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RAS guanyl-releasing protein 2 (Calcium and DAG-regulated guanine nucleotide exchange factor I) (CalDAG-GEFI) (Cdc25-like protein) (hCDC25L) (F25B3.3 kinase-like protein)

 GRP2_HUMAN              Reviewed;         609 AA.
Q7LDG7; A6NDC7; O00538; Q9UL65;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
07-NOV-2018, entry version 141.
RecName: Full=RAS guanyl-releasing protein 2;
AltName: Full=Calcium and DAG-regulated guanine nucleotide exchange factor I;
Short=CalDAG-GEFI;
AltName: Full=Cdc25-like protein;
Short=hCDC25L;
AltName: Full=F25B3.3 kinase-like protein;
Name=RASGRP2; Synonyms=CDC25L, MCG7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=9341881; DOI=10.1007/s004390050562;
Kedra D., Seroussi E., Fransson I., Trifunovic J., Clark M.,
Lagercrantz J., Blennow E., Mehlin H., Dumanski J.;
"The germinal centre kinase gene and a novel CDC25-like gene are
located in the vicinity of the PYGM gene on 11q13.";
Hum. Genet. 100:611-619(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
TISSUE=Frontal cortex;
PubMed=9789079; DOI=10.1073/pnas.95.22.13278;
Kawasaki H., Springett G.M., Toki S., Canales J.J., Harlan P.,
Blumenstiel J.P., Chen E.J., Bany I.A., Mochizuki N., Ashbacher A.,
Matsuda M., Housman D.E., Graybiel A.M.;
"A Rap guanine nucleotide exchange factor enriched highly in the basal
ganglia.";
Proc. Natl. Acad. Sci. U.S.A. 95:13278-13283(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ACTIVITY
REGULATION, SUBCELLULAR LOCATION, TOPOLOGY, PALMITOYLATION AT CYS-7
(ISOFORM 2), MYRISTOYLATION AT GLY-2 (ISOFORM 2), AND TISSUE
SPECIFICITY.
PubMed=10918068; DOI=10.1074/jbc.M006087200;
Clyde-Smith J., Silins G., Gartside M., Grimmond S., Etheridge M.,
Apolloni A., Hayward N., Hancock J.F.;
"Characterization of RasGRP2, a plasma membrane-targeted, dual
specificity Ras/Rap exchange factor.";
J. Biol. Chem. 275:32260-32267(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[8]
ALTERNATIVE SPLICING (ISOFORM 3).
PubMed=11278453; DOI=10.1074/jbc.M008970200;
Dupuy A.J., Morgan K., von Lintig F.C., Shen H., Acar H., Hasz D.E.,
Jenkins N.A., Copeland N.G., Boss G.R., Largaespada D.A.;
"Activation of the Rap1 guanine nucleotide exchange gene, CalDAG-GEF
I, in BXH-2 murine myeloid leukemia.";
J. Biol. Chem. 276:11804-11811(2001).
[9]
FUNCTION, AND INTERACTION WITH RAP1.
PubMed=14702343; DOI=10.1074/jbc.M310717200;
Katagiri K., Shimonaka M., Kinashi T.;
"Rap1-mediated lymphocyte function-associated antigen-1 activation by
the T cell antigen receptor is dependent on phospholipase C-gamma1.";
J. Biol. Chem. 279:11875-11881(2004).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH F-ACTIN.
PubMed=14988412; DOI=10.1074/jbc.M313013200;
Caloca M.J., Zugaza J.L., Vicente-Manzanares M., Sanchez-Madrid F.,
Bustelo X.R.;
"F-actin-dependent translocation of the Rap1 GDP/GTP exchange factor
RasGRP2.";
J. Biol. Chem. 279:20435-20446(2004).
[11]
FUNCTION IN T-LYMPHOCYTES ADHESION, AND TISSUE SPECIFICITY.
PubMed=17702895; DOI=10.1182/blood-2007-03-077628;
Ghandour H., Cullere X., Alvarez A., Luscinskas F.W., Mayadas T.N.;
"Essential role for Rap1 GTPase and its guanine exchange factor
CalDAG-GEFI in LFA-1 but not VLA-4 integrin mediated human T-cell
adhesion.";
Blood 110:3682-3690(2007).
[12]
FUNCTION IN INTEGRIN ACTIVATION, AND TISSUE SPECIFICITY.
