RAP1B_HUMAN
ID RAP1B_HUMAN Reviewed; 184 AA.
AC P61224; B2R5Z2; B4DQI8; B4DW74; B4DW94; P09526; Q502X3; Q5TZR4; Q6DCA1;
AC Q6LES0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Ras-related protein Rap-1b;
DE EC=3.6.5.2 {ECO:0000269|PubMed:18309292};
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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-reactive
RT 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 sequenced by
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 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., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., 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., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., 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., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 AT
RP SER-39.
RX PubMed=3141412; DOI=10.1016/s0021-9258(18)37454-4;
RA Bokoch G.M., Parkos C.A., Mumby S.M.;
RT "Purification and characterization of the 22,000-dalton GTP-binding protein
RT 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 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., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [15]
RP ISOPRENYLATION AT CYS-181, AND METHYLATION 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., Takai Y.;
RT "Posttranslationally processed structure of the human platelet protein smg
RT p21B: evidence for geranylgeranylation and carboxyl methylation of the C-
RT terminal cysteine.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8960-8964(1990).
RN [16]
RP PHOSPHORYLATION AT SER-179 BY PKA, AND MUTAGENESIS OF SER-179.
RX PubMed=8463283; DOI=10.1016/s0021-9258(18)53207-5;
RA Altschuler D., Lapetina E.G.;
RT "Mutational analysis of the cAMP-dependent protein kinase-mediated
RT phosphorylation site of Rap1b.";
RL J. Biol. Chem. 268:7527-7531(1993).
RN [17]
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 small
RT G protein (RAP and RAB)-mediated signaling pathway.";
RL Genomics 90:249-260(2007).
RN [18]
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 [19]
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., Linnemann J.R.,
RA Spanjaard E., Brouwer P.M., van der Meer A.J., Zwartkruis F.J., Rehmann H.,
RA 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 [20]
RP INTERACTION WITH RAP1GDS1.
RX PubMed=24415755; DOI=10.1074/jbc.m113.527192;
RA Schuld N.J., Vervacke J.S., Lorimer E.L., Simon N.C., Hauser A.D.,
RA Barbieri J.T., Distefano M.D., Williams C.L.;
RT "The chaperone protein SmgGDS interacts with small GTPases entering the
RT prenylation pathway by recognizing the last amino acid in the CAAX motif.";
RL J. Biol. Chem. 289:6862-6876(2014).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-167 IN COMPLEX WITH GTP ANALOG
RP AND RAP1GAP, CATALYTIC ACTIVITY, SUBUNIT, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF 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 and
RT arginine residues.";
RL EMBO J. 27:1145-1153(2008).
RN [22]
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., Bos J.L.;
RT "Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B.";
RL Nature 455:124-127(2008).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-167 OF MUTANT VAL-12 IN COMPLEX
RP WITH KRIT1; GTP ANALOG AND MAGNESIUM, AND INTERACTION WITH 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-related
RT protein 1 (Rap1) and adaptor protein Krev interaction trapped 1 (KRIT1).";
RL J. Biol. Chem. 287:22317-22327(2012).
CC -!- FUNCTION: GTP-binding protein that possesses intrinsic GTPase activity.
CC Contributes to the polarizing activity of KRIT1 and CDH5 in the
CC establishment and maintenance of correct endothelial cell polarity and
CC vascular lumen. Required for the localization of phosphorylated PRKCZ,
CC PARD3 and TIAM1 to the cell junction. Plays a role in the establishment
CC of basal endothelial barrier function. {ECO:0000269|PubMed:18660803,
CC ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:21840392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000269|PubMed:18309292};
CC -!- ACTIVITY REGULATION: Activated by binding to the GTPase-activating
CC protein RAP1GAP. Activated by guanine nucleotide-exchange factor (GEF)
CC EPAC2 in a cAMP-dependent manner. {ECO:0000269|PubMed:18309292}.
CC -!- SUBUNIT: Heterodimer with RAP1GAP (PubMed:18309292). Interacts with
CC EPAC2 (PubMed:18660803). Interacts with SGSM1 (PubMed:17509819).
