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O95398

- RPGF3_HUMAN

UniProt

O95398 - RPGF3_HUMAN

Protein

Rap guanine nucleotide exchange factor 3

Gene

RAPGEF3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 6 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    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.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi245 – 363119cAMPAdd
    BLAST

    GO - Molecular functioni

    1. cAMP binding Source: UniProtKB-KW
    2. cAMP-dependent protein kinase regulator activity Source: InterPro
    3. guanyl-nucleotide exchange factor activity Source: ProtInc
    4. protein binding Source: IntAct
    5. Rap guanyl-nucleotide exchange factor activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. blood coagulation Source: Reactome
    3. cAMP-mediated signaling Source: BHF-UCL
    4. cell proliferation Source: ProtInc
    5. cellular response to cAMP Source: UniProtKB
    6. energy reserve metabolic process Source: Reactome
    7. establishment of endothelial barrier Source: UniProtKB
    8. platelet activation Source: Reactome
    9. positive regulation of angiogenesis Source: UniProtKB
    10. positive regulation of cAMP catabolic process Source: BHF-UCL
    11. positive regulation of Rap GTPase activity Source: UniProtKB
    12. positive regulation of stress fiber assembly Source: UniProtKB
    13. Rap protein signal transduction Source: UniProtKB
    14. regulation of actin cytoskeleton reorganization Source: UniProtKB
    15. regulation of insulin secretion Source: Reactome
    16. signal transduction Source: ProtInc
    17. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Keywords - Biological processi

    Angiogenesis

    Keywords - Ligandi

    cAMP, cAMP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_18325. Regulation of insulin secretion.
    REACT_23898. Rap1 signalling.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:RAPGEF3
    Synonyms:CGEF1, EPAC, EPAC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:16629. RAPGEF3.

    Subcellular locationi

    Endomembrane system 1 Publication

    GO - Cellular componenti

    1. cAMP-dependent protein kinase complex Source: InterPro
    2. endomembrane system Source: UniProtKB-SubCell
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: ProtInc
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi315 – 3151L → W: Abolishes activation of RAP1A. 1 Publication
    Mutagenesisi321 – 3211R → K: Reduces activation of RAP1A. 1 Publication
    Mutagenesisi342 – 3421F → A or T: Diminishes GEF activity dependence on cAMP concentration. 1 Publication
    Mutagenesisi412 – 4121D → A: Abolishes interaction with PDE3B. 1 Publication
    Mutagenesisi415 – 4151E → A: Abolishes interaction with PDE3B. 1 Publication
    Mutagenesisi417 – 4171F → A: Abolishes interaction with PDE3B. 1 Publication
    Mutagenesisi420 – 4201D → A: Abolishes interaction with PDE3B. 1 Publication
    Mutagenesisi421 – 4211F → A: Abolishes interaction with PDE3B. 1 Publication

    Organism-specific databases

    PharmGKBiPA134910959.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 923923Rap guanine nucleotide exchange factor 3PRO_0000068867Add
    BLAST

    Proteomic databases

    PaxDbiO95398.
    PRIDEiO95398.

    PTM databases

    PhosphoSiteiO95398.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiO95398.
    BgeeiO95398.
    CleanExiHS_RAPGEF3.
    GenevestigatoriO95398.

    Organism-specific databases

    HPAiCAB004386.
    HPA040365.
    HPA043518.

    Interactioni

    Subunit structurei

    Interacts with PDE3B.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDE3BQ133708EBI-6172806,EBI-6172856

    Protein-protein interaction databases

    IntActiO95398. 3 interactions.
    MINTiMINT-6741771.
    STRINGi9606.ENSP00000395708.

    Structurei

    3D structure databases

    ProteinModelPortaliO95398.
    SMRiO95398. Positions 89-923.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini110 – 18677DEPPROSITE-ProRule annotationAdd
    BLAST
    Domaini384 – 518135N-terminal Ras-GEFPROSITE-ProRule annotationAdd
    BLAST
    Domaini662 – 889228Ras-GEFPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni218 – 24225Interaction with PDE3BAdd
    BLAST
    Regioni398 – 42225Interaction with PDE3BAdd
    BLAST

    Domaini

    The DEP domain is involved in membrane localization independent from regulation by cAMP.1 Publication

    Sequence similaritiesi

    Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation
    Contains 1 DEP domain.PROSITE-ProRule annotation
    Contains 1 N-terminal Ras-GEF domain.PROSITE-ProRule annotation
    Contains 1 Ras-GEF domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0664.
    HOGENOMiHOG000230545.
    InParanoidiO95398.
    KOiK08014.
    OMAiNSFFAVM.
    OrthoDBiEOG7ZD1TF.
    PhylomeDBiO95398.
    TreeFamiTF313184.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    1.10.840.10. 1 hit.
    2.60.120.10. 1 hit.
    InterProiIPR002373. 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]
    PfamiPF00027. cNMP_binding. 1 hit.
    PF00610. DEP. 1 hit.
    PF00617. RasGEF. 1 hit.
    PF00618. RasGEF_N. 1 hit.
    [Graphical view]
    PRINTSiPR00103. CAMPKINASE.
    SMARTiSM00100. cNMP. 1 hit.
    SM00049. DEP. 1 hit.
    SM00147. RasGEF. 1 hit.
    SM00229. RasGEFN. 1 hit.
    [Graphical view]
    SUPFAMiSSF48366. SSF48366. 3 hits.
    SSF51206. SSF51206. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS50042. 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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95398-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MKVGWPGESC WQVGLAVEDS PALGAPRVGA LPDVVPEGTL LNMVLRRMHR    50
    PRSCSYQLLL EHQRPSCIQG LRWTPLTNSE ESLDFSESLE QASTERVLRA 100
    GRQLHRHLLA TCPNLIRDRK YHLRLYRQCC SGRELVDGIL ALGLGVHSRS 150
    QVVGICQVLL DEGALCHVKH DWAFQDRDAQ FYRFPGPEPE PVRTHEMEEE 200
    LAEAVALLSQ RGPDALLTVA LRKPPGQRTD EELDLIFEEL LHIKAVAHLS 250
    NSVKRELAAV LLFEPHSKAG TVLFSQGDKG TSWYIIWKGS VNVVTHGKGL 300
    VTTLHEGDDF GQLALVNDAP RAATIILRED NCHFLRVDKQ DFNRIIKDVE 350
    AKTMRLEEHG KVVLVLERAS QGAGPSRPPT PGRNRYTVMS GTPEKILELL 400
    LEAMGPDSSA HDPTETFLSD FLLTHRVFMP SAQLCAALLH HFHVEPAGGS 450
    EQERSTYVCN KRQQILRLVS QWVALYGSML HTDPVATSFL QKLSDLVGRD 500
    TRLSNLLREQ WPERRRCHRL ENGCGNASPQ MKARNLPVWL PNQDEPLPGS 550
    SCAIQVGDKV PYDICRPDHS VLTLQLPVTA SVREVMAALA QEDGWTKGQV 600
    LVKVNSAGDA IGLQPDARGV ATSLGLNERL FVVNPQEVHE LIPHPDQLGP 650
    TVGSAEGLDL VSAKDLAGQL TDHDWSLFNS IHQVELIHYV LGPQHLRDVT 700
    TANLERFMRR FNELQYWVAT ELCLCPVPGP RAQLLRKFIK LAAHLKEQKN 750
    LNSFFAVMFG LSNSAISRLA HTWERLPHKV RKLYSALERL LDPSWNHRVY 800
    RLALAKLSPP VIPFMPLLLK DMTFIHEGNH TLVENLINFE KMRMMARAAR 850
    MLHHCRSHNP VPLSPLRSRV SHLHEDSQVA RISTCSEQSL STRSPASTWA 900
    YVQQLKVIDN QRELSRLSRE LEP 923
    Length:923
    Mass (Da):103,751
    Last modified:January 11, 2011 - v6
    Checksum:i8B3A24341F20515F
    GO
    Isoform 2 (identifier: O95398-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:598
    Mass (Da):66,067
    Checksum:i8F67017CA93D36F8
    GO
    Isoform 3 (identifier: O95398-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-42: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:881
    Mass (Da):99,452
    Checksum:i67093C76C1830478
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti64 – 641R → H in AAD12740. (PubMed:9856955)Curated
    Sequence conflicti64 – 641R → H in AAD02890. (PubMed:9856955)Curated
    Sequence conflicti106 – 1061R → Q in AAD12740. (PubMed:9856955)Curated
    Sequence conflicti106 – 1061R → Q in AAD02890. (PubMed:9856955)Curated
    Sequence conflicti116 – 1161I → T in AAC83381. (PubMed:9853756)Curated
    Sequence conflicti330 – 3301D → Y in AAD12740. (PubMed:9856955)Curated
    Sequence conflicti330 – 3301D → Y in AAD02890. (PubMed:9856955)Curated
    Sequence conflicti394 – 3941E → D in AAD12740. (PubMed:9856955)Curated
    Sequence conflicti394 – 3941E → D in AAD02890. (PubMed:9856955)Curated
    Sequence conflicti406 – 4061P → L in AAD12740. (PubMed:9856955)Curated
    Sequence conflicti406 – 4061P → L in AAD02890. (PubMed:9856955)Curated
    Sequence conflicti414 – 4141T → K in AAD12740. (PubMed:9856955)Curated
    Sequence conflicti414 – 4141T → K in AAD02890. (PubMed:9856955)Curated
    Sequence conflicti491 – 4911Q → H in AAD12740. (PubMed:9856955)Curated
    Sequence conflicti638 – 6381V → A in AAC83381. (PubMed:9853756)Curated
    Sequence conflicti736 – 7361R → K in AAD12740. (PubMed:9856955)Curated
    Sequence conflicti751 – 7511L → V in AAD12740. (PubMed:9856955)Curated
    Sequence conflicti765 – 7651A → P in AAD12740. (PubMed:9856955)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161A → P.1 Publication
    Corresponds to variant rs11168230 [ dbSNP | Ensembl ].
    VAR_047924
    Natural varianti193 – 1931R → G.5 Publications
    Corresponds to variant rs2016123 [ dbSNP | Ensembl ].
    VAR_047925
    Natural varianti374 – 3741G → S.
    Corresponds to variant rs12422983 [ dbSNP | Ensembl ].
    VAR_047926
    Natural varianti517 – 5171C → Y.
    Corresponds to variant rs61709815 [ dbSNP | Ensembl ].
    VAR_061784

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4242Missing in isoform 3. 1 PublicationVSP_047007Add
    BLAST
    Alternative sequencei533 – 59866ARNLP…GWTKG → VSAWPQFLSSAPPGLQAPPS PPDPEGLCGRGKLSSHRHTL GSLIGVHGALAACGALGQAV PGGAEA in isoform 2. 1 PublicationVSP_007608Add
    BLAST
    Alternative sequencei599 – 923325Missing in isoform 2. 1 PublicationVSP_007609Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS31784.1. [O95398-3]
    CCDS41775.1. [O95398-1]
    RefSeqiNP_001092002.1. NM_001098532.2.
    NP_006096.2. NM_006105.5.
    UniGeneiHs.8578.

    Genome annotation databases

    EnsembliENST00000389212; ENSP00000373864; ENSG00000079337. [O95398-1]
    ENST00000395358; ENSP00000378764; ENSG00000079337. [O95398-2]
    ENST00000405493; ENSP00000384521; ENSG00000079337. [O95398-3]
    ENST00000449771; ENSP00000395708; ENSG00000079337. [O95398-1]
    ENST00000549151; ENSP00000448619; ENSG00000079337. [O95398-3]
    GeneIDi10411.
    KEGGihsa:10411.
    UCSCiuc001rpz.4. human. [O95398-1]
    uc001rqb.3. human. [O95398-2]
    uc009zkp.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS31784.1. [O95398-3 ]
    CCDS41775.1. [O95398-1 ]
    RefSeqi NP_001092002.1. NM_001098532.2.
    NP_006096.2. NM_006105.5.
    UniGenei Hs.8578.

    3D structure databases

    ProteinModelPortali O95398.
    SMRi O95398. Positions 89-923.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O95398. 3 interactions.
    MINTi MINT-6741771.
    STRINGi 9606.ENSP00000395708.

    Chemistry

    ChEMBLi CHEMBL2029197.

    PTM databases

    PhosphoSitei O95398.

    Proteomic databases

    PaxDbi O95398.
    PRIDEi O95398.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli 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 ]
    GeneIDi 10411.
    KEGGi hsa:10411.
    UCSCi uc001rpz.4. human. [O95398-1 ]
    uc001rqb.3. human. [O95398-2 ]
    uc009zkp.3. human.

    Organism-specific databases

    CTDi 10411.
    GeneCardsi GC12M048128.
    HGNCi HGNC:16629. RAPGEF3.
    HPAi CAB004386.
    HPA040365.
    HPA043518.
    MIMi 606057. gene.
    neXtProti NX_O95398.
    PharmGKBi PA134910959.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0664.
    HOGENOMi HOG000230545.
    InParanoidi O95398.
    KOi K08014.
    OMAi NSFFAVM.
    OrthoDBi EOG7ZD1TF.
    PhylomeDBi O95398.
    TreeFami TF313184.

    Enzyme and pathway databases

    Reactomei REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_18325. Regulation of insulin secretion.
    REACT_23898. Rap1 signalling.

    Miscellaneous databases

    ChiTaRSi RAPGEF3. human.
    GeneWikii RAPGEF3.
    GenomeRNAii 10411.
    NextBioi 13603411.
    PROi O95398.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95398.
    Bgeei O95398.
    CleanExi HS_RAPGEF3.
    Genevestigatori O95398.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    1.10.840.10. 1 hit.
    2.60.120.10. 1 hit.
    InterProi IPR002373. 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 ]
    Pfami PF00027. cNMP_binding. 1 hit.
    PF00610. DEP. 1 hit.
    PF00617. RasGEF. 1 hit.
    PF00618. RasGEF_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00103. CAMPKINASE.
    SMARTi SM00100. cNMP. 1 hit.
    SM00049. DEP. 1 hit.
    SM00147. RasGEF. 1 hit.
    SM00229. RasGEFN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48366. SSF48366. 3 hits.
    SSF51206. SSF51206. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS50042. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. 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.
      , 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.
      , 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. 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. Cited for: MUTAGENESIS OF LEU-315 AND PHE-342.
    9. 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.

    Entry informationi

    Entry nameiRPGF3_HUMAN
    AccessioniPrimary (citable) accession number: O95398
    Secondary accession number(s): A8K2G5
    , E7EQC8, O95634, Q8WVN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2003
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 135 of the entry and version 6 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 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3