GRP1_HUMAN - dbPTM
GRP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRP1_HUMAN
UniProt AC O95267
Protein Name RAS guanyl-releasing protein 1
Gene Name RASGRP1
Organism Homo sapiens (Human).
Sequence Length 797
Subcellular Localization Cytoplasm, cytosol. Cell membrane
Peripheral membrane protein. Golgi apparatus membrane
Peripheral membrane protein. Endoplasmic reticulum membrane
Peripheral membrane protein. Found both in the cytosol and associated with membranes. Relocalizatio
Protein Description Functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. [PubMed: 15899849]
Protein Sequence MGTLGKAREAPRKPSHGCRAASKARLEAKPANSPFPSHPSLAHITQFRMMVSLGHLAKGASLDDLIDSCIQSFDADGNLCRSNQLLQVMLTMHRIVISSAELLQKVITLYKDALAKNSPGLCLKICYFVRYWITEFWVMFKMDASLTDTMEEFQELVKAKGEELHCRLIDTTQINARDWSRKLTQRIKSNTSKKRKVSLLFDHLEPEELSEHLTYLEFKSFRRISFSDYQNYLVNSCVKENPTMERSIALCNGISQWVQLMVLSRPTPQLRAEVFIKFIQVAQKLHQLQNFNTLMAVIGGLCHSSISRLKETSSHVPHEINKVLGEMTELLSSSRNYDNYRRAYGECTDFKIPILGVHLKDLISLYEAMPDYLEDGKVNVHKLLALYNHISELVQLQEVAPPLEANKDLVHLLTLSLDLYYTEDEIYELSYAREPRNHRAPPLTPSKPPVVVDWASGVSPKPDPKTISKHVQRMVDSVFKNYDHDQDGYISQEEFEKIAASFPFSFCVMDKDREGLISRDEITAYFMRASSIYSKLGLGFPHNFQETTYLKPTFCDNCAGFLWGVIKQGYRCKDCGMNCHKQCKDLVVFECKKRAKNPVAPTENNTSVGPVSNLCSLGAKDLLHAPEEGPFTFPNGEAVEHGEESKDRTIMLMGVSSQKISLRLKRAVAHKATQTESQPWIGSEGPSGPFVLSSPRKTAQDTLYVLPSPTSPCPSPVLVRKRAFVKWENKDSLIKSKEELRHLRLPTYQELEQEINTLKADNDALKIQLKYAQKKIESLQLEKSNHVLAQMEQGDCS
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
45PhosphorylationHPSLAHITQFRMMVS
CCCHHHHHHHHHHHH		16.28-
82PhosphorylationADGNLCRSNQLLQVM
CCCCCCCHHHHHHHH		28.1227732954
91PhosphorylationQLLQVMLTMHRIVIS
HHHHHHHHHHHHHHC		7.88-
160UbiquitinationFQELVKAKGEELHCR
HHHHHHHHCCEEEEE		62.22-
184PhosphorylationRDWSRKLTQRIKSNT
HHHHHHHHHHHHCCC		20.8823908768
198PhosphorylationTSKKRKVSLLFDHLE
CCCHHHEEEEECCCC		23.5328634298
210PhosphorylationHLEPEELSEHLTYLE
CCCHHHHHHHCCCEE		26.67-
215PhosphorylationELSEHLTYLEFKSFR
HHHHHCCCEEECCCC		15.59-
310UbiquitinationHSSISRLKETSSHVP
HHHHHHHHHHHCCCC		58.81-
314PhosphorylationSRLKETSSHVPHEIN
HHHHHHHCCCCHHHH		35.60-
322UbiquitinationHVPHEINKVLGEMTE
CCCHHHHHHHHHHHH		44.49-
351UbiquitinationYGECTDFKIPILGVH
HCCCCCCCCCEEEEE		50.84-
366PhosphorylationLKDLISLYEAMPDYL
HHHHHHHHHHCCHHH		8.5429759185
377UbiquitinationPDYLEDGKVNVHKLL
CHHHHCCCCCHHHHH		42.85-
444PhosphorylationNHRAPPLTPSKPPVV
CCCCCCCCCCCCCEE		31.1526074081
446PhosphorylationRAPPLTPSKPPVVVD
CCCCCCCCCCCEEEE		53.1926074081
447UbiquitinationAPPLTPSKPPVVVDW
CCCCCCCCCCEEEEC		55.32-
477PhosphorylationHVQRMVDSVFKNYDH
HHHHHHHHHHHCCCC		20.3124719451
480UbiquitinationRMVDSVFKNYDHDQD
HHHHHHHHCCCCCCC		53.06-
489PhosphorylationYDHDQDGYISQEEFE
CCCCCCCCCCHHHHH		12.9928796482
491PhosphorylationHDQDGYISQEEFEKI
CCCCCCCCHHHHHHH		24.0525849741
511UbiquitinationFSFCVMDKDREGLIS
EEEEEECCCCCCCCC		40.36-
518PhosphorylationKDREGLISRDEITAY
CCCCCCCCHHHHHHH		38.4322985185
584UbiquitinationMNCHKQCKDLVVFEC
CCCCHHHCCEEEEEE		52.16-
592UbiquitinationDLVVFECKKRAKNPV
CEEEEEEHHHCCCCC		37.79-
