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Rap guanine nucleotide exchange factor 2 (Cyclic nucleotide ras GEF) (CNrasGEF) (Neural RAP guanine nucleotide exchange protein) (nRap GEP) (PDZ domain-containing guanine nucleotide exchange factor 1) (PDZ-GEF1) (RA-GEF-1) (Ras/Rap1-associating GEF-1)

 RPGF2_HUMAN             Reviewed;        1499 AA.
Q9Y4G8; D3DP27;
29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
22-NOV-2017, entry version 156.
RecName: Full=Rap guanine nucleotide exchange factor 2;
AltName: Full=Cyclic nucleotide ras GEF;
Short=CNrasGEF;
AltName: Full=Neural RAP guanine nucleotide exchange protein;
Short=nRap GEP;
AltName: Full=PDZ domain-containing guanine nucleotide exchange factor 1;
Short=PDZ-GEF1;
AltName: Full=RA-GEF-1;
AltName: Full=Ras/Rap1-associating GEF-1;
Name=RAPGEF2; Synonyms=KIAA0313, NRAPGEP, PDZGEF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain {ECO:0000269|PubMed:9205841};
PubMed=9205841; DOI=10.1093/dnares/4.2.141;
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 4:141-150(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, AND INTERACTION WITH MAGI2.
PubMed=10548487; DOI=10.1006/bbrc.1999.1619;
Ohtsuka T., Hata Y., Ide N., Yasuda T., Inoue E., Inoue T.,
Mizoguchi A., Takai Y.;
"nRap GEP: a novel neural GDP/GTP exchange protein for rap1 small G
protein that interacts with synaptic scaffolding molecule (S-SCAM).";
Biochem. Biophys. Res. Commun. 265:38-44(1999).
[4]
FUNCTION, AND INTERACTION WITH HRAS AND RAP1A.
PubMed=10608844; DOI=10.1074/jbc.274.53.37815;
Liao Y., Kariya K., Hu C.-D., Shibatohge M., Goshima M., Okada T.,
Watari Y., Gao X., Jin T.-G., Yamawaki-Kataoka Y., Kataoka T.;
"RA-GEF, a novel Rap1A guanine nucleotide exchange factor containing a
Ras/Rap1A-associating domain, is conserved between nematode and
humans.";
J. Biol. Chem. 274:37815-37820(1999).
[5] {ECO:0000305}
FUNCTION.
PubMed=10608883; DOI=10.1074/jbc.274.53.38125;
de Rooij J., Boenink N.M., van Triest M., Cool R.H., Wittinghofer A.,
Bos J.L.;
"PDZ-GEF1, a guanine nucleotide exchange factor specific for Rap1 and
Rap2.";
J. Biol. Chem. 274:38125-38130(1999).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-211; ARG-215;
396-PRO--PHE-399 AND 1497-SER-VAL-1499.
PubMed=10801446; DOI=10.1016/S0960-9822(00)00473-5;
Pham N., Cheglakov I., Koch C.A., de Hoog C.L., Moran M.F., Rotin D.;
"The guanine nucleotide exchange factor CNrasGEF activates ras in
response to cAMP and cGMP.";
Curr. Biol. 10:555-558(2000).
[7]
INTERACTION WITH MAGI1, AND TISSUE SPECIFICITY.
PubMed=11168587; DOI=10.1046/j.1365-2443.2000.00385.x;
Mino A., Ohtsuka T., Inoue E., Takai Y.;
"Membrane-associated guanylate kinase with inverted orientation
(MAGI)-1/brain angiogenesis inhibitor 1-associated protein (BAP1) as a
scaffolding molecule for Rap small G protein GDP/GTP exchange protein
at tight junctions.";
Genes Cells 5:1009-1016(2000).
[8] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10934204; DOI=10.1074/jbc.M005327200;
Rebhun J.F., Castro A.F., Quilliam L.A.;
"Identification of guanine nucleotide exchange factors (GEFs) for the
Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction.";
J. Biol. Chem. 275:34901-34908(2000).
[9]
FUNCTION, INTERACTION WITH RAP1A, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 606-PRO--LYS-626.
PubMed=11359771; DOI=10.1074/jbc.M101737200;
Liao Y., Satoh T., Gao X., Jin T.G., Hu C.D., Kataoka T.;
"RA-GEF-1, a guanine nucleotide exchange factor for Rap1, is activated
by translocation induced by association with Rap1*GTP and enhances
Rap1-dependent B-Raf activation.";
J. Biol. Chem. 276:28478-28483(2001).
[10]
INTERACTION WITH HRAS AND NEDD4, UBIQUITINATION BY NEDD4, AND
MUTAGENESIS OF ARG-898; TYR-1406 AND TYR-1428.
PubMed=11598133; DOI=10.1074/jbc.M108373200;
Pham N., Rotin D.;
"Nedd4 regulates ubiquitination and stability of the guanine-
nucleotide exchange factor CNrasGEF.";
J. Biol. Chem. 276:46995-47003(2001).
[11]
FUNCTION, AND INTERACTION WITH ADRB1.
PubMed=12391161; DOI=10.1128/MCB.22.22.7942-7952.2002;
Pak Y., Pham N., Rotin D.;
"Direct binding of the beta1 adrenergic receptor to the cyclic AMP-
dependent guanine nucleotide exchange factor CNrasGEF leads to Ras
activation.";
Mol. Cell. Biol. 22:7942-7952(2002).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
FUNCTION.
PubMed=16272156; DOI=10.1074/jbc.M507595200;
Amsen E.M., Pham N., Pak Y., Rotin D.;
"The guanine nucleotide exchange factor CNrasGEF regulates
melanogenesis and cell survival in melanoma cells.";
J. Biol. Chem. 281:121-128(2006).
[14]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH KIDINS220; MAGI2 AND NTRK1,
AND SUBCELLULAR LOCATION.
PubMed=17724123; DOI=10.1083/jcb.200610073;
Hisata S., Sakisaka T., Baba T., Yamada T., Aoki K., Matsuda M.,
Takai Y.;
"Rap1-PDZ-GEF1 interacts with a neurotrophin receptor at late
endosomes, leading to sustained activation of Rap1 and ERK and neurite
outgrowth.";
J. Cell Biol. 178:843-860(2007).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1022, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
FUNCTION.
PubMed=21840392; DOI=10.1016/j.cellsig.2011.07.022;
Pannekoek W.J., van Dijk J.J., Chan O.Y., Huveneers S.,
Linnemann J.R., Spanjaard E., Brouwer P.M., van der Meer A.J.,
Zwartkruis F.J., Rehmann H., de Rooij J., Bos J.L.;
"Epac1 and PDZ-GEF cooperate in Rap1 mediated endothelial junction
control.";
Cell. Signal. 23:2056-2064(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1022; SER-1080;
SER-1089; SER-1095 AND SER-1159, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=23800469; DOI=10.1126/scisignal.2003993;
Emery A.C., Eiden M.V., Mustafa T., Eiden L.E.;
"Rapgef2 Connects GPCR-Mediated cAMP Signals to ERK Activation in
Neuronal and Endocrine Cells.";
Sci. Signal. 6:RA51-RA51(2013).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: 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
(PubMed:23800469, PubMed:10801446) or not (PubMed:10608844,
PubMed:10548487, PubMed:11359771). 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. {ECO:0000269|PubMed:10548487,
ECO:0000269|PubMed:10608844, ECO:0000269|PubMed:10608883,
ECO:0000269|PubMed:10801446, ECO:0000269|PubMed:10934204,
ECO:0000269|PubMed:11359771, ECO:0000269|PubMed:12391161,
ECO:0000269|PubMed:16272156, ECO:0000269|PubMed:17724123,
ECO:0000269|PubMed:21840392, ECO:0000269|PubMed:23800469}.
-!- SUBUNIT: Interacts with CDH1, CTNNB1 and TJP1 (By similarity).
Interacts (via C-terminal domain) with MAGI2 (via PDZ and WW
domains); the interaction occurs before or after NGF stimulation.
Interacts with KIDINS220 and NTRK1; the interactions occur after
NGF stimulation (By similarity). Found in a complex, at least
composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex is
mainly formed at late endosomes in a neuronal growth factor (NGF)-
dependent manner. Interacts (via C-terminal domain) with NEDD4
(via WW domains); this interaction leads to ubiquitination and
degradation via the proteasome pathway in a cAMP-independent
manner. Interacts with MAGI1 isoform 3 (via PDZ domain). Interacts
with ADRB1 (via C-terminal PDZ motif); the interaction is direct.
Interacts (via Ras-associating domain) with RAP1A (via GTP-bound
active form). Interacts weakly with HRAS (via GDP- and GTP-bound
forms). Interacts (via C-terminal domain) with MAGI2 (via PDZ and
WW domains). {ECO:0000250, ECO:0000269|PubMed:10548487,
ECO:0000269|PubMed:10608844, ECO:0000269|PubMed:11168587,
ECO:0000269|PubMed:11359771, ECO:0000269|PubMed:11598133,
ECO:0000269|PubMed:12391161, ECO:0000269|PubMed:17724123}.
-!- INTERACTION:
Q96QZ7-3:MAGI1; NbExp=2; IntAct=EBI-307079, EBI-8769674;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
Cell membrane. Late endosome. Cell junction {ECO:0000250}.
Note=Associated with the synaptic plasma membrane. Colocalizes
with ADRB1 at the plasma membrane. Synaptosome. Enriched in
synaptic plasma membrane and neuronal cell body. Colocalized with
CTNNB1 at cell-cell contacts (By similarity). Localized diffusely
in the cytoplasm before neuronal growth factor (NGF) stimulation.
Recruited to late endosomes after NGF stimulation. Colocalized
with the high affinity nerve growth factor receptor NTRK1 at late
endosomes. Translocated to the perinuclear region in a RAP1A-
dependent manner. Translocated to the cell membrane.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in primary neuronal and endocrine
cells (at protein level). Highest expression levels in brain.
Lower expression levels in heart, kidney, lung, placenta and blood
leukocytes. {ECO:0000269|PubMed:10934204,
ECO:0000269|PubMed:11168587, ECO:0000269|PubMed:23800469}.
-!- DOMAIN: The Ras-associating domain is necessary for the Rap
guanine nucleotide exchange activity. The N-terminal regionis
necessary for cAMP-binding. The PDZ domain is necessary for its
targeting to the cell membrane.
-!- PTM: Ubiquitinated by NEDD4, leading to proteasomal degradation.
{ECO:0000269|PubMed:11598133}.
-!- PTM: Phosphorylation by PLK2 promotes its activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the RAPGEF2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA20772.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB002311; BAA20772.2; ALT_INIT; mRNA.
EMBL; CH471056; EAX04847.1; -; Genomic_DNA.
EMBL; CH471056; EAX04848.1; -; Genomic_DNA.
CCDS; CCDS43277.1; -.
RefSeq; NP_055062.1; NM_014247.2.
UniGene; Hs.744884; -.
ProteinModelPortal; Q9Y4G8; -.
SMR; Q9Y4G8; -.
BioGrid; 115045; 62.
IntAct; Q9Y4G8; 38.
MINT; MINT-109918; -.
STRING; 9606.ENSP00000264431; -.
iPTMnet; Q9Y4G8; -.
PhosphoSitePlus; Q9Y4G8; -.
BioMuta; RAPGEF2; -.
DMDM; 34395737; -.
EPD; Q9Y4G8; -.
MaxQB; Q9Y4G8; -.
PaxDb; Q9Y4G8; -.
PeptideAtlas; Q9Y4G8; -.
PRIDE; Q9Y4G8; -.
Ensembl; ENST00000264431; ENSP00000264431; ENSG00000109756.
GeneID; 9693; -.
KEGG; hsa:9693; -.
UCSC; uc003iqg.5; human.
CTD; 9693; -.
DisGeNET; 9693; -.
EuPathDB; HostDB:ENSG00000109756.8; -.
GeneCards; RAPGEF2; -.
HGNC; HGNC:16854; RAPGEF2.
HPA; HPA057169; -.
MIM; 609530; gene.
neXtProt; NX_Q9Y4G8; -.
OpenTargets; ENSG00000109756; -.
PharmGKB; PA130413152; -.
eggNOG; KOG3542; Eukaryota.
eggNOG; ENOG410XS6B; LUCA.
GeneTree; ENSGT00880000137870; -.
HOGENOM; HOG000247009; -.
HOVERGEN; HBG056658; -.
InParanoid; Q9Y4G8; -.
KO; K08018; -.
OMA; ADQTCKY; -.
OrthoDB; EOG091G00NU; -.
PhylomeDB; Q9Y4G8; -.
TreeFam; TF313184; -.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
SIGNOR; Q9Y4G8; -.
ChiTaRS; RAPGEF2; human.
GeneWiki; RAPGEF2; -.
GenomeRNAi; 9693; -.
PRO; PR:Q9Y4G8; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000109756; -.
CleanEx; HS_RAPGEF2; -.
ExpressionAtlas; Q9Y4G8; baseline and differential.
Genevisible; Q9Y4G8; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0031697; F:beta-1 adrenergic receptor binding; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
GO; GO:0030552; F:cAMP binding; IDA:UniProtKB.
GO; GO:0019992; F:diacylglycerol binding; NAS:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; IDA:UniProtKB.
GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
GO; GO:0017034; F:Rap guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0004871; F:signal transducer activity; TAS:UniProtKB.
GO; GO:0050699; F:WW domain binding; IDA:UniProtKB.
GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IDA:UniProtKB.
GO; GO:0001568; P:blood vessel development; ISS:UniProtKB.
GO; GO:0031547; P:brain-derived neurotrophic factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0019933; P:cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
GO; GO:0071321; P:cellular response to cGMP; IDA:UniProtKB.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
GO; GO:0061028; P:establishment of endothelial barrier; IMP:UniProtKB.
GO; GO:0090557; P:establishment of endothelial intestinal barrier; IMP:UniProtKB.
GO; GO:0021884; P:forebrain neuron development; ISS:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; TAS:UniProtKB.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0030033; P:microvillus assembly; IGI:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IDA:UniProtKB.
GO; GO:0048022; P:negative regulation of melanin biosynthetic process; ISS:UniProtKB.
GO; GO:0038180; P:nerve growth factor signaling pathway; ISS:UniProtKB.
GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; IDA:UniProtKB.
GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:2000670; P:positive regulation of dendritic cell apoptotic process; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
GO; GO:2001224; P:positive regulation of neuron migration; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0032092; P:positive regulation of protein binding; ISS:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:2001214; P:positive regulation of vasculogenesis; ISS:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0032486; P:Rap protein signal transduction; IMP:UniProtKB.
GO; GO:1901888; P:regulation of cell junction assembly; IMP:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:UniProtKB.
GO; GO:0021591; P:ventricular system development; ISS:UniProtKB.
CDD; cd00038; CAP_ED; 1.
CDD; cd00155; RasGEF; 1.
CDD; cd06224; REM; 1.
Gene3D; 1.10.840.10; -; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR000159; RA_dom.
InterPro; IPR030739; RapGEF2.
InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
InterPro; IPR023578; Ras_GEF_dom_sf.
InterPro; IPR001895; RASGEF_cat_dom.
InterPro; IPR036964; RASGEF_cat_dom_sf.
InterPro; IPR014710; RmlC-like_jellyroll.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR23113:SF217; PTHR23113:SF217; 1.
Pfam; PF00595; PDZ; 1.
Pfam; PF00788; RA; 1.
Pfam; PF00617; RasGEF; 1.
Pfam; PF00618; RasGEF_N; 1.
SMART; SM00100; cNMP; 1.
SMART; SM00228; PDZ; 1.
SMART; SM00314; RA; 1.
SMART; SM00147; RasGEF; 1.
SMART; SM00229; RasGEFN; 1.
SUPFAM; SSF48366; SSF48366; 3.
SUPFAM; SSF50156; SSF50156; 1.
SUPFAM; SSF51206; SSF51206; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50042; CNMP_BINDING_3; 1.
PROSITE; PS50106; PDZ; 1.
PROSITE; PS50200; RA; 1.
PROSITE; PS50009; RASGEF_CAT; 1.
PROSITE; PS50212; RASGEF_NTER; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; Endosome; GTPase activation;
Guanine-nucleotide releasing factor; Membrane; Neurogenesis;
Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 1499 Rap guanine nucleotide exchange factor 2.
/FTId=PRO_0000068865.
DOMAIN 267 380 N-terminal Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00135}.
DOMAIN 385 470 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143, ECO:0000305}.
DOMAIN 606 692 Ras-associating. {ECO:0000255|PROSITE-
ProRule:PRU00166}.
DOMAIN 717 944 Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00168}.
NP_BIND 135 254 cNMP.
COMPBIAS 1108 1166 Ser-rich.
MOD_RES 501 501 Phosphoserine.
{ECO:0000250|UniProtKB:F1M386}.
MOD_RES 644 644 Phosphothreonine; by PLK2.
{ECO:0000250|UniProtKB:F1M386}.
MOD_RES 806 806 Phosphoserine; by PLK2.
{ECO:0000250|UniProtKB:F1M386}.
MOD_RES 930 930 Phosphoserine.
{ECO:0000250|UniProtKB:F1M386}.
MOD_RES 933 933 Phosphoserine; by PLK2.
{ECO:0000250|UniProtKB:F1M386}.
MOD_RES 1022 1022 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1080 1080 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1089 1089 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1095 1095 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1116 1116 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CHG7}.
MOD_RES 1120 1120 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CHG7}.
MOD_RES 1159 1159 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1176 1176 Phosphoserine; by PLK2.
{ECO:0000250|UniProtKB:F1M386}.
MUTAGEN 211 211 K->R: Abolishes cAMP-binding.
{ECO:0000269|PubMed:10801446}.
MUTAGEN 215 215 R->D: Does not abolishe cAMP-binding.
{ECO:0000269|PubMed:10801446}.
MUTAGEN 396 399 PLPF->AAA: Loss of cell membrane
targeting. {ECO:0000269|PubMed:10801446}.
MUTAGEN 606 626 Missing: Abolishes interaction with RAP1A
GTP-bound form and translocation from the
cytoplasm to the perinuclear region. Does
not abolish GEF activity on RAP1A.
{ECO:0000269|PubMed:11359771}.
MUTAGEN 898 898 R->D: Does not inhibit interaction with
NEDD4. Does not interact with HRAS.
Reduces ubiquitination.
{ECO:0000269|PubMed:11598133}.
MUTAGEN 1406 1406 Y->A: Abolishes interaction with NEDD4
and NEDD4-induced ubiquitination and
degradation; when associated with A-1428.
{ECO:0000269|PubMed:11598133}.
MUTAGEN 1428 1428 Y->A: Abolishes interaction with NEDD4
and NEDD4-induced ubiquitination and
degradation; when associated with A-1406.
{ECO:0000269|PubMed:11598133}.
MUTAGEN 1497 1499 SAV->AAA: No loss of cell membrane
targeting. {ECO:0000269|PubMed:10801446}.
SEQUENCE 1499 AA; 167417 MW; 1909E8A12637E001 CRC64;
MKPLAIPANH GVMGQQEKHS LPADFTKLHL TDSLHPQVTH VSSSHSGCSI TSDSGSSSLS
DIYQATESEA GDMDLSGLPE TAVDSEDDDD EEDIERASDP LMSRDIVRDC LEKDPIDRTD
DDIEQLLEFM HQLPAFANMT MSVRRELCAV MVFAVVERAG TIVLNDGEEL DSWSVILNGS
VEVTYPDGKA EILCMGNSFG VSPTMDKEYM KGVMRTKVDD CQFVCIAQQD YCRILNQVEK
NMQKVEEEGE IVMVKEHREL DRTGTRKGHI VIKGTSERLT MHLVEEHSVV DPTFIEDFLL
TYRTFLSSPM EVGKKLLEWF NDPSLRDKVT RVVLLWVNNH FNDFEGDPAM TRFLEEFENN
LEREKMGGHL RLLNIACAAK AKRRLMTLTK PSREAPLPFI LLGGSEKGFG IFVDSVDSGS
KATEAGLKRG DQILEVNGQN FENIQLSKAM EILRNNTHLS ITVKTNLFVF KELLTRLSEE
KRNGAPHLPK IGDIKKASRY SIPDLAVDVE QVIGLEKVNK KSKANTVGGR NKLKKILDKT
RISILPQKPY NDIGIGQSQD DSIVGLRQTK HIPTALPVSG TLSSSNPDLL QSHHRILDFS
ATPDLPDQVL RVFKADQQSR YIMISKDTTA KEVVIQAIRE FAVTATPDQY SLCEVSVTPE
GVIKQRRLPD QLSKLADRIQ LSGRYYLKNN METETLCSDE DAQELLRESQ ISLLQLSTVE
VATQLSMRNF ELFRNIEPTE YIDDLFKLRS KTSCANLKRF EEVINQETFW VASEILRETN
QLKRMKIIKH FIKIALHCRE CKNFNSMFAI ISGLNLAPVA RLRTTWEKLP NKYEKLFQDL
QDLFDPSRNM AKYRNVLNSQ NLQPPIIPLF PVIKKDLTFL HEGNDSKVDG LVNFEKLRMI
AKEIRHVGRM ASVNMDPALM FRTRKKKWRS LGSLSQGSTN ATVLDVAQTG GHKKRVRRSS
FLNAKKLYED AQMARKVKQY LSNLELEMDE ESLQTLSLQC EPATNTLPKN PGDKKPVKSE
TSPVAPRAGS QQKAQSLPQP QQQPPPAHKI NQGLQVPAVS LYPSRKKVPV KDLPPFGINS
PQALKKILSL SEEGSLERHK KQAEDTISNA SSQLSSPPTS PQSSPRKGYT LAPSGTVDNF
SDSGHSEISS RSSIVSNSSF DSVPVSLHDE RRQRHSVSIV ETNLGMGRME RRTMIEPDQY
SLGSYAPMSE GRGLYATATV ISSPSTEELS QDQGDRASLD AADSGRGSWT SCSSGSHDNI
QTIQHQRSWE TLPFGHTHFD YSGDPAGLWA SSSHMDQIMF SDHSTKYNRQ NQSRESLEQA
QSRASWASST GYWGEDSEGD TGTIKRRGGK DVSIEAESSS LTSVTTEETK PVPMPAHIAV
ASSTTKGLIA RKEGRYREPP PTPPGYIGIP ITDFPEGHSH PARKPPDYNV ALQRSRMVAR
SSDTAGPSSV QQPHGHPTSS RPVNKPQWHK PNESDPRLAP YQSQGFSTEE DEDEQVSAV


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