RGPS2_HUMAN - dbPTM
RGPS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGPS2_HUMAN
UniProt AC Q86X27
Protein Name Ras-specific guanine nucleotide-releasing factor RalGPS2
Gene Name RALGPS2
Organism Homo sapiens (Human).
Sequence Length 583
Subcellular Localization Cytoplasm. Cell membrane. Associates with membranes through the PH domain..
Protein Description Guanine nucleotide exchange factor for the small GTPase RALA. May be involved in cytoskeletal organization. May also be involved in the stimulation of transcription in a Ras-independent fashion (By similarity)..
Protein Sequence MDLMNGQASSVNIAATASEKSSSSESLSDKGSELKKSFDAVVFDVLKVTPEEYAGQITLMDVPVFKAIQPDELSSCGWNKKEKYSSAPNAVAFTRRFNHVSFWVVREILHAQTLKIRAEVLSHYIKTAKKLYELNNLHALMAVVSGLQSAPIFRLTKTWALLSRKDKTTFEKLEYVMSKEDNYKRLRDYISSLKMTPCIPYLGIYLSDLTYIDSAYPSTGSILENEQRSNLMNNILRIISDLQQSCEYDIPMLPHVQKYLNSVQYIEELQKFVEDDNYKLSLKIEPGTSTPRSAASREDLVGPEVGASPQSGRKSVAAEGALLPQTPPSPRNLIPHGHRKCHSLGYNFIHKMNTAEFKSATFPNAGPRHLLDDSVMEPHAPSRGQAESSTLSSGISIGSSDGSELSEETSWPAFERNRLYHSLGPVTRVARNGYRSHMKASSSAESEDLAVHLYPGAVTIQGVLRRKTLLKEGKKPTVASWTKYWAALCGTQLFYYAAKSLKATERKHFKSTSNKNVSVIGWMVMMADDPEHPDLFLLTDSEKGNSYKFQAGNRMNAMLWFKHLSAACQSNKQQVPTNLMTFE
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
9PhosphorylationDLMNGQASSVNIAAT
CCCCCCCCCCEEEEE		27.2520068231
10PhosphorylationLMNGQASSVNIAATA
CCCCCCCCCEEEEEC		23.3820068231
21PhosphorylationAATASEKSSSSESLS
EEECCCCCCCCCCCC		31.2523403867
22PhosphorylationATASEKSSSSESLSD
EECCCCCCCCCCCCH		49.2923403867
23PhosphorylationTASEKSSSSESLSDK
ECCCCCCCCCCCCHH		45.2626055452
24PhosphorylationASEKSSSSESLSDKG
CCCCCCCCCCCCHHH		32.9023403867
26PhosphorylationEKSSSSESLSDKGSE
CCCCCCCCCCHHHHH		34.8125849741
28PhosphorylationSSSSESLSDKGSELK
CCCCCCCCHHHHHHH		46.7023403867
32PhosphorylationESLSDKGSELKKSFD
CCCCHHHHHHHHHHC		45.5623403867
37PhosphorylationKGSELKKSFDAVVFD
HHHHHHHHHCEEEEE		27.1130278072
79UbiquitinationELSSCGWNKKEKYSS
HHHCCCCCCHHHCCC		30.7023000965
83UbiquitinationCGWNKKEKYSSAPNA
CCCCCHHHCCCCCCE		60.3523000965
84PhosphorylationGWNKKEKYSSAPNAV
CCCCHHHCCCCCCEE		14.6728258704
86PhosphorylationNKKEKYSSAPNAVAF
CCHHHCCCCCCEEHH		44.6628258704
94PhosphorylationAPNAVAFTRRFNHVS
CCCEEHHHHCCCCHH		15.9328258704
101PhosphorylationTRRFNHVSFWVVREI
HHCCCCHHHHHHHHH		13.0728258704
122PhosphorylationKIRAEVLSHYIKTAK
HHHHHHHHHHHHHHH		21.3028258704
124PhosphorylationRAEVLSHYIKTAKKL
HHHHHHHHHHHHHHH		10.7520068231
158PhosphorylationPIFRLTKTWALLSRK
CHHHHHHHHHHHCCC		15.67-
175PhosphorylationTTFEKLEYVMSKEDN
CHHHHHHHHHCCCHH		16.3423663014
178PhosphorylationEKLEYVMSKEDNYKR
HHHHHHHCCCHHHHH		23.8923663014
183PhosphorylationVMSKEDNYKRLRDYI
HHCCCHHHHHHHHHH		15.1423663014
191PhosphorylationKRLRDYISSLKMTPC
HHHHHHHHHCCCCCC		24.3224719451
259PhosphorylationMLPHVQKYLNSVQYI
CHHHHHHHHHHHHHH		8.2722817900
265PhosphorylationKYLNSVQYIEELQKF
HHHHHHHHHHHHHHH		14.2422817900
271UbiquitinationQYIEELQKFVEDDNY
HHHHHHHHHHHCCCE		65.09-
278PhosphorylationKFVEDDNYKLSLKIE
HHHHCCCEEEEEEEC		21.94-
279UbiquitinationFVEDDNYKLSLKIEP
HHHCCCEEEEEEECC		37.5423000965
281PhosphorylationEDDNYKLSLKIEPGT
HCCCEEEEEEECCCC		24.3824719451
283 (in isoform 1)Ubiquitination-41.4721906983
283UbiquitinationDNYKLSLKIEPGTST
CCEEEEEEECCCCCC		41.4721906983
283UbiquitinationDNYKLSLKIEPGTST
CCEEEEEEECCCCCC		41.4723000965
288PhosphorylationSLKIEPGTSTPRSAA
EEEECCCCCCCCCCC		39.8929255136
289PhosphorylationLKIEPGTSTPRSAAS
EEECCCCCCCCCCCC		42.1829255136
290PhosphorylationKIEPGTSTPRSAASR
EECCCCCCCCCCCCH		23.6625849741
293PhosphorylationPGTSTPRSAASREDL
CCCCCCCCCCCHHHC		29.4123927012
296PhosphorylationSTPRSAASREDLVGP
CCCCCCCCHHHCCCC		35.6019664994
308PhosphorylationVGPEVGASPQSGRKS
CCCCCCCCCCCCCCC		19.9719664994
311PhosphorylationEVGASPQSGRKSVAA
CCCCCCCCCCCCHHH		43.9030266825
315PhosphorylationSPQSGRKSVAAEGAL
CCCCCCCCHHHCCCC		18.6729255136
326PhosphorylationEGALLPQTPPSPRNL
CCCCCCCCCCCCCCC		34.9229255136
329PhosphorylationLLPQTPPSPRNLIPH
CCCCCCCCCCCCCCC		37.3819664994
343PhosphorylationHGHRKCHSLGYNFIH
CCCHHCHHCCCHHHH		32.7223401153
346PhosphorylationRKCHSLGYNFIHKMN
HHCHHCCCHHHHCCC		16.5223927012
354PhosphorylationNFIHKMNTAEFKSAT
HHHHCCCHHHHHHCC		24.8627251275
358MethylationKMNTAEFKSATFPNA
CCCHHHHHHCCCCCC		30.59115976155
359PhosphorylationMNTAEFKSATFPNAG
CCHHHHHHCCCCCCC		37.5530266825
361PhosphorylationTAEFKSATFPNAGPR
HHHHHHCCCCCCCCC		46.8723401153
374PhosphorylationPRHLLDDSVMEPHAP
CCCCCCCCCCCCCCC		24.0329255136
382PhosphorylationVMEPHAPSRGQAESS
CCCCCCCCCCCCCCC		50.2329255136
420PhosphorylationAFERNRLYHSLGPVT
HHHHCCHHHHCCHHH		6.0221945579
422O-linked_GlycosylationERNRLYHSLGPVTRV
HHCCHHHHCCHHHHH		22.82OGP
422PhosphorylationERNRLYHSLGPVTRV
HHCCHHHHCCHHHHH		22.8221945579
427PhosphorylationYHSLGPVTRVARNGY
HHHCCHHHHHHHCCH		23.6629255136
441PhosphorylationYRSHMKASSSAESED
HHHHCCCCCCCCCCC		21.2128348404
442PhosphorylationRSHMKASSSAESEDL
HHHCCCCCCCCCCCC		38.1328348404
443PhosphorylationSHMKASSSAESEDLA
HHCCCCCCCCCCCCC		33.2928348404
446PhosphorylationKASSSAESEDLAVHL
CCCCCCCCCCCCHHH		35.8128348404
477PhosphorylationLKEGKKPTVASWTKY
HHCCCCCCCHHHHHH		37.27-
511PhosphorylationTERKHFKSTSNKNVS
HHHHHHHCCCCCCEE		35.80-
512PhosphorylationERKHFKSTSNKNVSV
HHHHHHCCCCCCEEE		36.59-
513PhosphorylationRKHFKSTSNKNVSVI
HHHHHCCCCCCEEEE		53.55-
539PhosphorylationHPDLFLLTDSEKGNS
CCCEEEEECCCCCCE		39.3630576142
546PhosphorylationTDSEKGNSYKFQAGN
ECCCCCCEEEECCCC		38.0730576142
548UbiquitinationSEKGNSYKFQAGNRM
CCCCCEEEECCCCCC		30.71-
548MalonylationSEKGNSYKFQAGNRM
CCCCCEEEECCCCCC		30.7126320211
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 RGPS2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGPS2_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 RGPS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
1433Z_HUMANYWHAZphysical
28514442
1433G_HUMANYWHAGphysical
28514442
CING_HUMANCGNphysical
27173435
KI13B_HUMANKIF13Bphysical
27173435
GGYF2_HUMANGIGYF2physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
CBY1_HUMANCBY1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
NADK_HUMANNADKphysical
27173435
HDAC4_HUMANHDAC4physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
NGAP_HUMANRASAL2physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RGPS2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-329, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-296; SER-308;THR-326 AND SER-329, AND MASS SPECTROMETRY.
"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-308; SER-311; THR-326AND SER-329, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422, 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 THR-326; SER-329 ANDSER-343, AND MASS SPECTROMETRY.

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