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Q9EQZ6

- RPGF4_MOUSE

UniProt

Q9EQZ6 - RPGF4_MOUSE

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Protein

Rap guanine nucleotide exchange factor 4

Gene

Rapgef4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Guanine nucleotide exchange factor (GEF) for RAP1A, RAP1B and RAP2A small GTPases that is activated by binding cAMP. Seems not to activate RAB3A. Involved in cAMP-dependent, PKA-independent exocytosis through interaction with RIMS2.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi43 – 166124cAMP 1Add
BLAST
Nucleotide bindingi356 – 476121cAMP 2Add
BLAST

GO - Molecular functioni

  1. cAMP binding Source: UniProtKB
  2. cAMP-dependent protein kinase regulator activity Source: InterPro
  3. guanyl-nucleotide exchange factor activity Source: MGI
  4. Ras GTPase binding Source: UniProtKB
  5. Ras guanyl-nucleotide exchange factor activity Source: UniProtKB

GO - Biological processi

  1. calcium ion-dependent exocytosis Source: MGI
  2. cAMP-mediated signaling Source: MGI
  3. insulin secretion Source: MGI
  4. positive regulation of GTPase activity Source: GOC
  5. positive regulation of Ras GTPase activity Source: GOC
  6. regulation of exocytosis Source: MGI
  7. small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Exocytosis

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_237855. Rap1 signalling.
REACT_246176. Integrin alphaIIb beta3 signaling.
REACT_248547. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_263148. Regulation of insulin secretion.

Names & Taxonomyi

Protein namesi
Recommended name:
Rap guanine nucleotide exchange factor 4
Alternative name(s):
Exchange factor directly activated by cAMP 2
Exchange protein directly activated by cAMP 2
Short name:
EPAC 2
cAMP-dependent Rap1 guanine-nucleotide exchange factor
cAMP-regulated guanine nucleotide exchange factor II
Short name:
cAMP-GEFII
Gene namesi
Name:Rapgef4
Synonyms:Cgef2, Epac2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1917723. Rapgef4.

Subcellular locationi

Cytoplasm. Membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  1. cAMP-dependent protein kinase complex Source: InterPro
  2. cytosol Source: MGI
  3. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi467 – 4671L → A: Less than 10% of the wild-type maximal activity. 1 Publication
Mutagenesisi498 – 4981Y → F: 2-fold reduction in maximal activity. 1 Publication
Mutagenesisi569 – 5691Y → A: 2-fold reduction in maximal activity. 1 Publication
Mutagenesisi569 – 5691Y → F: 2-fold reduction in maximal activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10111011Rap guanine nucleotide exchange factor 4PRO_0000068871Add
BLAST

Proteomic databases

MaxQBiQ9EQZ6.
PaxDbiQ9EQZ6.
PRIDEiQ9EQZ6.

PTM databases

PhosphoSiteiQ9EQZ6.

Expressioni

Tissue specificityi

Expressed in cerebellum, pituitary, adrenal gland and liver.1 Publication

Gene expression databases

BgeeiQ9EQZ6.
CleanExiMM_RAPGEF4.
ExpressionAtlasiQ9EQZ6. baseline and differential.
GenevestigatoriQ9EQZ6.

Interactioni

Subunit structurei

Interacts with RAP1B, RIMS1 and RIMS2. Probably part of a complex with RIMS2 and GTP-activated RAB3A.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HRASP011123EBI-772212,EBI-350145From a different organism.

Protein-protein interaction databases

BioGridi208026. 3 interactions.
DIPiDIP-32333N.
IntActiQ9EQZ6. 2 interactions.