PubMed=17576779; DOI=10.1084/jem.20070058;
Pasvolsky R., Feigelson S.W., Kilic S.S., Simon A.J., Tal-Lapidot G.,
Grabovsky V., Crittenden J.R., Amariglio N., Safran M., Graybiel A.M.,
Rechavi G., Ben-Dor S., Etzioni A., Alon R.;
"A LAD-III syndrome is associated with defective expression of the
Rap-1 activator CalDAG-GEFI in lymphocytes, neutrophils, and
platelets.";
J. Exp. Med. 204:1571-1582(2007).
[13]
LACK OF INVOLVEMENT IN LAD3.
PubMed=19064721; DOI=10.1182/blood-2008-10-182154;
Kuijpers T.W., van de Vijver E., Weterman M.A.J., de Boer M.,
Tool A.T.J., van den Berg T.K., Moser M., Jakobs M.E., Seeger K.,
Sanal O., Uenal S., Cetin M., Roos D., Verhoeven A.J., Baas F.;
"LAD-1/variant syndrome is caused by mutations in FERMT3.";
Blood 113:4740-4746(2009).
[14]
LACK OF INVOLVEMENT IN LAD3.
PubMed=19234463; DOI=10.1038/nm.1931;
Svensson L., Howarth K., McDowall A., Patzak I., Evans R., Ussar S.,
Moser M., Metin A., Fried M., Tomlinson I., Hogg N.;
"Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3
affecting integrin activation.";
Nat. Med. 15:306-312(2009).
[15]
LACK OF INVOLVEMENT IN LAD3.
PubMed=19234460; DOI=10.1038/nm.1917;
Malinin N.L., Zhang L., Choi J., Ciocea A., Razorenova O., Ma Y.-Q.,
Podrez E.A., Tosi M., Lennon D.P., Caplan A.I., Shurin S.B.,
Plow E.F., Byzova T.V.;
"A point mutation in KINDLIN3 ablates activation of three integrin
subfamilies in humans.";
Nat. Med. 15:313-318(2009).
[16]
FUNCTION, INVOLVEMENT IN BDPLT18, VARIANT BDPLT18 TRP-248, AND
CHARACTERIZATION OF VARIANT BDPLT18 TRP-248.
PubMed=24958846; DOI=10.1084/jem.20130477;
Canault M., Ghalloussi D., Grosdidier C., Guinier M., Perret C.,
Chelghoum N., Germain M., Raslova H., Peiretti F., Morange P.E.,
Saut N., Pillois X., Nurden A.T., Cambien F., Pierres A.,
van den Berg T.K., Kuijpers T.W., Alessi M.C., Tregouet D.A.;
"Human CalDAG-GEFI gene (RASGRP2) mutation affects platelet function
and causes severe bleeding.";
J. Exp. Med. 211:1349-1362(2014).
[17]
FUNCTION, VARIANTS BDPLT18 113-ARG--LEU-609 DEL AND PHE-381, AND
CHARACTERIZATION OF VARIANTS BDPLT18 113-ARG--LEU-609 DEL AND PHE-381.
PubMed=27235135; DOI=10.1182/blood-2015-11-683102;
Lozano M.L., Cook A., Bastida J.M., Paul D.S., Iruin G., Cid A.R.,
Adan-Pedroso R., Ramon Gonzalez-Porras J., Hernandez-Rivas J.M.,
Fletcher S.J., Johnson B., Morgan N., Ferrer-Marin F., Vicente V.,
Sondek J., Watson S.P., Bergmeier W., Rivera J.;
"Novel mutations in RASGRP2, which encodes CalDAG-GEFI, abrogate Rap1
activation, causing platelet dysfunction.";
Blood 128:1282-1289(2016).
[18]
STRUCTURE BY NMR OF 417-497 IN COMPLEX WITH CALCIUM.
PubMed=23908768; DOI=10.7554/eLife.00813;
Iwig J.S., Vercoulen Y., Das R., Barros T., Limnander A., Che Y.,
Pelton J.G., Wemmer D.E., Roose J.P., Kuriyan J.;
"Structural analysis of autoinhibition in the Ras-specific exchange
factor RasGRP1.";
Elife 2:E00813-E00813(2013).
[19]
VARIANT BDPLT18 ASP-305.
PubMed=28726538; DOI=10.1080/09537104.2017.1332759;
Bermejo E., Alberto M.F., Paul D.S., Cook A.A., Nurden P.,
Sanchez Luceros A., Nurden A.T., Bergmeier W.;
"Marked bleeding diathesis in patients with platelet dysfunction due
to a novel mutation in RASGRP2, encoding CalDAG-GEFI (p.Gly305Asp).";
Platelets 2017:1-3(2017).
