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Q8CHG7

- RPGF2_MOUSE

UniProt

Q8CHG7 - RPGF2_MOUSE

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Protein

Rap guanine nucleotide exchange factor 2

Gene

Rapgef2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi135 – 254120cNMPAdd
BLAST

GO - Molecular functioni

  1. beta-1 adrenergic receptor binding Source: UniProtKB
  2. cAMP binding Source: UniProtKB
  3. GTPase activator activity Source: UniProtKB-KW
  4. PDZ domain binding Source: UniProtKB
  5. Rap guanyl-nucleotide exchange factor activity Source: UniProtKB
  6. Ras guanyl-nucleotide exchange factor activity Source: UniProtKB
  7. WW domain binding Source: UniProtKB

GO - Biological processi

  1. adenylate cyclase-activating adrenergic receptor signaling pathway Source: UniProtKB
  2. blood vessel development Source: UniProtKB
  3. brain-derived neurotrophic factor receptor signaling pathway Source: UniProtKB
  4. cAMP-mediated signaling Source: UniProtKB
  5. cellular response to cAMP Source: UniProtKB
  6. cellular response to cGMP Source: UniProtKB
  7. cellular response to nerve growth factor stimulus Source: UniProtKB
  8. establishment of endothelial barrier Source: UniProtKB
  9. forebrain neuron development Source: UniProtKB
  10. G-protein coupled receptor signaling pathway Source: UniProtKB
  11. negative regulation of cell proliferation Source: UniProtKB
  12. negative regulation of dendrite morphogenesis Source: UniProtKB
  13. negative regulation of melanin biosynthetic process Source: UniProtKB
  14. nerve growth factor signaling pathway Source: UniProtKB
  15. neuron migration Source: UniProtKB
  16. neuron projection development Source: UniProtKB
  17. neuropeptide signaling pathway Source: UniProtKB
  18. positive regulation of cAMP-dependent protein kinase activity Source: UniProtKB
  19. positive regulation of cAMP-mediated signaling Source: UniProtKB
  20. positive regulation of dendritic cell apoptotic process Source: UniProtKB
  21. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  22. positive regulation of neuron migration Source: UniProtKB
  23. positive regulation of neuron projection development Source: UniProtKB
  24. positive regulation of protein binding Source: UniProtKB
  25. positive regulation of protein kinase activity Source: UniProtKB
  26. positive regulation of Rap GTPase activity Source: UniProtKB
  27. positive regulation of Ras GTPase activity Source: UniProtKB
  28. positive regulation of vasculogenesis Source: UniProtKB
  29. Rap protein signal transduction Source: UniProtKB
  30. regulation of cell junction assembly Source: UniProtKB
  31. regulation of synaptic plasticity Source: UniProtKB
  32. ventricular system development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, GTPase activation, Guanine-nucleotide releasing factor

Keywords - Biological processi

Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Rap guanine nucleotide exchange factor 2
Alternative name(s):
Cyclic nucleotide ras GEF
Short name:
CNrasGEF
Neural RAP guanine nucleotide exchange protein
Short name:
nRap GEP
PDZ domain-containing guanine nucleotide exchange factor 1
Short name:
PDZ-GEF1
RA-GEF-1
Ras/Rap1-associating GEF-1
Gene namesi
Name:Rapgef2
Synonyms:Kiaa0313, Pdzgef1
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:2659071. Rapgef2.

Subcellular locationi

Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Cell membrane By similarity. Late endosome By similarity. Cell junction By similarity
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. Colocalized with CTNNB1 at cell-cell contacts (By similarity).By similarity

GO - Cellular componenti

  1. cell-cell junction Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. late endosome Source: UniProtKB
  4. membrane Source: UniProtKB
  5. neuronal cell body Source: UniProtKB
  6. neuron projection Source: UniProtKB
  7. perinuclear region of cytoplasm Source: UniProtKB
  8. plasma membrane Source: UniProtKB
  9. protein complex Source: UniProtKB
  10. synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice appear normal until 7.5 dpc, but become grossly abnormal and dead at mid-gestation. Show severe defects in yolk sac blood and major vessels formation. Show impair callosal axons to cross the midline during cortical development. Show disruption of all three midline commissure fibers crossing, the corpus callosum, the anterior commissure and the dorsal hippocampal commissure during cortical develpoment. Conditional knockout mice in which rapgef2 is lacking within the dorsal telencephalon result in malformation of the cortical brain structures: developed an ectopic cortical mass (ECM) extending throughout the rostro-caudal axis of the cerebral hemisphere. Mice show also an enlargement of the lateral ventricles and the agenesis of interhemispheric connections: the corpus callosum, the dorsal hippocampus commissure and the anterior commissure (PubMed:19453629).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14961496Rap guanine nucleotide exchange factor 2PRO_0000068866Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei644 – 6441Phosphothreonine; by PLK2By similarity
Modified residuei806 – 8061Phosphoserine; by PLK2By similarity
Modified residuei933 – 9331Phosphoserine; by PLK2By similarity
Modified residuei1022 – 10221Phosphoserine; alternate1 Publication
Modified residuei1022 – 10221Phosphoserine; by PLK2; alternate1 Publication
Modified residuei1175 – 11751Phosphoserine; by PLK2By similarity

Post-translational modificationi

Ubiquitinated by NEDD4, leading to proteasomal degradation.By similarity
Phosphorylation by PLK2 promotes its activity.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ8CHG7.
PRIDEiQ8CHG7.

PTM databases

PhosphoSiteiQ8CHG7.

Expressioni

Tissue specificityi

Expressed in all layers of the cerebral cortex, hippocampus and cerebellum. Expressed in the cortical plate, cingulate cortex and the subventricular zone. Expressed in neurons and endocrine cells (at protein level). Expressed in melanoma cells.4 Publications

Developmental stagei

Expressed in the yolk sacs at vascular endothelial cells at 7.5 dpc. Expressed in the glial sling (GS) at the cortico-septal boundary at 17.5 dpc (at proteion level).2 Publications

Gene expression databases

BgeeiQ8CHG7.
CleanExiMM_RAPGEF2.
ExpressionAtlasiQ8CHG7. baseline and differential.
GenevestigatoriQ8CHG7.

Interactioni

Subunit structurei

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). Interacts with CDH1, CTNNB1 and TJP1 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ8CHG7. 3 interactions.
MINTiMINT-4133098.

Structurei

3D structure databases

ProteinModelPortaliQ8CHG7.
SMRiQ8CHG7. Positions 107-366, 397-464, 668-913.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 380114N-terminal Ras-GEFPROSITE-ProRule annotationAdd
BLAST
Domaini385 – 47086PDZPROSITE-ProRule annotationAdd
BLAST
Domaini606 – 69287Ras-associatingPROSITE-ProRule annotationAdd
BLAST
Domaini717 – 944228Ras-GEFPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1107 – 116559Ser-richAdd
BLAST
Compositional biasi1398 – 147982Pro-richAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the RAPGEF2 family.Curated
Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation
Contains 1 N-terminal Ras-GEF domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 1 Ras-associating domain.PROSITE-ProRule annotation
Contains 1 Ras-GEF domain.CuratedPROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG307777.
GeneTreeiENSGT00760000118894.
HOGENOMiHOG000247009.
HOVERGENiHBG056658.
InParanoidiQ8CHG7.
KOiK08018.
OMAiRILDFNT.
OrthoDBiEOG71VSRT.

Family and domain databases

Gene3Di1.10.840.10. 1 hit.
2.30.42.10. 1 hit.
2.60.120.10. 1 hit.
InterProiIPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR001478. PDZ.
IPR000159. Ras-assoc.
IPR000651. Ras-like_Gua-exchang_fac_N.
IPR023578. Ras_GEF_dom.
IPR001895. RASGEF_cat_dom.
IPR014710. RmlC-like_jellyroll.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00027. cNMP_binding. 1 hit.
PF00595. PDZ. 1 hit.
PF00788. RA. 1 hit.
PF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
[Graphical view]
SMARTiSM00100. cNMP. 1 hit.
SM00228. PDZ. 1 hit.
SM00314. RA. 1 hit.
SM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 1 hit.
[Graphical view]
SUPFAMiSSF48366. SSF48366. 3 hits.
SSF50156. SSF50156. 1 hit.
SSF51206. SSF51206. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50042. CNMP_BINDING_3. 1 hit.
PS50106. PDZ. 1 hit.
PS50200. RA. 1 hit.
PS50009. RASGEF_CAT. 1 hit.
PS50212. RASGEF_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CHG7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKPLAAPANH GVLGQQEKQS LPADFTKLHL TDSLHPQVTH VSSSHSGCSI
60 70 80 90 100
TSDSGSSSLS DIYQATESEA GDMDLSGLPE TAVDSEDDDD EEDIERASDP
110 120 130 140 150
LMSRDIVRDC LEKDPIDRTD DDIEQLLEFM HQLPAFANMT MSVRRELCAV
160 170 180 190 200
MVFAVVERAG TIVLNDGEEL DSWSVILNGS VEVTYPDGKA EILCMGNSFG
210 220 230 240 250
VSPTMDKEYM KGVMRTKVDD CQFVCIAQQD YCRILNQVEK NMQKVEEEGE
260 270 280 290 300
IVMVKEHREL DRTGTRKGHI VIKGTSERLT MHLVEEHSVV DPTFIEDFLL
310 320 330 340 350
TYRTFLSSPM EVGKKLLEWF NDPSLRDKVT RVVLLWVNNH FNDFEGDPAM
360 370 380 390 400
TRFLEEFENN LEREKMGGHL RLLNIACAAK AKRRLMTLTK PSREAPLPFI
410 420 430 440 450
LLGGSEKGFG IFVDSVDSCS KATEAGLKRG DQILEVNGQN FENIQLSKAM
460 470 480 490 500
EILRNNTHLS ITVKTNLFVF KELLTRLSEE KRNGAPHLPK IGDIKKASRY
510 520 530 540 550
SIPDLAVDVE QVIGLEKVNK KSKANTVGGR NKLKKILDKT RISILPQKPY
560 570 580 590 600
NDIGIGQSQD DSIVGLRQTK HIPAALPVSG TLSSSNPDLL QSHHRILDFS
610 620 630 640 650
TTPDLPDQVL RVFKADQQSR YIMISKDTTA KEVVIQAIRE FAVTATPEQY
660 670 680 690 700
SLCEVSVTPE GVIKQRRLPD QLSKLADRIQ LSGRYYLKNN METETLCSDE
710 720 730 740 750
DAQELLRESQ ISLLQLSTVE VATQLSMRNF ELFRNIEPTE YIDDLFKLKS
760 770 780 790 800
KTSCANLKKF EEVINQETFW VASEILRETN QLKRMKIIKH FIKIALHCRE
810 820 830 840 850
CKNFNSMFAI ISGLNLAPVA RLRTTWEKLP NKYEKLFQDL QDLFDPSRNM
860 870 880 890 900
AKYRNVLSGQ NLQPPVIPLF PVIKKDLTFL HEGNDSKVDG LVNFEKLRMI
910 920 930 940 950
AKEIRHVGRM ASVNMDPALM FRTRKKKWRS LGSLSQGSAN ATVLDVAQTG
960 970 980 990 1000
GHKKRVRRSS FLNAKKLYED AQMARKVKQY LSNLELEMDE ESLQTLSLQC
1010 1020 1030 1040 1050
EPATSTLPKN PGDKKPVKSE TSPVAPRAGP QQKVQPQQPL AQPQPPHKVS
1060 1070 1080 1090 1100
QGLQVPAVSL YPSRKKVPVK DLPPFGINSP QALKKILSLS EEGSLERHRK
1110 1120 1130 1140 1150
QAEDTISNAS SQLSSPPTSP QSSPRKGYAL ALSGTVDNFS DSGHSEISSR
1160 1170 1180 1190 1200
SSIVSNSSFD SVPVSLHDER RQRHSVSIVE SNLGVGRMER RTLMEPDQYS
1210 1220 1230 1240 1250
LGSYAPVSES RGLYAAATVI SSPSTEELSH DQGDRASLDA ADSGRGSWTS
1260 1270 1280 1290 1300
CSSGSHDNIQ TIQHQRSWET LPFGHTHFDY SGDAASIWAS GGHMDQMMFS
1310 1320 1330 1340 1350
DHSTKYNRQN QSRESLEQAQ SRASWASSTG YWGEDSEGDT GTIKRRGGKD
1360 1370 1380 1390 1400
VSAEAESSSM VPVTTEEAKP VPMPAHIAVT PSTTKGLIAR KEGRYREPPP
1410 1420 1430 1440 1450
TPPGYVGIPI ADFPEGPCHP ARKPPDYNVA LQRSRMVARP TEAPAPGQTP
1460 1470 1480 1490
PAAAASRPGS KPQWHKPSDA DPRLAPFQPQ GFAGAEEDED EQVSAV
Length:1,496
Mass (Da):166,415
Last modified:December 14, 2011 - v2
Checksum:iC2FDE48E5E21A86F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC124358 Genomic DNA. No translation available.
AC157941 Genomic DNA. No translation available.
AC164560 Genomic DNA. No translation available.
AB093228 mRNA. Translation: BAC41412.1.
RefSeqiXP_006502317.1. XM_006502254.1.
UniGeneiMm.31220.
Mm.462396.

Genome annotation databases

EnsembliENSMUST00000118100; ENSMUSP00000114119; ENSMUSG00000062232.
GeneIDi76089.
KEGGimmu:76089.
UCSCiuc008pnl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC124358 Genomic DNA. No translation available.
AC157941 Genomic DNA. No translation available.
AC164560 Genomic DNA. No translation available.
AB093228 mRNA. Translation: BAC41412.1 .
RefSeqi XP_006502317.1. XM_006502254.1.
UniGenei Mm.31220.
Mm.462396.

3D structure databases

ProteinModelPortali Q8CHG7.
SMRi Q8CHG7. Positions 107-366, 397-464, 668-913.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8CHG7. 3 interactions.
MINTi MINT-4133098.

PTM databases

PhosphoSitei Q8CHG7.

Proteomic databases

PaxDbi Q8CHG7.
PRIDEi Q8CHG7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000118100 ; ENSMUSP00000114119 ; ENSMUSG00000062232 .
GeneIDi 76089.
KEGGi mmu:76089.
UCSCi uc008pnl.1. mouse.

Organism-specific databases

CTDi 9693.
MGIi MGI:2659071. Rapgef2.
Rougei Search...

Phylogenomic databases

eggNOGi NOG307777.
GeneTreei ENSGT00760000118894.
HOGENOMi HOG000247009.
HOVERGENi HBG056658.
InParanoidi Q8CHG7.
KOi K08018.
OMAi RILDFNT.
OrthoDBi EOG71VSRT.

Miscellaneous databases

PROi Q8CHG7.
SOURCEi Search...

Gene expression databases

Bgeei Q8CHG7.
CleanExi MM_RAPGEF2.
ExpressionAtlasi Q8CHG7. baseline and differential.
Genevestigatori Q8CHG7.

Family and domain databases

Gene3Di 1.10.840.10. 1 hit.
2.30.42.10. 1 hit.
2.60.120.10. 1 hit.
InterProi IPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR001478. PDZ.
IPR000159. Ras-assoc.
IPR000651. Ras-like_Gua-exchang_fac_N.
IPR023578. Ras_GEF_dom.
IPR001895. RASGEF_cat_dom.
IPR014710. RmlC-like_jellyroll.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF00027. cNMP_binding. 1 hit.
PF00595. PDZ. 1 hit.
PF00788. RA. 1 hit.
PF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
[Graphical view ]
SMARTi SM00100. cNMP. 1 hit.
SM00228. PDZ. 1 hit.
SM00314. RA. 1 hit.
SM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 1 hit.
[Graphical view ]
SUPFAMi SSF48366. SSF48366. 3 hits.
SSF50156. SSF50156. 1 hit.
SSF51206. SSF51206. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEi PS50042. CNMP_BINDING_3. 1 hit.
PS50106. PDZ. 1 hit.
PS50200. RA. 1 hit.
PS50009. RASGEF_CAT. 1 hit.
PS50212. RASGEF_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H.
    DNA Res. 9:179-188(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-1496.
    Tissue: Brain1 Publication.
  3. "The guanine nucleotide exchange factor CNrasGEF regulates melanogenesis and cell survival in melanoma cells."
    Amsen E.M., Pham N., Pak Y., Rotin D.
    J. Biol. Chem. 281:121-128(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. "Defective vascular morphogenesis and mid-gestation embryonic death in mice lacking RA-GEF-1."
    Wei P., Satoh T., Edamatsu H., Aiba A., Setsu T., Terashima T., Kitazawa S., Nakao K., Yoshikawa Y., Tamada M., Kataoka T.
    Biochem. Biophys. Res. Commun. 363:106-112(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Impaired vascular development in the yolk sac and allantois in mice lacking RA-GEF-1."
    Kanemura H., Satoh T., Bilasy S.E., Ueda S., Hirashima M., Kataoka T.
    Biochem. Biophys. Res. Commun. 387:754-759(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Dorsal telencephalon-specific RA-GEF-1 knockout mice develop heterotopic cortical mass and commissural fiber defect."
    Bilasy S.E., Satoh T., Ueda S., Wei P., Kanemura H., Aiba A., Terashima T., Kataoka T.
    Eur. J. Neurosci. 29:1994-2008(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  9. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1022, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "RA-GEF-1 (Rapgef2) is essential for proper development of the midline commissures."
    Bilasy S.E., Satoh T., Terashima T., Kataoka T.
    Neurosci. Res. 71:200-209(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  11. "Rapgef2 Connects GPCR-Mediated cAMP Signals to ERK Activation in Neuronal and Endocrine Cells."
    Emery A.C., Eiden M.V., Mustafa T., Eiden L.E.
    Sci. Signal. 6:RA51-RA51(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiRPGF2_MOUSE
AccessioniPrimary (citable) accession number: Q8CHG7
Secondary accession number(s): E9QMD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: December 14, 2011
Last modified: October 29, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3