Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Ras-related protein R-Ras2  

UniProtKB / Swiss-Prot ID :  RRAS2_HUMAN

Gene Name (Synonyms) : 
RRAS2, TC21  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane; Lipid-anchor; Cytoplasmic side (By similarity). Note=Inner surface of plasma membrane possibly with attachment requiring acylation of the C-terminal cysteine (By similarity with RAS). 

Protein Function :  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 MAAAGWRDGSGQEKYRLVVVGGGGVGKSALTIQFIQSYFVTDYDPTIEDSYTKQCVIDDRAARLDILDTA...
Predicted Secondary Structure CCCCCCCCCCCCCEEEEEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEECCEEEEEEEEECC...
Protein Variant
LocationDescription
72Q -> L (in an ovarian cancer sample;somatic mutation).
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAAGW
---CCCCCC
13.15UniProtKB
Link-
10PhosphoserineWRDGSGQEK
CCCCCCCCE
41.41Phosphositeplus
Link-
55S-nitrosocysteineYTKQCVIDD
EEEEEEECC
2.86dbSNO
Link
183S-nitrosocysteineQEQECPPSP
HHCCCCCCC
6.33dbSNO
Link-
186PhosphoserineECPPSPEPT
CCCCCCCCC
27.34HPRD
Link-
186PhosphoserineECPPSPEPT
CCCCCCCCC
27.34PhosphoELM
Link-
186PhosphoserineECPPSPEPT
CCCCCCCCC
27.34Phosphositeplus
Link-
186PhosphoserineECPPSPEPT
CCCCCCCCC
27.34SysPTM
Link-
186Phosphoserine.ECPPSPEPT
CCCCCCCCC
27.34UniProtKB
Link-
190PhosphothreonineSPEPTRKEK
CCCCCCCCC
53.35HPRD
Link-
190PhosphothreonineSPEPTRKEK
CCCCCCCCC
53.35Phosphositeplus
Link-
190Phosphothreonine.SPEPTRKEK
CCCCCCCCC
53.35UniProtKB
Link-
201S-farnesyl cysteine.KGCHCVIF
CCCCCEEC
2.67UniProtKB
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
LEG4_HUMANphysical interactionMINT-63952MINT16169070
KU70_HUMANphysical interactionMINT-63953MINT16169070
Q6FG89_HUMANphysical interactionMINT-63953MINT16169070
PAWR_HUMANphysical interactionEBI-737624
intact16169070
LEG4_HUMANphysical interactionEBI-735675
intact16169070
KU70_HUMANphysical interactionEBI-733187
intact16169070
FETUA_HUMANin vitroHPRD:02518HPRD11788587
AFAD_HUMANin vitro
yeast 2-hybrid
HPRD:02518HPRD11788587
10224125
RAF1_HUMANin vivo
yeast 2-hybrid
HPRD:02518HPRD10064593
11788587
PTN1_HUMANin vitroHPRD:02518HPRD11788587
P85A_HUMANin vivoHPRD:02518HPRD11850823
ARAF_HUMANyeast 2-hybridHPRD:02518HPRD12620389
SMAD3_HUMANin vivoHPRD:02518HPRD15761153
SMAD4_HUMANin vivoHPRD:02518HPRD15761153
SMUF2_HUMANin vivoHPRD:02518HPRD15761153
PRAF1_HUMANENSP00000256196STRING
RAF1_HUMANENSP00000256196STRING
RIN1_HUMANENSP00000256196STRING
- top -

Disease Reference
Kegg disease
OMIM disease
167000Ovarian cancer (OC)
Drug Reference
There are no disease associations of PTM sites.
- top -
Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
Prenylation
ReferencePubMed
"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.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures