RBCC

Full text data of RAP2B

RAP2B [Confidence: high (present in two of the MS resources)]
Ras-related protein Rap-2b; Flags: Precursor

hRBCD IPI00018364
IPI00018364 Ras-related protein Rap-2b Ras-related protein Rap-2b membrane n/a n/a 5 3 3 n/a 3 n/a 2 n/a 6 5 1 4 2 3 4 4 3 3 cytoplasmic and membrane associated n/a found at its expected molecular weight found at molecular weight

UniProt P61225
ID RAP2B_HUMAN Reviewed; 183 AA.
AC P61225; P17964; Q96EG5; Q9CXG0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2004, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Ras-related protein Rap-2b;
DE Flags: Precursor;
GN Name=RAP2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Platelet;
RX PubMed=2115998; DOI=10.1093/nar/18.14.4281;
RA Farrell F.X., Ohmstede C.A., Reep B.R., Lapetina E.G.;
RT "cDNA sequence of a new ras-related gene (rap2b) isolated from human
RT platelets with sequence homology to rap2.";
RL Nucleic Acids Res. 18:4281-4281(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Platelet;
RX PubMed=2118648; DOI=10.1073/pnas.87.17.6527;
RA Ohmstede C.A., Farrell F.X., Reep B.R., Clemetson K.J., Lapetina E.G.;
RT "RAP2B: a RAS-related GTP-binding protein from platelets.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6527-6531(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ISOPRENYLATION AT CYS-180.
RX PubMed=8424780;
RA Farrell F.X., Yamamoto K., Lapetina E.G.;
RT "Prenyl group identification of rap2 proteins: a ras superfamily
RT member other than ras that is farnesylated.";
RL Biochem. J. 289:349-355(1993).
RN [6]
RP FUNCTION.
RX PubMed=11877431; DOI=10.1074/jbc.M112024200;
RA Evellin S., Nolte J., Tysack K., vom Dorp F., Thiel M.,
RA Weernink P.A.O., Jakobs K.H., Webb E.J., Lomasney J.W., Schmidt M.;
RT "Stimulation of phospholipase C-epsilon by the M3 muscarinic
RT acetylcholine receptor mediated by cyclic AMP and the GTPase Rap2B.";
RL J. Biol. Chem. 277:16805-16813(2002).
RN [7]
RP INTERACTION WITH PLCE1.
RX PubMed=12444546; DOI=10.1038/sj.onc.1206003;
RA Song C., Satoh T., Edamatsu H., Wu D., Tadano M., Gao X., Kataoka T.;
RT "Differential roles of Ras and Rap1 in growth factor-dependent
RT activation of phospholipase C epsilon.";
RL Oncogene 21:8105-8113(2002).
RN [8]
RP FUNCTION.
RX PubMed=15143162; DOI=10.1128/MCB.24.11.4664-4676.2004;
RA Stope M.B., Vom Dorp F., Szatkowski D., Boehm A., Keiper M., Nolte J.,
RA Oude Weernink P.A., Rosskopf D., Evellin S., Jakobs K.H., Schmidt M.;
RT "Rap2B-dependent stimulation of phospholipase C-epsilon by epidermal
RT growth factor receptor mediated by c-Src phosphorylation of RasGRP3.";
RL Mol. Cell. Biol. 24:4664-4676(2004).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16540189; DOI=10.1016/j.bbamcr.2006.02.001;
RA Greco F., Ciana A., Pietra D., Balduini C., Minetti G., Torti M.;
RT "Rap2, but not Rap1 GTPase is expressed in human red blood cells and
RT is involved in vesiculation.";
RL Biochim. Biophys. Acta 1763:330-335(2006).
RN [10]
RP INTERACTION WITH SGSM1; SGSM2 AND SGSM3.
RX PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013;
RA Yang H., Sasaki T., Minoshima S., Shimizu N.;
RT "Identification of three novel proteins (SGSM1, 2, 3) which modulate
RT small G protein (RAP and RAB)-mediated signaling pathway.";
RL Genomics 90:249-260(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Small GTP-binding protein which cycles between a GDP-
