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Q9Y4G8

- RPGF2_HUMAN

UniProt

Q9Y4G8 - RPGF2_HUMAN

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Protein
Rap guanine nucleotide exchange factor 2
Gene
RAPGEF2, KIAA0313, NRAPGEP, PDZGEF1
Organism
Homo sapiens (Human)
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 (1 Publication, 1 Publication) or not (1 Publication, 1 Publication, 1 Publication). 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.11 Publications

Regions

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

GO - Molecular functioni

  1. PDZ domain binding Source: UniProtKB
  2. Rap GTPase activator activity Source: UniProtKB
  3. Rap guanyl-nucleotide exchange factor activity Source: UniProtKB
  4. Ras guanyl-nucleotide exchange factor activity Source: UniProtKB
  5. WW domain binding Source: UniProtKB
  6. beta-1 adrenergic receptor binding Source: UniProtKB
  7. cAMP binding Source: UniProtKB
  8. calcium ion binding Source: UniProtKB
  9. diacylglycerol binding Source: UniProtKB
  10. protein binding Source: UniProtKB
  11. signal transducer activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: UniProtKB
  2. MAPK cascade Source: UniProtKB
  3. Rap protein signal transduction Source: UniProtKB
  4. adenylate cyclase-activating adrenergic receptor signaling pathway Source: UniProtKB
  5. blood vessel development Source: UniProtKB
  6. brain-derived neurotrophic factor receptor signaling pathway Source: UniProtKB
  7. cAMP-mediated signaling Source: UniProtKB
  8. cellular response to cAMP Source: UniProtKB
  9. cellular response to cGMP Source: UniProtKB
  10. cellular response to nerve growth factor stimulus Source: UniProtKB
  11. establishment of endothelial barrier Source: UniProtKB
  12. forebrain neuron development Source: UniProtKB
  13. intracellular signal transduction Source: UniProtKB
  14. negative regulation of cell proliferation Source: UniProtKB
  15. negative regulation of dendrite morphogenesis Source: UniProtKB
  16. negative regulation of melanin biosynthetic process Source: UniProtKB
  17. nerve growth factor signaling pathway Source: UniProtKB
  18. neuron migration Source: UniProtKB
  19. neuron projection development Source: UniProtKB
  20. neuropeptide signaling pathway Source: UniProtKB
  21. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  22. positive regulation of Rap GTPase activity Source: UniProtKB
  23. positive regulation of Ras GTPase activity Source: UniProtKB
  24. positive regulation of cAMP-dependent protein kinase activity Source: UniProtKB
  25. positive regulation of cAMP-mediated signaling Source: UniProtKB
  26. positive regulation of dendritic cell apoptotic process Source: UniProtKB
  27. positive regulation of neuron migration Source: UniProtKB
  28. positive regulation of neuron projection development Source: UniProtKB
  29. positive regulation of protein binding Source: UniProtKB
  30. positive regulation of protein kinase activity Source: UniProtKB
  31. positive regulation of vasculogenesis Source: UniProtKB
  32. regulation of cell junction assembly Source: UniProtKB
  33. regulation of synaptic plasticity Source: UniProtKB
  34. small GTPase mediated signal transduction Source: UniProtKB
  35. 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, NRAPGEP, PDZGEF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:16854. RAPGEF2.

Subcellular locationi

Cytoplasm. Cytoplasmperinuclear region. Cell membrane. Late endosome. Cell junction By similarity
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.3 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi211 – 2111K → R: Abolishes cAMP-binding. 1 Publication
Mutagenesisi215 – 2151R → D: Does not abolishe cAMP-binding. 1 Publication
Mutagenesisi396 – 3994PLPF → AAA: Loss of cell membrane targeting. 1 Publication
Mutagenesisi606 – 62621Missing: Abolishes interaction with RAP1A GTP-bound form and translocation from the cytoplasm to the perinuclear region. Does not abolish GEF activity on RAP1A. 1 Publication
Add
BLAST
Mutagenesisi898 – 8981R → D: Does not inhibit interaction with NEDD4. Does not interact with HRAS. Reduces ubiquitination. 1 Publication
Mutagenesisi1406 – 14061Y → A: Abolishes interaction with NEDD4 and NEDD4-induced ubiquitination and degradation; when associated with A-1428. 1 Publication
Mutagenesisi1428 – 14281Y → A: Abolishes interaction with NEDD4 and NEDD4-induced ubiquitination and degradation; when associated with A-1406. 1 Publication
Mutagenesisi1497 – 14993SAV → AAA: No loss of cell membrane targeting.

Organism-specific databases

PharmGKBiPA130413152.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14991499Rap guanine nucleotide exchange factor 2
PRO_0000068865Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei644 – 6441Phosphothreonine; by PLK2 By similarity
Modified residuei806 – 8061Phosphoserine; by PLK2 By similarity
Modified residuei933 – 9331Phosphoserine; by PLK2 By similarity
Modified residuei1022 – 10221Phosphoserine1 Publication
Modified residuei1176 – 11761Phosphoserine; by PLK2 By similarity

Post-translational modificationi

Ubiquitinated by NEDD4, leading to proteasomal degradation.1 Publication
Phosphorylation by PLK2 promotes its activity By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y4G8.
PaxDbiQ9Y4G8.
PRIDEiQ9Y4G8.

PTM databases

PhosphoSiteiQ9Y4G8.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

ArrayExpressiQ9Y4G8.
BgeeiQ9Y4G8.
CleanExiHS_RAPGEF2.
GenevestigatoriQ9Y4G8.

Organism-specific databases

HPAiHPA057169.

Interactioni

Subunit structurei

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).7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAGI1Q96QZ7-32EBI-307079,EBI-8769674

Protein-protein interaction databases

BioGridi115045. 15 interactions.
IntActiQ9Y4G8. 16 interactions.
MINTiMINT-109918.
STRINGi9606.ENSP00000264431.

Structurei

3D structure databases

ProteinModelPortaliQ9Y4G8.
SMRiQ9Y4G8. Positions 107-366, 397-464, 716-907.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 380114N-terminal Ras-GEF
Add
BLAST
Domaini385 – 47086PDZ
Add
BLAST
Domaini606 – 69287Ras-associating
Add
BLAST
Domaini717 – 944228Ras-GEF
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1108 – 116659Ser-rich
Add
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.

Sequence similaritiesi

Belongs to the RAPGEF2 family.
Contains 1 PDZ (DHR) domain.
Contains 1 Ras-GEF domain.

Phylogenomic databases

eggNOGiNOG307777.
HOGENOMiHOG000247009.
HOVERGENiHBG056658.
InParanoidiQ9Y4G8.
KOiK08018.
OMAiRILDFNT.
OrthoDBiEOG71VSRT.
PhylomeDBiQ9Y4G8.
TreeFamiTF313184.

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. RasGRF_CDC25.
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.

Q9Y4G8-1 [UniParc]FASTAAdd to Basket

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MKPLAIPANH GVMGQQEKHS LPADFTKLHL TDSLHPQVTH VSSSHSGCSI     50
TSDSGSSSLS DIYQATESEA GDMDLSGLPE TAVDSEDDDD EEDIERASDP 100
LMSRDIVRDC LEKDPIDRTD DDIEQLLEFM HQLPAFANMT MSVRRELCAV 150
MVFAVVERAG TIVLNDGEEL DSWSVILNGS VEVTYPDGKA EILCMGNSFG 200
VSPTMDKEYM KGVMRTKVDD CQFVCIAQQD YCRILNQVEK NMQKVEEEGE 250
IVMVKEHREL DRTGTRKGHI VIKGTSERLT MHLVEEHSVV DPTFIEDFLL 300
TYRTFLSSPM EVGKKLLEWF NDPSLRDKVT RVVLLWVNNH FNDFEGDPAM 350
TRFLEEFENN LEREKMGGHL RLLNIACAAK AKRRLMTLTK PSREAPLPFI 400
LLGGSEKGFG IFVDSVDSGS KATEAGLKRG DQILEVNGQN FENIQLSKAM 450
EILRNNTHLS ITVKTNLFVF KELLTRLSEE KRNGAPHLPK IGDIKKASRY 500
SIPDLAVDVE QVIGLEKVNK KSKANTVGGR NKLKKILDKT RISILPQKPY 550
NDIGIGQSQD DSIVGLRQTK HIPTALPVSG TLSSSNPDLL QSHHRILDFS 600
ATPDLPDQVL RVFKADQQSR YIMISKDTTA KEVVIQAIRE FAVTATPDQY 650
SLCEVSVTPE GVIKQRRLPD QLSKLADRIQ LSGRYYLKNN METETLCSDE 700
DAQELLRESQ ISLLQLSTVE VATQLSMRNF ELFRNIEPTE YIDDLFKLRS 750
KTSCANLKRF EEVINQETFW VASEILRETN QLKRMKIIKH FIKIALHCRE 800
CKNFNSMFAI ISGLNLAPVA RLRTTWEKLP NKYEKLFQDL QDLFDPSRNM 850
AKYRNVLNSQ NLQPPIIPLF PVIKKDLTFL HEGNDSKVDG LVNFEKLRMI 900
AKEIRHVGRM ASVNMDPALM FRTRKKKWRS LGSLSQGSTN ATVLDVAQTG 950
GHKKRVRRSS FLNAKKLYED AQMARKVKQY LSNLELEMDE ESLQTLSLQC 1000
EPATNTLPKN PGDKKPVKSE TSPVAPRAGS QQKAQSLPQP QQQPPPAHKI 1050
NQGLQVPAVS LYPSRKKVPV KDLPPFGINS PQALKKILSL SEEGSLERHK 1100
KQAEDTISNA SSQLSSPPTS PQSSPRKGYT LAPSGTVDNF SDSGHSEISS 1150
RSSIVSNSSF DSVPVSLHDE RRQRHSVSIV ETNLGMGRME RRTMIEPDQY 1200
SLGSYAPMSE GRGLYATATV ISSPSTEELS QDQGDRASLD AADSGRGSWT 1250
SCSSGSHDNI QTIQHQRSWE TLPFGHTHFD YSGDPAGLWA SSSHMDQIMF 1300
SDHSTKYNRQ NQSRESLEQA QSRASWASST GYWGEDSEGD TGTIKRRGGK 1350
DVSIEAESSS LTSVTTEETK PVPMPAHIAV ASSTTKGLIA RKEGRYREPP 1400
PTPPGYIGIP ITDFPEGHSH PARKPPDYNV ALQRSRMVAR SSDTAGPSSV 1450
QQPHGHPTSS RPVNKPQWHK PNESDPRLAP YQSQGFSTEE DEDEQVSAV 1499
Length:1,499
Mass (Da):167,417
Last modified:November 1, 1999 - v1
Checksum:i1909E8A12637E001
GO

Sequence cautioni

The sequence BAA20772.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB002311 mRNA. Translation: BAA20772.2. Different initiation.
CH471056 Genomic DNA. Translation: EAX04847.1.
CH471056 Genomic DNA. Translation: EAX04848.1.
CCDSiCCDS43277.1.
RefSeqiNP_055062.1. NM_014247.2.
UniGeneiHs.744884.

Genome annotation databases

EnsembliENST00000264431; ENSP00000264431; ENSG00000109756.
GeneIDi9693.
KEGGihsa:9693.
UCSCiuc003iqg.4. human.

Polymorphism databases

DMDMi34395737.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB002311 mRNA. Translation: BAA20772.2 . Different initiation.
CH471056 Genomic DNA. Translation: EAX04847.1 .
CH471056 Genomic DNA. Translation: EAX04848.1 .
CCDSi CCDS43277.1.
RefSeqi NP_055062.1. NM_014247.2.
UniGenei Hs.744884.

3D structure databases

ProteinModelPortali Q9Y4G8.
SMRi Q9Y4G8. Positions 107-366, 397-464, 716-907.
ModBasei Search...

Protein-protein interaction databases

BioGridi 115045. 15 interactions.
IntActi Q9Y4G8. 16 interactions.
MINTi MINT-109918.
STRINGi 9606.ENSP00000264431.

PTM databases

PhosphoSitei Q9Y4G8.

Polymorphism databases

DMDMi 34395737.