596UbiquitinationFECKKRAKNPVAPTE
EEEHHHCCCCCCCCC		66.86-
620UbiquitinationNLCSLGAKDLLHAPE
HHHHCCCHHHCCCCC		47.30-
646UbiquitinationVEHGEESKDRTIMLM
CCCCCCCCCCEEEEE		55.28-
657PhosphorylationIMLMGVSSQKISLRL
EEEEECCHHHHHHHH		32.84-
661PhosphorylationGVSSQKISLRLKRAV
ECCHHHHHHHHHHHH		17.93-
673PhosphorylationRAVAHKATQTESQPW
HHHHCCCCCCCCCCC		40.6126074081
675PhosphorylationVAHKATQTESQPWIG
HHCCCCCCCCCCCCC		33.0026074081
677PhosphorylationHKATQTESQPWIGSE
CCCCCCCCCCCCCCC		44.9526074081
683PhosphorylationESQPWIGSEGPSGPF
CCCCCCCCCCCCCCE		30.1926074081
687PhosphorylationWIGSEGPSGPFVLSS
CCCCCCCCCCEEECC		70.7029978859
693PhosphorylationPSGPFVLSSPRKTAQ
CCCCEEECCCCCCCC		32.7530576142
694PhosphorylationSGPFVLSSPRKTAQD
CCCEEECCCCCCCCC		25.2717081983
697UbiquitinationFVLSSPRKTAQDTLY
EEECCCCCCCCCEEE		52.15-
698PhosphorylationVLSSPRKTAQDTLYV
EECCCCCCCCCEEEE		30.7226074081
702PhosphorylationPRKTAQDTLYVLPSP
CCCCCCCEEEECCCC		14.1226074081
704PhosphorylationKTAQDTLYVLPSPTS
CCCCCEEEECCCCCC		11.3126074081
708PhosphorylationDTLYVLPSPTSPCPS
CEEEECCCCCCCCCC		36.3328796482
710PhosphorylationLYVLPSPTSPCPSPV
EEECCCCCCCCCCCC		50.0328796482
711PhosphorylationYVLPSPTSPCPSPVL
EECCCCCCCCCCCCE		28.0828796482
715PhosphorylationSPTSPCPSPVLVRKR
CCCCCCCCCCEEECC		34.0628796482
730UbiquitinationAFVKWENKDSLIKSK
CEEEECCCCHHCCCH		36.86-
732PhosphorylationVKWENKDSLIKSKEE
EEECCCCHHCCCHHH		33.3426074081
736PhosphorylationNKDSLIKSKEELRHL
CCCHHCCCHHHHHHC		38.0026074081
747PhosphorylationLRHLRLPTYQELEQE
HHHCCCCCHHHHHHH		42.2926074081
748PhosphorylationRHLRLPTYQELEQEI
HHCCCCCHHHHHHHH		9.6926074081
759UbiquitinationEQEINTLKADNDALK
HHHHHHHHCCCCHHH		52.21-
766UbiquitinationKADNDALKIQLKYAQ
HCCCCHHHHHHHHHH		30.08-
770UbiquitinationDALKIQLKYAQKKIE
CHHHHHHHHHHHHHH		23.36-
775UbiquitinationQLKYAQKKIESLQLE
HHHHHHHHHHHHHHH		39.36-
783UbiquitinationIESLQLEKSNHVLAQ
HHHHHHHHHHCHHHH		66.21-
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
184TPhosphorylationKinasePRKCQQ04759
GPS
184TPhosphorylationKinasePKC-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRP1_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 GRP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GRP1_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
152700Systemic lupus erythematosus (SLE)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GRP1_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-694, AND MASSSPECTROMETRY.
"A diacylglycerol-protein kinase C-RasGRP1 pathway directs Rasactivation upon antigen receptor stimulation of T cells.";
Roose J.P., Mollenauer M., Gupta V.A., Stone J.C., Weiss A.;
Mol. Cell. Biol. 25:4426-4441(2005).
Cited for: FUNCTION, AND PHOSPHORYLATION AT THR-184.
"Phosphorylation of RasGRP3 on threonine 133 provides a mechanisticlink between PKC and Ras signaling systems in B cells.";
Zheng Y., Liu H., Coughlin J.J., Zheng J., Li L., Stone J.C.;
Blood 105:3648-3654(2005).
Cited for: PHOSPHORYLATION AT THR-184 BY PKC.

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