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O95398 (RPGF3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rap guanine nucleotide exchange factor 3
Alternative name(s):
Exchange factor directly activated by cAMP 1
Exchange protein directly activated by cAMP 1
Short name=EPAC 1
Rap1 guanine-nucleotide-exchange factor directly activated by cAMP
cAMP-regulated guanine nucleotide exchange factor I
Short name=cAMP-GEFI
Gene names
Name:RAPGEF3
Synonyms:CGEF1, EPAC, EPAC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length923 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide exchange factor (GEF) for RAP1A and RAP2A small GTPases that is activated by binding cAMP. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which it activates the PI3K gamma complex and which is involved in angiogenesis. Plays a role in the modulation of the cAMP-induced dynamic control of endothelial barrier function through a pathway that is independent on Rho-mediated signaling. Required for the actin rearrangement at cell-cell junctions, such as stress fibers and junctional actin. Ref.6 Ref.7 Ref.9

Subunit structure

Interacts with PDE3B. Ref.10

Subcellular location

Endomembrane system Ref.7.

Tissue specificity

Widely expressed with highest levels in adult kidney, heart, thyroid and brain, and fetal kidney. Ref.1

Domain

The DEP domain is involved in membrane localization independent from regulation by cAMP. Ref.7

Sequence similarities

Contains 1 cyclic nucleotide-binding domain.

Contains 1 DEP domain.

Contains 1 N-terminal Ras-GEF domain.

Contains 1 Ras-GEF domain.

Caution

It is uncertain whether Met-1 or Met-43 is the initiator.

Sequence caution

The sequence AAD02890.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAD12740.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processAngiogenesis
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandcAMP
cAMP-binding
Nucleotide-binding
   Molecular functionGuanine-nucleotide releasing factor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRap protein signal transduction

Inferred from mutant phenotype Ref.9. Source: UniProtKB

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

blood coagulation

Traceable author statement. Source: Reactome

cAMP-mediated signaling

Non-traceable author statement PubMed 16177794. Source: BHF-UCL

cell proliferation

Traceable author statement Ref.6. Source: ProtInc

cellular response to cAMP

Inferred from direct assay Ref.9. Source: UniProtKB

energy reserve metabolic process

Traceable author statement. Source: Reactome

establishment of endothelial barrier

Inferred from mutant phenotype Ref.9. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

positive regulation of Rap GTPase activity

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of angiogenesis

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of cAMP catabolic process

Non-traceable author statement PubMed 16177794. Source: BHF-UCL

positive regulation of stress fiber assembly

Inferred from mutant phenotype Ref.9. Source: UniProtKB

regulation of actin cytoskeleton reorganization

Inferred from mutant phenotype Ref.9. Source: UniProtKB

regulation of insulin secretion

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement Ref.6. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcAMP-dependent protein kinase complex

Inferred from electronic annotation. Source: InterPro

endomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

membrane

Traceable author statement Ref.7. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionRap guanyl-nucleotide exchange factor activity

Inferred from mutant phenotype Ref.9. Source: UniProtKB

cAMP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cAMP-dependent protein kinase regulator activity

Inferred from electronic annotation. Source: InterPro

guanyl-nucleotide exchange factor activity

Traceable author statement Ref.6. Source: ProtInc

protein binding

Inferred from physical interaction Ref.10. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDE3BQ133708EBI-6172806,EBI-6172856

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95398-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O95398-2)

The sequence of this isoform differs from the canonical sequence as follows:
     533-598: ARNLPVWLPN...LAQEDGWTKG → VSAWPQFLSS...GQAVPGGAEA
     599-923: Missing.
Isoform 3 (identifier: O95398-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 923923Rap guanine nucleotide exchange factor 3
PRO_0000068867

Regions

Domain110 – 18677DEP
Domain384 – 518135N-terminal Ras-GEF
Domain662 – 889228Ras-GEF
Nucleotide binding245 – 363119cAMP
Region218 – 24225Interaction with PDE3B
Region398 – 42225Interaction with PDE3B

