ARHG2_MOUSE - dbPTM
ARHG2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARHG2_MOUSE
UniProt AC Q60875
Protein Name Rho guanine nucleotide exchange factor 2
Gene Name Arhgef2
Organism Mus musculus (Mouse).
Sequence Length 985
Subcellular Localization Cytoplasm, cytoskeleton . Cytoplasm . Cell junction, tight junction . Golgi apparatus . Cytoplasm, cytoskeleton, spindle . Cytoplasmic vesicle . Localizes to the tips of cortical microtubules of the mitotic spindle during cell division, and is furthe
Protein Description Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Overexpression activates Rho-, but not Rac-GTPases, and increases paracellular permeability (By similarity). Involved in neuronal progenitor cell division and differentiation. [PubMed: 28453519 Involved in the migration of precerebellar neurons]
Protein Sequence MSRIESLTRARIDRSKEQATKTREKEKMKEAKDARYTNGHLFTTISVSGMTMCYACNKSITAKEALICPTCNVTIHNRCKDTLANCTKVKQKQQKAALLRNNTALQSVSLRSKTTTRERPTSAIYPSDSFRQSLLGSRRGLSSLSLAKSVSTTNIAGHFNDESPLGLRQILSQSTDSLNMRNRTLSVESLIDEGVEVFYNELMSDFEMDEKDFEADSWSLAVDSSFLQQHKKEVMKKQDVIYELIQTELHHVRTLKIMTRLFRTGMLEELQMEPEVVQGLFPCVDELSDIHTRFLNQLLERRRQALCPGSTRNFVIHRLGDLLISQFSGSNAEQMRKTYSEFCSRHTKALKLYKELYARDKRFQQFIRKMTRSAVLKRHGVQECILLVTQRITKYPVLINRILQNSHGVEEEYQDLASALGLVKELLSNVDQDVHELEKEARLQEIYNRMDPRAQTPVPGKGPFGRDELLRRKLIHEGCLLWKTATGRFKDVLLLLMTDVLVFLQEKDQKYIFTSLDKPSVVSLQNLIVRDIANQAKGMFLISSGPPEMYEVHAASRDDRTTWIRVIQQSVRLCPSREDFPLIETEDKAYLRRIKTKLQQKNQALVELLQKNVELFAEMVHFQALKAGFVGMPPPALPRGLFRLESFESLRGERLLKDALREVEGLKDLLLGPCVDLPMTSREPALPLDSDSGSCPGVTANGEARTFNGSIELCRADSDSSQKDRNGNQLRSPQEEVLQPLINLYGLLHGLQAVVVQQERLMEALFPEGPERWEKLSRANSRDGEAGRAAVASVTPEKQATELALLQRQHTLLQEELRRCQRLGEERATEAGSLEARLRESEQARALLEREAEEIRRQLAALGQNEPLPAEAPWARRPLDPRRRSLPAGDALYLSFNPPQPSRGHDRLDLPVTVRSLHRPFDDREAQELGSPEDRLQDSSDPDTGSEEEVSSRLSPPHSPRDFTRMQDIPEETESRDGEPTASES
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSRIESLTR
------CCHHHHHHH		41.8029176673
6Phosphorylation--MSRIESLTRARID
--CCHHHHHHHHHHH		32.4429176673
8PhosphorylationMSRIESLTRARIDRS
CCHHHHHHHHHHHHC		31.4029514104
82 (in isoform 5)Phosphorylation-17.1727566939
92 (in isoform 5)Phosphorylation-49.3227566939
93 (in isoform 5)Phosphorylation-47.7327566939
103PhosphorylationAALLRNNTALQSVSL
HHHHHCCCHHHEEEC		32.0920415495
107PhosphorylationRNNTALQSVSLRSKT
HCCCHHHEEECCCCC		17.9628066266
109PhosphorylationNTALQSVSLRSKTTT
CCHHHEEECCCCCCC		24.2622942356
114PhosphorylationSVSLRSKTTTRERPT
EEECCCCCCCCCCCC		34.3519667072
116PhosphorylationSLRSKTTTRERPTSA
