Full text data of RAP1B
RAP1B
[Confidence: high (present in two of the MS resources)]
Ras-related protein Rap-1b (GTP-binding protein smg p21B; Flags: Precursor)
Ras-related protein Rap-1b (GTP-binding protein smg p21B; Flags: Precursor)
hRBCD
IPI00015148
IPI00015148 Ras-related protein Rap-1b Ras-related protein Rap-1b membrane n/a n/a n/a 1 n/a n/a 2 1 6 n/a n/a 4 n/a n/a n/a n/a n/a 4 4 n/a membrane n/a found at its expected molecular weight found at molecular weight
IPI00015148 Ras-related protein Rap-1b Ras-related protein Rap-1b membrane n/a n/a n/a 1 n/a n/a 2 1 6 n/a n/a 4 n/a n/a n/a n/a n/a 4 4 n/a membrane n/a found at its expected molecular weight found at molecular weight
UniProt
P61224
ID RAP1B_HUMAN Reviewed; 184 AA.
AC P61224; B2R5Z2; B4DQI8; B4DW74; B4DW94; P09526; Q502X3; Q5TZR4;
read moreAC Q6DCA1; Q6LES0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Ras-related protein Rap-1b;
DE AltName: Full=GTP-binding protein smg p21B;
DE Flags: Precursor;
GN Name=RAP1B; ORFNames=OK/SW-cl.11;
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] (ISOFORM 1).
RX PubMed=3137530; DOI=10.1093/nar/16.15.7719;
RA Pizon V., Lerosey I., Chardin P., Tavitian A.;
RT "Nucleotide sequence of a human cDNA encoding a ras-related protein
RT (rap1B).";
RL Nucleic Acids Res. 16:7719-7719(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Chondrosarcoma, Placenta, and Testis;
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 [12]
RP PROTEIN SEQUENCE OF 1-35, SUBCELLULAR LOCATION, AND ADP-RIBOSYLATION
RP AT SER-39.
RX PubMed=3141412;
RA Bokoch G.M., Parkos C.A., Mumby S.M.;
RT "Purification and characterization of the 22,000-dalton GTP-binding
RT protein substrate for ADP-ribosylation by botulinum toxin, G22K.";
RL J. Biol. Chem. 263:16744-16749(1988).
RN [13]
RP PROTEIN SEQUENCE OF 146-180, AND PHOSPHORYLATION.
RX PubMed=1696481; DOI=10.1016/0006-291X(90)92182-Y;
RA Siess W., Winegar D.A., Lapetina E.G.;
RT "Rap1-B is phosphorylated by protein kinase A in intact human
RT platelets.";
RL Biochem. Biophys. Res. Commun. 170:944-950(1990).
RN [14]
RP PROTEIN SEQUENCE OF 168-176.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [15]
RP ISOPRENYLATION AT CYS-181.
RC TISSUE=Platelet;
RX PubMed=2123345; DOI=10.1073/pnas.87.22.8960;
RA Kawata M., Farnsworth C.C., Yoshida Y., Gelb M.H., Glomset J.A.,
RA Takai Y.;
RT "Posttranslationally processed structure of the human platelet protein
RT smg p21B: evidence for geranylgeranylation and carboxyl methylation of
RT the C-terminal cysteine.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8960-8964(1990).
RN [16]
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 [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20332120; DOI=10.1242/jcs.059329;
RA Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G.,
RA Chapon F., Dejana E.;
RT "CCM1 regulates vascular-lumen organization by inducing endothelial
RT polarity.";
RL J. Cell Sci. 123:1073-1080(2010).
RN [18]
RP FUNCTION.
RX PubMed=21840392; DOI=10.1016/j.cellsig.2011.07.022;
RA Pannekoek W.J., van Dijk J.J., Chan O.Y., Huveneers S.,
RA Linnemann J.R., Spanjaard E., Brouwer P.M., van der Meer A.J.,
RA Zwartkruis F.J., Rehmann H., de Rooij J., Bos J.L.;
RT "Epac1 and PDZ-GEF cooperate in Rap1 mediated endothelial junction
RT control.";
RL Cell. Signal. 23:2056-2064(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-167 IN COMPLEX WITH GTP
RP ANALOG AND RAP1GAP, SUBUNIT, ENZYME REGULATION, AND MUTAGENESIS OF
RP TYR-32; GLN-63 AND PHE-64.
RX PubMed=18309292; DOI=10.1038/emboj.2008.30;
RA Scrima A., Thomas C., Deaconescu D., Wittinghofer A.;
RT "The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine
RT and arginine residues.";
RL EMBO J. 27:1145-1153(2008).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-167 IN COMPLEX WITH EPAC2,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-37.
RX PubMed=18660803; DOI=10.1038/nature07187;
RA Rehmann H., Arias-Palomo E., Hadders M.A., Schwede F., Llorca O.,
RA Bos J.L.;
RT "Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B.";
RL Nature 455:124-127(2008).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-167 OF MUTANT VAL-12 IN
RP COMPLEX WITH KRIT1; GTP ANALOG AND MAGNESIUM, AND INTERACTION WITH
RP KRIT1.
RX PubMed=22577140; DOI=10.1074/jbc.M112.361295;
RA Li X., Zhang R., Draheim K.M., Liu W., Calderwood D.A., Boggon T.J.;
RT "Structural basis for small G protein effector interaction of Ras-
RT related protein 1 (Rap1) and adaptor protein Krev interaction trapped
RT 1 (KRIT1).";
RL J. Biol. Chem. 287:22317-22327(2012).
