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Protein

Ras-specific guanine nucleotide-releasing factor 2

Gene

Rasgrf2

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

Functioni

Functions as a calcium-regulated nucleotide exchange factor activating both Ras and RAC1 through the exchange of bound GDP for GTP. Preferentially activates HRAS in vivo compared to RRAS based on their different types of prenylation. Functions in synaptic plasticity by contributing to the induction of long term potentiation.8 Publications

GO - Molecular functioni

GO - Biological processi

  • long-term synaptic potentiation Source: MGI
  • regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: MGI
  • regulation of Rho protein signal transduction Source: InterPro
  • small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Calcium, Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-specific guanine nucleotide-releasing factor 2
Short name:
Ras-GRF2
Alternative name(s):
Ras guanine nucleotide exchange factor 2
Gene namesi
Name:Rasgrf2
Synonyms:Grf2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:109137. Rasgrf2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice do not display overt phenotype.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1022 – 10221R → E: Loss of interaction with Ras. Loss of Ras activation. Loss of ubiquitination. 1 Publication
Mutagenesisi1092 – 10921R → E: Partial loss of interaction with Ras. Partial loss of Ras activation. Partial loss of ubiquitination. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11891189Ras-specific guanine nucleotide-releasing factor 2PRO_0000312864Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei725 – 7251PhosphoserineCombined sources
Modified residuei726 – 7261PhosphoserineCombined sources
Modified residuei736 – 7361Phosphoserine; by CDK5By similarity
Modified residuei745 – 7451PhosphoserineCombined sources
Modified residuei749 – 7491PhosphoserineCombined sources
Modified residuei801 – 8011PhosphoserineCombined sources
Modified residuei805 – 8051PhosphoserineCombined sources
Modified residuei924 – 9241PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by CDK5; down-regulates RASGRF2-mediated RAC1 activation.2 Publications
Ubiquitinated upon interaction with Ras. Ubiquitination leads to degradation through the 26S proteasome.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP70392.
PRIDEiP70392.

PTM databases

iPTMnetiP70392.
PhosphoSiteiP70392.

Expressioni

Tissue specificityi

Expressed in brain in the nucleus of the solitary tract. Not observed in the hippocampus (at protein level).1 Publication

Developmental stagei

Expression increases in the cortex from birth to adulthood.1 Publication

Interactioni

Subunit structurei

Homooligomer and heterooligomer with RASGRF1. Interacts with Ras and RAC1. Interacts in a calcium-dependent manner with calmodulin. Interacts with EPB49 and probably CDK5R1. Interacts with the AMPA receptor through GRIA1. Interacts with microtubules.6 Publications

Protein-protein interaction databases

BioGridi202601. 1 interaction.
IntActiP70392. 4 interactions.
MINTiMINT-1753415.

Structurei

3D structure databases

ProteinModelPortaliP70392.
SMRiP70392. Positions 954-1186.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 133112PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini205 – 23430IQPROSITE-ProRule annotationAdd
BLAST
Domaini243 – 429187DHPROSITE-ProRule annotationAdd
BLAST
Domaini470 – 588119PH 2PROSITE-ProRule annotationAdd
BLAST
Domaini635 – 755121N-terminal Ras-GEFPROSITE-ProRule annotationAdd
BLAST
Domaini954 – 1186233Ras-GEFPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni743 – 7519Regulates proteasomal degradation
Regioni1051 – 108030Responsible of the affinity for farnesylated versus geranylgeranylated RasAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili158 – 19336Sequence analysisAdd
BLAST

Domaini

The Ras-GEF domain and the N-terminal Ras-GEF domain form a Ras-binding site and mediate Ras activation.By similarity
The IQ domain mediates the calcium-dependent interaction with calmodulin but is dispensable for the Ras-GEF activity.
The DH (DBL-homology) domain mediates interaction with RASGRF1 and probably EPB49 and is required for RAC1 activation.

Sequence similaritiesi

Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 IQ domain.PROSITE-ProRule annotation
Contains 1 N-terminal Ras-GEF domain.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation
Contains 1 Ras-GEF domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

HOVERGENiHBG005208.
InParanoidiP70392.
KOiK12326.
PhylomeDBiP70392.

