dbPTM

RRAGC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RRAGC_HUMAN
UniProt AC	Q9HB90
Protein Name	Ras-related GTP-binding protein C
Gene Name	RRAGC {ECO:0000312\|HGNC:HGNC:19902}
Organism	Homo sapiens (Human).
Sequence Length	399
Subcellular Localization	Cytoplasm . Nucleus . Lysosome . Predominantly cytoplasmic. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state of associated RRAGA (PubMed:11073942).
Protein Description	Guanine nucleotide-binding protein forming heterodimeric Rag complexes required for the amino acid-induced relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. This is a crucial step in the activation of the TOR signaling cascade by amino acids..
Protein Sequence	MSLQYGAEETPLAGSYGAADSFPKDFGYGVEEEEEEAAAAGGGVGAGAGGGCGPGGADSSKPRILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKIYKDDISNSSFVNFQIWDFPGQMDFFDPTFDYEMIFRGTGALIYVIDAQDDYMEALTRLHITVSKAYKVNPDMNFEVFIHKVDGLSDDHKIETQRDIHQRANDDLADAGLEKLHLSFYLTSIYDHSIFEAFSKVVQKLIPQLPTLENLLNIFISNSGIEKAFLFDVVSKIYIATDSSPVDMQSYELCCDMIDVVIDVSCIYGLKEDGSGSAYDKESMAIIKLNNTTVLYLKEVTKFLALVCILREESFERKGLIDYNFHCFRKAIHEVFEVGVTSHRSCGHQTSASSLKALTHNGTPRNAI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSLQYGAEE ------CCCCCCCCC	24.95	25159151
2	Acetylation	------MSLQYGAEE ------CCCCCCCCC	24.95	20068231
5	Phosphorylation	---MSLQYGAEETPL ---CCCCCCCCCCCC	24.48	30108239
10	Phosphorylation	LQYGAEETPLAGSYG CCCCCCCCCCCCCCC	18.33	29255136
15	Phosphorylation	EETPLAGSYGAADSF CCCCCCCCCCCCCCC	18.13	29255136
16	Phosphorylation	ETPLAGSYGAADSFP CCCCCCCCCCCCCCC	15.18	29255136
21	Phosphorylation	GSYGAADSFPKDFGY CCCCCCCCCCCCCCC	38.43	29255136
28	Phosphorylation	SFPKDFGYGVEEEEE CCCCCCCCCCCHHHH	20.28	28796482
72	Phosphorylation	LLMGLRRSGKSSIQK EEEECHHCCCCCCEE	44.10	22673903
75	Phosphorylation	GLRRSGKSSIQKVVF ECHHCCCCCCEEEEE	35.88	26699800
76	Phosphorylation	LRRSGKSSIQKVVFH CHHCCCCCCEEEEEE	32.31	26699800
79	Ubiquitination	SGKSSIQKVVFHKMS CCCCCCEEEEEECCC	38.40	21890473
85	Sulfoxidation	QKVVFHKMSPNETLF EEEEEECCCCCCEEE	6.38	21406390
86	Phosphorylation	KVVFHKMSPNETLFL EEEEECCCCCCEEEE	29.40	23927012
90	Phosphorylation	HKMSPNETLFLESTN ECCCCCCEEEEEECC	29.47	23927012
95	Phosphorylation	NETLFLESTNKIYKD CCEEEEEECCCEECC	39.15	29255136
96	Phosphorylation	ETLFLESTNKIYKDD CEEEEEECCCEECCC	31.02	29255136
100	Phosphorylation	LESTNKIYKDDISNS EEECCCEECCCCCCC	15.24	26434776
137	Phosphorylation	YEMIFRGTGALIYVI HHEEEECCCEEEEEE	18.28	24043423
142	Phosphorylation	RGTGALIYVIDAQDD ECCCEEEEEEECCCH	7.69	24043423
150	Phosphorylation	VIDAQDDYMEALTRL EEECCCHHHHHHHHH	12.73	24043423
151	Sulfoxidation	IDAQDDYMEALTRLH EECCCHHHHHHHHHE	2.90	30846556
155	Phosphorylation	DDYMEALTRLHITVS CHHHHHHHHHEEEEE	37.93	24043423
242	Phosphorylation	KLIPQLPTLENLLNI HHHCCCCCHHHHHHH	56.12	20068231
252	Phosphorylation	NLLNIFISNSGIEKA HHHHHHHCCCCHHHH	17.75	20068231
327	Phosphorylation	LNNTTVLYLKEVTKF ECCCEEEEHHHHHHH	16.05	-
329	Ubiquitination	NTTVLYLKEVTKFLA CCEEEEHHHHHHHHH	36.26	-
361	Malonylation	YNFHCFRKAIHEVFE CCHHHHHHHHHHHHH	31.29	26320211
376	Phosphorylation	VGVTSHRSCGHQTSA HCCCCCCCCCCCCCH	21.01	30108239
381	Phosphorylation	HRSCGHQTSASSLKA CCCCCCCCCHHHHHH	22.15	25849741
382	Phosphorylation	RSCGHQTSASSLKAL CCCCCCCCHHHHHHH	21.42	25159151
384	Phosphorylation	CGHQTSASSLKALTH CCCCCCHHHHHHHHC	35.65	27794612
385	Phosphorylation	GHQTSASSLKALTHN CCCCCHHHHHHHHCC	33.34	23401153
387	Methylation	QTSASSLKALTHNGT CCCHHHHHHHHCCCC	43.21	115977383
390	Phosphorylation	ASSLKALTHNGTPRN HHHHHHHHCCCCCCC	20.39	30108239
394	Phosphorylation	KALTHNGTPRNAI-- HHHHCCCCCCCCC--	25.13	30266825

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
21	S	Phosphorylation	Kinase	MTOR	P42345	PSP
394	T	Phosphorylation	Kinase	MTOR	P42345	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RRAGC_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 RRAGC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SQSTM_HUMAN	SQSTM1	physical	21981924
RPTOR_HUMAN	RPTOR	physical	21981924
RRAGB_HUMAN	RRAGB	physical	21981924
MTOR_HUMAN	MTOR	physical	21981924
RRAGA_HUMAN	RRAGA	physical	21981924
RPTOR_HUMAN	RPTOR	physical	18497260
LTOR1_HUMAN	LAMTOR1	physical	22424946
RRAGB_HUMAN	RRAGB	physical	22424946
WNT2_HUMAN	WNT2	physical	21988832
RRAGB_HUMAN	RRAGB	physical	24337580
RPTOR_HUMAN	RPTOR	physical	24337580
MTOR_HUMAN	MTOR	physical	24337580
RRAGD_HUMAN	RRAGD	physical	24337580
RRAGA_HUMAN	RRAGA	physical	24337580
RRAGA_HUMAN	RRAGA	physical	20381137
RRAGB_HUMAN	RRAGB	physical	20381137
LTOR3_HUMAN	LAMTOR3	physical	20381137
LTOR2_HUMAN	LAMTOR2	physical	20381137
LTOR1_HUMAN	LAMTOR1	physical	20381137
TSC2_HUMAN	TSC2	physical	24529380
TSC1_HUMAN	TSC1	physical	24529380
RPTOR_HUMAN	RPTOR	physical	25446900

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 RRAGC_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.	19413330 [Abstract]