CC bound inactive and a GTP-bound active form. Involved in EGFR and
CC CHRM3 signaling pathways through stimulation of PLCE1. May play a
CC role in cytoskeletal rearrangements and regulate cell spreading
CC through activation of the effector TNIK. May regulate membrane
CC vesiculation in red blood cells.
CC -!- SUBUNIT: Interacts with PLCE1. Interacts with SGSM1, SGSM2 and
CC SGSM3. The GTP-bound form of RAP2B interacts with RUNDC3A (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor;
CC Cytoplasmic side. Note=Associated with red blood cells-released
CC vesicles.
CC -!- TISSUE SPECIFICITY: Expressed in red blood cells (at protein
CC level).
CC -!- DOMAIN: The effector domain mediates the interaction with RUNDC3A
CC (By similarity).
CC -!- PTM: Palmitoylated. Palmitoylation is required for association
CC with recycling endosome membranes and activation of TNIK (By
CC similarity).
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RAP2BID275.html";
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DR EMBL; X52987; CAA37178.1; -; mRNA.
DR EMBL; AF493915; AAM12629.1; -; mRNA.
DR EMBL; BC012362; AAH12362.1; -; mRNA.
DR PIR; A33121; TVHUR2.
DR RefSeq; NP_002877.2; NM_002886.3.
DR UniGene; Hs.98643; -.
DR ProteinModelPortal; P61225; -.
DR SMR; P61225; 1-167.
DR IntAct; P61225; 4.
DR MINT; MINT-5000383; -.
DR STRING; 9606.ENSP00000319096; -.
DR PhosphoSite; P61225; -.
DR DMDM; 47117762; -.
DR PaxDb; P61225; -.
DR PeptideAtlas; P61225; -.
DR PRIDE; P61225; -.
DR DNASU; 5912; -.
DR Ensembl; ENST00000323534; ENSP00000319096; ENSG00000181467.
DR GeneID; 5912; -.
DR KEGG; hsa:5912; -.
DR UCSC; uc003ezr.3; human.
DR CTD; 5912; -.
DR GeneCards; GC03P152880; -.
DR HGNC; HGNC:9862; RAP2B.
DR MIM; 179541; gene.
DR neXtProt; NX_P61225; -.
DR PharmGKB; PA34223; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000233973; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P61225; -.
DR KO; K07838; -.
DR OMA; QFTGINE; -.
DR OrthoDB; EOG7QVM41; -.
DR PhylomeDB; P61225; -.
DR ChiTaRS; RAP2B; human.
DR GeneWiki; RAP2B; -.
DR GenomeRNAi; 5912; -.
DR NextBio; 23008; -.
DR PRO; PR:P61225; -.
DR ArrayExpress; P61225; -.
DR Bgee; P61225; -.
DR CleanEx; HS_RAP2B; -.
DR Genevestigator; P61225; -.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
DR GO; GO:0061097; P:regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00173; RAS; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Endosome; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Palmitate; Prenylation;
KW Reference proteome.
FT CHAIN 1 180 Ras-related protein Rap-2b.
FT /FTId=PRO_0000030215.
FT PROPEP 181 183 Removed in mature form.
FT /FTId=PRO_0000030216.
FT NP_BIND 10 17 GTP (By similarity).
FT NP_BIND 57 61 GTP (By similarity).
FT NP_BIND 116 119 GTP (By similarity).
FT MOTIF 32 40 Effector region (Probable).
FT MOD_RES 180 180 Cysteine methyl ester (Probable).
FT LIPID 180 180 S-geranylgeranyl cysteine.
FT CONFLICT 170 170 P -> S (in Ref. 1; CAA37178 and 2; no
FT nucleotide entry).
SQ SEQUENCE 183 AA; 20504 MW; A1139C2D5E7F5865 CRC64;
MREYKVVVLG SGGVGKSALT VQFVTGSFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG
TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI IRVKRYERVP MILVGNKVDL
EGEREVSYGE GKALAEEWSC PFMETSAKNK ASVDELFAEI VRQMNYAAQP NGDEGCCSAC
VIL
//

