RPGF2_MOUSE - dbPTM
RPGF2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPGF2_MOUSE
UniProt AC Q8CHG7
Protein Name Rap guanine nucleotide exchange factor 2
Gene Name Rapgef2
Organism Mus musculus (Mouse).
Sequence Length 1496
Subcellular Localization Cytoplasm. Cytoplasm, perinuclear region. Cell membrane. Late endosome. Cell junction. Associated with the synaptic plasma membrane. Localized diffusely in the cytoplasm before neuronal growth factor (NGF) stimulation. Recruited to late endosomes aft
Protein Description Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP or not. Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Provides also inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions..
Protein Sequence MKPLAAPANHGVLGQQEKQSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLSDIYQATESEAGDMDLSGLPETAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTDDDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAGTIVLNDGEELDSWSVILNGSVEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEKNMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLLTYRTFLSSPMEVGKKLLEWFNDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENNLEREKMGGHLRLLNIACAAKAKRRLMTLTKPSREAPLPFILLGGSEKGFGIFVDSVDSCSKATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEEKRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKTRISILPQKPYNDIGIGQSQDDSIVGLRQTKHIPAALPVSGTLSSSNPDLLQSHHRILDFSTTPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIREFAVTATPEQYSLCEVSVTPEGVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVEVATQLSMRNFELFRNIEPTEYIDDLFKLKSKTSCANLKKFEEVINQETFWVASEILRETNQLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDLQDLFDPSRNMAKYRNVLSGQNLQPPVIPLFPVIKKDLTFLHEGNDSKVDGLVNFEKLRMIAKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSANATVLDVAQTGGHKKRVRRSSFLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATSTLPKNPGDKKPVKSETSPVAPRAGPQQKVQPQQPLAQPQPPHKVSQGLQVPAVSLYPSRKKVPVKDLPPFGINSPQALKKILSLSEEGSLERHRKQAEDTISNASSQLSSPPTSPQSSPRKGYALALSGTVDNFSDSGHSEISSRSSIVSNSSFDSVPVSLHDERRQRHSVSIVESNLGVGRMERRTLMEPDQYSLGSYAPVSESRGLYAAATVISSPSTEELSHDQGDRASLDAADSGRGSWTSCSSGSHDNIQTIQHQRSWETLPFGHTHFDYSGDAASIWASGGHMDQMMFSDHSTKYNRQNQSRESLEQAQSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSAEAESSSMVPVTTEEAKPVPMPAHIAVTPSTTKGLIARKEGRYREPPPTPPGYVGIPIADFPEGPCHPARKPPDYNVALQRSRMVARPTEAPAPGQTPPAAAASRPGSKPQWHKPSDADPRLAPFQPQGFAGAEEDEDEQVSAV
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
60PhosphorylationDSGSSSLSDIYQATE
CCCCCCHHHHHHHHH
24.7417203969
62PhosphorylationGSSSLSDIYQATESE
CCCCHHHHHHHHHHC
2.1717203969
307PhosphorylationLTYRTFLSSPMEVGK
HHHHHHHCCHHHHHH
28.3617203969
308PhosphorylationTYRTFLSSPMEVGKK
HHHHHHCCHHHHHHH
30.3417203969
418PhosphorylationIFVDSVDSCSKATEA
EEEECHHHCCHHHHH
20.3817203969
420PhosphorylationVDSVDSCSKATEAGL
EECHHHCCHHHHHHH
29.3117203969
460PhosphorylationLRNNTHLSITVKTNL
HHCCCCEEEEEECCH
14.4929472430
462PhosphorylationNNTHLSITVKTNLFV
CCCCEEEEEECCHHH
16.7529472430
478PhosphorylationKELLTRLSEEKRNGA
HHHHHHHCHHHHCCC
40.1829899451
498PhosphorylationIGDIKKASRYSIPDL