Natural variations

Alternative sequence1 – 4242Missing in isoform 3.
VSP_047007
Alternative sequence533 – 59866ARNLP…GWTKG → VSAWPQFLSSAPPGLQAPPS PPDPEGLCGRGKLSSHRHTL GSLIGVHGALAACGALGQAV PGGAEA in isoform 2.
VSP_007608
Alternative sequence599 – 923325Missing in isoform 2.
VSP_007609
Natural variant161A → P. Ref.5
Corresponds to variant rs11168230 [ dbSNP | Ensembl ].
VAR_047924
Natural variant1931R → G. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6
Corresponds to variant rs2016123 [ dbSNP | Ensembl ].
VAR_047925
Natural variant3741G → S.
Corresponds to variant rs12422983 [ dbSNP | Ensembl ].
VAR_047926
Natural variant5171C → Y.
Corresponds to variant rs61709815 [ dbSNP | Ensembl ].
VAR_061784

Experimental info

Mutagenesis3151L → W: Abolishes activation of RAP1A. Ref.8
Mutagenesis3211R → K: Reduces activation of RAP1A. Ref.1
Mutagenesis3421F → A or T: Diminishes GEF activity dependence on cAMP concentration. Ref.8
Mutagenesis4121D → A: Abolishes interaction with PDE3B. Ref.10
Mutagenesis4151E → A: Abolishes interaction with PDE3B. Ref.10
Mutagenesis4171F → A: Abolishes interaction with PDE3B. Ref.10
Mutagenesis4201D → A: Abolishes interaction with PDE3B. Ref.10
Mutagenesis4211F → A: Abolishes interaction with PDE3B. Ref.10
Sequence conflict641R → H in AAD12740. Ref.1
Sequence conflict641R → H in AAD02890. Ref.1
Sequence conflict1061R → Q in AAD12740. Ref.1
Sequence conflict1061R → Q in AAD02890. Ref.1
Sequence conflict1161I → T in AAC83381. Ref.6
Sequence conflict3301D → Y in AAD12740. Ref.1
Sequence conflict3301D → Y in AAD02890. Ref.1
Sequence conflict3941E → D in AAD12740. Ref.1
Sequence conflict3941E → D in AAD02890. Ref.1
Sequence conflict4061P → L in AAD12740. Ref.1
Sequence conflict4061P → L in AAD02890. Ref.1
Sequence conflict4141T → K in AAD12740. Ref.1
Sequence conflict4141T → K in AAD02890. Ref.1
Sequence conflict4911Q → H in AAD12740. Ref.1
Sequence conflict6381V → A in AAC83381. Ref.6
Sequence conflict7361R → K in AAD12740. Ref.1
Sequence conflict7511L → V in AAD12740. Ref.1
Sequence conflict7651A → P in AAD12740. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 6.
Checksum: 8B3A24341F20515F

FASTA923103,751
        10         20         30         40         50         60 
MKVGWPGESC WQVGLAVEDS PALGAPRVGA LPDVVPEGTL LNMVLRRMHR PRSCSYQLLL 

        70         80         90        100        110        120 
EHQRPSCIQG LRWTPLTNSE ESLDFSESLE QASTERVLRA GRQLHRHLLA TCPNLIRDRK 

       130        140        150        160        170        180 
YHLRLYRQCC SGRELVDGIL ALGLGVHSRS QVVGICQVLL DEGALCHVKH DWAFQDRDAQ 

       190        200        210        220        230        240 
FYRFPGPEPE PVRTHEMEEE LAEAVALLSQ RGPDALLTVA LRKPPGQRTD EELDLIFEEL 

       250        260        270        280        290        300 
LHIKAVAHLS NSVKRELAAV LLFEPHSKAG TVLFSQGDKG TSWYIIWKGS VNVVTHGKGL 