ECCCCCCCCCCCCCC		35.4519854140
121PhosphorylationTTTRERPTSAIYPSD
CCCCCCCCCCCCCCH		36.6923684622
122PhosphorylationTTRERPTSAIYPSDS
CCCCCCCCCCCCCHH		18.4927087446
125PhosphorylationERPTSAIYPSDSFRQ
CCCCCCCCCCHHHHH		9.0826745281
127PhosphorylationPTSAIYPSDSFRQSL
CCCCCCCCHHHHHHH		28.9922817900
129PhosphorylationSAIYPSDSFRQSLLG
CCCCCCHHHHHHHHC		27.0219854140
133PhosphorylationPSDSFRQSLLGSRRG
CCHHHHHHHHCCCCC		22.7028066266
137PhosphorylationFRQSLLGSRRGLSSL
HHHHHHCCCCCHHHH		20.8326824392
142PhosphorylationLGSRRGLSSLSLAKS
HCCCCCHHHHHHHCC		31.8626824392
143PhosphorylationGSRRGLSSLSLAKSV
CCCCCHHHHHHHCCC		27.3326745281
145PhosphorylationRRGLSSLSLAKSVST
CCCHHHHHHHCCCCC		28.3826745281
149PhosphorylationSSLSLAKSVSTTNIA
HHHHHHCCCCCCCCC		18.7225521595
151PhosphorylationLSLAKSVSTTNIAGH
HHHHCCCCCCCCCCC		36.2825521595
152PhosphorylationSLAKSVSTTNIAGHF
HHHCCCCCCCCCCCC		23.0021082442
153PhosphorylationLAKSVSTTNIAGHFN
HHCCCCCCCCCCCCC		19.6823527152
163PhosphorylationAGHFNDESPLGLRQI
CCCCCCCCCCHHHHH		28.4328725479
172PhosphorylationLGLRQILSQSTDSLN
CHHHHHHHHCCCCCC		24.5827087446
174PhosphorylationLRQILSQSTDSLNMR
HHHHHHHCCCCCCCC		30.7025521595
175PhosphorylationRQILSQSTDSLNMRN
HHHHHHCCCCCCCCC		23.2127087446
177PhosphorylationILSQSTDSLNMRNRT
HHHHCCCCCCCCCCC		23.0227087446
184PhosphorylationSLNMRNRTLSVESLI
CCCCCCCCCCHHHHH		27.2529550500
186PhosphorylationNMRNRTLSVESLIDE
CCCCCCCCHHHHHHH		24.1929550500
189PhosphorylationNRTLSVESLIDEGVE
CCCCCHHHHHHHCHH		28.5929550500
338PhosphorylationNAEQMRKTYSEFCSR
CHHHHHHHHHHHHHH		23.1627149854
339PhosphorylationAEQMRKTYSEFCSRH
HHHHHHHHHHHHHHH		14.8327149854
340PhosphorylationEQMRKTYSEFCSRHT
HHHHHHHHHHHHHHH		29.4527149854
344PhosphorylationKTYSEFCSRHTKALK
HHHHHHHHHHHHHHH		32.2027149854
354UbiquitinationTKALKLYKELYARDK
HHHHHHHHHHHHHHH		52.2422790023
354AcetylationTKALKLYKELYARDK
HHHHHHHHHHHHHHH		52.24-
395PhosphorylationVTQRITKYPVLINRI
HHHHHHCCHHHHHHH		7.02-
646PhosphorylationRGLFRLESFESLRGE
CCCEEHHHHHHHHHH		38.6227087446
649PhosphorylationFRLESFESLRGERLL
EEHHHHHHHHHHHHH		22.7427742792
674GlutathionylationKDLLLGPCVDLPMTS
HHHHHCCCCCCCCCC		3.3624333276
680PhosphorylationPCVDLPMTSREPALP
CCCCCCCCCCCCCCC		23.77-
692PhosphorylationALPLDSDSGSCPGVT
CCCCCCCCCCCCCCC		36.24-
706PhosphorylationTANGEARTFNGSIEL
CCCCEEEEECCEEEE		28.6227087446
710PhosphorylationEARTFNGSIELCRAD
EEEEECCEEEEEECC		17.6225521595
718PhosphorylationIELCRADSDSSQKDR
EEEEECCCCCCCCCC		38.1127087446
720PhosphorylationLCRADSDSSQKDRNG
EEECCCCCCCCCCCC		38.3230635358
