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Protein

Rap guanine nucleotide exchange factor 3

Gene

RAPGEF3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 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. 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. negative regulation of syncytium formation by plasma membrane fusion Source: UniProtKB
  9. platelet activation Source: Reactome
  10. positive regulation of angiogenesis Source: UniProtKB
  11. positive regulation of cAMP catabolic process Source: BHF-UCL
  12. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
  13. positive regulation of protein acetylation Source: UniProtKB
  14. positive regulation of protein export from nucleus Source: UniProtKB
  15. positive regulation of Rap GTPase activity Source: UniProtKB
  16. positive regulation of stress fiber assembly Source: UniProtKB
  17. positive regulation of syncytium formation by plasma membrane fusion Source: UniProtKB
  18. Rap protein signal transduction Source: UniProtKB
  19. regulation of actin cytoskeleton reorganization Source: UniProtKB
  20. regulation of insulin secretion Source: Reactome
  21. signal transduction Source: ProtInc
  22. 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 Componenti: 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: UniProtKB
  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 3PRO_0000068867Add
BLAST

Proteomic databases

MaxQBiO95398.
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

BgeeiO95398.
CleanExiHS_RAPGEF3.
ExpressionAtlasiO95398. baseline and differential.
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.
GeneTreeiENSGT00780000121847.
HOGENOMiHOG000230545.
InParanoidiO95398.
KOiK08014.
OMAiWVATELC.
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. RASGEF_cat_dom.
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. AlignAdd to basket

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

        10         20         30         40         50
MKVGWPGESC WQVGLAVEDS PALGAPRVGA LPDVVPEGTL LNMVLRRMHR
60 70 80 90 100
PRSCSYQLLL EHQRPSCIQG LRWTPLTNSE ESLDFSESLE QASTERVLRA
110 120 130 140 150
GRQLHRHLLA TCPNLIRDRK YHLRLYRQCC SGRELVDGIL ALGLGVHSRS
160 170 180 190 200
QVVGICQVLL DEGALCHVKH DWAFQDRDAQ FYRFPGPEPE PVRTHEMEEE
210 220 230 240 250
LAEAVALLSQ RGPDALLTVA LRKPPGQRTD EELDLIFEEL LHIKAVAHLS
260 270 280 290 300
NSVKRELAAV LLFEPHSKAG TVLFSQGDKG TSWYIIWKGS VNVVTHGKGL
310 320 330 340 350
VTTLHEGDDF GQLALVNDAP RAATIILRED NCHFLRVDKQ DFNRIIKDVE
360 370 380 390 400
AKTMRLEEHG KVVLVLERAS QGAGPSRPPT PGRNRYTVMS GTPEKILELL
410 420 430 440 450
LEAMGPDSSA HDPTETFLSD FLLTHRVFMP SAQLCAALLH HFHVEPAGGS
460 470 480 490 500
EQERSTYVCN KRQQILRLVS QWVALYGSML HTDPVATSFL QKLSDLVGRD
510 520 530 540 550
TRLSNLLREQ WPERRRCHRL ENGCGNASPQ MKARNLPVWL PNQDEPLPGS
560 570 580 590 600
SCAIQVGDKV PYDICRPDHS VLTLQLPVTA SVREVMAALA QEDGWTKGQV
610 620 630 640 650
LVKVNSAGDA IGLQPDARGV ATSLGLNERL FVVNPQEVHE LIPHPDQLGP
660 670 680 690 700
TVGSAEGLDL VSAKDLAGQL TDHDWSLFNS IHQVELIHYV LGPQHLRDVT
710 720 730 740 750
TANLERFMRR FNELQYWVAT ELCLCPVPGP RAQLLRKFIK LAAHLKEQKN
760 770 780 790 800
LNSFFAVMFG LSNSAISRLA HTWERLPHKV RKLYSALERL LDPSWNHRVY
810 820 830 840 850
RLALAKLSPP VIPFMPLLLK DMTFIHEGNH TLVENLINFE KMRMMARAAR
860 870 880 890 900
MLHHCRSHNP VPLSPLRSRV SHLHEDSQVA RISTCSEQSL STRSPASTWA
910 920
YVQQLKVIDN QRELSRLSRE LEP
Length:923
Mass (Da):103,751
Last modified:January 10, 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.Curated
The sequence AAD12740.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL2029197.

PTM databases

PhosphoSiteiO95398.

Proteomic databases

MaxQBiO95398.
PaxDbiO95398.
PRIDEiO95398.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.

Organism-specific databases

CTDi10411.
GeneCardsiGC12M048128.
HGNCiHGNC:16629. RAPGEF3.
HPAiCAB004386.
HPA040365.
HPA043518.
MIMi606057. gene.
neXtProtiNX_O95398.
PharmGKBiPA134910959.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0664.
GeneTreeiENSGT00780000121847.
HOGENOMiHOG000230545.
InParanoidiO95398.
KOiK08014.
OMAiWVATELC.
OrthoDBiEOG7ZD1TF.
PhylomeDBiO95398.
TreeFamiTF313184.

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.

Miscellaneous databases

ChiTaRSiRAPGEF3. human.
GeneWikiiRAPGEF3.
GenomeRNAii10411.
NextBioi13603411.
PROiO95398.
SOURCEiSearch...

Gene expression databases

BgeeiO95398.
CleanExiHS_RAPGEF3.
ExpressionAtlasiO95398. baseline and differential.
GenevestigatoriO95398.

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. RASGEF_cat_dom.
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]
ProtoNetiSearch...

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(2003) [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(2005) [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(2003) [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(1997) [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(1999) [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(2010) [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 19, 2003
Last sequence update: January 10, 2011
Last modified: March 31, 2015
This is version 140 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

Caution

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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.