Structurei

Secondary structure

1
1011
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 196Combined sources
Beta strandi23 – 253Combined sources
Helixi28 – 3811Combined sources
Turni42 – 465Combined sources
Helixi49 – 5810Combined sources
Beta strandi60 – 645Combined sources
Beta strandi69 – 713Combined sources
Beta strandi79 – 868Combined sources
Beta strandi88 – 925Combined sources
Beta strandi94 – 963Combined sources
Helixi98 – 1003Combined sources
Beta strandi102 – 1076Combined sources
Helixi115 – 1195Combined sources
Beta strandi124 – 13916Combined sources
Helixi140 – 15011Combined sources
Helixi151 – 1533Combined sources
Turni154 – 1574Combined sources
Turni160 – 1623Combined sources
Helixi202 – 21716Combined sources
Helixi219 – 2213Combined sources
Beta strandi222 – 2265Combined sources
Beta strandi231 – 2377Combined sources
Helixi238 – 24710Combined sources
Beta strandi248 – 2503Combined sources
Helixi255 – 26713Combined sources
Beta strandi270 – 2756Combined sources
Beta strandi282 – 2843Combined sources
Beta strandi286 – 2894Combined sources
Helixi290 – 2923Combined sources
Beta strandi293 – 2964Combined sources
Helixi303 – 3108Combined sources
Helixi329 – 3335Combined sources
Helixi336 – 3383Combined sources
Helixi341 – 35111Combined sources
Helixi355 – 3573Combined sources
Helixi362 – 3687Combined sources
Turni369 – 3713Combined sources
Beta strandi373 – 3775Combined sources
Beta strandi383 – 3853Combined sources
Beta strandi393 – 4008Combined sources
Beta strandi402 – 4065Combined sources
Turni407 – 4093Combined sources
Beta strandi410 – 4156Combined sources
Helixi423 – 4286Combined sources
Beta strandi433 – 4386Combined sources
Beta strandi440 – 44910Combined sources
Helixi450 – 4567Combined sources
Turni457 – 4604Combined sources
Beta strandi465 – 4695Combined sources
Beta strandi472 – 4798Combined sources
Beta strandi498 – 5036Combined sources
Helixi505 – 51410Combined sources
Helixi520 – 5223Combined sources
Helixi523 – 54018Combined sources
Helixi543 – 55412Combined sources
Beta strandi559 – 5613Combined sources
Helixi563 – 58826Combined sources
Helixi589 – 5946Combined sources
Helixi596 – 61621Combined sources
Helixi617 – 6204Combined sources
Helixi622 – 6298Combined sources
Beta strandi668 – 6758Combined sources
Turni677 – 6793Combined sources
Beta strandi681 – 6877Combined sources
Helixi692 – 70312Combined sources
Beta strandi710 – 7145Combined sources
Beta strandi720 – 7223Combined sources
Helixi731 – 7333Combined sources
Beta strandi739 – 7435Combined sources
Helixi745 – 7506Combined sources
Helixi755 – 7573Combined sources
Helixi765 – 7684Combined sources
Helixi773 – 78917Combined sources
Helixi793 – 8019Combined sources
Helixi803 – 8053Combined sources
Helixi811 – 83222Combined sources
Helixi837 – 85620Combined sources
Helixi860 – 87112Combined sources
Helixi873 – 8764Combined sources
Helixi879 – 8846Combined sources
Helixi887 – 89812Combined sources
Helixi903 – 91513Combined sources
Helixi924 – 93714Combined sources
Beta strandi940 – 9423Combined sources
Beta strandi945 – 9473Combined sources
Helixi948 – 96417Combined sources
Beta strandi965 – 9673Combined sources
Beta strandi973 – 9753Combined sources
Helixi981 – 9877Combined sources
Helixi996 – 100611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O7FX-ray2.50A1-481[»]
2BYVX-ray2.70E1-1011[»]
3CF6X-ray2.20E324-1011[»]
4F7ZX-ray2.60A1-1011[»]
4MGIX-ray2.80E324-1011[»]
4MGKX-ray2.70E324-1011[»]
4MGYX-ray2.60E324-1011[»]
4MGZX-ray3.00E324-1011[»]
4MH0X-ray2.40E324-1011[»]
ProteinModelPortaliQ9EQZ6.
SMRiQ9EQZ6. Positions 10-1009.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9EQZ6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini216 – 29176DEPPROSITE-ProRule annotationAdd
BLAST
Domaini496 – 634139N-terminal Ras-GEFPROSITE-ProRule annotationAdd
BLAST
Domaini772 – 1009238Ras-GEFPROSITE-ProRule annotationAdd
BLAST

Domaini

The N-terminal nucleotide phosphate binding region cAMP 1 has a much lower affinity for cAMP as compared to cAMP 2.By similarity
The DEP domain is involved in membrane localization independent from regulation by cAMP.By similarity

Sequence similaritiesi

Contains 2 cyclic nucleotide-binding domains.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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0664.
GeneTreeiENSGT00770000120448.
HOGENOMiHOG000230545.
HOVERGENiHBG056985.
InParanoidiQ9EQZ6.
KOiK04351.
OMAiTIYDWEL.
OrthoDBiEOG7ZD1TF.
TreeFamiTF313184.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.840.10. 1 hit.
2.60.120.10. 2 hits.
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. 2 hits.
PF00610. DEP. 1 hit.
PF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
[Graphical view]
PRINTSiPR00103. CAMPKINASE.
SMARTiSM00100. cNMP. 2 hits.
SM00049. DEP. 1 hit.
SM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 1 hit.
[Graphical view]
SUPFAMiSSF48366. SSF48366. 2 hits.
SSF51206. SSF51206. 2 hits.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50042. CNMP_BINDING_3. 2 hits.
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 promoter usage and alternative splicing. Align

Isoform 1 (identifier: Q9EQZ6-1) [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
MVAAHAAHSQ SSAEWIACLD KRPLERSSED VDIIFTRLKG VKAFEKFHPN
60 70 80 90 100
LLRQICLCGY YENLEKGITL FRQGDIGTNW YAVLAGSLDV KVSETSSHQD
110 120 130 140 150
AVTICTLGIG TAFGESILDN TPRHATIVTR ESSELLRIEQ EDFKALWEKY
160 170 180 190 200
RQYMAGLLAP PYGVMETGSN NDRIPDKENT PLIEPHVPLR PAHTITKVPS
210 220 230 240 250
EKILRAGKIL RIAILSRAPH MIRDRKYHLK TYRQCCVGTE LVDWMIQQTS
260 270 280 290 300
CVHSRTQAVG MWQVLLEDGV LNHVDQERHF QDKYLFYRFL DDEREDAPLP
310 320 330 340 350
TEEEKKECDE ELQDTMLLLS QMGPDAHMRM ILRKPPGQRT VDDLEIIYDE
360 370 380 390 400
LLHIKALSHL STTVKRELAG VLIFESHAKG GTVLFNQGEE GTSWYIILKG
410 420 430 440 450
SVNVVIYGKG VVCTLHEGDD FGKLALVNDA PRAASIVLRE DNCHFLRVDK
460 470 480 490 500
EDFNRILRDV EANTVRLKEH DQDVLVLEKV PAGNRAANQG NSQPQQKYTV
510 520 530 540 550
MSGTPEKILE HFLETIRLEP SLNEATDSVL NDFVMMHCVF MPNTQLCPAL
560 570 580 590 600
VAHYHAQPSQ GTEQERMDYA LNNKRRVIRL VLQWAAMYGD LLQEDDVAMA
610 620 630 640 650
FLEEFYVSVS DDARMMAAFK EQLPELEKIV KQISEDAKAP QKKHKVLLQQ
660 670 680 690 700
FNTGDERAQK RQPIRGSDEV LFKVYCIDHT YTTIRVPVAA SVKEVISAVA
710 720 730 740 750
DKLGSGEGLI IVKMNSGGEK VVLKSNDVSV FTTLTINGRL FACPREQFDS
760 770 780 790 800
LTPLPEQEGP TTGTVGTFEL MSSKDLAYQM TTYDWELFNC VHELELIYHT
810 820 830 840 850
FGRHNFKKTT ANLDLFLRRF NEIQFWVVTE VCLCSQLSKR VQLLKKFIKI
860 870 880 890 900
AAHCKEYKNL NSFFAIVMGL SNVAVSRLAL TWEKLPSKFK KFYAEFESLM
910 920 930 940 950
DPSRNHRAYR LTAAKLEPPL IPFMPLLIKD MTFTHEGNKT FIDNLVNFEK
960 970 980 990 1000
MRMIANTART VRYYRSQPFN PDAAQANKNH QDVRSYVRQL NVIDNQRTLS
1010
QMSHRLEPRR P

Note: Produced by alternative promoter usage.

Length:1,011
Mass (Da):115,491
Last modified:March 1, 2001 - v1
Checksum:i449BC537475B03AA
GO
Isoform 2 (identifier: Q9EQZ6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-315: Missing.

Note: Produced by alternative promoter usage.

Show »
Length:696
Mass (Da):79,440
Checksum:i4006240D4B85A747
GO
Isoform 3 (identifier: Q9EQZ6-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     180-197: Missing.

Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.

Show »
Length:993
Mass (Da):113,489
Checksum:iF503405FD9A9C12F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti313 – 3131Q → E in BAB23633. (PubMed:16141072)Curated
Sequence conflicti452 – 4521D → E in BAB23633. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 315315Missing in isoform 2. 2 PublicationsVSP_007614Add
BLAST
Alternative sequencei180 – 19718Missing in isoform 3. 1 PublicationVSP_007615Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF115480 mRNA. Translation: AAD09132.1.
AB021132 mRNA. Translation: BAB18976.1.
AB037668 mRNA. Translation: BAB72180.1.
AK004874 mRNA. Translation: BAB23633.1.
CCDSiCCDS16120.1. [Q9EQZ6-3]
CCDS57176.1. [Q9EQZ6-1]
RefSeqiNP_001191094.1. NM_001204165.1. [Q9EQZ6-1]
NP_001191095.1. NM_001204166.1.
NP_062662.1. NM_019688.2. [Q9EQZ6-3]
UniGeneiMm.196153.