CC -!- FUNCTION: GTP-binding protein that possesses intrinsic GTPase
CC activity. Contributes to the polarizing activity of KRIT1 and CDH5
CC in the establishment and maintenance of correct endothelial cell
CC polarity and vascular lumen. Required for the localization of
CC phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays
CC a role in the establishment of basal endothelial barrier function.
CC -!- ENZYME REGULATION: Activated by binding to the GTPase-activating
CC protein RAP1GAP. Activated by guanine nucleotide-exchange factor
CC (GEF) EPAC2 in a cAMP-dependent manner.
CC -!- SUBUNIT: Heterodimer with RAP1GAP. Interacts with EPAC2, SGSM1,
CC SGSM2 and SGSM3. Interacts with KRIT1.
CC -!- INTERACTION:
CC Q12967:RALGDS; NbExp=2; IntAct=EBI-358143, EBI-365861;
CC P47736:RAP1GAP; NbExp=3; IntAct=EBI-358143, EBI-722307;
CC P0CG48:UBC; NbExp=2; IntAct=EBI-358143, EBI-3390054;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm, cytosol. Cell
CC junction. Note=May shuttle between plasma membrane and cytosol.
CC Presence of KRIT1 and CDH5 is required for its localization to the
CC cell junction.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P61224-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61224-2; Sequence=VSP_045305;
CC Name=3;
CC IsoId=P61224-3; Sequence=VSP_045304;
CC Name=4;
CC IsoId=P61224-4; Sequence=VSP_045303;
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/RAP1BID273.html";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/rap1b/";
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DR EMBL; X08004; CAB46488.1; -; mRNA.
DR EMBL; AL080212; CAB45777.1; -; mRNA.
DR EMBL; AB062128; BAB93460.1; -; mRNA.
DR EMBL; AF493913; AAM12627.1; -; mRNA.
DR EMBL; AK298818; BAG60950.1; -; mRNA.
DR EMBL; AK301401; BAG62936.1; -; mRNA.
DR EMBL; AK301428; BAG62956.1; -; mRNA.
DR EMBL; AK312371; BAG35289.1; -; mRNA.
DR EMBL; CR407689; CAG28617.1; -; mRNA.
DR EMBL; BT020093; AAV38896.1; -; mRNA.
DR EMBL; EF581377; ABQ52130.1; -; Genomic_DNA.
DR EMBL; AC015550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97189.1; -; Genomic_DNA.
DR EMBL; BC000176; AAH00176.1; -; mRNA.
DR EMBL; BC078173; AAH78173.1; -; mRNA.
DR EMBL; BC095467; AAH95467.1; -; mRNA.
DR PIR; S01952; TVHUR1.
DR RefSeq; NP_001010942.1; NM_001010942.2.
DR RefSeq; NP_001238846.1; NM_001251917.1.
DR RefSeq; NP_001238847.1; NM_001251918.1.
DR RefSeq; NP_001238850.1; NM_001251921.1.
DR RefSeq; NP_001238851.1; NM_001251922.1.
DR RefSeq; NP_056461.1; NM_015646.5.
DR RefSeq; XP_005269110.1; XM_005269053.1.
DR UniGene; Hs.369920; -.
DR PDB; 3BRW; X-ray; 3.40 A; D=1-167.
DR PDB; 3CF6; X-ray; 2.20 A; R=1-167.
DR PDB; 4DXA; X-ray; 1.95 A; A=1-167.
DR PDB; 4HDO; X-ray; 1.67 A; B=1-167.
DR PDB; 4HDQ; X-ray; 1.95 A; B=1-167.
DR PDB; 4M8N; X-ray; 3.29 A; E/F/G/H=1-166.
DR PDBsum; 3BRW; -.
DR PDBsum; 3CF6; -.
DR PDBsum; 4DXA; -.
DR PDBsum; 4HDO; -.
DR PDBsum; 4HDQ; -.
DR PDBsum; 4M8N; -.
DR ProteinModelPortal; P61224; -.
DR SMR; P61224; 1-167.
DR DIP; DIP-35407N; -.
DR IntAct; P61224; 30.
DR MINT; MINT-1133272; -.
DR STRING; 9606.ENSP00000250559; -.
DR PhosphoSite; P61224; -.
DR DMDM; 47117723; -.
DR OGP; P09526; -.
DR PaxDb; P61224; -.
DR PRIDE; P61224; -.
DR DNASU; 5908; -.
DR Ensembl; ENST00000250559; ENSP00000250559; ENSG00000127314.
DR Ensembl; ENST00000341355; ENSP00000441275; ENSG00000127314.
DR Ensembl; ENST00000393436; ENSP00000377085; ENSG00000127314.
DR Ensembl; ENST00000450214; ENSP00000399986; ENSG00000127314.
DR Ensembl; ENST00000537460; ENSP00000439966; ENSG00000127314.
DR Ensembl; ENST00000539091; ENSP00000444830; ENSG00000127314.
DR Ensembl; ENST00000540209; ENSP00000446318; ENSG00000127314.
DR Ensembl; ENST00000542145; ENSP00000440014; ENSG00000127314.
DR GeneID; 5908; -.
DR KEGG; hsa:5908; -.
DR UCSC; uc010stf.2; human.
DR CTD; 5908; -.
DR GeneCards; GC12P069005; -.
DR H-InvDB; HIX0032084; -.
DR HGNC; HGNC:9857; RAP1B.
DR MIM; 179530; gene.
DR neXtProt; NX_P61224; -.
DR PharmGKB; PA34219; -.
DR eggNOG; COG1100; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P61224; -.
DR KO; K07836; -.
DR OMA; RDSTHPR; -.