CC Interacts with SGSM2 (PubMed:17509819). Interacts with SGSM3
CC (PubMed:17509819). Interacts with KRIT1 (PubMed:22577140). Interacts
CC with RAP1GDS1 (PubMed:24415755). {ECO:0000269|PubMed:17509819,
CC ECO:0000269|PubMed:18309292, ECO:0000269|PubMed:18660803,
CC ECO:0000269|PubMed:22577140, ECO:0000269|PubMed:24415755}.
CC -!- INTERACTION:
CC P61224; P27797: CALR; NbExp=3; IntAct=EBI-358143, EBI-1049597;
CC P61224; P36957: DLST; NbExp=3; IntAct=EBI-358143, EBI-351007;
CC P61224; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-358143, EBI-11522433;
CC P61224; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-358143, EBI-1055945;
CC P61224; Q12967: RALGDS; NbExp=2; IntAct=EBI-358143, EBI-365861;
CC P61224; Q12967-6: RALGDS; NbExp=3; IntAct=EBI-358143, EBI-12005546;
CC P61224; P47736: RAP1GAP; NbExp=3; IntAct=EBI-358143, EBI-722307;
CC P61224; Q8WWW0: RASSF5; NbExp=3; IntAct=EBI-358143, EBI-367390;
CC P61224; Q9EQZ6-3: Rapgef4; Xeno; NbExp=3; IntAct=EBI-358143, EBI-15566495;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3141412}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:3141412}. Cell junction
CC {ECO:0000269|PubMed:20332120}. Note=May shuttle between plasma membrane
CC and cytosol (PubMed:3141412). Presence of KRIT1 and CDH5 is required
CC for its localization to the cell junction (PubMed:20332120).
CC {ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:3141412}.
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 {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC 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 CCDS; CCDS58252.1; -. [P61224-2]
DR CCDS; CCDS58253.1; -. [P61224-3]
DR CCDS; CCDS58254.1; -. [P61224-4]
DR CCDS; CCDS8984.1; -. [P61224-1]
DR PIR; S01952; TVHUR1.
DR RefSeq; NP_001010942.1; NM_001010942.2. [P61224-1]
DR RefSeq; NP_001238846.1; NM_001251917.1. [P61224-4]
DR RefSeq; NP_001238847.1; NM_001251918.1. [P61224-4]
DR RefSeq; NP_001238850.1; NM_001251921.1. [P61224-3]
DR RefSeq; NP_001238851.1; NM_001251922.1. [P61224-2]
DR RefSeq; NP_056461.1; NM_015646.5. [P61224-1]
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 PDB; 4MGI; X-ray; 2.80 A; R=1-167.
DR PDB; 4MGK; X-ray; 2.70 A; R=1-167.
DR PDB; 4MGY; X-ray; 2.60 A; R=1-167.
DR PDB; 4MGZ; X-ray; 3.00 A; R=1-167.
DR PDB; 4MH0; X-ray; 2.40 A; R=1-167.
DR PDB; 5KHO; X-ray; 2.78 A; C/D=1-167.
DR PDB; 6AXF; X-ray; 3.10 A; B/D/F/H/J/L/N/P=1-167.
DR PDB; 6BA6; NMR; -; B=1-167.
DR PDB; 6KYK; X-ray; 2.82 A; C/D/E/F=1-167.
DR PDB; 6OQ3; X-ray; 1.85 A; B=1-167.
DR PDB; 6OQ4; X-ray; 1.75 A; B=1-167.
DR PDB; 6UZK; X-ray; 1.92 A; B=1-167.
DR PDB; 7C7I; X-ray; 2.28 A; A/B=1-167.
DR PDB; 7C7J; X-ray; 2.39 A; A/B=1-167.
DR PDBsum; 3BRW; -.
DR PDBsum; 3CF6; -.
DR PDBsum; 4DXA; -.
DR PDBsum; 4HDO; -.
DR PDBsum; 4HDQ; -.
DR PDBsum; 4M8N; -.
DR PDBsum; 4MGI; -.
DR PDBsum; 4MGK; -.
DR PDBsum; 4MGY; -.
DR PDBsum; 4MGZ; -.
DR PDBsum; 4MH0; -.
DR PDBsum; 5KHO; -.
DR PDBsum; 6AXF; -.
DR PDBsum; 6BA6; -.
DR PDBsum; 6KYK; -.
DR PDBsum; 6OQ3; -.
DR PDBsum; 6OQ4; -.
DR PDBsum; 6UZK; -.
DR PDBsum; 7C7I; -.
DR PDBsum; 7C7J; -.
DR AlphaFoldDB; P61224; -.
DR SMR; P61224; -.
DR BioGRID; 111843; 172.
DR CORUM; P61224; -.
DR DIP; DIP-35407N; -.
DR IntAct; P61224; 68.
DR MINT; P61224; -.
DR STRING; 9606.ENSP00000250559; -.
DR GlyGen; P61224; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61224; -.
DR PhosphoSitePlus; P61224; -.
DR SwissPalm; P61224; -.
DR BioMuta; RAP1B; -.
DR DMDM; 47117723; -.
DR OGP; P09526; -.
DR EPD; P61224; -.
DR jPOST; P61224; -.
DR MassIVE; P61224; -.
DR MaxQB; P61224; -.
DR PaxDb; P61224; -.
DR PeptideAtlas; P61224; -.
DR PRIDE; P61224; -.
DR ProteomicsDB; 4879; -.
DR ProteomicsDB; 5316; -.
DR ProteomicsDB; 5324; -.
DR ProteomicsDB; 57277; -. [P61224-1]
DR TopDownProteomics; P61224-1; -. [P61224-1]
DR TopDownProteomics; P61224-2; -. [P61224-2]
DR Antibodypedia; 44258; 192 antibodies from 25 providers.
DR DNASU; 5908; -.
DR Ensembl; ENST00000250559.14; ENSP00000250559.9; ENSG00000127314.18. [P61224-1]
DR Ensembl; ENST00000341355.9; ENSP00000441275.1; ENSG00000127314.18. [P61224-1]
DR Ensembl; ENST00000393436.9; ENSP00000377085.5; ENSG00000127314.18. [P61224-1]
DR Ensembl; ENST00000450214.6; ENSP00000399986.2; ENSG00000127314.18. [P61224-4]
DR Ensembl; ENST00000537460.5; ENSP00000439966.1; ENSG00000127314.18. [P61224-1]
DR Ensembl; ENST00000539091.5; ENSP00000444830.1; ENSG00000127314.18. [P61224-4]
DR Ensembl; ENST00000540209.5; ENSP00000446318.1; ENSG00000127314.18. [P61224-3]
DR Ensembl; ENST00000542145.5; ENSP00000440014.1; ENSG00000127314.18. [P61224-2]
DR GeneID; 5908; -.
DR KEGG; hsa:5908; -.
DR MANE-Select; ENST00000250559.14; ENSP00000250559.9; NM_001010942.3; NP_001010942.1.
DR UCSC; uc001sub.5; human. [P61224-1]
DR CTD; 5908; -.
DR DisGeNET; 5908; -.
DR GeneCards; RAP1B; -.
DR HGNC; HGNC:9857; RAP1B.
DR HPA; ENSG00000127314; Low tissue specificity.
DR MIM; 179530; gene.
DR neXtProt; NX_P61224; -.
DR OpenTargets; ENSG00000127314; -.
DR PharmGKB; PA34219; -.
DR VEuPathDB; HostDB:ENSG00000127314; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000154429; -.
DR InParanoid; P61224; -.
DR OMA; CYRKQWV; -.
DR PhylomeDB; P61224; -.
DR TreeFam; TF313014; -.
DR PathwayCommons; P61224; -.
DR Reactome; R-HSA-354192; Integrin signaling.
DR Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-HSA-392517; Rap1 signalling.
DR Reactome; R-HSA-5674135; MAP2K and MAPK activation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
DR Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
DR Reactome; R-HSA-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants.
