dbPTM

RASN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RASN_HUMAN
UniProt AC	P01111
Protein Name	GTPase NRas
Gene Name	NRAS
Organism	Homo sapiens (Human).
Sequence Length	189
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side . Golgi apparatus membrane Lipid-anchor . Shuttles between the plasma membrane and the Golgi apparatus.
Protein Description	Ras proteins bind GDP/GTP and possess intrinsic GTPase activity..
Protein Sequence	MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMKKLNSSDDGTQGCMGLPCVVM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTEYKLVVV ------CCCEEEEEE	48.28	19690332
4	Phosphorylation	----MTEYKLVVVGA ----CCCEEEEEECC	10.64	19690332
32	Phosphorylation	QNHFVDEYDPTIEDS HHHCCCCCCCCCCHH	23.82	25884760
35	Phosphorylation	FVDEYDPTIEDSYRK CCCCCCCCCCHHHCC	33.82	28348404
35	O-linked_Glycosylation	FVDEYDPTIEDSYRK CCCCCCCCCCHHHCC	33.82	19744486
39	Phosphorylation	YDPTIEDSYRKQVVI CCCCCCHHHCCEEEE	17.66	23401153
40	Phosphorylation	DPTIEDSYRKQVVID CCCCCHHHCCEEEEC	33.86	23403867
64	Phosphorylation	DTAGQEEYSAMRDQY HHCCHHHHHHHHHHH	10.85	22322096
65	Phosphorylation	TAGQEEYSAMRDQYM HCCHHHHHHHHHHHH	20.90	28796482
67	Sulfoxidation	GQEEYSAMRDQYMRT CHHHHHHHHHHHHHH	3.89	28465586
88	Methylation	VFAINNSKSFADINL EEEECCCCCHHHHHH	52.28	23644510
89	Phosphorylation	FAINNSKSFADINLY EEECCCCCHHHHHHH	26.03	30712867
111	Sulfoxidation	KDSDDVPMVLVGNKC CCCCCCCEEEECCCC	3.51	21406390
117	Ubiquitination	PMVLVGNKCDLPTRT CEEEECCCCCCCCCC	24.17	-
118	S-nitrosylation	MVLVGNKCDLPTRTV EEEECCCCCCCCCCC	8.24	22178444
118	S-nitrosocysteine	MVLVGNKCDLPTRTV EEEECCCCCCCCCCC	8.24	-
128	Ubiquitination	PTRTVDTKQAHELAK CCCCCCHHHHHHHHH	40.81	21906983
135	Acetylation	KQAHELAKSYGIPFI HHHHHHHHHHCCCEE	57.76	27452117
135	Ubiquitination	KQAHELAKSYGIPFI HHHHHHHHHHCCCEE	57.76	-
136	Phosphorylation	QAHELAKSYGIPFIE HHHHHHHHHCCCEEE	24.00	28152594
137	Phosphorylation	AHELAKSYGIPFIET HHHHHHHHCCCEEEC	20.54	28152594
147	Ubiquitination	PFIETSAKTRQGVED CEEECCCCHHHCHHH	43.96	2190698
148	Phosphorylation	FIETSAKTRQGVEDA EEECCCCHHHCHHHH	28.13	-
157	Phosphorylation	QGVEDAFYTLVREIR HCHHHHHHHHHHHHH	10.82	25884760
158	Phosphorylation	GVEDAFYTLVREIRQ CHHHHHHHHHHHHHH	16.60	-
181	S-palmitoylation	SDDGTQGCMGLPCVV CCCCCCCCCCCCEEE	1.09	2661017
186	Farnesylation	QGCMGLPCVVM---- CCCCCCCEEEC----	4.30	2661017
186	Methylation	QGCMGLPCVVM---- CCCCCCCEEEC----	4.30	10412982
186	Farnesylation	QGCMGLPCVVM---- CCCCCCCEEEC----	4.30	2661017

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
32	Y	Phosphorylation	Kinase	SRC	P12931	PSP
89	S	Phosphorylation	Kinase	G11	P49842	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:24746824

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
89	S	Phosphorylation	30712867
Phosphorylation at Ser-89 by STK19 enhances NRAS-association with its downstream effectors.
104	K	Acetylation	-
Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs).
170	K	ubiquitylation	30442762
Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at Lys-170 in a non-degradative manner, leading to inhibit Ras signaling by decreasing Ras association with membranes.