[20]
VARIANTS BDPLT18 236-GLN--LEU-609 DEL AND TYR-296, AND
CHARACTERIZATION OF VARIANTS BDPLT18 236-GLN--LEU-609 DEL AND TYR-296.
PubMed=28762304; DOI=10.1080/09537104.2017.1336214;
Sevivas T., Bastida J.M., Paul D.S., Caparros E., Palma-Barqueros V.,
Coucelo M., Marques D., Ferrer-Marin F., Gonzalez-Porras J.R.,
Vicente V., Hernandez-Rivas J.M., Watson S.P., Lozano M.L.,
Bergmeier W., Rivera J.;
"Identification of two novel mutations in RASGRP2 affecting platelet
CalDAG-GEFI expression and function in patients with bleeding
diathesis.";
Platelets 2017:1-4(2017).
-!- FUNCTION: Functions as a calcium- and DAG-regulated nucleotide
exchange factor specifically activating Rap through the exchange
of bound GDP for GTP. May also activates other GTPases such as
RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of
platelets and adhesion of T-lymphocytes and neutrophils probably
through inside-out integrin activation. May function in the
muscarinic acetylcholine receptor M1/CHRM1 signaling pathway.
{ECO:0000269|PubMed:10918068, ECO:0000269|PubMed:14702343,
ECO:0000269|PubMed:17576779, ECO:0000269|PubMed:17702895,
ECO:0000269|PubMed:24958846, ECO:0000269|PubMed:27235135}.
-!- ACTIVITY REGULATION: Isoform 1 and isoform 2 are differently
regulated by calcium and DAG. {ECO:0000269|PubMed:10918068}.
-!- SUBUNIT: Forms a signaling complex with RAP1 and BRAF (By
similarity). Interacts with RAP1. Interacts with F-actin.
{ECO:0000250, ECO:0000269|PubMed:14702343,
ECO:0000269|PubMed:14988412}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane;
Peripheral membrane protein. Cell junction, synapse, synaptosome
{ECO:0000305}. Cell projection, ruffle membrane {ECO:0000305};
Peripheral membrane protein {ECO:0000305}. Note=Found both in the
cytosol and associated with membranes. Isoform 2 mainly localizes
to the cell membrane. Enriched at juxtamembrane areas and membrane
ruffles through association with F-actin. Localizes to the cell
bodies and axons of striatal neurons (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=CalDAG-GEFI, CalDAG-GEFIa;
IsoId=Q7LDG7-1; Sequence=Displayed;
Name=2; Synonyms=RasGRP2;
IsoId=Q7LDG7-2; Sequence=VSP_030574;
Note=Initiator Met-1 is removed. Contains a N-myristoyl glycine
at position 2. Contains a S-palmitoyl cysteine at position 7.
{ECO:0000269|PubMed:10918068};
Name=3; Synonyms=CalDAG-GEFIb;
IsoId=Q7LDG7-3; Sequence=VSP_030575, VSP_030576;
Note=The corresponding protein is not undetectable.;
Name=4;
IsoId=Q7LDG7-4; Sequence=VSP_054132;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in platelets, neutrophils and T
lymphocytes (at protein level). Expressed in brain where it is
enriched in the striatum. Also expressed in the hematopoietic
system. Detected in heart, brain, lung, placenta, liver, skeletal
muscle and kidney. {ECO:0000269|PubMed:10918068,
ECO:0000269|PubMed:17576779, ECO:0000269|PubMed:17702895,
ECO:0000269|PubMed:9341881, ECO:0000269|PubMed:9789079}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal brain, lung, liver and
kidney. {ECO:0000269|PubMed:9789079}.
-!- DOMAIN: The N-terminal Ras-GEF domain mediates association with F-
actin.
-!- PTM: Isoform 2 is palmitoylated and myristoylated.
{ECO:0000269|PubMed:10918068}.
-!- DISEASE: Bleeding disorder, platelet-type 18 (BDPLT18)
[MIM:615888]: A disorder characterized by increased bleeding
tendency due to platelet dysfunction. Clinical features include
epistaxis, hematomas, bleeding after tooth extraction, and
menorrhagia. {ECO:0000269|PubMed:24958846,
ECO:0000269|PubMed:27235135, ECO:0000269|PubMed:28726538,
ECO:0000269|PubMed:28762304}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the RASGRP family. {ECO:0000305}.
-!- CAUTION: Defects in RASGRP2 were initially thought
(PubMed:17576779) to be the cause of leukocyte adhesion deficiency
type 3 (LAD3), a syndrome characterized by recurrent bacterial
infections and major bleeding disorders. However, it was later
shown (PubMed:19064721, PubMed:19234463 and PubMed:19234460) that
it is not the case and that LAD3 is caused by defects in FERMT3
gene. {ECO:0000305|PubMed:17576779}.
-!- WEB RESOURCE: Name=RASGRP2base; Note=RASGRP2 mutation db;
URL="http://structure.bmc.lu.se/idbase/RASGRP2base/";
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EMBL; Y12336; CAA73005.1; -; mRNA.
EMBL; AF081194; AAC79698.1; -; mRNA.
EMBL; U78170; AAD12741.1; -; mRNA.
EMBL; AF043722; AAF07219.1; -; mRNA.
EMBL; AF043723; AAF07220.1; -; mRNA.
EMBL; AK092882; BAG52620.1; -; mRNA.
EMBL; AP001462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW74281.1; -; Genomic_DNA.
EMBL; BC117151; AAI17152.1; -; mRNA.
CCDS; CCDS31598.1; -. [Q7LDG7-1]
RefSeq; NP_001092140.1; NM_001098670.1. [Q7LDG7-1]
RefSeq; NP_001092141.1; NM_001098671.1. [Q7LDG7-1]
RefSeq; NP_001305327.1; NM_001318398.1.
RefSeq; NP_722541.1; NM_153819.1. [Q7LDG7-1]
RefSeq; XP_011543022.1; XM_011544720.1. [Q7LDG7-4]
RefSeq; XP_011543023.1; XM_011544721.1. [Q7LDG7-4]
RefSeq; XP_011543024.1; XM_011544722.1. [Q7LDG7-4]
RefSeq; XP_011543025.1; XM_011544723.2. [Q7LDG7-4]
RefSeq; XP_016872573.1; XM_017017084.1. [Q7LDG7-4]
UniGene; Hs.99491; -.
PDB; 2MA2; NMR; -; A=417-497.
PDB; 6AXF; X-ray; 3.10 A; A/C/E/G/I/K/M/O=1-394.
PDBsum; 2MA2; -.
PDBsum; 6AXF; -.
ProteinModelPortal; Q7LDG7; -.
SMR; Q7LDG7; -.
BioGrid; 115529; 2.
IntAct; Q7LDG7; 3.
STRING; 9606.ENSP00000338864; -.
iPTMnet; Q7LDG7; -.
PhosphoSitePlus; Q7LDG7; -.
SwissPalm; Q7LDG7; -.
BioMuta; RASGRP2; -.
DMDM; 74713056; -.
EPD; Q7LDG7; -.
MaxQB; Q7LDG7; -.
PaxDb; Q7LDG7; -.
PeptideAtlas; Q7LDG7; -.
PRIDE; Q7LDG7; -.
ProteomicsDB; 68852; -.
ProteomicsDB; 68853; -. [Q7LDG7-2]
ProteomicsDB; 68854; -. [Q7LDG7-3]
Ensembl; ENST00000354024; ENSP00000338864; ENSG00000068831. [Q7LDG7-1]
Ensembl; ENST00000377494; ENSP00000366714; ENSG00000068831. [Q7LDG7-4]
Ensembl; ENST00000377497; ENSP00000366717; ENSG00000068831. [Q7LDG7-1]
Ensembl; ENST00000394432; ENSP00000377953; ENSG00000068831. [Q7LDG7-1]
GeneID; 10235; -.
KEGG; hsa:10235; -.
UCSC; uc001oau.4; human. [Q7LDG7-1]
CTD; 10235; -.
DisGeNET; 10235; -.
EuPathDB; HostDB:ENSG00000068831.18; -.
GeneCards; RASGRP2; -.
HGNC; HGNC:9879; RASGRP2.
HPA; HPA015667; -.
MalaCards; RASGRP2; -.
MIM; 605577; gene.
MIM; 615888; phenotype.
neXtProt; NX_Q7LDG7; -.
OpenTargets; ENSG00000068831; -.
Orphanet; 420566; Bleeding disorder due to CalDAG-GEFI deficiency.
PharmGKB; PA34241; -.
eggNOG; KOG3417; Eukaryota.
eggNOG; ENOG410XR96; LUCA.