DR SignaLink; P61224; -.
DR SIGNOR; P61224; -.
DR BioGRID-ORCS; 5908; 128 hits in 1018 CRISPR screens.
DR ChiTaRS; RAP1B; human.
DR EvolutionaryTrace; P61224; -.
DR GeneWiki; RAP1B; -.
DR GenomeRNAi; 5908; -.
DR Pharos; P61224; Tbio.
DR PRO; PR:P61224; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P61224; protein.
DR Bgee; ENSG00000127314; Expressed in monocyte and 100 other tissues.
DR ExpressionAtlas; P61224; baseline and differential.
DR Genevisible; P61224; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
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:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
DR GO; GO:0061028; P:establishment of endothelial barrier; IMP:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IEA:Ensembl.
DR GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0033625; P:positive regulation of integrin activation; IMP:ARUK-UCL.
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 CDD; cd04175; Rap1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038851; Rap1.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 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; Cytoplasm; Direct protein sequencing; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Reference proteome.
FT CHAIN 1..181
FT /note="Ras-related protein Rap-1b"
FT /id="PRO_0000030209"
FT PROPEP 182..184
FT /note="Removed in mature form"
FT /id="PRO_0000030210"
FT REGION 25..67
FT /note="Interaction with KRIT1"
FT /evidence="ECO:0000269|PubMed:22577140"
FT MOTIF 32..40
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT BINDING 10..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:18309292,
FT ECO:0000269|PubMed:22577140"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:18309292,
FT ECO:0000269|PubMed:22577140"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:18309292,
FT ECO:0000269|PubMed:22577140"
FT BINDING 147..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:18309292,
FT ECO:0000269|PubMed:22577140"
FT MOD_RES 39
FT /note="ADP-ribosylserine; by botulinum toxin"
FT /evidence="ECO:0000305|PubMed:3141412"
FT MOD_RES 179
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:8463283"
FT MOD_RES 181
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:2123345"
FT LIPID 181
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:2123345"
FT VAR_SEQ 20..61
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045303"
FT VAR_SEQ 43..61
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045304"
FT VAR_SEQ 62..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045305"
FT MUTAGEN 12
FT /note="G->V: Constitutively activated."
FT MUTAGEN 25
FT /note="Q->A: Impairs interaction with KRIT1."
FT MUTAGEN 32
FT /note="Y->A: 25-fold reduction in RAP1GAP-stimulated GTPase
FT activity."
FT /evidence="ECO:0000269|PubMed:18309292"
FT MUTAGEN 32
FT /note="Y->F: 2-fold reduction in RAP1GAP-stimulated GTPase
FT activity."
FT /evidence="ECO:0000269|PubMed:18309292"
FT MUTAGEN 37
FT /note="E->A: Strong reduction in nucleotide exchange with
FT EPAC2."
FT /evidence="ECO:0000269|PubMed:18660803"
FT MUTAGEN 38
FT /note="D->A: Impairs interaction with KRIT1."
FT MUTAGEN 63
FT /note="Q->E: Abolishes complex formation with RAP1GAP. Loss
FT GTPase activity."
FT /evidence="ECO:0000269|PubMed:18309292"
FT MUTAGEN 64
FT /note="F->A: Abolishes complex formation with RAP1GAP. Loss
FT GTPase activity."
FT /evidence="ECO:0000269|PubMed:18309292"
FT MUTAGEN 179
FT /note="S->A: Abolishes phosphorylation by PKA."
FT /evidence="ECO:0000269|PubMed:8463283"
FT CONFLICT 8
FT /note="V -> F (in Ref. 11; AAH95467)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="K -> N (in Ref. 11; AAH78173)"
FT /evidence="ECO:0000305"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:4HDO"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:6AXF"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:4HDO"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:3CF6"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:4HDO"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:4HDO"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:4DXA"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4M8N"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:4HDO"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:4HDO"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:4HDO"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:4HDO"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3BRW"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:4HDO"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6BA6"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4HDO"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:4HDO"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:4HDO"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:4HDO"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:4HDO"
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