Genome annotation databases

EnsembliENSMUST00000090826; ENSMUSP00000088336; ENSMUSG00000049044. [Q9EQZ6-1]
ENSMUST00000102698; ENSMUSP00000099759; ENSMUSG00000049044. [Q9EQZ6-3]
GeneIDi56508.
KEGGimmu:56508.
UCSCiuc008kbn.2. mouse. [Q9EQZ6-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF115480 mRNA. Translation: AAD09132.1 .
AB021132 mRNA. Translation: BAB18976.1 .
AB037668 mRNA. Translation: BAB72180.1 .
AK004874 mRNA. Translation: BAB23633.1 .
CCDSi CCDS16120.1. [Q9EQZ6-3 ]
CCDS57176.1. [Q9EQZ6-1 ]
RefSeqi NP_001191094.1. NM_001204165.1. [Q9EQZ6-1 ]
NP_001191095.1. NM_001204166.1.
NP_062662.1. NM_019688.2. [Q9EQZ6-3 ]
UniGenei Mm.196153.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1O7F X-ray 2.50 A 1-481 [» ]
2BYV X-ray 2.70 E 1-1011 [» ]
3CF6 X-ray 2.20 E 324-1011 [» ]
4F7Z X-ray 2.60 A 1-1011 [» ]
4MGI X-ray 2.80 E 324-1011 [» ]
4MGK X-ray 2.70 E 324-1011 [» ]
4MGY X-ray 2.60 E 324-1011 [» ]
4MGZ X-ray 3.00 E 324-1011 [» ]
4MH0 X-ray 2.40 E 324-1011 [» ]
ProteinModelPortali Q9EQZ6.
SMRi Q9EQZ6. Positions 10-1009.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208026. 3 interactions.
DIPi DIP-32333N.
IntActi Q9EQZ6. 2 interactions.

PTM databases

PhosphoSitei Q9EQZ6.

Proteomic databases

MaxQBi Q9EQZ6.
PaxDbi Q9EQZ6.
PRIDEi Q9EQZ6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000090826 ; ENSMUSP00000088336 ; ENSMUSG00000049044 . [Q9EQZ6-1 ]
ENSMUST00000102698 ; ENSMUSP00000099759 ; ENSMUSG00000049044 . [Q9EQZ6-3 ]
GeneIDi 56508.
KEGGi mmu:56508.
UCSCi uc008kbn.2. mouse. [Q9EQZ6-1 ]

Organism-specific databases

CTDi 11069.
MGIi MGI:1917723. Rapgef4.

Phylogenomic databases

eggNOGi COG0664.
GeneTreei ENSGT00770000120448.
HOGENOMi HOG000230545.
HOVERGENi HBG056985.
InParanoidi Q9EQZ6.
KOi K04351.
OMAi TIYDWEL.
OrthoDBi EOG7ZD1TF.
TreeFami TF313184.

Enzyme and pathway databases

Reactomei REACT_237855. Rap1 signalling.
REACT_246176. Integrin alphaIIb beta3 signaling.
REACT_248547. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_263148. Regulation of insulin secretion.

Miscellaneous databases

EvolutionaryTracei Q9EQZ6.
NextBioi 312814.
PROi Q9EQZ6.
SOURCEi Search...

Gene expression databases

Bgeei Q9EQZ6.
CleanExi MM_RAPGEF4.
ExpressionAtlasi Q9EQZ6. baseline and differential.
Genevestigatori Q9EQZ6.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
1.10.840.10. 1 hit.
2.60.120.10. 2 hits.
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. RASGEF_cat_dom.
IPR014710. RmlC-like_jellyroll.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00027. cNMP_binding. 2 hits.
PF00610. DEP. 1 hit.
PF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
[Graphical view ]
PRINTSi PR00103. CAMPKINASE.
SMARTi SM00100. cNMP. 2 hits.
SM00049. DEP. 1 hit.
SM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 1 hit.
[Graphical view ]
SUPFAMi SSF48366. SSF48366. 2 hits.
SSF51206. SSF51206. 2 hits.
SSF54236. SSF54236. 1 hit.
PROSITEi PS50042. CNMP_BINDING_3. 2 hits.
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. "A brain cAMP-dependent Rap1 guanine-nucleotide exchange factor."
    Gaudriault G.E., Takaya K., Vale W.W.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH RIMS1 AND RIMS2.
  3. "Characterization of the gene EPAC2: structure, chromosomal localization, tissue expression, and identification of the liver-specific isoform."
    Ueno H., Shibasaki T., Iwanaga T., Takahashi K., Yokoyama Y., Liu L.M., Yokoi N., Ozaki N., Matsukura S., Yano H., Seino S.
    Genomics 78:91-98(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE PROMOTER USAGE.
    Tissue: Liver.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Liver.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-463.
  6. "Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B."
    Rehmann H., Arias-Palomo E., Hadders M.A., Schwede F., Llorca O., Bos J.L.
    Nature 455:124-127(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 324-1011 IN COMPLEX WITH CAMP ANALOG AND RAP1B, SUBUNIT, MUTAGENESIS OF LEU-467; TYR-498 AND TYR-569.

Entry informationi

Entry nameiRPGF4_MOUSE
AccessioniPrimary (citable) accession number: Q9EQZ6
Secondary accession number(s): Q8VIP9, Q9CW52, Q9Z1P0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3