Proteomic databases

MaxQBi Q9Y4G8.
PaxDbi Q9Y4G8.
PRIDEi Q9Y4G8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264431 ; ENSP00000264431 ; ENSG00000109756 .
GeneIDi 9693.
KEGGi hsa:9693.
UCSCi uc003iqg.4. human.

Organism-specific databases

CTDi 9693.
GeneCardsi GC04P160025.
HGNCi HGNC:16854. RAPGEF2.
HPAi HPA057169.
MIMi 609530. gene.
neXtProti NX_Q9Y4G8.
PharmGKBi PA130413152.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG307777.
HOGENOMi HOG000247009.
HOVERGENi HBG056658.
InParanoidi Q9Y4G8.
KOi K08018.
OMAi RILDFNT.
OrthoDBi EOG71VSRT.
PhylomeDBi Q9Y4G8.
TreeFami TF313184.

Miscellaneous databases

GeneWikii RAPGEF2.
GenomeRNAii 9693.
NextBioi 36405.
PROi Q9Y4G8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y4G8.
Bgeei Q9Y4G8.
CleanExi HS_RAPGEF2.
Genevestigatori Q9Y4G8.

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. RasGRF_CDC25.
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. "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."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "nRap GEP: a novel neural GDP/GTP exchange protein for rap1 small G protein that interacts with synaptic scaffolding molecule (S-SCAM)."
    Ohtsuka T., Hata Y., Ide N., Yasuda T., Inoue E., Inoue T., Mizoguchi A., Takai Y.
    Biochem. Biophys. Res. Commun. 265:38-44(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAGI2.
  4. "RA-GEF, a novel Rap1A guanine nucleotide exchange factor containing a Ras/Rap1A-associating domain, is conserved between nematode and humans."
    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.
    J. Biol. Chem. 274:37815-37820(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HRAS AND RAP1A.
  5. "PDZ-GEF1, a guanine nucleotide exchange factor specific for Rap1 and Rap2."
    de Rooij J., Boenink N.M., van Triest M., Cool R.H., Wittinghofer A., Bos J.L.
    J. Biol. Chem. 274:38125-38130(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "The guanine nucleotide exchange factor CNrasGEF activates ras in response to cAMP and cGMP."
    Pham N., Cheglakov I., Koch C.A., de Hoog C.L., Moran M.F., Rotin D.
    Curr. Biol. 10:555-558(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-211; ARG-215; 396-PRO--PHE-399 AND 1497-SER-VAL-1499.
  7. "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."
    Mino A., Ohtsuka T., Inoue E., Takai Y.
    Genes Cells 5:1009-1016(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAGI1, TISSUE SPECIFICITY.
  8. "Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction."
    Rebhun J.F., Castro A.F., Quilliam L.A.
    J. Biol. Chem. 275:34901-34908(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  9. "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."
    Liao Y., Satoh T., Gao X., Jin T.G., Hu C.D., Kataoka T.
    J. Biol. Chem. 276:28478-28483(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAP1A, SUBCELLULAR LOCATION, MUTAGENESIS OF 606-PRO--LYS-626.
  10. "Nedd4 regulates ubiquitination and stability of the guanine-nucleotide exchange factor CNrasGEF."
    Pham N., Rotin D.
    J. Biol. Chem. 276:46995-47003(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HRAS AND NEDD4, UBIQUITINATION BY NEDD4, MUTAGENESIS OF ARG-898; TYR-1406 AND TYR-1428.
  11. "Direct binding of the beta1 adrenergic receptor to the cyclic AMP-dependent guanine nucleotide exchange factor CNrasGEF leads to Ras activation."
    Pak Y., Pham N., Rotin D.
    Mol. Cell. Biol. 22:7942-7952(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ADRB1.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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.
  14. "Rap1-PDZ-GEF1 interacts with a neurotrophin receptor at late endosomes, leading to sustained activation of Rap1 and ERK and neurite outgrowth."
    Hisata S., Sakisaka T., Baba T., Yamada T., Aoki K., Matsuda M., Takai Y.
    J. Cell Biol. 178:843-860(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH KIDINS220; MAGI2 AND NTRK1, SUBCELLULAR LOCATION.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1022, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: FUNCTION.
  21. "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_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4G8
Secondary accession number(s): D3DP27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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