MIM 179541
*RECORD*
*FIELD* NO
179541
*FIELD* TI
*179541 RAS-RELATED PROTEIN 2B; RAP2B
*FIELD* TX

CLONING

Ohmstede et al. (1990) screened a platelet cDNA library with monoclonal
read moreantibody that recognizes a highly conserved epitope of Ras p21 (see
190020) involved in GTP binding. They identified a protein that is
structurally and functionally similar to but distinct from RAP1A
(179520), RAP1B (179530), and RAP2A (179540). RAP2B has a characteristic
Ras-type C-terminal motif for polyisoprenylation, and 2 C-terminal
cysteines suggesting that it may also be palmitoylated. Recombinant
RAP2B had an apparent molecular mass of 22 kD. The deduced RAP2B protein
contains 183 amino acids (Farrell et al., 1990). By RT-PCR, Greco et al.
(2006) detected RAP2B in purified human reticulocytes. Western blot
analysis of fractionated cells revealed the association of RAP2B with
cell membranes.

GENE FUNCTION

Ohmstede et al. (1990) demonstrated that recombinant RAP2B bound GTP. By
cell fractionated and Western blot analysis, Torti et al. (1993) found
that RAB2B was detergent soluble in resting platelets, but a significant
amount of RAP2B was associated with the cytoskeleton in platelets
aggregated with thrombin (176930), a thromboxane analog, or a
Ca(2+)-ATPase inhibitor. Translocation of RAP2B to the cytoskeleton was
strictly dependent on platelet aggregation. Inhibition of fibrinogen
(see FGA, 134820) binding to the glycoprotein IIb (607759)-IIIa (173470)
complex completely prevented the interaction of RAP2B with the
cytoskeleton.

Greco et al. (2006) found that membrane-associated RAP2B was activated
upon treatment of normal human reticulocytes with calcium and a calcium
ionophore. RAP2B was enriched in microvesicles released by
calcium-activated reticulocytes, suggesting a role for RAP2B in membrane
shedding.

MAPPING

The International Radiation Hybrid Mapping Consortium mapped the RAP2B
gene to chromosome 3 (TMAP SHGC-77468).

*FIELD* RF
1. Farrell, F. X.; Ohmstede, C.-A.; Reep, B. R.; Lapetina, E. G.:
cDNA sequence of a new ras-related gene (rap2b) isolated from human
platelets with sequence homology to rap2. Nucleic Acids Res. 18:
4281 only, 1990.

2. Greco, F.; Ciana, A.; Pietra, D.; Balduini, C.; Minetti, G.; Torti,
M.: Rap2, but not Rap1 GTPase is expressed in human red blood cells
and is involved in vesiculation. Biochim. Biophys. Acta 1763: 330-335,
2006.

3. Ohmstede, C.-A.; Farrell, F. X.; Reep, B. R.; Clemetson, K. J.;
Lapetina, E. G.: RAP2B: a RAS-related GTP-binding protein from platelets. Proc.
Nat. Acad. Sci. 87: 6527-6531, 1990.

4. Torti, M.; Ramaschi, G.; Sinigaglia, F.; Lapetina, E. G.; Balduini,
C.: Association of the low molecular weight GTP-binding protein rap2B
with the cytoskeleton during platelet aggregation. Proc. Nat. Acad.
Sci. 90: 7553-7557, 1993.

*FIELD* CN
Patricia A. Hartz - updated: 10/12/2006

*FIELD* CD
Victor A. McKusick: 10/8/1990

*FIELD* ED
carol: 10/13/2006
terry: 10/12/2006
mark: 1/11/1997
supermim: 3/16/1992
carol: 10/16/1990
carol: 10/8/1990

RBCC Red Blood Cell Collection

Full text data of RAP2B