DR OrthoDB; EOG7QVM41; -.
DR PhylomeDB; P61224; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P61224; -.
DR ChiTaRS; RAP1B; human.
DR EvolutionaryTrace; P61224; -.
DR GeneWiki; RAP1B; -.
DR GenomeRNAi; 5908; -.
DR NextBio; 22980; -.
DR PRO; PR:P61224; -.
DR ArrayExpress; P61224; -.
DR Bgee; P61224; -.
DR CleanEx; HS_RAP1B; -.
DR Genevestigator; P61224; -.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid particle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0061028; P:establishment of endothelial barrier; IMP:UniProtKB.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0032486; P:Rap protein signal transduction; IMP:UniProtKB.
DR GO; GO:1901888; P:regulation of cell junction assembly; IMP:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
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 3D-structure; ADP-ribosylation; Alternative splicing; Cell junction;
KW Cell membrane; Complete proteome; Cytoplasm;
KW Direct protein sequencing; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Reference proteome.
FT CHAIN 1 181 Ras-related protein Rap-1b.
FT /FTId=PRO_0000030209.
FT PROPEP 182 184 Removed in mature form.
FT /FTId=PRO_0000030210.
FT NP_BIND 10 18 GTP.
FT NP_BIND 57 61 GTP.
FT NP_BIND 116 119 GTP.
FT NP_BIND 147 149 GTP.
FT REGION 25 67 Interaction with KRIT1.
FT MOTIF 32 40 Effector region (Probable).
FT MOD_RES 39 39 ADP-ribosylserine; by botulinum toxin
FT (Probable).
FT MOD_RES 179 179 Phosphoserine; by PKA.
FT MOD_RES 181 181 Cysteine methyl ester.
FT LIPID 181 181 S-geranylgeranyl cysteine.
FT VAR_SEQ 20 61 Missing (in isoform 4).
FT /FTId=VSP_045303.
FT VAR_SEQ 43 61 Missing (in isoform 3).
FT /FTId=VSP_045304.
FT VAR_SEQ 62 108 Missing (in isoform 2).
FT /FTId=VSP_045305.
FT MUTAGEN 12 12 G->V: Constitutively activated.
FT MUTAGEN 25 25 Q->A: Impairs interaction with KRIT1.
FT MUTAGEN 32 32 Y->A: 25-fold reduction in RAP1GAP-
FT stimulated GTPase activity.
FT MUTAGEN 32 32 Y->F: 2-fold reduction in RAP1GAP-
FT stimulated GTPase activity.
FT MUTAGEN 37 37 E->A: Strong reduction in nucleotide
FT exchange with EPAC2.
FT MUTAGEN 38 38 D->A: Impairs interaction with KRIT1.
FT MUTAGEN 63 63 Q->E: Abolishes complex formation with
FT RAP1GAP. Loss GTPase activity.
FT MUTAGEN 64 64 F->A: Abolishes complex formation with
FT RAP1GAP. Loss GTPase activity.
FT CONFLICT 8 8 V -> F (in Ref. 11; AAH95467).
FT CONFLICT 16 16 K -> N (in Ref. 11; AAH78173).
FT STRAND 2 9
FT HELIX 16 25
FT TURN 27 29
FT STRAND 36 46
FT STRAND 49 58
FT STRAND 60 62
FT HELIX 68 74
FT STRAND 76 83
FT HELIX 87 91
FT HELIX 93 104
FT STRAND 105 107
FT STRAND 111 116
FT HELIX 121 123
FT HELIX 128 137
FT STRAND 142 145
FT TURN 148 151
FT HELIX 154 166
SQ SEQUENCE 184 AA; 20825 MW; CE976895E5965224 CRC64;
MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDAQQ CMLEILDTAG
TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI LRVKDTDDVP MILVGNKCDL
EDERVVGKEQ GQNLARQWNN CAFLESSAKS KINVNEIFYD LVRQINRKTP VPGKARKKSS
CQLL
//
ID RAP1B_HUMAN Reviewed; 184 AA.
AC P61224; B2R5Z2; B4DQI8; B4DW74; B4DW94; P09526; Q502X3; Q5TZR4;
read moreAC Q6DCA1; Q6LES0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Ras-related protein Rap-1b;
DE AltName: Full=GTP-binding protein smg p21B;
DE Flags: Precursor;
GN Name=RAP1B; ORFNames=OK/SW-cl.11;
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] (ISOFORM 1).
RX PubMed=3137530; DOI=10.1093/nar/16.15.7719;
RA Pizon V., Lerosey I., Chardin P., Tavitian A.;
RT "Nucleotide sequence of a human cDNA encoding a ras-related protein
RT (rap1B).";
RL Nucleic Acids Res. 16:7719-7719(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-
RT reactive CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Chondrosarcoma, Placenta, and Testis;
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 [12]
RP PROTEIN SEQUENCE OF 1-35, SUBCELLULAR LOCATION, AND ADP-RIBOSYLATION
RP AT SER-39.
RX PubMed=3141412;
RA Bokoch G.M., Parkos C.A., Mumby S.M.;
RT "Purification and characterization of the 22,000-dalton GTP-binding
RT protein substrate for ADP-ribosylation by botulinum toxin, G22K.";
RL J. Biol. Chem. 263:16744-16749(1988).
RN [13]
RP PROTEIN SEQUENCE OF 146-180, AND PHOSPHORYLATION.
RX PubMed=1696481; DOI=10.1016/0006-291X(90)92182-Y;
RA Siess W., Winegar D.A., Lapetina E.G.;
RT "Rap1-B is phosphorylated by protein kinase A in intact human
RT platelets.";
RL Biochem. Biophys. Res. Commun. 170:944-950(1990).