CCCHHHHHCCCCCCC
40.4026239621
500PhosphorylationDIKKASRYSIPDLAV
CHHHHHCCCCCCCCC
14.4126239621
501PhosphorylationIKKASRYSIPDLAVD
HHHHHCCCCCCCCCC
26.9126239621
558PhosphorylationNDIGIGQSQDDSIVG
CCCCCCCCCCCCCCC
30.2929899451
579PhosphorylationIPAALPVSGTLSSSN
CCCCCCCCCCCCCCC
24.9125619855
581PhosphorylationAALPVSGTLSSSNPD
CCCCCCCCCCCCCHH
18.8925619855
583PhosphorylationLPVSGTLSSSNPDLL
CCCCCCCCCCCHHHH
31.4025619855
584PhosphorylationPVSGTLSSSNPDLLQ
CCCCCCCCCCHHHHH
36.9322324799
585PhosphorylationVSGTLSSSNPDLLQS
CCCCCCCCCHHHHHH
49.3527087446
592PhosphorylationSNPDLLQSHHRILDF
CCHHHHHHCCEECCC
22.6425619855
600PhosphorylationHHRILDFSTTPDLPD
CCEECCCCCCCCCCH
30.9129899451
601PhosphorylationHRILDFSTTPDLPDQ
CEECCCCCCCCCCHH
42.2020415495
602PhosphorylationRILDFSTTPDLPDQV
EECCCCCCCCCCHHH
17.3820415495
619PhosphorylationVFKADQQSRYIMISK
HHEHHCCCCEEEEEC
22.78-
621PhosphorylationKADQQSRYIMISKDT
EHHCCCCEEEEECCC
10.49-
644PhosphorylationAIREFAVTATPEQYS
HHHHHCCCCCHHHCC
22.76-
698PhosphorylationMETETLCSDEDAQEL
CCCCEECCHHHHHHH
47.3429899451
806PhosphorylationRECKNFNSMFAIISG
HHCCCHHHHHHHHHC
15.90-
930PhosphorylationTRKKKWRSLGSLSQG
CCCHHHHHHCCCCCC
35.6525521595
933PhosphorylationKKWRSLGSLSQGSAN
HHHHHHCCCCCCCCC
30.0925521595
935PhosphorylationWRSLGSLSQGSANAT
HHHHCCCCCCCCCCE
33.9028066266
938PhosphorylationLGSLSQGSANATVLD
HCCCCCCCCCCEEEH
15.6528066266
942PhosphorylationSQGSANATVLDVAQT
CCCCCCCEEEHHHHH
22.7826804993
959PhosphorylationHKKRVRRSSFLNAKK
CHHHHCHHHCCCHHH
18.1925521595
960PhosphorylationKKRVRRSSFLNAKKL
HHHHCHHHCCCHHHH
31.7625521595
980PhosphorylationMARKVKQYLSNLELE
HHHHHHHHHHHCCCC
13.3322802335
982PhosphorylationRKVKQYLSNLELEMD
HHHHHHHHHCCCCCC
34.1422802335
992PhosphorylationELEMDEESLQTLSLQ
CCCCCHHHHHHHEEE
24.5922802335
995PhosphorylationMDEESLQTLSLQCEP
CCHHHHHHHEEEEEE
24.4922802335
1019PhosphorylationGDKKPVKSETSPVAP
CCCCCCCCCCCCCCC
46.4725521595
1021PhosphorylationKKPVKSETSPVAPRA
CCCCCCCCCCCCCCC
45.4827742792
1022PhosphorylationKPVKSETSPVAPRAG
CCCCCCCCCCCCCCC
17.2125521595
1061PhosphorylationQVPAVSLYPSRKKVP
CCCEEEECCCCCCCC
7.5229514104
1079PhosphorylationLPPFGINSPQALKKI
CCCCCCCCHHHHHHH
19.2327087446
1088PhosphorylationQALKKILSLSEEGSL
HHHHHHHCCCCCCCH
33.0726239621
1090PhosphorylationLKKILSLSEEGSLER
HHHHHCCCCCCCHHH
30.1726824392
1094PhosphorylationLSLSEEGSLERHRKQ
HCCCCCCCHHHHHHH
30.2723527152
1105PhosphorylationHRKQAEDTISNASSQ
HHHHHHHHHHHHHHH
20.1526643407
1107PhosphorylationKQAEDTISNASSQLS
HHHHHHHHHHHHHHC
28.5623737553
1110PhosphorylationEDTISNASSQLSSPP
HHHHHHHHHHHCCCC
23.9127087446
1111PhosphorylationDTISNASSQLSSPPT
HHHHHHHHHHCCCCC
32.5027087446
1114PhosphorylationSNASSQLSSPPTSPQ
HHHHHHHCCCCCCCC
32.9125521595
1115PhosphorylationNASSQLSSPPTSPQS
HHHHHHCCCCCCCCC
43.4125521595
1118PhosphorylationSQLSSPPTSPQSSPR
HHHCCCCCCCCCCCC
57.3227087446
1119PhosphorylationQLSSPPTSPQSSPRK
HHCCCCCCCCCCCCC
27.0725521595
1122PhosphorylationSPPTSPQSSPRKGYA
CCCCCCCCCCCCCEE
45.7723737553
1123PhosphorylationPPTSPQSSPRKGYAL
CCCCCCCCCCCCEEE
24.3923737553
1128PhosphorylationQSSPRKGYALALSGT