       310        320        330        340        350        360 
VTTLHEGDDF GQLALVNDAP RAATIILRED NCHFLRVDKQ DFNRIIKDVE AKTMRLEEHG 

       370        380        390        400        410        420 
KVVLVLERAS QGAGPSRPPT PGRNRYTVMS GTPEKILELL LEAMGPDSSA HDPTETFLSD 

       430        440        450        460        470        480 
FLLTHRVFMP SAQLCAALLH HFHVEPAGGS EQERSTYVCN KRQQILRLVS QWVALYGSML 

       490        500        510        520        530        540 
HTDPVATSFL QKLSDLVGRD TRLSNLLREQ WPERRRCHRL ENGCGNASPQ MKARNLPVWL 

       550        560        570        580        590        600 
PNQDEPLPGS SCAIQVGDKV PYDICRPDHS VLTLQLPVTA SVREVMAALA QEDGWTKGQV 

       610        620        630        640        650        660 
LVKVNSAGDA IGLQPDARGV ATSLGLNERL FVVNPQEVHE LIPHPDQLGP TVGSAEGLDL 

       670        680        690        700        710        720 
VSAKDLAGQL TDHDWSLFNS IHQVELIHYV LGPQHLRDVT TANLERFMRR FNELQYWVAT 

       730        740        750        760        770        780 
ELCLCPVPGP RAQLLRKFIK LAAHLKEQKN LNSFFAVMFG LSNSAISRLA HTWERLPHKV 

       790        800        810        820        830        840 
RKLYSALERL LDPSWNHRVY RLALAKLSPP VIPFMPLLLK DMTFIHEGNH TLVENLINFE 

       850        860        870        880        890        900 
KMRMMARAAR MLHHCRSHNP VPLSPLRSRV SHLHEDSQVA RISTCSEQSL STRSPASTWA 

       910        920 
YVQQLKVIDN QRELSRLSRE LEP 

« Hide

Isoform 2 [UniParc].

Checksum: 8F67017CA93D36F8
Show »

FASTA59866,067
Isoform 3 [UniParc].

Checksum: 67093C76C1830478
Show »

FASTA88199,452

References

« Hide 'large scale' references
[1]"A family of cAMP-binding proteins that directly activate rap1."
Kawasaki H., Springett G.M., Mochizuki N., Toki S., Nakaya M., Matsuda M., Housman D.E., Graybiel A.M.
Science 282:2275-2279(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, MUTAGENESIS OF ARG-321, VARIANT GLY-193.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT GLY-193.
Tissue: Thalamus.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-193.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS PRO-16 AND GLY-193.
Tissue: Kidney.
[6]"Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP."
de Rooij J., Zwartkruis F.J.T., Verheijen M.H., Cool R.H., Nijman S.M., Wittinghofer A., Bos J.L.
Nature 396:474-477(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-923 (ISOFORM 1), FUNCTION, VARIANT GLY-193.
Tissue: Muscle.
[7]"Mechanism of regulation of the Epac family of cAMP-dependent RapGEFs."
de Rooij J., Rehmann H., van Triest M., Cool R.H., Wittinghofer A., Bos J.L.
J. Biol. Chem. 275:20829-20836(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN DEP, SUBCELLULAR LOCATION.
[8]"Structure and regulation of the cAMP-binding domains of Epac2."
Rehmann H., Prakash B., Wolf E., Rueppel A., De Rooij J., Bos J.L., Wittinghofer A.
Nat. Struct. Biol. 10:26-32(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LEU-315 AND PHE-342.
[9]"Epac1 and PDZ-GEF cooperate in Rap1 mediated endothelial junction control."
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.
Cell. Signal. 23:2056-2064(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"A phosphodiesterase 3B-based signaling complex integrates exchange protein activated by cAMP 1 and phosphatidylinositol 3-kinase signals in human arterial endothelial cells."
Wilson L.S., Baillie G.S., Pritchard L.M., Umana B., Terrin A., Zaccolo M., Houslay M.D., Maurice D.H.
J. Biol. Chem. 286:16285-16296(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDE3B, MUTAGENESIS OF ASP-412; GLU-415; PHE-417; ASP-420 AND PHE-421.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U78168 mRNA. Translation: AAD12740.1. Different initiation.
U78169 mRNA. Translation: AAD02890.1. Different initiation.
AK290230 mRNA. Translation: BAF82919.1.
AC004241 Genomic DNA. No translation available.
AC137054 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW57944.1.
BC017728 mRNA. Translation: AAH17728.2.
AF103905 mRNA. Translation: AAC83381.1.
CCDSCCDS31784.1. [O95398-3]
CCDS41775.1. [O95398-1]
RefSeqNP_001092002.1. NM_001098532.2.
NP_006096.2. NM_006105.5.
UniGeneHs.8578.

