dbPTM

RASH_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RASH_RAT
UniProt AC	P20171
Protein Name	GTPase HRas
Gene Name	Hras
Organism	Rattus norvegicus (Rat).
Sequence Length	189
Subcellular Localization	Cell membrane . Cell membrane Lipid-anchor Cytoplasmic side. Golgi apparatus. Golgi apparatus membrane Lipid-anchor. Shuttles between the plasma membrane and the Golgi apparatus (By similarity). The active GTP-bound form is localized most strongly
Protein Description	Ras proteins bind GDP/GTP and possess intrinsic GTPase activity..
Protein Sequence	MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MTEYKLVV -------CCCEEEEE	6.07	-
2	Acetylation	------MTEYKLVVV ------CCCEEEEEE	48.28	-
39	Phosphorylation	YDPTIEDSYRKQVVI CCCCCCHHHCCEEEE	17.66	30181290
118	S-nitrosocysteine	MVLVGNKCDLAARTV EEEECCHHHHHHHHH	6.34	-
118	S-nitrosylation	MVLVGNKCDLAARTV EEEECCHHHHHHHHH	6.34	-
181	S-palmitoylation	PDESGPGCMSCKCVL CCCCCCCCCCCEEEE	1.72	27307232
184	Other	SGPGCMSCKCVLS-- CCCCCCCCEEEEC--	1.25	-
184	S-palmitoylation	SGPGCMSCKCVLS-- CCCCCCCCEEEEC--	1.25	27307232
186	Methylation	PGCMSCKCVLS---- CCCCCCEEEEC----	4.34	3290900
186	Farnesylation	PGCMSCKCVLS---- CCCCCCEEEEC----	4.34	3290900
186	Farnesylation	PGCMSCKCVLS---- CCCCCCEEEEC----	4.34	3290900

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 RASH_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
104	K	Acetylation	-
Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs).
170	K	ubiquitylation	-
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 RASH_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
RAF1_RAT	Raf1	physical	9679960
ARAF_RAT	Araf	physical	9679960

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RASH_RAT

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"Posttranslational modification of the Ha-ras oncogene protein:evidence for a third class of protein carboxyl methyltransferases."; Clarke S., Vogel J.P., Deschenes R.J., Stock J.; Proc. Natl. Acad. Sci. U.S.A. 85:4643-4647(1988). Cited for: ISOPRENYLATION AT CYS-186, CLEAVAGE, AND METHYLATION AT CYS-186.	3290900 [Abstract]
Prenylation
Reference	PubMed
"Posttranslational modification of the Ha-ras oncogene protein:evidence for a third class of protein carboxyl methyltransferases."; Clarke S., Vogel J.P., Deschenes R.J., Stock J.; Proc. Natl. Acad. Sci. U.S.A. 85:4643-4647(1988). Cited for: ISOPRENYLATION AT CYS-186, CLEAVAGE, AND METHYLATION AT CYS-186.	3290900 [Abstract]