RN [14]
RP PROTEIN SEQUENCE OF 168-176.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [15]
RP ISOPRENYLATION AT CYS-181.
RC TISSUE=Platelet;
RX PubMed=2123345; DOI=10.1073/pnas.87.22.8960;
RA Kawata M., Farnsworth C.C., Yoshida Y., Gelb M.H., Glomset J.A.,
RA Takai Y.;
RT "Posttranslationally processed structure of the human platelet protein
RT smg p21B: evidence for geranylgeranylation and carboxyl methylation of
RT the C-terminal cysteine.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8960-8964(1990).
RN [16]
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 [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20332120; DOI=10.1242/jcs.059329;
RA Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G.,
RA Chapon F., Dejana E.;
RT "CCM1 regulates vascular-lumen organization by inducing endothelial
RT polarity.";
RL J. Cell Sci. 123:1073-1080(2010).
RN [18]
RP FUNCTION.
RX PubMed=21840392; DOI=10.1016/j.cellsig.2011.07.022;
RA Pannekoek W.J., van Dijk J.J., Chan O.Y., Huveneers S.,
RA Linnemann J.R., Spanjaard E., Brouwer P.M., van der Meer A.J.,
RA Zwartkruis F.J., Rehmann H., de Rooij J., Bos J.L.;
RT "Epac1 and PDZ-GEF cooperate in Rap1 mediated endothelial junction
RT control.";
RL Cell. Signal. 23:2056-2064(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-167 IN COMPLEX WITH GTP
RP ANALOG AND RAP1GAP, SUBUNIT, ENZYME REGULATION, AND MUTAGENESIS OF
RP TYR-32; GLN-63 AND PHE-64.
RX PubMed=18309292; DOI=10.1038/emboj.2008.30;
RA Scrima A., Thomas C., Deaconescu D., Wittinghofer A.;
RT "The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine
RT and arginine residues.";
RL EMBO J. 27:1145-1153(2008).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-167 IN COMPLEX WITH EPAC2,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-37.
RX PubMed=18660803; DOI=10.1038/nature07187;
RA Rehmann H., Arias-Palomo E., Hadders M.A., Schwede F., Llorca O.,
RA Bos J.L.;
RT "Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B.";
RL Nature 455:124-127(2008).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-167 OF MUTANT VAL-12 IN
RP COMPLEX WITH KRIT1; GTP ANALOG AND MAGNESIUM, AND INTERACTION WITH
RP KRIT1.
RX PubMed=22577140; DOI=10.1074/jbc.M112.361295;
RA Li X., Zhang R., Draheim K.M., Liu W., Calderwood D.A., Boggon T.J.;
RT "Structural basis for small G protein effector interaction of Ras-
RT related protein 1 (Rap1) and adaptor protein Krev interaction trapped
RT 1 (KRIT1).";
RL J. Biol. Chem. 287:22317-22327(2012).
CC -!- FUNCTION: GTP-binding protein that possesses intrinsic GTPase
CC activity. Contributes to the polarizing activity of KRIT1 and CDH5
CC in the establishment and maintenance of correct endothelial cell
CC polarity and vascular lumen. Required for the localization of
CC phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays
CC a role in the establishment of basal endothelial barrier function.
CC -!- ENZYME REGULATION: Activated by binding to the GTPase-activating
CC protein RAP1GAP. Activated by guanine nucleotide-exchange factor
CC (GEF) EPAC2 in a cAMP-dependent manner.
CC -!- SUBUNIT: Heterodimer with RAP1GAP. Interacts with EPAC2, SGSM1,
CC SGSM2 and SGSM3. Interacts with KRIT1.
CC -!- INTERACTION:
CC Q12967:RALGDS; NbExp=2; IntAct=EBI-358143, EBI-365861;
CC P47736:RAP1GAP; NbExp=3; IntAct=EBI-358143, EBI-722307;
CC P0CG48:UBC; NbExp=2; IntAct=EBI-358143, EBI-3390054;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm, cytosol. Cell
CC junction. Note=May shuttle between plasma membrane and cytosol.
CC Presence of KRIT1 and CDH5 is required for its localization to the
CC cell junction.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P61224-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61224-2; Sequence=VSP_045305;
CC Name=3;
CC IsoId=P61224-3; Sequence=VSP_045304;
CC Name=4;
CC IsoId=P61224-4; Sequence=VSP_045303;
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/RAP1BID273.html";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/rap1b/";
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DR EMBL; X08004; CAB46488.1; -; mRNA.
DR EMBL; AL080212; CAB45777.1; -; mRNA.
DR EMBL; AB062128; BAB93460.1; -; mRNA.
DR EMBL; AF493913; AAM12627.1; -; mRNA.
DR EMBL; AK298818; BAG60950.1; -; mRNA.
DR EMBL; AK301401; BAG62936.1; -; mRNA.
DR EMBL; AK301428; BAG62956.1; -; mRNA.
DR EMBL; AK312371; BAG35289.1; -; mRNA.
DR EMBL; CR407689; CAG28617.1; -; mRNA.
DR EMBL; BT020093; AAV38896.1; -; mRNA.
DR EMBL; EF581377; ABQ52130.1; -; Genomic_DNA.
DR EMBL; AC015550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97189.1; -; Genomic_DNA.
DR EMBL; BC000176; AAH00176.1; -; mRNA.
DR EMBL; BC078173; AAH78173.1; -; mRNA.
DR EMBL; BC095467; AAH95467.1; -; mRNA.
DR PIR; S01952; TVHUR1.