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 RASN_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GDS1_HUMAN	RAP1GDS1	physical	11948427
PK3CG_HUMAN	PIK3CG	physical	11136978
DNJB1_HUMAN	DNAJB1	physical	18624398
EF1A1_HUMAN	EEF1A1	physical	18624398
SORCN_HUMAN	SRI	physical	18624398
RS20_HUMAN	RPS20	physical	18624398
RNH2B_HUMAN	RNASEH2B	physical	22939629
VAT1_HUMAN	VAT1	physical	22939629
SPAS2_HUMAN	SPATS2	physical	22939629
RGL2_HUMAN	RGL2	physical	21988832
FACE2_HUMAN	RCE1	genetic	28162770
ICMT_HUMAN	ICMT	genetic	28162770
RAF1_HUMAN	RAF1	genetic	28162770
SHOC2_HUMAN	SHOC2	genetic	28162770
PREX1_HUMAN	PREX1	genetic	28162770
GOGA7_HUMAN	GOLGA7	genetic	28162770
BRAF_HUMAN	BRAF	physical	7499408
MP2K7_HUMAN	MAP2K7	physical	7499408

Drug and Disease Associations

Kegg Disease
H00003	Acute myeloid leukemia (AML)
H00010	Multiple myeloma
H00016	Oral cancer
H00032	Thyroid cancer
H00033	Adrenal carcinoma
H00038	Malignant melanoma
H00048	Hepatocellular carcinoma
H00108	Autoimmune lymphoproliferative syndromes (ALPS), including the following five diseases: CD95 (Fas) d
H00523	Noonan syndrome and related disorders, including: Noonan syndrome (NS); Leopard syndrome (LS); Noona
OMIM Disease
607785	Leukemia, juvenile myelomonocytic (JMML)
613224	Noonan syndrome 6 (NS6)
614470	RAS-associated autoimmune leukoproliferative disorder (RALD)
137550	Melanocytic nevus syndrome, congenital (CMNS)
249400	Melanosis, neurocutaneous (NCMS)
162900	Keratinocytic non-epidermolytic nevus (KNEN)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RASN_HUMAN

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"An acylation cycle regulates localization and activity ofpalmitoylated Ras isoforms."; Rocks O., Peyker A., Kahms M., Verveer P.J., Koerner C.,Lumbierres M., Kuhlmann J., Waldmann H., Wittinghofer A.,Bastiaens P.I.H.; Science 307:1746-1752(2005). Cited for: PALMITOYLATION, AND SUBCELLULAR LOCATION.	15705808 [Abstract]
"DHHC9 and GCP16 constitute a human protein fatty acyltransferase withspecificity for H- and N-Ras."; Swarthout J.T., Lobo S., Farh L., Croke M.R., Greentree W.K.,Deschenes R.J., Linder M.E.; J. Biol. Chem. 280:31141-31148(2005). Cited for: PALMITOYLATION AT CYS-181.	16000296 [Abstract]
"All ras proteins are polyisoprenylated but only some arepalmitoylated."; Hancock J.F., Magee A.I., Childs J.E., Marshall C.J.; Cell 57:1167-1177(1989). Cited for: PALMITOYLATION AT CYS-181, AND ISOPRENYLATION AT CYS-186.	2661017 [Abstract]
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 THR-2 AND TYR-4, AND MASSSPECTROMETRY.	19690332 [Abstract]
Prenylation
Reference	PubMed
"All ras proteins are polyisoprenylated but only some arepalmitoylated."; Hancock J.F., Magee A.I., Childs J.E., Marshall C.J.; Cell 57:1167-1177(1989). Cited for: PALMITOYLATION AT CYS-181, AND ISOPRENYLATION AT CYS-186.	2661017 [Abstract]

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