1Lphysical
22863883
GSHB_HUMANGSSphysical
22863883
RASL1_HUMANRASAL1physical
22863883
1433B_HUMANYWHABphysical
22863883
LTOR5_HUMANLAMTOR5physical
22980980
LTOR4_HUMANLAMTOR4physical
22980980
RRAGC_HUMANRRAGCphysical
24337580
RPTOR_HUMANRPTORphysical
24337580
MTOR_HUMANMTORphysical
24337580
RRAGD_HUMANRRAGDphysical
24337580
LTOR3_HUMANLAMTOR3physical
20381137
LTOR2_HUMANLAMTOR2physical
20381137
LTOR1_HUMANLAMTOR1physical
20381137
S38A9_HUMANSLC38A9physical
25567906
LTOR1_HUMANLAMTOR1physical
25567906
LTOR2_HUMANLAMTOR2physical
25567906
RRAGC_HUMANRRAGCphysical
25567906

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

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Related Literatures of Post-Translational Modification

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