DR RefSeq; NP_001010942.1; NM_001010942.2.
DR RefSeq; NP_001238846.1; NM_001251917.1.
DR RefSeq; NP_001238847.1; NM_001251918.1.
DR RefSeq; NP_001238850.1; NM_001251921.1.
DR RefSeq; NP_001238851.1; NM_001251922.1.
DR RefSeq; NP_056461.1; NM_015646.5.
DR RefSeq; XP_005269110.1; XM_005269053.1.
DR UniGene; Hs.369920; -.
DR PDB; 3BRW; X-ray; 3.40 A; D=1-167.
DR PDB; 3CF6; X-ray; 2.20 A; R=1-167.
DR PDB; 4DXA; X-ray; 1.95 A; A=1-167.
DR PDB; 4HDO; X-ray; 1.67 A; B=1-167.
DR PDB; 4HDQ; X-ray; 1.95 A; B=1-167.
DR PDB; 4M8N; X-ray; 3.29 A; E/F/G/H=1-166.
DR PDBsum; 3BRW; -.
DR PDBsum; 3CF6; -.
DR PDBsum; 4DXA; -.
DR PDBsum; 4HDO; -.
DR PDBsum; 4HDQ; -.
DR PDBsum; 4M8N; -.
DR ProteinModelPortal; P61224; -.
DR SMR; P61224; 1-167.
DR DIP; DIP-35407N; -.
DR IntAct; P61224; 30.
DR MINT; MINT-1133272; -.
DR STRING; 9606.ENSP00000250559; -.
DR PhosphoSite; P61224; -.
DR DMDM; 47117723; -.
DR OGP; P09526; -.
DR PaxDb; P61224; -.
DR PRIDE; P61224; -.
DR DNASU; 5908; -.
DR Ensembl; ENST00000250559; ENSP00000250559; ENSG00000127314.
DR Ensembl; ENST00000341355; ENSP00000441275; ENSG00000127314.
DR Ensembl; ENST00000393436; ENSP00000377085; ENSG00000127314.
DR Ensembl; ENST00000450214; ENSP00000399986; ENSG00000127314.
DR Ensembl; ENST00000537460; ENSP00000439966; ENSG00000127314.
DR Ensembl; ENST00000539091; ENSP00000444830; ENSG00000127314.
DR Ensembl; ENST00000540209; ENSP00000446318; ENSG00000127314.
DR Ensembl; ENST00000542145; ENSP00000440014; ENSG00000127314.
DR GeneID; 5908; -.
DR KEGG; hsa:5908; -.
DR UCSC; uc010stf.2; human.
DR CTD; 5908; -.
DR GeneCards; GC12P069005; -.
DR H-InvDB; HIX0032084; -.
DR HGNC; HGNC:9857; RAP1B.
DR MIM; 179530; gene.
DR neXtProt; NX_P61224; -.
DR PharmGKB; PA34219; -.
DR eggNOG; COG1100; -.
DR HOVERGEN; HBG009351; -.
DR InParanoid; P61224; -.
DR KO; K07836; -.
DR OMA; RDSTHPR; -.
DR OrthoDB; EOG7QVM41; -.
DR PhylomeDB; P61224; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P61224; -.
DR ChiTaRS; RAP1B; human.
DR EvolutionaryTrace; P61224; -.
DR GeneWiki; RAP1B; -.
DR GenomeRNAi; 5908; -.
DR NextBio; 22980; -.
DR PRO; PR:P61224; -.
DR ArrayExpress; P61224; -.
DR Bgee; P61224; -.
DR CleanEx; HS_RAP1B; -.
DR Genevestigator; P61224; -.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid particle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0061028; P:establishment of endothelial barrier; IMP:UniProtKB.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0032486; P:Rap protein signal transduction; IMP:UniProtKB.
DR GO; GO:1901888; P:regulation of cell junction assembly; IMP:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
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 3D-structure; ADP-ribosylation; Alternative splicing; Cell junction;
KW Cell membrane; Complete proteome; Cytoplasm;
KW Direct protein sequencing; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Reference proteome.
FT CHAIN 1 181 Ras-related protein Rap-1b.
FT /FTId=PRO_0000030209.
FT PROPEP 182 184 Removed in mature form.
FT /FTId=PRO_0000030210.
FT NP_BIND 10 18 GTP.
FT NP_BIND 57 61 GTP.
FT NP_BIND 116 119 GTP.
FT NP_BIND 147 149 GTP.
FT REGION 25 67 Interaction with KRIT1.
FT MOTIF 32 40 Effector region (Probable).
FT MOD_RES 39 39 ADP-ribosylserine; by botulinum toxin
FT (Probable).
FT MOD_RES 179 179 Phosphoserine; by PKA.
FT MOD_RES 181 181 Cysteine methyl ester.
FT LIPID 181 181 S-geranylgeranyl cysteine.
FT VAR_SEQ 20 61 Missing (in isoform 4).
FT /FTId=VSP_045303.
FT VAR_SEQ 43 61 Missing (in isoform 3).
FT /FTId=VSP_045304.
FT VAR_SEQ 62 108 Missing (in isoform 2).
FT /FTId=VSP_045305.
FT MUTAGEN 12 12 G->V: Constitutively activated.
FT MUTAGEN 25 25 Q->A: Impairs interaction with KRIT1.
FT MUTAGEN 32 32 Y->A: 25-fold reduction in RAP1GAP-
FT stimulated GTPase activity.
FT MUTAGEN 32 32 Y->F: 2-fold reduction in RAP1GAP-
FT stimulated GTPase activity.
FT MUTAGEN 37 37 E->A: Strong reduction in nucleotide
FT exchange with EPAC2.