Family and domain databases

Gene3Di1.10.840.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
InterProiIPR000219. DH-domain.
IPR000048. IQ_motif_EF-hand-BS.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000651. Ras-like_Gua-exchang_fac_N.
IPR019804. Ras_G-nucl-exch_fac_CS.
IPR023578. Ras_GEF_dom.
IPR001895. RASGEF_cat_dom.
IPR030744. RasGRF2.
[Graphical view]
PANTHERiPTHR23113:SF187. PTHR23113:SF187. 3 hits.
PfamiPF00169. PH. 1 hit.
PF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 2 hits.
SM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF48366. SSF48366. 2 hits.
SSF50729. SSF50729. 2 hits.
PROSITEiPS50010. DH_2. 1 hit.
PS50096. IQ. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS00720. RASGEF. 1 hit.
PS50009. RASGEF_CAT. 1 hit.
PS50212. RASGEF_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P70392-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKSVRYNEG HALYLAMLAR KEGTKRGFLS KKAAEASRWH EKWFALYQNV
60 70 80 90 100
LFYFEGEQSG RPAGMYLLEG CSCERTPAPP RTNAGPAGAR DALDKQYYFT
110 120 130 140 150
VLFGHDGQKP LELRCEEEQA GKEWMEAIHQ ASYADILIER EVLMQKYIHL
160 170 180 190 200
VQIVETEKIA TNQLRHQLED QDTEIERLKS EIVALNKTKE RMRPYHVHQE
210 220 230 240 250
EEDPDIKKIK KVQSFMRGWL CRRKWKTIVQ DYICSPHAES MRKRNQIVFT
260 270 280 290 300
MVEAETEYVH QLYILVNGFL RPLRMAASSK KPPINHDDVS SIFLNSETIM
310 320 330 340 350
FLHEIFHQGL KARLANWPTL VLADLFDILL PMLNIYQEFV RNHQYSLQVL
360 370 380 390 400
ANCKQNRDFD KLLKQYEANP ACEGRMLETF LTYPMFQIPR YIITLHELLA
410 420 430 440 450
HTPHEHVERK SLEFAKSKLE ELSRVMHDEV SDTENIRKNL AIERMIVEGC
460 470 480 490 500
DILLDTSQTF IRQGSLIQVP SVERGKLSKV RLGSLSLKKE GERQCFLFTK
510 520 530 540 550
HFLICTRSSG GKLHLLKTGG VLSLIQCTLI EEPDGSDDDP KGSGHMFGHL
560 570 580 590 600
DFKIVVEPPD AASFTVVLLA PSRQEKAAWM SDISQCVDNI RCNGLMTIVF
610 620 630 640 650
EENSKVTVPH MIKSDARLHK DDTDICFSKT LNSCKVPQIR YASVERLLER
660 670 680 690 700
LTDLRFLSID FLNTFLHTYR IFTTATVVLA KLSDIYKRPF TSIPVRSLEL
710 720 730 740 750
FFATSQNNRE HLVDGKSPRL CRKFSSPPPL AVSRTSSPVR ARKLSLTSSL
760 770 780 790 800
NSRIGALDLT NSSSSSSPTT TTHSPAASPP PHTAVLESAP ADKAGDSADM
810 820 830 840 850
SPCRSPTTPR HLRYRQPGGQ VADSAHCSVS PASAFAIATA AAGHGSPPGF
860 870 880 890 900
NNERTCDKEF IIRRTATNRV LNVLRHWVSK HAQDFELNNE LKMNVLNLLE
910 920 930 940 950
EVLRDPDLLP QERKATANIL RALSQDDQDD IHLKLEDIIQ MTDCPKAECF
960 970 980 990 1000
ETLSAMELAE QITLLDHIVF RSIPYEEFLG QGWMKLDKNE RTPYIMKTSQ
1010 1020 1030 1040 1050
HFNEMSNLVA SQIMNYADIS SRANAIEKWV AVADICRCLH NYNGVLEITS
1060 1070 1080 1090 1100
ALNRSAIYRL KKTWAKVSKQ TKALMDKLQK TVSSEGRFKN LRETLKNCNP
1110 1120 1130 1140 1150
PAVPYLGMYL TDLAFIEEGT PNFTEEGLVN FSKMRMISHI IREIRQFQQT
1160 1170 1180
AYRIDQQPKV IQYLLDKALV IDEDSLYELS LKIEPRLPA
Length:1,189
Mass (Da):135,668
Last modified:May 1, 2000 - v2
Checksum:i42E346B623F18E59
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1023 – 10231A → P in AAF18297 (PubMed:11909944).Curated
Sequence conflicti1056 – 10561A → P in AAF18297 (PubMed:11909944).Curated
Sequence conflicti1061 – 10611K → R in BAE34529 (PubMed:16141072).Curated
Sequence conflicti1076 – 10761D → N in BAE34529 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67326 mRNA. Translation: AAC53058.2.
AK158472 mRNA. Translation: BAE34529.1.
AH008805 Genomic DNA. Translation: AAF18297.1.
PIRiT42726.
RefSeqiNP_033053.2. NM_009027.3.
UniGeneiMm.248630.

Genome annotation databases

GeneIDi19418.
KEGGimmu:19418.
UCSCiuc029sco.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67326 mRNA. Translation: AAC53058.2.
AK158472 mRNA. Translation: BAE34529.1.
AH008805 Genomic DNA. Translation: AAF18297.1.
PIRiT42726.
RefSeqiNP_033053.2. NM_009027.3.
UniGeneiMm.248630.

3D structure databases

ProteinModelPortaliP70392.
SMRiP70392. Positions 954-1186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202601. 1 interaction.
IntActiP70392. 4 interactions.
MINTiMINT-1753415.

PTM databases

iPTMnetiP70392.
PhosphoSiteiP70392.

Proteomic databases

MaxQBiP70392.
PRIDEiP70392.

Protocols and materials databases

DNASUi19418.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi19418.
KEGGimmu:19418.
UCSCiuc029sco.1. mouse.

Organism-specific databases

CTDi5924.
MGIiMGI:109137. Rasgrf2.

Phylogenomic databases

HOVERGENiHBG005208.
InParanoidiP70392.
KOiK12326.
PhylomeDBiP70392.

Miscellaneous databases

NextBioi296559.
PROiP70392.
SOURCEiSearch...

Family and domain databases

Gene3Di1.10.840.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
InterProiIPR000219. DH-domain.
IPR000048. IQ_motif_EF-hand-BS.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000651. Ras-like_Gua-exchang_fac_N.
IPR019804. Ras_G-nucl-exch_fac_CS.
IPR023578. Ras_GEF_dom.
IPR001895. RASGEF_cat_dom.
IPR030744. RasGRF2.
[Graphical view]
PANTHERiPTHR23113:SF187. PTHR23113:SF187. 3 hits.
PfamiPF00169. PH. 1 hit.
PF00617. RasGEF. 1 hit.
PF00618. RasGEF_N. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 2 hits.
SM00147. RasGEF. 1 hit.
SM00229. RasGEFN. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF48366. SSF48366. 2 hits.
SSF50729. SSF50729. 2 hits.
PROSITEiPS50010. DH_2. 1 hit.
PS50096. IQ. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS00720. RASGEF. 1 hit.
PS50009. RASGEF_CAT. 1 hit.
PS50212. RASGEF_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of Ras-GRF2, a novel guanine nucleotide exchange factor for Ras."
    Fam N.P., Fan W.-T., Wang Z., Zhang L.-J., Chen H., Moran M.F.
    Mol. Cell. Biol. 17:1396-1406(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAS AND CALMODULIN, SUBCELLULAR LOCATION.
    Tissue: Brain.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Inner ear.
  3. "Ras binding triggers ubiquitination of the Ras exchange factor Ras-GRF2."
    de Hoog C.L., Koehler J.A., Goldstein M.D., Taylor P., Figeys D., Moran M.F.
    Mol. Cell. Biol. 21:2107-2117(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 464-474 AND 723-734, PHOSPHORYLATION, UBIQUITINATION, MUTAGENESIS OF ARG-1022 AND ARG-1092.
  4. "Targeted disruption of Ras-Grf2 shows its dispensability for mouse growth and development."
    Fernandez-Medarde A., Esteban L.M., Nunez A., Porteros A., Tessarollo L., Santos E.
    Mol. Cell. Biol. 22:2498-2504(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 922-1189, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  5. "The exchange factor Ras-GRF2 activates Ras-dependent and Rac-dependent mitogen-activated protein kinase pathways."
    Fan W.-T., Koch C.A., de Hoog C.L., Fam N.P., Moran M.F.
    Curr. Biol. 8:935-938(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAS AND RAC1.
  6. "Ras-specific exchange factor GRF: oligomerization through its Dbl homology domain and calcium-dependent activation of Raf."
    Anborgh P.H., Qian X., Papageorge A.G., Vass W.C., DeClue J.E., Lowy D.R.
    Mol. Cell. Biol. 19:4611-4622(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RASGRF1.
  7. "Calmodulin-independent coordination of Ras and extracellular signal-regulated kinase activation by Ras-GRF2."
    de Hoog C.L., Fan W.-T., Goldstein M.D., Moran M.F., Koch C.A.
    Mol. Cell. Biol. 20:2727-2733(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Prenylation of target GTPases contributes to signaling specificity of Ras-guanine nucleotide exchange factors."
    Gotoh T., Tian X., Feig L.A.
    J. Biol. Chem. 276:38029-38035(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Dematin interacts with the Ras-guanine nucleotide exchange factor Ras-GRF2 and modulates mitogen-activated protein kinase pathways."
    Lutchman M., Kim A.C., Cheng L., Whitehead I.P., Oh S.S., Hanspal M., Boukharov A.A., Hanada T., Chishti A.H.
    Eur. J. Biochem. 269:638-649(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPB49.
  10. "Developmentally regulated role for Ras-GRFs in coupling NMDA glutamate receptors to Ras, Erk and CREB."
    Tian X., Gotoh T., Tsuji K., Lo E.H., Huang S., Feig L.A.
    EMBO J. 23:1567-1575(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
  11. "p35/cyclin-dependent kinase 5 phosphorylation of ras guanine nucleotide releasing factor 2 (RasGRF2) mediates Rac-dependent extracellular signal-regulated kinase 1/2 activity, altering RasGRF2 and microtubule-associated protein 1b distribution in neurons."
    Kesavapany S., Amin N., Zheng Y.-L., Nijhara R., Jaffe H., Sihag R., Gutkind J.S., Takahashi S., Kulkarni A., Grant P., Pant H.C.
    J. Neurosci. 24:4421-4431(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CDK5.
  12. "Activation of H-Ras in the endoplasmic reticulum by the RasGRF family guanine nucleotide exchange factors."
    Arozarena I., Matallanas D., Berciano M.T., Sanz-Moreno V., Calvo F., Munoz M.T., Egea G., Lafarga M., Crespo P.
    Mol. Cell. Biol. 24:1516-1530(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "The guanine nucleotide exchange factor RasGRF1 directly binds microtubules via DHPH2-mediated interaction."
    Forlani G., Baldassa S., Lavagni P., Sturani E., Zippel R.
    FEBS J. 273:2127-2138(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MICROTUBULES.
  14. "Age-dependent participation of Ras-GRF proteins in coupling calcium-permeable AMPA glutamate receptors to Ras/Erk signaling in cortical neurons."
    Tian X., Feig L.A.
    J. Biol. Chem. 281:7578-7582(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GRIA1.
  15. "Distinct roles for Ras-guanine nucleotide-releasing factor 1 (Ras-GRF1) and Ras-GRF2 in the induction of long-term potentiation and long-term depression."
    Li S., Tian X., Hartley D.M., Feig L.A.
    J. Neurosci. 26:1721-1729(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-725; SER-726; SER-745; SER-749; SER-801; SER-805 AND SER-924, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Lung.

Entry informationi

Entry nameiRGRF2_MOUSE
AccessioniPrimary (citable) accession number: P70392
Secondary accession number(s): Q3TYN3, Q9QX51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Preferentially activates HRAS in vivo compared to R-RAS based on their different types of prenylation.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

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 one 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.