RGL2_HUMAN - dbPTM
RGL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGL2_HUMAN
UniProt AC O15211
Protein Name Ral guanine nucleotide dissociation stimulator-like 2
Gene Name RGL2
Organism Homo sapiens (Human).
Sequence Length 777
Subcellular Localization
Protein Description Probable guanine nucleotide exchange factor. Putative effector of Ras and/or Rap. Associates with the GTP-bound form of Rap 1A and H-Ras in vitro (By similarity)..
Protein Sequence MLPRPLRLLLDTSPPGGVVLSSFRSRDPEEGGGPGGLVVGGGQEEEEEEEEEAPVSVWDEEEDGAVFTVTSRQYRPLDPLVPMPPPRSSRRLRAGTLEALVRHLLDTRTSGTDVSFMSAFLATHRAFTSTPALLGLMADRLEALESHPTDELERTTEVAISVLSTWLASHPEDFGSEAKGQLDRLESFLLQTGYAAGKGVGGGSADLIRNLRSRVDPQAPDLPKPLALPGDPPADPTDVLVFLADHLAEQLTLLDAELFLNLIPSQCLGGLWGHRDRPGHSHLCPSVRATVTQFNKVAGAVVSSVLGATSTGEGPGEVTIRPLRPPQRARLLEKWIRVAEECRLLRNFSSVYAVVSALQSSPIHRLRAAWGEATRDSLRVFSSLCQIFSEEDNYSQSRELLVQEVKLQSPLEPHSKKAPRSGSRGGGVVPYLGTFLKDLVMLDAASKDELENGYINFDKRRKEFAVLSELRRLQNECRGYNLQPDHDIQRWLQGLRPLTEAQSHRVSCEVEPPGSSDPPAPRVLRPTLVISQWTEVLGSVGVPTPLVSCDRPSTGGDEAPTTPAPLLTRLAQHMKWPSVSSLDSALESSPSLHSPADPSHLSPPASSPRPSRGHRRSASCGSPLSGGAEEASGGTGYGGEGSGPGASDCRIIRVQMELGEDGSVYKSILVTSQDKAPSVISRVLKKNNRDSAVASEYELVQLLPGERELTIPASANVFYAMDGASHDFLLRQRRRSSTATPGVTSGPSASGTPPSEGGGGSFPRIKATGRKIARALF
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
12PhosphorylationPLRLLLDTSPPGGVV
CEEEEECCCCCCCEE
43.0029255136
13PhosphorylationLRLLLDTSPPGGVVL
EEEEECCCCCCCEEE
28.8529255136
21PhosphorylationPPGGVVLSSFRSRDP
CCCCEEEEEECCCCC
18.8023403867
22PhosphorylationPGGVVLSSFRSRDPE
CCCEEEEEECCCCCC
22.1023403867
25PhosphorylationVVLSSFRSRDPEEGG
EEEEEECCCCCCCCC
38.7420068231
116UbiquitinationTSGTDVSFMSAFLAT
CCCCCHHHHHHHHHH
4.5021906983
187PhosphorylationGQLDRLESFLLQTGY
HHHHHHHHHHHHHCC
26.2827499020
194PhosphorylationSFLLQTGYAAGKGVG
HHHHHHCCCCCCCCC
9.1827642862
198UbiquitinationQTGYAAGKGVGGGSA
HHCCCCCCCCCCCHH
45.7721906983
356PhosphorylationSSVYAVVSALQSSPI
CHHHHHHHHHHCCHH
19.3628348404
360PhosphorylationAVVSALQSSPIHRLR
HHHHHHHCCHHHHHH
38.6428348404
361PhosphorylationVVSALQSSPIHRLRA
HHHHHHCCHHHHHHH
18.2128348404
394PhosphorylationIFSEEDNYSQSRELL
HHCCCCCCHHHHHHH
22.0227642862
409PhosphorylationVQEVKLQSPLEPHSK
HHHHHCCCCCCCCCC
41.7225159151
415PhosphorylationQSPLEPHSKKAPRSG
CCCCCCCCCCCCCCC
46.7123403867
431PhosphorylationRGGGVVPYLGTFLKD
CCCCCHHCHHHHHHH
13.22-
434PhosphorylationGVVPYLGTFLKDLVM
CCHHCHHHHHHHHHH
24.1718491316
446PhosphorylationLVMLDAASKDELENG
HHHHCCCCHHHHHHC
42.2218491316
454PhosphorylationKDELENGYINFDKRR
HHHHHHCCCCCHHHH
12.31-
459UbiquitinationNGYINFDKRRKEFAV
HCCCCCHHHHHHHHH
50.38-
515PhosphorylationCEVEPPGSSDPPAPR
EEECCCCCCCCCCCC
37.0221815630
516PhosphorylationEVEPPGSSDPPAPRV
EECCCCCCCCCCCCC
61.1121815630
561PhosphorylationTGGDEAPTTPAPLLT
CCCCCCCCCCHHHHH
53.0825850435
562PhosphorylationGGDEAPTTPAPLLTR
CCCCCCCCCHHHHHH
19.1826657352
568PhosphorylationTTPAPLLTRLAQHMK
CCCHHHHHHHHHHCC
31.1825850435
578PhosphorylationAQHMKWPSVSSLDSA
HHHCCCCCHHHHHHH
33.2526657352