FT MUTAGEN 38 38 D->A: Impairs interaction with KRIT1.
FT MUTAGEN 63 63 Q->E: Abolishes complex formation with
FT RAP1GAP. Loss GTPase activity.
FT MUTAGEN 64 64 F->A: Abolishes complex formation with
FT RAP1GAP. Loss GTPase activity.
FT CONFLICT 8 8 V -> F (in Ref. 11; AAH95467).
FT CONFLICT 16 16 K -> N (in Ref. 11; AAH78173).
FT STRAND 2 9
FT HELIX 16 25
FT TURN 27 29
FT STRAND 36 46
FT STRAND 49 58
FT STRAND 60 62
FT HELIX 68 74
FT STRAND 76 83
FT HELIX 87 91
FT HELIX 93 104
FT STRAND 105 107
FT STRAND 111 116
FT HELIX 121 123
FT HELIX 128 137
FT STRAND 142 145
FT TURN 148 151
FT HELIX 154 166
SQ SEQUENCE 184 AA; 20825 MW; CE976895E5965224 CRC64;
MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDAQQ CMLEILDTAG
TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI LRVKDTDDVP MILVGNKCDL
EDERVVGKEQ GQNLARQWNN CAFLESSAKS KINVNEIFYD LVRQINRKTP VPGKARKKSS
CQLL
//
MIM
179530
*RECORD*
*FIELD* NO
179530
*FIELD* TI
*179530 RAS-RELATED PROTEIN RAP1B; RAP1B
*FIELD* TX
DESCRIPTION
RAP1B and RAP1A (179520) belong to a superfamily of RAS (see
read more190020)-like small GTP-binding proteins involved in cell signaling.
CLONING
Pizon et al. (1988) cloned human RAP1B. The deduced 184-amino acid
protein is 95% identical to RAP1A. RAP1B shares several properties with
the RAS protein, suggesting that it may bind GTP/GDP and have a membrane
location.
Matsui et al. (1990) reported the amino acid sequence of RAP1B, which
they called SMG p21B, purified from bovine brain and human platelets.
The bovine and human proteins are identical.
GENE FUNCTION
Hoshijima et al. (1988) and Kawata et al. (1989) reported that RAP1B is
phosphorylated by cAMP-dependent protein kinase (see 601639) on ser179.
Kawata et al., 1990 found that phosphorylation enhanced GDP/GTP
exchange.
Kawata et al. (1990) determined that purified human platelet RAP1B is
posttranslationally modified by the geranylgeranylation of cys181.
Further modifications cause proteolytic removal of the last 3 C-terminal
amino acids, followed by partial methylation of the remaining terminal
cysteinyl carboxyl group. Kawata et al. (1990) suggested that
geranylgeranylation and methylation of RAP1B are important, because they
found that C-terminal modification was required for the binding of RAP1B
to membranes.
Lova et al. (2003) noted that, in resting cells, RAP1B is mainly located
at the membrane, but translocates to the cytosol upon activation. In
activated platelets, RAP1B interacts with the reorganized actin-based
cytoskeleton. RAP1B is activated by phosphorylation, increased
intracellular Ca(2+), and by agonist-induced stimulation of Gi (139310),
which results in the rapid binding of GTP to RAP1B. Lova et al. (2003)
found that stimulation of Gi-dependent signaling could activate human
platelet RAP1B through phosphatidylinositol(3,4,5)-trisphosphate
(PtdIns(3,4,5)P3), but not PtdIns(3,4)P2. They concluded that the PI3
kinase (see 601232) pathway of RAP1B activation may contribute to
potentiation of platelet aggregation.
Schwamborn and Puschel (2004) found that localization of Rap1b to the
tip of a single neurite in rat hippocampal neurons was a decisive step
in determining which neurite became the axon.
MAPPING
By in situ hybridization, Rousseau-Merck et al. (1990) mapped the RAP1B
gene to chromosome 12q14.
BIOCHEMICAL FEATURES
- Crystal Structure
Rehmann et al. (2008) determined the structure of EPAC2 (606058) in
complex with a cAMP analog (Sp-cAMPS) and RAP1B by x-ray crystallography
and single-particle electron microscopy. The structure represents the
cAMP-activated state of the EPAC2 protein with the RAP1B protein trapped
in the course of the exchange reaction. Comparison with the inactive
conformation revealed that cAMP binding causes conformational changes
that allow the cyclic nucleotide binding domain to swing from a position
blocking the Rap binding site toward a docking site at the Ras exchange
motif domain.
ANIMAL MODEL
Chrzanowska-Wodnicka et al. (2005) generated Rap1b -/- mice and observed
a bleeding defect due to defective platelet function. Aggregation of
Rap1b-null platelets was reduced in response to stimulation with both G
protein-coupled receptor (GPCR; see 600239)-linked and GPCR-independent
agonists and was found to be due to decreased agonist-induced activation
of integrin alpha-IIb-beta-3 (see 607759, 173470) and signaling
downstream. In vivo, Rap1b-null mice were protected from arterial
thrombosis. Chrzanowska-Wodnicka et al. (2005) concluded that RAP1B is
involved in a common pathway of integrin activation, is required for
normal hemostasis in vivo, and may be a clinically relevant
antithrombotic therapy target.
*FIELD* RF
1. Chrzanowska-Wodnicka, M.; Smyth, S. S.; Schoenwaelder, S. M.; Fischer,
T. H.; White, G. C., II: Rap1b is required for normal platelet function
and hemostasis in mice. J. Clin. Invest. 115: 680-687, 2005. Note:
Erratum: J. Clin. Invest. 115: 2296 only, 2005.