GeneTree; ENSGT00880000137870; -.
HOGENOM; HOG000293171; -.
HOVERGEN; HBG007513; -.
InParanoid; Q7LDG7; -.
KO; K12361; -.
OMA; MISYFLR; -.
OrthoDB; EOG091G03RN; -.
PhylomeDB; Q7LDG7; -.
TreeFam; TF312918; -.
Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-HSA-392517; Rap1 signalling.
GeneWiki; RASGRP2; -.
GenomeRNAi; 10235; -.
PRO; PR:Q7LDG7; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000068831; Expressed in 208 organ(s), highest expression level in blood.
CleanEx; HS_RASGRP2; -.
ExpressionAtlas; Q7LDG7; baseline and differential.
Genevisible; Q7LDG7; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
GO; GO:0019992; F:diacylglycerol binding; NAS:UniProtKB.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; TAS:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; NAS:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; NAS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
CDD; cd00029; C1; 1.
CDD; cd00051; EFh; 1.
CDD; cd00155; RasGEF; 1.
CDD; cd06224; REM; 1.
Gene3D; 1.10.840.10; -; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR008937; Ras-like_GEF.
InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
InterPro; IPR023578; Ras_GEF_dom_sf.
InterPro; IPR001895; RASGEF_cat_dom.
InterPro; IPR036964; RASGEF_cat_dom_sf.
PANTHER; PTHR23113; PTHR23113; 1.
Pfam; PF00130; C1_1; 1.
Pfam; PF13202; EF-hand_5; 1.
Pfam; PF00617; RasGEF; 1.
Pfam; PF00618; RasGEF_N; 1.
SMART; SM00109; C1; 1.
SMART; SM00054; EFh; 2.
SMART; SM00147; RasGEF; 1.
SMART; SM00229; RasGEFN; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF48366; SSF48366; 1.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 2.
PROSITE; PS50009; RASGEF_CAT; 1.
PROSITE; PS50212; RASGEF_NTER; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell junction;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Disease mutation; Guanine-nucleotide releasing factor; Membrane;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Synapse; Synaptosome; Zinc; Zinc-finger.
CHAIN 1 609 RAS guanyl-releasing protein 2.
/FTId=PRO_0000315608.
DOMAIN 4 126 N-terminal Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00135}.
DOMAIN 154 387 Ras-GEF. {ECO:0000255|PROSITE-
ProRule:PRU00168}.
DOMAIN 426 461 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 455 490 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 439 450 1. {ECO:0000255|PROSITE-ProRule:PRU00448,
ECO:0000305|PubMed:23908768}.
CA_BIND 468 479 2. {ECO:0000255|PROSITE-ProRule:PRU00448,
ECO:0000305|PubMed:23908768}.
ZN_FING 498 548 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QUG9}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QUG9}.
MOD_RES 147 147 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QUG9}.
MOD_RES 554 554 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QUG9}.
MOD_RES 576 576 Phosphoserine.
{ECO:0000250|UniProtKB:P0C643}.
VAR_SEQ 1 1 M -> MGTQRLCGRGTQGWPGSSEQHVQEATSSAGLHSGVD
ELGVRSEPGGRLPERSLGPAHPAPAAM (in isoform
2). {ECO:0000303|PubMed:10918068}.
/FTId=VSP_030574.
VAR_SEQ 125 125 P -> CVGAEHRGLGGHSVSYTICA (in isoform 3).
{ECO:0000305}.
/FTId=VSP_030575.
VAR_SEQ 126 609 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_030576.
VAR_SEQ 590 590 P -> PA (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054132.
VARIANT 113 609 Missing (in BDPLT18).
{ECO:0000269|PubMed:27235135}.
/FTId=VAR_079614.
VARIANT 236 609 Missing (in BDPLT18; lack of mutant
protein in platelets from a patient
homozygous for the mutation).
{ECO:0000269|PubMed:28762304}.
/FTId=VAR_079615.
VARIANT 248 248 G -> W (in BDPLT18; prevents Rap1
activation upon calcium stimulation;
reduces platelet adhesion and spreading;
dbSNP:rs587777529).
{ECO:0000269|PubMed:24958846}.
/FTId=VAR_071474.
VARIANT 296 296 C -> Y (in BDPLT18; lack of mutant
protein in platelets from a patient
homozygous for the mutation).
{ECO:0000269|PubMed:28762304}.
/FTId=VAR_079616.
