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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
60 | Phosphorylation | DSGSSSLSDIYQATE CCCCCCHHHHHHHHH | 24.74 | 17203969 | |
62 | Phosphorylation | GSSSLSDIYQATESE CCCCHHHHHHHHHHC | 2.17 | 17203969 | |
307 | Phosphorylation | LTYRTFLSSPMEVGK HHHHHHHCCHHHHHH | 28.36 | 17203969 | |
308 | Phosphorylation | TYRTFLSSPMEVGKK HHHHHHCCHHHHHHH | 30.34 | 17203969 | |
418 | Phosphorylation | IFVDSVDSCSKATEA EEEECHHHCCHHHHH | 20.38 | 17203969 | |
420 | Phosphorylation | VDSVDSCSKATEAGL EECHHHCCHHHHHHH | 29.31 | 17203969 | |
460 | Phosphorylation | LRNNTHLSITVKTNL HHCCCCEEEEEECCH | 14.49 | 29472430 | |
462 | Phosphorylation | NNTHLSITVKTNLFV CCCCEEEEEECCHHH | 16.75 | 29472430 | |
478 | Phosphorylation | KELLTRLSEEKRNGA HHHHHHHCHHHHCCC | 40.18 | 29899451 | |
498 | Phosphorylation | IGDIKKASRYSIPDL CCCHHHHHCCCCCCC | 40.40 | 26239621 | |
500 | Phosphorylation | DIKKASRYSIPDLAV CHHHHHCCCCCCCCC | 14.41 | 26239621 | |
501 | Phosphorylation | IKKASRYSIPDLAVD HHHHHCCCCCCCCCC | 26.91 | 26239621 | |
558 | Phosphorylation | NDIGIGQSQDDSIVG CCCCCCCCCCCCCCC | 30.29 | 29899451 | |
579 | Phosphorylation | IPAALPVSGTLSSSN CCCCCCCCCCCCCCC | 24.91 | 25619855 | |
581 | Phosphorylation | AALPVSGTLSSSNPD CCCCCCCCCCCCCHH | 18.89 | 25619855 | |
583 | Phosphorylation | LPVSGTLSSSNPDLL CCCCCCCCCCCHHHH | 31.40 | 25619855 | |
584 | Phosphorylation | PVSGTLSSSNPDLLQ CCCCCCCCCCHHHHH | 36.93 | 22324799 | |
585 | Phosphorylation | VSGTLSSSNPDLLQS CCCCCCCCCHHHHHH | 49.35 | 27087446 | |
592 | Phosphorylation | SNPDLLQSHHRILDF CCHHHHHHCCEECCC | 22.64 | 25619855 | |
600 | Phosphorylation | HHRILDFSTTPDLPD CCEECCCCCCCCCCH | 30.91 | 29899451 | |
601 | Phosphorylation | HRILDFSTTPDLPDQ CEECCCCCCCCCCHH | 42.20 | 20415495 | |
602 | Phosphorylation | RILDFSTTPDLPDQV EECCCCCCCCCCHHH | 17.38 | 20415495 | |
619 | Phosphorylation | VFKADQQSRYIMISK HHEHHCCCCEEEEEC | 22.78 | - | |
621 | Phosphorylation | KADQQSRYIMISKDT EHHCCCCEEEEECCC | 10.49 | - | |
644 | Phosphorylation | AIREFAVTATPEQYS HHHHHCCCCCHHHCC | 22.76 | - | |
698 | Phosphorylation | METETLCSDEDAQEL CCCCEECCHHHHHHH | 47.34 | 29899451 | |
806 | Phosphorylation | RECKNFNSMFAIISG HHCCCHHHHHHHHHC | 15.90 | - | |
930 | Phosphorylation | TRKKKWRSLGSLSQG CCCHHHHHHCCCCCC | 35.65 | 25521595 | |
933 | Phosphorylation | KKWRSLGSLSQGSAN HHHHHHCCCCCCCCC | 30.09 | 25521595 | |
935 | Phosphorylation | WRSLGSLSQGSANAT HHHHCCCCCCCCCCE | 33.90 | 28066266 | |
938 | Phosphorylation | LGSLSQGSANATVLD HCCCCCCCCCCEEEH | 15.65 | 28066266 | |
942 | Phosphorylation | SQGSANATVLDVAQT CCCCCCCEEEHHHHH | 22.78 | 26804993 | |
959 | Phosphorylation | HKKRVRRSSFLNAKK CHHHHCHHHCCCHHH | 18.19 | 25521595 | |
960 | Phosphorylation | KKRVRRSSFLNAKKL HHHHCHHHCCCHHHH | 31.76 | 25521595 | |
980 | Phosphorylation | MARKVKQYLSNLELE HHHHHHHHHHHCCCC | 13.33 | 22802335 | |
982 | Phosphorylation | RKVKQYLSNLELEMD HHHHHHHHHCCCCCC | 34.14 | 22802335 | |
992 | Phosphorylation | ELEMDEESLQTLSLQ CCCCCHHHHHHHEEE | 24.59 | 22802335 | |
995 | Phosphorylation | MDEESLQTLSLQCEP CCHHHHHHHEEEEEE | 24.49 | 22802335 | |
1019 | Phosphorylation | GDKKPVKSETSPVAP CCCCCCCCCCCCCCC | 46.47 | 25521595 | |
1021 | Phosphorylation | KKPVKSETSPVAPRA CCCCCCCCCCCCCCC | 45.48 | 27742792 | |
1022 | Phosphorylation | KPVKSETSPVAPRAG CCCCCCCCCCCCCCC | 17.21 | 25521595 | |
1061 | Phosphorylation | QVPAVSLYPSRKKVP CCCEEEECCCCCCCC | 7.52 | 29514104 | |
1079 | Phosphorylation | LPPFGINSPQALKKI CCCCCCCCHHHHHHH | 19.23 | 27087446 | |
1088 | Phosphorylation | QALKKILSLSEEGSL HHHHHHHCCCCCCCH | 33.07 | 26239621 | |
1090 | Phosphorylation | LKKILSLSEEGSLER HHHHHCCCCCCCHHH | 30.17 | 26824392 | |
1094 | Phosphorylation | LSLSEEGSLERHRKQ HCCCCCCCHHHHHHH | 30.27 | 23527152 | |
1105 | Phosphorylation | HRKQAEDTISNASSQ HHHHHHHHHHHHHHH | 20.15 | 26643407 | |
1107 | Phosphorylation | KQAEDTISNASSQLS HHHHHHHHHHHHHHC | 28.56 | 23737553 | |
1110 | Phosphorylation | EDTISNASSQLSSPP HHHHHHHHHHHCCCC | 23.91 | 27087446 | |
1111 | Phosphorylation | DTISNASSQLSSPPT HHHHHHHHHHCCCCC | 32.50 | 27087446 | |
1114 | Phosphorylation | SNASSQLSSPPTSPQ HHHHHHHCCCCCCCC | 32.91 | 25521595 | |
1115 | Phosphorylation | NASSQLSSPPTSPQS HHHHHHCCCCCCCCC | 43.41 | 25521595 | |
1118 | Phosphorylation | SQLSSPPTSPQSSPR HHHCCCCCCCCCCCC | 57.32 | 27087446 | |
1119 | Phosphorylation | QLSSPPTSPQSSPRK HHCCCCCCCCCCCCC | 27.07 | 25521595 | |
1122 | Phosphorylation | SPPTSPQSSPRKGYA CCCCCCCCCCCCCEE | 45.77 | 23737553 | |
1123 | Phosphorylation | PPTSPQSSPRKGYAL CCCCCCCCCCCCEEE | 24.39 | 23737553 | |
1128 | Phosphorylation | QSSPRKGYALALSGT CCCCCCCEEEEEECE | 11.07 | 29514104 | |
1151 | Phosphorylation | HSEISSRSSIVSNSS CCCCCCCCCCCCCCC | 26.77 | 25338131 | |
1152 | Phosphorylation | SEISSRSSIVSNSSF CCCCCCCCCCCCCCC | 26.37 | 26370283 | |
1155 | Phosphorylation | SSRSSIVSNSSFDSV CCCCCCCCCCCCCCC | 29.35 | 26370283 | |
1157 | Phosphorylation | RSSIVSNSSFDSVPV CCCCCCCCCCCCCCC | 25.52 | 29550500 | |
1158 | Phosphorylation | SSIVSNSSFDSVPVS CCCCCCCCCCCCCCC | 37.01 | 30372032 | |
1165 | O-linked_Glycosylation | SFDSVPVSLHDERRQ CCCCCCCCCCHHHHH | 17.57 | 22517741 | |
1175 | Phosphorylation | DERRQRHSVSIVESN HHHHHHCCEEEECCC | 21.54 | 19060867 | |
1177 | Phosphorylation | RRQRHSVSIVESNLG HHHHCCEEEECCCCC | 24.75 | 19060867 | |
1200 | Phosphorylation | LMEPDQYSLGSYAPV CCCCCCCCCCCCCCC | 22.18 | 29514104 | |
1221 | Phosphorylation | YAAATVISSPSTEEL EEEEEEEECCCHHHH | 31.68 | 29899451 | |
1222 | Phosphorylation | AAATVISSPSTEELS EEEEEEECCCHHHHC | 16.25 | 29899451 | |
1224 | Phosphorylation | ATVISSPSTEELSHD EEEEECCCHHHHCCC | 50.85 | 29899451 | |
1225 | Phosphorylation | TVISSPSTEELSHDQ EEEECCCHHHHCCCC | 36.54 | 29899451 | |
1229 | Phosphorylation | SPSTEELSHDQGDRA CCCHHHHCCCCCCCH | 28.44 | 29899451 | |
1237 | Phosphorylation | HDQGDRASLDAADSG CCCCCCHHCCHHHCC | 27.89 | 29899451 | |
1247 | Phosphorylation | AADSGRGSWTSCSSG HHHCCCCCCCCCCCC | 26.31 | 25777480 | |
1249 | Phosphorylation | DSGRGSWTSCSSGSH HCCCCCCCCCCCCCC | 22.89 | 25777480 | |
1250 | Phosphorylation | SGRGSWTSCSSGSHD CCCCCCCCCCCCCCC | 13.02 | 25777480 | |
1252 | Phosphorylation | RGSWTSCSSGSHDNI CCCCCCCCCCCCCCC | 37.18 | 26643407 | |
1253 | Phosphorylation | GSWTSCSSGSHDNIQ CCCCCCCCCCCCCCC | 48.95 | 26643407 | |
1255 | Phosphorylation | WTSCSSGSHDNIQTI CCCCCCCCCCCCCEE | 29.61 | 26643407 | |
1261 | Phosphorylation | GSHDNIQTIQHQRSW CCCCCCCEEEECCCC | 20.86 | 25367039 | |
1312 | Phosphorylation | KYNRQNQSRESLEQA HHHHCHHCHHHHHHH | 45.63 | 29899451 | |
1315 | Phosphorylation | RQNQSRESLEQAQSR HCHHCHHHHHHHHHH | 35.78 | 29899451 | |
1324 | Phosphorylation | EQAQSRASWASSTGY HHHHHHHHHHHHCCC | 23.28 | 26643407 | |
1327 | Phosphorylation | QSRASWASSTGYWGE HHHHHHHHHCCCCCC | 23.36 | 26643407 | |
1328 | Phosphorylation | SRASWASSTGYWGED HHHHHHHHCCCCCCC | 20.36 | 25338131 | |
1331 | Phosphorylation | SWASSTGYWGEDSEG HHHHHCCCCCCCCCC | 15.44 | 25338131 | |
1336 | Phosphorylation | TGYWGEDSEGDTGTI CCCCCCCCCCCCCCE | 38.89 | 29899451 | |
1340 | Phosphorylation | GEDSEGDTGTIKRRG CCCCCCCCCCEEECC | 47.27 | - | |
1342 | Phosphorylation | DSEGDTGTIKRRGGK CCCCCCCCEEECCCC | 25.97 | - | |
1364 | O-linked_Glycosylation | SSSMVPVTTEEAKPV CCCCCCCCCCCCCCC | 23.55 | 22517741 | |
1365 | O-linked_Glycosylation | SSMVPVTTEEAKPVP CCCCCCCCCCCCCCC | 31.87 | 22517741 | |
1401 | Phosphorylation | RYREPPPTPPGYVGI CCCCCCCCCCCCCCC | 48.14 | 21659605 | |
1427 | Phosphorylation | PARKPPDYNVALQRS CCCCCCCCCHHHHHC | 19.81 | 29514104 | |
1449 | Phosphorylation | EAPAPGQTPPAAAAS CCCCCCCCCCHHHHC | 36.84 | 28066266 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
644 | T | Phosphorylation | Kinase | PLK2 | P53351 | Uniprot |
806 | S | Phosphorylation | Kinase | PLK2 | P53351 | Uniprot |
933 | S | Phosphorylation | Kinase | PLK2 | P53351 | Uniprot |
1022 | S | Phosphorylation | Kinase | PLK2 | P53351 | Uniprot |
1175 | S | Phosphorylation | Kinase | PLK2 | P53351 | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPGF2_MOUSE !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of RPGF2_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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. |