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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_CANLF             Reviewed;        1498 AA.
F1PBJ0;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
31-OCT-2012, sequence version 2.
12-SEP-2018, entry version 62.
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=NRAPGEP, PDZGEF1;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Boxer;
PubMed=16341006; DOI=10.1038/nature04338;
Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
"Genome sequence, comparative analysis and haplotype structure of the
domestic dog.";
Nature 438:803-819(2005).
[2]
INTERACTION WITH CDH1; CTNNB1 AND TJP1, AND SUBCELLULAR LOCATION.
PubMed=10873669; DOI=10.1006/bbrc.2000.3002;
Kawajiri A., Itoh N., Fukata M., Nakagawa M., Yamaga M., Iwamatsu A.,
Kaibuchi K.;
"Identification of a novel beta-catenin-interacting protein.";
Biochem. Biophys. Res. Commun. 273:712-717(2000).
-!- 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 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.
-!- SUBUNIT: 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 (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) (By
similarity). Interacts with CDH1, CTNNB1 and TJP1. {ECO:0000250,
ECO:0000269|PubMed:10873669}.
-!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:10873669}.
Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region
{ECO:0000250}. Cell membrane {ECO:0000250}. Late endosome
{ECO:0000250}. Note=Associated with the synaptic plasma membrane.
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 (By similarity). Colocalized with CTNNB1 and
TJP1 at cell-cell contacts. {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated by NEDD4, leading to proteasomal degradation.
{ECO:0000250}.
-!- PTM: Phosphorylation by PLK2 promotes its activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the RAPGEF2 family. {ECO:0000305}.
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EMBL; AAEX03010088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_003639545.1; XM_003639497.3.
IntAct; F1PBJ0; 1.
STRING; 9615.ENSCAFP00000012838; -.
PaxDb; F1PBJ0; -.
PRIDE; F1PBJ0; -.
Ensembl; ENSCAFT00000013877; ENSCAFP00000012838; ENSCAFG00000008719.
GeneID; 100856359; -.
KEGG; cfa:100856359; -.
CTD; 9693; -.
VGNC; VGNC:45347; RAPGEF2.
eggNOG; KOG3542; Eukaryota.
eggNOG; ENOG410XS6B; LUCA.
GeneTree; ENSGT00880000137870; -.
InParanoid; F1PBJ0; -.
KO; K08018; -.
OMA; EVCSEHN; -.
OrthoDB; EOG091G00NU; -.
TreeFam; TF313184; -.
Reactome; R-CFA-5673001; RAF/MAP kinase cascade.
Proteomes; UP000002254; Chromosome 15.
Bgee; ENSCAFG00000008719; Expressed in 3 organ(s), highest expression level in prefrontal cortex.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
GO; GO:0005770; C:late endosome; ISS: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; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0031697; F:beta-1 adrenergic receptor binding; ISS:UniProtKB.
GO; GO:0030552; F:cAMP binding; ISS:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
GO; GO:0070300; F:phosphatidic acid binding; IEA:Ensembl.
GO; GO:0017034; F:Rap guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
GO; GO:0050699; F:WW domain binding; ISS:UniProtKB.
GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS: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; ISS:UniProtKB.
GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
GO; GO:0071321; P:cellular response to cGMP; ISS:UniProtKB.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
GO; GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
GO; GO:0090557; P:establishment of endothelial intestinal barrier; IEA:Ensembl.
GO; GO:0021884; P:forebrain neuron development; ISS:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0030033; P:microvillus assembly; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISS: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; ISS:UniProtKB.
GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; ISS:UniProtKB.
GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB.
GO; GO:2000670; P:positive regulation of dendritic cell apoptotic process; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS: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; ISS:UniProtKB.
GO; GO:2001214; P:positive regulation of vasculogenesis; ISS:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
GO; GO:1901888; P:regulation of cell junction assembly; ISS:UniProtKB.
GO; GO:0021591; P:ventricular system development; ISS:UniProtKB.
CDD; cd00038; CAP_ED; 1.
CDD; cd00155; RasGEF; 1.
CDD; cd06224; REM; 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; 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 1498 Rap guanine nucleotide exchange factor 2.
/FTId=PRO_0000423854.
DOMAIN 267 380 N-terminal Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00135}.
DOMAIN 385 468 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 606 692 Ras-associating. {ECO:0000255|PROSITE-
ProRule:PRU00166}.
DOMAIN 717 944 Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00168}.
NP_BIND 135 252 cNMP.
COMPBIAS 87 90 Poly-Asp.
COMPBIAS 1038 1045 Poly-Pro.
COMPBIAS 1107 1165 Ser-rich.
MOD_RES 501 501 Phosphoserine.
{ECO:0000250|UniProtKB:F1M386}.
MOD_RES 644 644 Phosphothreonine.
{ECO:0000250|UniProtKB:F1M386}.
MOD_RES 806 806 Phosphoserine.
{ECO:0000250|UniProtKB:F1M386}.
MOD_RES 930 930 Phosphoserine.
{ECO:0000250|UniProtKB:F1M386}.
MOD_RES 933 933 Phosphoserine.
{ECO:0000250|UniProtKB:F1M386}.
MOD_RES 1022 1022 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CHG7}.
MOD_RES 1079 1079 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y4G8}.
MOD_RES 1088 1088 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y4G8}.
MOD_RES 1094 1094 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y4G8}.
MOD_RES 1115 1115 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CHG7}.
MOD_RES 1119 1119 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CHG7}.
MOD_RES 1158 1158 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y4G8}.
MOD_RES 1175 1175 Phosphoserine.
{ECO:0000250|UniProtKB:F1M386}.
SEQUENCE 1498 AA; 167320 MW; CCA24CD5403DB165 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
TTPDLPDQVL RVFKADQQSR YIMISKDTTA KEVVIQAIRE FAVTATPDQY SLCEVSVTPE
GVIKQRRLPD QLSKLADRIQ LSGRYYLKNN METETLCSDE DAQELLRESQ ISLLQLSTVE
VATQLSMRNF ELFRNIEPTE YIDDLFKLKS KTSCANLKKF 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 QQKAQAQPPP PQPQPQHKIN QGLQVPAVSL YPSRKKVPVK DLPPFGINSP
QALKKILSLS EEGSLERHKK QAEDTISNAS SQLSSPPTSP QSSPRKGYTL APSGTVDNFS
DSGHSEISSR SSIVSNSSFD SVPVSLHEER RQRHSVSIVE TNLGVGRMER RTMMEPDQYS
LGSYAPMAES RGLYATATVI SSPSTEELSQ DQGDRASLDA ADSGRGSWTS CSSGSHDNIQ
TIQHQRSWET LPFGHTHFDY SGDPAGLWAS SSHMDQIMFS DHSTKYNRQN QSRESLEQAQ
SRASWASSTG YWGEDSEGDT GTIKRRGGKD VSIEAESSSV TSVTTEETKP VPMPAHVAVT
SSTAKGLIVR KEGRYREPPP TPPGYIGIPI TDFPEGHSHP ARKPPDYNVA LQRSRMVARP
TDTAAPSPIQ QPHGHPASGR PVNKPQWHKP NECDPRLAPY QSQGFSTEED EDEQVSAV


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EIAAB34524 Grf2,Mouse,Mus musculus,Ras guanine nucleotide exchange factor 2,Rasgrf2,Ras-GRF2,Ras-specific guanine nucleotide-releasing factor 2
EIAAB34522 Grf2,Ras guanine nucleotide exchange factor 2,Rasgrf2,Ras-GRF2,Ras-specific guanine nucleotide-releasing factor 2,Rat,Rattus norvegicus
EIAAB34519 Cdc25,CDC25Mm,GNRP,Grf1,Guanine nucleotide-releasing protein,Mouse,Mus musculus,Rasgrf1,Ras-GRF1,Ras-specific guanine nucleotide-releasing factor 1,Ras-specific nucleotide exchange factor CDC25
EIAAB27123 Ephexin-1,Eph-interacting exchange protein,Neuronal guanine nucleotide exchange factor,Ngef,Rat,Rattus norvegicus
EIAAB27125 Ephexin-1,Eph-interacting exchange protein,Mouse,Mus musculus,Neuronal guanine nucleotide exchange factor,Ngef
EIAAB34521 CDC25,GNRP,GNRP,GRF1,Guanine nucleotide-releasing protein,Homo sapiens,Human,RASGRF1,Ras-GRF1,Ras-specific guanine nucleotide-releasing factor 1,Ras-specific nucleotide exchange factor CDC25


 

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