VARIANT 305 305 G -> D (in BDPLT18).
{ECO:0000269|PubMed:28726538}.
/FTId=VAR_079617.
VARIANT 381 381 S -> F (in BDPLT18; loss of guanyl-
nucleotide exchange factor activity;
dbSNP:rs767965347).
{ECO:0000269|PubMed:27235135}.
/FTId=VAR_079618.
VARIANT 493 493 G -> A (in dbSNP:rs2301562).
/FTId=VAR_038257.
HELIX 13 22 {ECO:0000244|PDB:6AXF}.
HELIX 33 42 {ECO:0000244|PDB:6AXF}.
HELIX 43 45 {ECO:0000244|PDB:6AXF}.
HELIX 49 65 {ECO:0000244|PDB:6AXF}.
HELIX 69 85 {ECO:0000244|PDB:6AXF}.
HELIX 87 92 {ECO:0000244|PDB:6AXF}.
HELIX 94 110 {ECO:0000244|PDB:6AXF}.
HELIX 116 118 {ECO:0000244|PDB:6AXF}.
HELIX 129 132 {ECO:0000244|PDB:6AXF}.
STRAND 137 140 {ECO:0000244|PDB:6AXF}.
HELIX 145 150 {ECO:0000244|PDB:6AXF}.
HELIX 155 170 {ECO:0000244|PDB:6AXF}.
HELIX 175 184 {ECO:0000244|PDB:6AXF}.
HELIX 191 212 {ECO:0000244|PDB:6AXF}.
HELIX 217 236 {ECO:0000244|PDB:6AXF}.
HELIX 240 250 {ECO:0000244|PDB:6AXF}.
HELIX 253 256 {ECO:0000244|PDB:6AXF}.
HELIX 259 263 {ECO:0000244|PDB:6AXF}.
HELIX 267 279 {ECO:0000244|PDB:6AXF}.
TURN 283 286 {ECO:0000244|PDB:6AXF}.
HELIX 287 294 {ECO:0000244|PDB:6AXF}.
HELIX 306 317 {ECO:0000244|PDB:6AXF}.
STRAND 320 323 {ECO:0000244|PDB:6AXF}.
HELIX 331 346 {ECO:0000244|PDB:6AXF}.
HELIX 347 349 {ECO:0000244|PDB:6AXF}.
HELIX 358 369 {ECO:0000244|PDB:6AXF}.
HELIX 374 384 {ECO:0000244|PDB:6AXF}.
HELIX 420 437 {ECO:0000244|PDB:2MA2}.
HELIX 448 454 {ECO:0000244|PDB:2MA2}.
TURN 455 457 {ECO:0000244|PDB:2MA2}.
HELIX 464 467 {ECO:0000244|PDB:2MA2}.
HELIX 477 486 {ECO:0000244|PDB:2MA2}.
STRAND 490 492 {ECO:0000244|PDB:2MA2}.
SEQUENCE 609 AA; 69248 MW; 8B1321F864D24BC7 CRC64;
MAGTLDLDKG CTVEELLRGC IEAFDDSGKV RDPQLVRMFL MMHPWYIPSS QLAAKLLHIY
QQSRKDNSNS LQVKTCHLVR YWISAFPAEF DLNPELAEQI KELKALLDQE GNRRHSSLID
IDSVPTYKWK RQVTQRNPVG QKKRKMSLLF DHLEPMELAE HLTYLEYRSF CKILFQDYHS
FVTHGCTVDN PVLERFISLF NSVSQWVQLM ILSKPTAPQR ALVITHFVHV AEKLLQLQNF
NTLMAVVGGL SHSSISRLKE THSHVSPETI KLWEGLTELV TATGNYGNYR RRLAACVGFR
FPILGVHLKD LVALQLALPD WLDPARTRLN GAKMKQLFSI LEELAMVTSL RPPVQANPDL
LSLLTVSLDQ YQTEDELYQL SLQREPRSKS SPTSPTSCTP PPRPPVLEEW TSAAKPKLDQ
ALVVEHIEKM VESVFRNFDV DGDGHISQEE FQIIRGNFPY LSAFGDLDQN QDGCISREEM
VSYFLRSSSV LGGRMGFVHN FQESNSLRPV ACRHCKALIL GIYKQGLKCR ACGVNCHKQC
KDRLSVECRR RAQSVSLEGS APSPSPMHSH HHRAFSFSLP RPGRRGSRPP EIREEEVQTV
EDGVFDIHL


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