dbPTM

RRAS2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RRAS2_HUMAN
UniProt AC	P62070
Protein Name	Ras-related protein R-Ras2
Gene Name	RRAS2
Organism	Homo sapiens (Human).
Sequence Length	204
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side. Inner surface of plasma membrane possibly with attachment requiring acylation of the C-terminal cysteine (By similarity with RAS).
Protein Description	It is a plasma membrane-associated GTP-binding protein with GTPase activity. Might transduce growth inhibitory signals across the cell membrane, exerting its effect through an effector shared with the Ras proteins but in an antagonistic fashion..
Protein Sequence	MAAAGWRDGSGQEKYRLVVVGGGGVGKSALTIQFIQSYFVTDYDPTIEDSYTKQCVIDDRAARLDILDTAGQEEFGAMREQYMRTGEGFLLVFSVTDRGSFEEIYKFQRQILRVKDRDEFPMILIGNKADLDHQRQVTQEEGQQLARQLKVTYMEASAKIRMNVDQAFHELVRVIRKFQEQECPPSPEPTRKEKDKKGCHCVIF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAGWRDG ------CCCCCCCCC	13.15	19413330
10	Phosphorylation	AAGWRDGSGQEKYRL CCCCCCCCCCCEEEE	41.41	28355574
15	Phosphorylation	DGSGQEKYRLVVVGG CCCCCCEEEEEEECC	14.39	-
29	Ubiquitination	GGGVGKSALTIQFIQ CCCCCHHHHHHHHHH	16.53	33845483
43	Phosphorylation	QSYFVTDYDPTIEDS HHHCCCCCCCCCCCC	17.92	25884760
51	Ubiquitination	DPTIEDSYTKQCVID CCCCCCCCCCEEEEC	30.22	29967540
55	S-nitrosylation	EDSYTKQCVIDDRAA CCCCCCEEEECCHHH	2.86	21278135
55	S-nitrosocysteine	EDSYTKQCVIDDRAA CCCCCCEEEECCHHH	2.86	-
71	Ubiquitination	LDILDTAGQEEFGAM CEEECHHCHHHHHHH	37.21	33845483
78	Sulfoxidation	GQEEFGAMREQYMRT CHHHHHHHHHHHHHH	5.05	30846556
93	Ubiquitination	GEGFLLVFSVTDRGS CCCEEEEEEEECCCC	4.98	29967540
100	Ubiquitination	FSVTDRGSFEEIYKF EEEECCCCHHHHHHH	30.31	23000965
105	Phosphorylation	RGSFEEIYKFQRQIL CCCHHHHHHHHHHHH	14.72	28152594
106	Acetylation	GSFEEIYKFQRQILR CCHHHHHHHHHHHHC	40.45	27452117
106	Ubiquitination	GSFEEIYKFQRQILR CCHHHHHHHHHHHHC	40.45	33845483
109	Phosphorylation	EEIYKFQRQILRVKD HHHHHHHHHHHCCCC	28.74	32142685
115	Ubiquitination	QRQILRVKDRDEFPM HHHHHCCCCCCCCCE	40.38	29967540
128	Ubiquitination	PMILIGNKADLDHQR CEEEEECHHHCCHHH	37.76	29967540
142	Ubiquitination	RQVTQEEGQQLARQL HHHCHHHHHHHHHHH	21.56	23000965
151	Phosphorylation	QLARQLKVTYMEASA HHHHHHHHEEHHHHH	6.70	32142685
155	Ubiquitination	QLKVTYMEASAKIRM HHHHEEHHHHHHHCC	29.11	23000965
157	Ubiquitination	KVTYMEASAKIRMNV HHEEHHHHHHHCCCH	19.45	29967540
177	Ubiquitination	ELVRVIRKFQEQECP HHHHHHHHHHHCCCC	40.03	23000965
183	Ubiquitination	RKFQEQECPPSPEPT HHHHHCCCCCCCCCC	6.33	-
183	S-nitrosocysteine	RKFQEQECPPSPEPT HHHHHCCCCCCCCCC	6.33	-
183	S-nitrosylation	RKFQEQECPPSPEPT HHHHHCCCCCCCCCC	6.33	21278135
186	Phosphorylation	QEQECPPSPEPTRKE HHCCCCCCCCCCCCC	27.34	19664994
190	Phosphorylation	CPPSPEPTRKEKDKK CCCCCCCCCCCCCCC	53.35	19664994
192	Ubiquitination	PSPEPTRKEKDKKGC CCCCCCCCCCCCCCC	72.15	29967540
199	S-palmitoylation	KEKDKKGCHCVIF-- CCCCCCCCEEEEC--	2.86	-
201	Methylation	KDKKGCHCVIF---- CCCCCCEEEEC----	2.67	-
201	Farnesylation	KDKKGCHCVIF---- CCCCCCEEEEC----	2.67	15308774
201	Farnesylation	KDKKGCHCVIF---- CCCCCCEEEEC----	2.67	15308774

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
186	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
186	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RRAS2_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 RRAS2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LEG4_HUMAN	LGALS4	physical	16169070
XRCC6_HUMAN	XRCC6	physical	16169070
RAF1_HUMAN	RAF1	physical	10783161
RAF1_HUMAN	RAF1	physical	10557073
GNDS_HUMAN	RALGDS	physical	11788587
RIN1_HUMAN	RIN1	physical	11788587
AFAD_HUMAN	MLLT4	physical	11788587
RIN1_HUMAN	RIN1	physical	19060904
TRAF2_HUMAN	TRAF2	physical	21988832

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
167000	Ovarian cancer (OC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RRAS2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-186 AND THR-190, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY.	19369195 [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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-186 AND THR-190, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY.	18691976 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASSSPECTROMETRY.	17081983 [Abstract]
Prenylation
Reference	PubMed
"A tagging-via-substrate technology for detection and proteomics offarnesylated proteins."; Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J.,Jaunbergs J., Weinbaum C., Tamanoi F., Falck J., Zhao Y.; Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004). Cited for: ISOPRENYLATION AT CYS-201.	15308774 [Abstract]