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O95398

- RPGF3_HUMAN

UniProt

O95398 - RPGF3_HUMAN

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Protein
Rap guanine nucleotide exchange factor 3
Gene
RAPGEF3, CGEF1, EPAC, EPAC1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 363119cAMP
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

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
Complete GO annotation...

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 3
PRO_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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini110 – 18677DEP
Add
BLAST
Domaini384 – 518135N-terminal Ras-GEF
Add
BLAST
Domaini662 – 889228Ras-GEF
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni218 – 24225Interaction with PDE3B
Add
BLAST
Regioni398 – 42225Interaction with PDE3B
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 DEP domain.
Contains 1 Ras-GEF domain.

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.

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.
VSP_047007Add
BLAST
Alternative sequencei533 – 59866ARNLP…GWTKG → VSAWPQFLSSAPPGLQAPPS PPDPEGLCGRGKLSSHRHTL GSLIGVHGALAACGALGQAV PGGAEA in isoform 2.
VSP_007608Add
BLAST
Alternative sequencei599 – 923325Missing in isoform 2.
VSP_007609Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641R → H in AAD12740. 1 Publication
Sequence conflicti64 – 641R → H in AAD02890. 1 Publication
Sequence conflicti106 – 1061R → Q in AAD12740. 1 Publication
Sequence conflicti106 – 1061R → Q in AAD02890. 1 Publication
Sequence conflicti116 – 1161I → T in AAC83381. 1 Publication
Sequence conflicti330 – 3301D → Y in AAD12740. 1 Publication
Sequence conflicti330 – 3301D → Y in AAD02890. 1 Publication
Sequence conflicti394 – 3941E → D in AAD12740. 1 Publication
Sequence conflicti394 – 3941E → D in AAD02890. 1 Publication
Sequence conflicti406 – 4061P → L in AAD12740. 1 Publication
Sequence conflicti406 – 4061P → L in AAD02890. 1 Publication
Sequence conflicti414 – 4141T → K in AAD12740. 1 Publication
Sequence conflicti414 – 4141T → K in AAD02890. 1 Publication
Sequence conflicti491 – 4911Q → H in AAD12740. 1 Publication
Sequence conflicti638 – 6381V → A in AAC83381. 1 Publication
Sequence conflicti736 – 7361R → K in AAD12740. 1 Publication
Sequence conflicti751 – 7511L → V in AAD12740. 1 Publication
Sequence conflicti765 – 7651A → P in AAD12740. 1 Publication

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

EnsembliENST00000171000; 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]
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...

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 ENST00000171000 ; 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 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 134 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

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