CCCCCCCEEEEEECE
11.0729514104
1151PhosphorylationHSEISSRSSIVSNSS
CCCCCCCCCCCCCCC
26.7725338131
1152PhosphorylationSEISSRSSIVSNSSF
CCCCCCCCCCCCCCC
26.3726370283
1155PhosphorylationSSRSSIVSNSSFDSV
CCCCCCCCCCCCCCC
29.3526370283
1157PhosphorylationRSSIVSNSSFDSVPV
CCCCCCCCCCCCCCC
25.5229550500
1158PhosphorylationSSIVSNSSFDSVPVS
CCCCCCCCCCCCCCC
37.0130372032
1165O-linked_GlycosylationSFDSVPVSLHDERRQ
CCCCCCCCCCHHHHH
17.5722517741
1175PhosphorylationDERRQRHSVSIVESN
HHHHHHCCEEEECCC
21.5419060867
1177PhosphorylationRRQRHSVSIVESNLG
HHHHCCEEEECCCCC
24.7519060867
1200PhosphorylationLMEPDQYSLGSYAPV
CCCCCCCCCCCCCCC
22.1829514104
1221PhosphorylationYAAATVISSPSTEEL
EEEEEEEECCCHHHH
31.6829899451
1222PhosphorylationAAATVISSPSTEELS
EEEEEEECCCHHHHC
16.2529899451
1224PhosphorylationATVISSPSTEELSHD
EEEEECCCHHHHCCC
50.8529899451
1225PhosphorylationTVISSPSTEELSHDQ
EEEECCCHHHHCCCC
36.5429899451
1229PhosphorylationSPSTEELSHDQGDRA
CCCHHHHCCCCCCCH
28.4429899451
1237PhosphorylationHDQGDRASLDAADSG
CCCCCCHHCCHHHCC
27.8929899451
1247PhosphorylationAADSGRGSWTSCSSG
HHHCCCCCCCCCCCC
26.3125777480
1249PhosphorylationDSGRGSWTSCSSGSH
HCCCCCCCCCCCCCC
22.8925777480
1250PhosphorylationSGRGSWTSCSSGSHD
CCCCCCCCCCCCCCC
13.0225777480
1252PhosphorylationRGSWTSCSSGSHDNI
CCCCCCCCCCCCCCC
37.1826643407
1253PhosphorylationGSWTSCSSGSHDNIQ
CCCCCCCCCCCCCCC
48.9526643407
1255PhosphorylationWTSCSSGSHDNIQTI
CCCCCCCCCCCCCEE
29.6126643407
1261PhosphorylationGSHDNIQTIQHQRSW
CCCCCCCEEEECCCC
20.8625367039
1312PhosphorylationKYNRQNQSRESLEQA
HHHHCHHCHHHHHHH
45.6329899451
1315PhosphorylationRQNQSRESLEQAQSR
HCHHCHHHHHHHHHH
35.7829899451
1324PhosphorylationEQAQSRASWASSTGY
HHHHHHHHHHHHCCC
23.2826643407
1327PhosphorylationQSRASWASSTGYWGE
HHHHHHHHHCCCCCC
23.3626643407
1328PhosphorylationSRASWASSTGYWGED
HHHHHHHHCCCCCCC
20.3625338131
1331PhosphorylationSWASSTGYWGEDSEG
HHHHHCCCCCCCCCC
15.4425338131
1336PhosphorylationTGYWGEDSEGDTGTI
CCCCCCCCCCCCCCE
38.8929899451
1340PhosphorylationGEDSEGDTGTIKRRG
CCCCCCCCCCEEECC
47.27-
1342PhosphorylationDSEGDTGTIKRRGGK
CCCCCCCCEEECCCC
25.97-
1364O-linked_GlycosylationSSSMVPVTTEEAKPV
CCCCCCCCCCCCCCC
23.5522517741
1365O-linked_GlycosylationSSMVPVTTEEAKPVP
CCCCCCCCCCCCCCC
31.8722517741
1401PhosphorylationRYREPPPTPPGYVGI
CCCCCCCCCCCCCCC
48.1421659605
1427PhosphorylationPARKPPDYNVALQRS
CCCCCCCCCHHHHHC
19.8129514104
1449PhosphorylationEAPAPGQTPPAAAAS
CCCCCCCCCCHHHHC
36.8428066266

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
644TPhosphorylationKinasePLK2P53351
Uniprot
806SPhosphorylationKinasePLK2P53351
Uniprot
933SPhosphorylationKinasePLK2P53351
Uniprot
1022SPhosphorylationKinasePLK2P53351
Uniprot
1175SPhosphorylationKinasePLK2P53351
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPGF2_MOUSE !!

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 RPGF2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RPGF2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RPGF2_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418 AND SER-420, ANDMASS SPECTROMETRY.

TOP