721PhosphorylationCRADSDSSQKDRNGN
EECCCCCCCCCCCCC		46.3630635358
777PhosphorylationPERWEKLSRANSRDG
HHHHHHHHHHHCCCC		40.1824719451
781PhosphorylationEKLSRANSRDGEAGR
HHHHHHHCCCCHHHH		30.6622324799
793PhosphorylationAGRAAVASVTPEKQA
HHHHHHHCCCHHHHH		21.6724068923
795PhosphorylationRAAVASVTPEKQATE
HHHHHCCCHHHHHHH		24.2026824392
801PhosphorylationVTPEKQATELALLQR
CCHHHHHHHHHHHHH		29.1024068923
811PhosphorylationALLQRQHTLLQEELR
HHHHHHHHHHHHHHH		22.3319060867
833PhosphorylationERATEAGSLEARLRE
HHHHHHCCHHHHHHH		30.0420531401
885PhosphorylationPLDPRRRSLPAGDAL
CCCCCCCCCCCCCEE		36.5727087446
893PhosphorylationLPAGDALYLSFNPPQ
CCCCCEEEEECCCCC		11.3025619855
895PhosphorylationAGDALYLSFNPPQPS
CCCEEEEECCCCCCC		14.9325619855
931PhosphorylationREAQELGSPEDRLQD
HHHHHHCCHHHHHCC		37.4325521595
939PhosphorylationPEDRLQDSSDPDTGS
HHHHHCCCCCCCCCC		24.5525521595
940PhosphorylationEDRLQDSSDPDTGSE
HHHHCCCCCCCCCCH		62.5425521595
944PhosphorylationQDSSDPDTGSEEEVS
CCCCCCCCCCHHHHH		48.2527742792
946PhosphorylationSSDPDTGSEEEVSSR
CCCCCCCCHHHHHHH		43.8827742792
951PhosphorylationTGSEEEVSSRLSPPH
CCCHHHHHHHCCCCC		17.0227742792
952PhosphorylationGSEEEVSSRLSPPHS
CCHHHHHHHCCCCCC		42.2827742792
955PhosphorylationEEVSSRLSPPHSPRD
HHHHHHCCCCCCCCC		34.9625521595
959PhosphorylationSRLSPPHSPRDFTRM
HHCCCCCCCCCCCCC		27.6627087446
964PhosphorylationPHSPRDFTRMQDIPE
CCCCCCCCCCCCCCC		29.5326160508
973PhosphorylationMQDIPEETESRDGEP
CCCCCCCCCCCCCCC		37.2826643407
975PhosphorylationDIPEETESRDGEPTA
CCCCCCCCCCCCCCC		42.9925266776
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
114TPhosphorylationKinasePRKACAP17612
GPS
122SPhosphorylationKinaseCDKL5Q3UTQ8
PSP
143SPhosphorylationKinasePAK4Q8BTW9
Uniprot
680TPhosphorylationKinaseMAPK1P63085
Uniprot
680TPhosphorylationKinaseMAPK3Q63844
Uniprot
885SPhosphorylationKinasePRKACAP17612
GPS
895SPhosphorylationKinasePAK4Q8BTW9
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
885SPhosphorylation

19144319
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 ARHG2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEB2_MOUSEPpp1r9bphysical
15996550
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARHG2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-646; SER-781;THR-795; SER-885; SER-931; SER-939; SER-940; THR-944; SER-955 ANDSER-959, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-959, AND MASSSPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646, AND MASSSPECTROMETRY.

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