3D structure databases

ProteinModelPortalO95398.
SMRO95398. Positions 89-923.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO95398. 3 interactions.
MINTMINT-6741771.
STRING9606.ENSP00000395708.

Chemistry

ChEMBLCHEMBL2029197.

PTM databases

PhosphoSiteO95398.

Proteomic databases

PaxDbO95398.
PRIDEO95398.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000171000; ENSP00000171000; ENSG00000079337. [O95398-3]
ENST00000389212; ENSP00000373864; ENSG00000079337. [O95398-1]
ENST00000395358; ENSP00000378764; ENSG00000079337. [O95398-2]
ENST00000405493; ENSP00000384521; ENSG00000079337. [O95398-3]
ENST00000449771; ENSP00000395708; ENSG00000079337. [O95398-1]
ENST00000549151; ENSP00000448619; ENSG00000079337. [O95398-3]
GeneID10411.
KEGGhsa:10411.
UCSCuc001rpz.4. human. [O95398-1]
uc001rqb.3. human. [O95398-2]

Organism-specific databases

CTD10411.
GeneCardsGC12M048128.
HGNCHGNC:16629. RAPGEF3.
HPACAB004386.
HPA040365.
HPA043518.
MIM606057. gene.
neXtProtNX_O95398.
PharmGKBPA134910959.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0664.
HOGENOMHOG000230545.
InParanoidO95398.
KOK08014.
OMANSFFAVM.
OrthoDBEOG7ZD1TF.
PhylomeDBO95398.
TreeFamTF313184.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressO95398.
BgeeO95398.
CleanExHS_RAPGEF3.
GenevestigatorO95398.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
1.10.840.10. 1 hit.
2.60.120.10. 1 hit.
InterProIPR002373. cAMP/cGMP_kin.
IPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR000591. DEP_dom.
IPR000651. Ras-like_Gua-exchang_fac_N.
IPR019804. Ras_G-nucl-exch_fac_CS.
IPR023578. Ras_GEF_dom.
IPR001895. RasGRF_CDC25.
IPR014710. RmlC-like_jellyroll.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00027. cNMP_binding. 1 hit.
PF00610. DEP. 1 hit.
PF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
[Graphical view]
PRINTSPR00103. CAMPKINASE.
SMARTSM00100. cNMP. 1 hit.
SM00049. DEP. 1 hit.
SM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 1 hit.
[Graphical view]
SUPFAMSSF48366. SSF48366. 3 hits.
SSF51206. SSF51206. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEPS50042. CNMP_BINDING_3. 1 hit.
PS50186. DEP. 1 hit.
PS00720. RASGEF. 1 hit.
PS50009. RASGEF_CAT. 1 hit.
PS50212. RASGEF_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAPGEF3. human.
GeneWikiRAPGEF3.
GenomeRNAi10411.
NextBio13603411.
PROO95398.
SOURCESearch...

Entry information

Entry nameRPGF3_HUMAN
AccessionPrimary (citable) accession number: O95398
Secondary accession number(s): A8K2G5 expand/collapse secondary AC list , E7EQC8, O95634, Q8WVN0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 133 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM