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Ras-specific guanine nucleotide-releasing factor 2 (Ras-GRF2) (Ras guanine nucleotide exchange factor 2)

 RGRF2_HUMAN             Reviewed;        1237 AA.
O14827; B9EG89; Q9UK56;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 2.
18-JUL-2018, entry version 154.
RecName: Full=Ras-specific guanine nucleotide-releasing factor 2;
Short=Ras-GRF2;
AltName: Full=Ras guanine nucleotide exchange factor 2;
Name=RASGRF2; Synonyms=GRF2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], OLIGOMERIZATION, INTERACTION WITH RASGRF1,
AND TISSUE SPECIFICITY.
TISSUE=Hippocampus;
PubMed=10373510; DOI=10.1128/MCB.19.7.4611;
Anborgh P.H., Qian X., Papageorge A.G., Vass W.C., DeClue J.E.,
Lowy D.R.;
"Ras-specific exchange factor GRF: oligomerization through its Dbl
homology domain and calcium-dependent activation of Raf.";
Mol. Cell. Biol. 19:4611-4622(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH EPB49, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=11856323; DOI=10.1046/j.0014-2956.2001.02694.x;
Lutchman M., Kim A.C., Cheng L., Whitehead I.P., Oh S.S., Hanspal M.,
Boukharov A.A., Hanada T., Chishti A.H.;
"Dematin interacts with the Ras-guanine nucleotide exchange factor
Ras-GRF2 and modulates mitogen-activated protein kinase pathways.";
Eur. J. Biochem. 269:638-649(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBCELLULAR LOCATION.
PubMed=12176907; DOI=10.1182/blood-2001-12-0193;
Rabiet M.-J., Tardif M., Braun L., Boulay F.;
"Inhibitory effects of a dominant-interfering form of the Rho-GTPase
Cdc42 in the chemoattractant-elicited signaling pathways leading to
NADPH oxidase activation in differentiated HL-60 cells.";
Blood 100:1835-1844(2002).
[6]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDK5R1,
PHOSPHORYLATION AT SER-737 BY CDK5, AND MUTAGENESIS OF SER-737.
PubMed=15128856; DOI=10.1523/JNEUROSCI.0690-04.2004;
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.;
"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.";
J. Neurosci. 24:4421-4431(2004).
[7]
SUBCELLULAR LOCATION.
PubMed=14749369; DOI=10.1128/MCB.24.4.1516-1530.2004;
Arozarena I., Matallanas D., Berciano M.T., Sanz-Moreno V., Calvo F.,
Munoz M.T., Egea G., Lafarga M., Crespo P.;
"Activation of H-Ras in the endoplasmic reticulum by the RasGRF family
guanine nucleotide exchange factors.";
Mol. Cell. Biol. 24:1516-1530(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[9]
VARIANTS [LARGE SCALE ANALYSIS] HIS-114; ASN-538 AND GLU-1216.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: 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. {ECO:0000269|PubMed:15128856}.
-!- SUBUNIT: Homooligomer and heterooligomer with RASGRF1. Interacts
with Ras and RAC1. Interacts in a calcium-dependent manner with
calmodulin (By similarity). Interacts with CDK5R1 and EPB49.
Interacts with the AMPA receptor through GRIA1 (By similarity).
Interacts with microtubules (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
membrane protein. Endoplasmic reticulum membrane; Peripheral
membrane protein. Note=Translocates to membranes when activated.
Found both at cell periphery and along the axon of neurons (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed with higher expression in
brain, followed by heart, lung, pancreas and kidney. Detected in
placenta. Expressed in brain and lung (at protein level).
{ECO:0000269|PubMed:10373510, ECO:0000269|PubMed:11856323}.
-!- DOMAIN: The Ras-GEF domain and the N-terminal Ras-GEF domain form
a Ras-binding site and mediate Ras activation. {ECO:0000250}.
-!- DOMAIN: The IQ domain mediates the calcium-dependent interaction
with calmodulin but is dispensable for the Ras-GEF activity.
{ECO:0000250}.
-!- DOMAIN: The DH (DBL-homology) domain mediates interaction with
RASGRF1 and EPB49 and is required for RAC1 activation.
-!- PTM: Phosphorylated by CDK5; down-regulates RASGRF2-mediated RAC1
activation. {ECO:0000269|PubMed:15128856}.
-!- PTM: Ubiquitinated upon interaction with Ras. Ubiquitination leads
to degradation through the 26S proteasome (By similarity).
{ECO:0000250}.
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EMBL; AF023130; AAB80953.1; -; mRNA.
EMBL; AF181250; AAD55268.1; -; mRNA.
EMBL; CH471084; EAW95863.1; -; mRNA.
EMBL; BC126112; AAI26113.1; -; mRNA.
EMBL; BC136296; AAI36297.1; -; mRNA.
CCDS; CCDS4052.1; -.
RefSeq; NP_008840.1; NM_006909.2.
UniGene; Hs.162129; -.
UniGene; Hs.684592; -.
ProteinModelPortal; O14827; -.
SMR; O14827; -.
BioGrid; 111859; 5.
IntAct; O14827; 3.
STRING; 9606.ENSP00000265080; -.
iPTMnet; O14827; -.
PhosphoSitePlus; O14827; -.
BioMuta; RASGRF2; -.
EPD; O14827; -.
PaxDb; O14827; -.
PeptideAtlas; O14827; -.
PRIDE; O14827; -.
ProteomicsDB; 48258; -.
Ensembl; ENST00000265080; ENSP00000265080; ENSG00000113319.
GeneID; 5924; -.
KEGG; hsa:5924; -.
UCSC; uc003kha.3; human.
CTD; 5924; -.
DisGeNET; 5924; -.
EuPathDB; HostDB:ENSG00000113319.11; -.
GeneCards; RASGRF2; -.
HGNC; HGNC:9876; RASGRF2.
HPA; HPA018679; -.
MIM; 606614; gene.
neXtProt; NX_O14827; -.
OpenTargets; ENSG00000113319; -.
PharmGKB; PA34239; -.
eggNOG; ENOG410IQ6Q; Eukaryota.
eggNOG; ENOG410XPWA; LUCA.
GeneTree; ENSGT00910000143985; -.
HOGENOM; HOG000046000; -.
HOVERGEN; HBG005208; -.
InParanoid; O14827; -.
KO; K12326; -.
OMA; QNNRGEH; -.
OrthoDB; EOG091G09V6; -.
PhylomeDB; O14827; -.
TreeFam; TF317296; -.
Reactome; R-HSA-193648; NRAGE signals death through JNK.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-442982; Ras activation upon Ca2+ influx through NMDA receptor.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
ChiTaRS; RASGRF2; human.
GeneWiki; RASGRF2; -.
GenomeRNAi; 5924; -.
PRO; PR:O14827; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113319; -.
CleanEx; HS_RASGRF2; -.
ExpressionAtlas; O14827; baseline and differential.
Genevisible; O14827; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; IMP:BHF-UCL.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:BHF-UCL.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
CDD; cd00155; RasGEF; 1.
CDD; cd06224; REM; 1.
CDD; cd00160; RhoGEF; 1.
Gene3D; 1.10.840.10; -; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
InterPro; IPR023578; Ras_GEF_dom_sf.
InterPro; IPR001895; RASGEF_cat_dom.
InterPro; IPR036964; RASGEF_cat_dom_sf.
InterPro; IPR030744; RasGRF2.
PANTHER; PTHR23113:SF187; PTHR23113:SF187; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00617; RasGEF; 1.
Pfam; PF00618; RasGEF_N; 1.
Pfam; PF00621; RhoGEF; 1.
SMART; SM00233; PH; 2.
SMART; SM00147; RasGEF; 1.
SMART; SM00229; RasGEFN; 2.
SMART; SM00325; RhoGEF; 1.
SUPFAM; SSF48065; SSF48065; 1.
SUPFAM; SSF48366; SSF48366; 2.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50096; IQ; 1.
PROSITE; PS50003; PH_DOMAIN; 2.
PROSITE; PS00720; RASGEF; 1.
PROSITE; PS50009; RASGEF_CAT; 1.
PROSITE; PS50212; RASGEF_NTER; 1.
1: Evidence at protein level;
Calcium; Calmodulin-binding; Cell membrane; Coiled coil;
Complete proteome; Cytoplasm; Endoplasmic reticulum;
Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 1237 Ras-specific guanine nucleotide-releasing
factor 2.
/FTId=PRO_0000312863.
DOMAIN 22 133 PH 1. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 205 234 IQ. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 243 429 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 470 588 PH 2. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 635 756 N-terminal Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00135}.
DOMAIN 1002 1234 Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00168}.
REGION 744 752 Regulates proteasomal degradation.
{ECO:0000250}.
REGION 1099 1128 Responsible of the affinity for
farnesylated versus geranylgeranylated
Ras. {ECO:0000250}.
COILED 155 193 {ECO:0000255}.
MOD_RES 726 726 Phosphoserine.
{ECO:0000250|UniProtKB:P70392}.
MOD_RES 727 727 Phosphoserine.
{ECO:0000250|UniProtKB:P70392}.
MOD_RES 737 737 Phosphoserine; by CDK5.
{ECO:0000269|PubMed:15128856}.
MOD_RES 746 746 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 848 848 Phosphoserine.
{ECO:0000250|UniProtKB:P70392}.
MOD_RES 852 852 Phosphoserine.
{ECO:0000250|UniProtKB:P70392}.
MOD_RES 972 972 Phosphoserine.
{ECO:0000250|UniProtKB:P70392}.
VARIANT 114 114 R -> H (in a colorectal cancer sample;
somatic mutation; dbSNP:rs779986744).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_037595.
VARIANT 538 538 D -> N (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_037596.
VARIANT 713 713 L -> W (in dbSNP:rs16878472).
/FTId=VAR_037597.
VARIANT 1216 1216 D -> E (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_037598.
MUTAGEN 737 737 S->A: Loss of phosphorylation by CDK5.
{ECO:0000269|PubMed:15128856}.
CONFLICT 561 561 A -> R (in Ref. 1; AAB80953).
{ECO:0000305}.
SEQUENCE 1237 AA; 140764 MW; A136CF4FA111FDD9 CRC64;
MQKSVRYNEG HALYLAFLAR KEGTKRGFLS KKTAEASRWH EKWFALYQNV LFYFEGEQSC
RPAGMYLLEG CSCERTPAPP RAGAGQGGVR DALDKQYYFT VLFGHEGQKP LELRCEEEQD
GKEWMEAIHQ ASYADILIER EVLMQKYIHL VQIVETEKIA ANQLRHQLED QDTEIERLKS
EIIALNKTKE RMRPYQSNQE DEDPDIKKIK KVQSFMRGWL CRRKWKTIVQ DYICSPHAES
MRKRNQIVFT MVEAESEYVH QLYILVNGFL RPLRMAASSK KPPISHDDVS SIFLNSETIM
FLHEIFHQGL KARIANWPTL ILADLFDILL PMLNIYQEFV RNHQYSLQVL ANCKQNRDFD
KLLKQYEANP ACEGRMLETF LTYPMFQIPR YIITLHELLA HTPHEHVERK SLEFAKSKLE
ELSRVMHDEV SDTENIRKNL AIERMIVEGC DILLDTSQTF IRQGSLIQVP SVERGKLSKV
RLGSLSLKKE GERQCFLFTK HFLICTRSSG GKLHLLKTGG VLSLIDCTLI EEPDASDDDS
KGSGQVFGHL DFKIVVEPPD AAAFTVVLLA PSRQEKAAWM SDISQCVDNI RCNGLMTIVF
EENSKVTVPH MIKSDARLHK DDTDICFSKT LNSCKVPQIR YASVERLLER LTDLRFLSID
FLNTFLHTYR IFTTAAVVLG KLSDIYKRPF TSIPVRSLEL FFATSQNNRG EHLVDGKSPR
LCRKFSSPPP LAVSRTSSPV RARKLSLTSP LNSKIGALDL TTSSSPTTTT QSPAASPPPH
TGQIPLDLSR GLSSPEQSPG TVEENVDNPR VDLCNKLKRS IQKAVLESAP ADRAGVESSP
AADTTELSPC RSPSTPRHLR YRQPGGQTAD NAHCSVSPAS AFAIATAAAG HGSPPGFNNT
ERTCDKEFII RRTATNRVLN VLRHWVSKHA QDFELNNELK MNVLNLLEEV LRDPDLLPQE
RKAAANILRA LSQDDQDDIH LKLEDIIQMT DCMKAECFES LSAMELAEQI TLLDHVIFRS
IPYEEFLGQG WMKLDKNERT PYIMKTSQHF NDMSNLVASQ IMNYADVSSR ANAIEKWVAV
ADICRCLHNY NGVLEITSAL NRSAIYRLKK TWAKVSKQTK ALMDKLQKTV SSEGRFKNLR
ETLKNCNPPA VPYLGMYLTD LAFIEEGTPN FTEEGLVNFS KMRMISHIIR EIRQFQQTSY
RIDHQPKVAQ YLLDKDLIID EDTLYELSLK IEPRLPA


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