580PhosphorylationHMKWPSVSSLDSALE
HCCCCCHHHHHHHHH
29.5327732954
581PhosphorylationMKWPSVSSLDSALES
CCCCCHHHHHHHHHH
33.7627732954
584PhosphorylationPSVSSLDSALESSPS
CCHHHHHHHHHHCCC
39.7929116813
588PhosphorylationSLDSALESSPSLHSP
HHHHHHHHCCCCCCC
48.6927732954
589PhosphorylationLDSALESSPSLHSPA
HHHHHHHCCCCCCCC
14.7727732954
591PhosphorylationSALESSPSLHSPADP
HHHHHCCCCCCCCCH
40.4327732954
594PhosphorylationESSPSLHSPADPSHL
HHCCCCCCCCCHHHC
27.3827732954
599PhosphorylationLHSPADPSHLSPPAS
CCCCCCHHHCCCCCC
37.2927732954
602PhosphorylationPADPSHLSPPASSPR
CCCHHHCCCCCCCCC
24.3425921289
606PhosphorylationSHLSPPASSPRPSRG
HHCCCCCCCCCCCCC
46.8027732954
607PhosphorylationHLSPPASSPRPSRGH
HCCCCCCCCCCCCCC
27.3427732954
611PhosphorylationPASSPRPSRGHRRSA
CCCCCCCCCCCCCCC
52.7729116813
617PhosphorylationPSRGHRRSASCGSPL
CCCCCCCCCCCCCCC
25.2123401153
619PhosphorylationRGHRRSASCGSPLSG
CCCCCCCCCCCCCCC
21.9123927012
622PhosphorylationRRSASCGSPLSGGAE
CCCCCCCCCCCCCCC
27.3123927012
625PhosphorylationASCGSPLSGGAEEAS
CCCCCCCCCCCCCCC
38.2728450419
632PhosphorylationSGGAEEASGGTGYGG
CCCCCCCCCCCCCCC
40.8228450419
635PhosphorylationAEEASGGTGYGGEGS
CCCCCCCCCCCCCCC
30.6523927012
637PhosphorylationEASGGTGYGGEGSGP
CCCCCCCCCCCCCCC
23.0723927012
671PhosphorylationVYKSILVTSQDKAPS
EEEEEEEECCCCCHH
19.7529214152
672PhosphorylationYKSILVTSQDKAPSV
EEEEEEECCCCCHHH
28.9821815630
697PhosphorylationDSAVASEYELVQLLP
CCCHHCHHHHHHCCC
16.4527642862
736PhosphorylationLLRQRRRSSTATPGV
HHHHHHHCCCCCCCC
30.1727251789
737PhosphorylationLRQRRRSSTATPGVT
HHHHHHCCCCCCCCC
21.9026657352
738PhosphorylationRQRRRSSTATPGVTS
HHHHHCCCCCCCCCC
35.4826657352
740PhosphorylationRRRSSTATPGVTSGP
HHHCCCCCCCCCCCC
22.2122199227
744PhosphorylationSTATPGVTSGPSASG
CCCCCCCCCCCCCCC
33.6022199227
745PhosphorylationTATPGVTSGPSASGT
CCCCCCCCCCCCCCC
46.4222199227
748PhosphorylationPGVTSGPSASGTPPS
CCCCCCCCCCCCCCC
38.2922199227
750PhosphorylationVTSGPSASGTPPSEG
CCCCCCCCCCCCCCC
47.7622199227
752PhosphorylationSGPSASGTPPSEGGG
CCCCCCCCCCCCCCC
29.5426657352
755PhosphorylationSASGTPPSEGGGGSF
CCCCCCCCCCCCCCC
50.5030175587
761PhosphorylationPSEGGGGSFPRIKAT
CCCCCCCCCHHHHHC
35.0425850435
768PhosphorylationSFPRIKATGRKIARA
CCHHHHHCHHHHHHH
32.3022210691

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
737SPhosphorylationKinasePKA-FAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGL2_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 RGL2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAP1B_HUMANRAP1Bphysical
8939933
CC90B_HUMANCCDC90Bphysical
16169070
KAT5_HUMANKAT5physical
16169070
KAT7_HUMANKAT7physical
16169070
U119A_HUMANUNC119physical
16169070
DPYL1_HUMANCRMP1physical
16169070
EF1G_HUMANEEF1Gphysical
16169070
RAC1_HUMANRAC1physical
8939933
RALA_HUMANRALAphysical
8939933
RASH_HUMANHRASphysical
8939933
NT2NL_HUMANNOTCH2NLphysical
25416956

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 RGL2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-13, AND MASSSPECTROMETRY.

TOP