2. Hoshijima, M.; Kikuchi, A.; Kawata, M.; Ohmori, T.; Hashimoto,
E.; Yamamura, H.; Takai, Y.: Phosphorylation by cyclic AMP-dependent
protein kinase of a human platelet Mr 22,000 GTP-binding protein (smg
p21) having the same putative effector domain as the ras gene products. Biochem.
Biophys. Res. Commun. 157: 851-860, 1988.
3. Kawata, M.; Farnsworth, C. C.; Yoshida, Y.; Gelb, M. H.; Glomset,
J. A.; Takai, Y.: Posttranslationally processed structure of the
human platelet protein smg p21B: evidence for geranylgeranylation
and carboxyl methylation of the C-terminal cysteine. Proc. Nat. Acad.
Sci. 87: 8960-8964, 1990.
4. Kawata, M.; Kikuchi, A.; Hoshijima, M.; Yamamoto, K.; Hashimoto,
E.; Yamamura, H.; Takai, Y.: Phosphorylation of smg p21, a ras p21-like
GTP-binding protein, by cyclic AMP-dependent protein kinase in a cell-free
system and in response to prostaglandin E1 in intact human platelets. J.
Biol. Chem. 264: 15688-15695, 1989.
5. Lova, P.; Paganini, S.; Hirsch, E.; Barberis, L.; Wymann, M.; Sinigaglia,
F.; Balduini, C.; Torti, M.: A selective role for phosphatidylinositol
3,4,5-trisphosphate in the Gi-dependent activation of platelet Rap1B. J.
Biol. Chem. 278: 131-138, 2003.
6. Matsui, Y.; Kikuchi, A.; Kawata, M.; Kondo, J.; Teranishi, Y.;
Takai, Y.: Molecular cloning of smg p21B and identification of smg
p21 purified from bovine brain and human platelets as smg p21B. Biochem.
Biophys. Res. Commun. 166: 1010-1016, 1990.
7. Pizon, V.; Lerosey, I.; Chardin, P.; Tavitian, A.: Nucleotide
sequence of a human cDNA encoding ras-related protein (rap1B). Nucleic
Acids Res. 16: 7719 only, 1988.
8. Rehmann, H.; Arias-Palomo, E.; Hadders, M. A.; Schwede, F.; Llorca,
O.; Bos, J. L.: Structure of Epac2 in complex with a cyclic AMP analogue
and RAP1B. Nature 455: 124-127, 2008.
9. Rousseau-Merck, M. F.; Pizon, V.; Tavitian, A.; Berger, R.: Chromosome
mapping of the human RAS-related RAP1A, RAP1B, and RAP2 genes to chromosomes
1p12-p13, 12q14, and 13q34, respectively. Cytogenet. Cell Genet. 53:
2-4, 1990.
10. Schwamborn, J. C.; Puschel, A. W.: The sequential activity of
the GTPases Rap1B and Cdc42 determines neuronal polarity. Nature
Neurosci. 7: 923-929, 2004.
*FIELD* CN
Ada Hamosh - updated: 9/24/2008
Marla J. F. O'Neill - updated: 4/11/2005
Patricia A. Hartz - updated: 10/11/2004
*FIELD* CD
Victor A. McKusick: 9/6/1989
*FIELD* ED
alopez: 09/26/2008
terry: 9/24/2008
mgross: 10/6/2005
tkritzer: 4/13/2005
terry: 4/11/2005
mgross: 10/11/2004
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 9/6/1989
*RECORD*
*FIELD* NO
179530
*FIELD* TI
*179530 RAS-RELATED PROTEIN RAP1B; RAP1B
*FIELD* TX
DESCRIPTION
RAP1B and RAP1A (179520) belong to a superfamily of RAS (see
read more190020)-like small GTP-binding proteins involved in cell signaling.
CLONING
Pizon et al. (1988) cloned human RAP1B. The deduced 184-amino acid
protein is 95% identical to RAP1A. RAP1B shares several properties with
the RAS protein, suggesting that it may bind GTP/GDP and have a membrane
location.
Matsui et al. (1990) reported the amino acid sequence of RAP1B, which
they called SMG p21B, purified from bovine brain and human platelets.
The bovine and human proteins are identical.
GENE FUNCTION
Hoshijima et al. (1988) and Kawata et al. (1989) reported that RAP1B is
phosphorylated by cAMP-dependent protein kinase (see 601639) on ser179.
Kawata et al., 1990 found that phosphorylation enhanced GDP/GTP
exchange.
Kawata et al. (1990) determined that purified human platelet RAP1B is
posttranslationally modified by the geranylgeranylation of cys181.
Further modifications cause proteolytic removal of the last 3 C-terminal
amino acids, followed by partial methylation of the remaining terminal
cysteinyl carboxyl group. Kawata et al. (1990) suggested that
geranylgeranylation and methylation of RAP1B are important, because they
found that C-terminal modification was required for the binding of RAP1B
to membranes.
Lova et al. (2003) noted that, in resting cells, RAP1B is mainly located
at the membrane, but translocates to the cytosol upon activation. In
activated platelets, RAP1B interacts with the reorganized actin-based
cytoskeleton. RAP1B is activated by phosphorylation, increased
intracellular Ca(2+), and by agonist-induced stimulation of Gi (139310),
which results in the rapid binding of GTP to RAP1B. Lova et al. (2003)
found that stimulation of Gi-dependent signaling could activate human
platelet RAP1B through phosphatidylinositol(3,4,5)-trisphosphate
(PtdIns(3,4,5)P3), but not PtdIns(3,4)P2. They concluded that the PI3
kinase (see 601232) pathway of RAP1B activation may contribute to
potentiation of platelet aggregation.
Schwamborn and Puschel (2004) found that localization of Rap1b to the
tip of a single neurite in rat hippocampal neurons was a decisive step
in determining which neurite became the axon.
MAPPING
By in situ hybridization, Rousseau-Merck et al. (1990) mapped the RAP1B
gene to chromosome 12q14.
BIOCHEMICAL FEATURES
- Crystal Structure
Rehmann et al. (2008) determined the structure of EPAC2 (606058) in
complex with a cAMP analog (Sp-cAMPS) and RAP1B by x-ray crystallography
and single-particle electron microscopy. The structure represents the
cAMP-activated state of the EPAC2 protein with the RAP1B protein trapped
in the course of the exchange reaction. Comparison with the inactive
conformation revealed that cAMP binding causes conformational changes
that allow the cyclic nucleotide binding domain to swing from a position
blocking the Rap binding site toward a docking site at the Ras exchange
motif domain.
ANIMAL MODEL
Chrzanowska-Wodnicka et al. (2005) generated Rap1b -/- mice and observed
a bleeding defect due to defective platelet function. Aggregation of
Rap1b-null platelets was reduced in response to stimulation with both G
protein-coupled receptor (GPCR; see 600239)-linked and GPCR-independent
agonists and was found to be due to decreased agonist-induced activation
of integrin alpha-IIb-beta-3 (see 607759, 173470) and signaling
downstream. In vivo, Rap1b-null mice were protected from arterial
thrombosis. Chrzanowska-Wodnicka et al. (2005) concluded that RAP1B is
involved in a common pathway of integrin activation, is required for
normal hemostasis in vivo, and may be a clinically relevant
antithrombotic therapy target.
*FIELD* RF
1. Chrzanowska-Wodnicka, M.; Smyth, S. S.; Schoenwaelder, S. M.; Fischer,
T. H.; White, G. C., II: Rap1b is required for normal platelet function
and hemostasis in mice. J. Clin. Invest. 115: 680-687, 2005. Note:
Erratum: J. Clin. Invest. 115: 2296 only, 2005.
2. Hoshijima, M.; Kikuchi, A.; Kawata, M.; Ohmori, T.; Hashimoto,
E.; Yamamura, H.; Takai, Y.: Phosphorylation by cyclic AMP-dependent
protein kinase of a human platelet Mr 22,000 GTP-binding protein (smg
p21) having the same putative effector domain as the ras gene products. Biochem.
Biophys. Res. Commun. 157: 851-860, 1988.
3. Kawata, M.; Farnsworth, C. C.; Yoshida, Y.; Gelb, M. H.; Glomset,
J. A.; Takai, Y.: Posttranslationally processed structure of the
human platelet protein smg p21B: evidence for geranylgeranylation
and carboxyl methylation of the C-terminal cysteine. Proc. Nat. Acad.
Sci. 87: 8960-8964, 1990.
4. Kawata, M.; Kikuchi, A.; Hoshijima, M.; Yamamoto, K.; Hashimoto,
E.; Yamamura, H.; Takai, Y.: Phosphorylation of smg p21, a ras p21-like
GTP-binding protein, by cyclic AMP-dependent protein kinase in a cell-free
system and in response to prostaglandin E1 in intact human platelets. J.
Biol. Chem. 264: 15688-15695, 1989.
5. Lova, P.; Paganini, S.; Hirsch, E.; Barberis, L.; Wymann, M.; Sinigaglia,
F.; Balduini, C.; Torti, M.: A selective role for phosphatidylinositol
3,4,5-trisphosphate in the Gi-dependent activation of platelet Rap1B. J.
Biol. Chem. 278: 131-138, 2003.
6. Matsui, Y.; Kikuchi, A.; Kawata, M.; Kondo, J.; Teranishi, Y.;
Takai, Y.: Molecular cloning of smg p21B and identification of smg
p21 purified from bovine brain and human platelets as smg p21B. Biochem.
Biophys. Res. Commun. 166: 1010-1016, 1990.
7. Pizon, V.; Lerosey, I.; Chardin, P.; Tavitian, A.: Nucleotide
sequence of a human cDNA encoding ras-related protein (rap1B). Nucleic
Acids Res. 16: 7719 only, 1988.
8. Rehmann, H.; Arias-Palomo, E.; Hadders, M. A.; Schwede, F.; Llorca,
O.; Bos, J. L.: Structure of Epac2 in complex with a cyclic AMP analogue
and RAP1B. Nature 455: 124-127, 2008.
9. Rousseau-Merck, M. F.; Pizon, V.; Tavitian, A.; Berger, R.: Chromosome
mapping of the human RAS-related RAP1A, RAP1B, and RAP2 genes to chromosomes
1p12-p13, 12q14, and 13q34, respectively. Cytogenet. Cell Genet. 53:
2-4, 1990.
10. Schwamborn, J. C.; Puschel, A. W.: The sequential activity of
the GTPases Rap1B and Cdc42 determines neuronal polarity. Nature
Neurosci. 7: 923-929, 2004.
*FIELD* CN
Ada Hamosh - updated: 9/24/2008
Marla J. F. O'Neill - updated: 4/11/2005
Patricia A. Hartz - updated: 10/11/2004
*FIELD* CD
Victor A. McKusick: 9/6/1989
*FIELD* ED
alopez: 09/26/2008
terry: 9/24/2008
mgross: 10/6/2005
tkritzer: 4/13/2005
terry: 4/11/2005
mgross: 10/11/2004
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 9/6/1989