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Ras-related protein Rap-1b (GTP-binding protein smg p21B)

 RAP1B_HUMAN             Reviewed;         184 AA.
P61224; B2R5Z2; B4DQI8; B4DW74; B4DW94; P09526; Q502X3; Q5TZR4;
Q6DCA1; Q6LES0;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 1.
18-JUL-2018, entry version 171.
RecName: Full=Ras-related protein Rap-1b;
AltName: Full=GTP-binding protein smg p21B;
Flags: Precursor;
Name=RAP1B; ORFNames=OK/SW-cl.11;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3137530; DOI=10.1093/nar/16.15.7719;
Pizon V., Lerosey I., Chardin P., Tavitian A.;
"Nucleotide sequence of a human cDNA encoding a ras-related protein
(rap1B).";
Nucleic Acids Res. 16:7719-7719(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
TISSUE=Amygdala;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Chondrosarcoma, Placenta, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PROTEIN SEQUENCE OF 1-35, SUBCELLULAR LOCATION, AND ADP-RIBOSYLATION
AT SER-39.
PubMed=3141412;
Bokoch G.M., Parkos C.A., Mumby S.M.;
"Purification and characterization of the 22,000-dalton GTP-binding
protein substrate for ADP-ribosylation by botulinum toxin, G22K.";
J. Biol. Chem. 263:16744-16749(1988).
[13]
PROTEIN SEQUENCE OF 146-180, AND PHOSPHORYLATION.
PubMed=1696481; DOI=10.1016/0006-291X(90)92182-Y;
Siess W., Winegar D.A., Lapetina E.G.;
"Rap1-B is phosphorylated by protein kinase A in intact human
platelets.";
Biochem. Biophys. Res. Commun. 170:944-950(1990).
[14]
PROTEIN SEQUENCE OF 168-176.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[15]
ISOPRENYLATION AT CYS-181, AND METHYLATION AT CYS-181.
TISSUE=Platelet;
PubMed=2123345; DOI=10.1073/pnas.87.22.8960;
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. Natl. Acad. Sci. U.S.A. 87:8960-8964(1990).
[16]
PHOSPHORYLATION AT SER-179 BY PKA, AND MUTAGENESIS OF SER-179.
PubMed=8463283;
Altschuler D., Lapetina E.G.;
"Mutational analysis of the cAMP-dependent protein kinase-mediated
phosphorylation site of Rap1b.";
J. Biol. Chem. 268:7527-7531(1993).
[17]
INTERACTION WITH SGSM1; SGSM2 AND SGSM3.
PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013;
Yang H., Sasaki T., Minoshima S., Shimizu N.;
"Identification of three novel proteins (SGSM1, 2, 3) which modulate
small G protein (RAP and RAB)-mediated signaling pathway.";
Genomics 90:249-260(2007).
[18]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20332120; DOI=10.1242/jcs.059329;
Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G.,
Chapon F., Dejana E.;
"CCM1 regulates vascular-lumen organization by inducing endothelial
polarity.";
J. Cell Sci. 123:1073-1080(2010).
[19]
FUNCTION.
PubMed=21840392; DOI=10.1016/j.cellsig.2011.07.022;
Pannekoek W.J., van Dijk J.J., Chan O.Y., Huveneers S.,
Linnemann J.R., Spanjaard E., Brouwer P.M., van der Meer A.J.,
Zwartkruis F.J., Rehmann H., de Rooij J., Bos J.L.;
"Epac1 and PDZ-GEF cooperate in Rap1 mediated endothelial junction
control.";
Cell. Signal. 23:2056-2064(2011).
[20]
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-167 IN COMPLEX WITH GTP
ANALOG AND RAP1GAP, SUBUNIT, ENZYME REGULATION, AND MUTAGENESIS OF
TYR-32; GLN-63 AND PHE-64.
PubMed=18309292; DOI=10.1038/emboj.2008.30;
Scrima A., Thomas C., Deaconescu D., Wittinghofer A.;
"The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine
and arginine residues.";
EMBO J. 27:1145-1153(2008).
[21]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-167 IN COMPLEX WITH EPAC2,
FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-37.
PubMed=18660803; DOI=10.1038/nature07187;
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).
[22]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-167 OF MUTANT VAL-12 IN
COMPLEX WITH KRIT1; GTP ANALOG AND MAGNESIUM, AND INTERACTION WITH
KRIT1.
PubMed=22577140; DOI=10.1074/jbc.M112.361295;
Li X., Zhang R., Draheim K.M., Liu W., Calderwood D.A., Boggon T.J.;
"Structural basis for small G protein effector interaction of Ras-
related protein 1 (Rap1) and adaptor protein Krev interaction trapped
1 (KRIT1).";
J. Biol. Chem. 287:22317-22327(2012).
-!- FUNCTION: GTP-binding protein that possesses intrinsic GTPase
activity. Contributes to the polarizing activity of KRIT1 and CDH5
in the establishment and maintenance of correct endothelial cell
polarity and vascular lumen. Required for the localization of
phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays
a role in the establishment of basal endothelial barrier function.
{ECO:0000269|PubMed:18660803, ECO:0000269|PubMed:20332120,
ECO:0000269|PubMed:21840392}.
-!- ENZYME REGULATION: Activated by binding to the GTPase-activating
protein RAP1GAP. Activated by guanine nucleotide-exchange factor
(GEF) EPAC2 in a cAMP-dependent manner.
{ECO:0000269|PubMed:18309292}.
-!- SUBUNIT: Heterodimer with RAP1GAP. Interacts with EPAC2, SGSM1,
SGSM2 and SGSM3. Interacts with KRIT1.
{ECO:0000269|PubMed:17509819, ECO:0000269|PubMed:18309292,
ECO:0000269|PubMed:18660803, ECO:0000269|PubMed:22577140}.
-!- INTERACTION:
Q12967:RALGDS; NbExp=2; IntAct=EBI-358143, EBI-365861;
P47736:RAP1GAP; NbExp=3; IntAct=EBI-358143, EBI-722307;
Q9EQZ6-3:Rapgef4 (xeno); NbExp=3; IntAct=EBI-358143, EBI-15566495;
Q8WWW0:RASSF5; NbExp=3; IntAct=EBI-358143, EBI-367390;
-!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm, cytosol. Cell
junction. Note=May shuttle between plasma membrane and cytosol.
Presence of KRIT1 and CDH5 is required for its localization to the
cell junction.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P61224-1; Sequence=Displayed;
Name=2;
IsoId=P61224-2; Sequence=VSP_045305;
Name=3;
IsoId=P61224-3; Sequence=VSP_045304;
Name=4;
IsoId=P61224-4; Sequence=VSP_045303;
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RAP1BID273.html";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/rap1b/";
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EMBL; X08004; CAB46488.1; -; mRNA.
EMBL; AL080212; CAB45777.1; -; mRNA.
EMBL; AB062128; BAB93460.1; -; mRNA.
EMBL; AF493913; AAM12627.1; -; mRNA.
EMBL; AK298818; BAG60950.1; -; mRNA.
EMBL; AK301401; BAG62936.1; -; mRNA.
EMBL; AK301428; BAG62956.1; -; mRNA.
EMBL; AK312371; BAG35289.1; -; mRNA.
EMBL; CR407689; CAG28617.1; -; mRNA.
EMBL; BT020093; AAV38896.1; -; mRNA.
EMBL; EF581377; ABQ52130.1; -; Genomic_DNA.
EMBL; AC015550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW97189.1; -; Genomic_DNA.
EMBL; BC000176; AAH00176.1; -; mRNA.
EMBL; BC078173; AAH78173.1; -; mRNA.
EMBL; BC095467; AAH95467.1; -; mRNA.
CCDS; CCDS58252.1; -. [P61224-2]
CCDS; CCDS58253.1; -. [P61224-3]
CCDS; CCDS58254.1; -. [P61224-4]
CCDS; CCDS8984.1; -. [P61224-1]
PIR; S01952; TVHUR1.
RefSeq; NP_001010942.1; NM_001010942.2. [P61224-1]
RefSeq; NP_001238846.1; NM_001251917.1. [P61224-4]
RefSeq; NP_001238847.1; NM_001251918.1. [P61224-4]
RefSeq; NP_001238850.1; NM_001251921.1. [P61224-3]
RefSeq; NP_001238851.1; NM_001251922.1. [P61224-2]
RefSeq; NP_056461.1; NM_015646.5. [P61224-1]
UniGene; Hs.369920; -.
PDB; 3BRW; X-ray; 3.40 A; D=1-167.
PDB; 3CF6; X-ray; 2.20 A; R=1-167.
PDB; 4DXA; X-ray; 1.95 A; A=1-167.
PDB; 4HDO; X-ray; 1.67 A; B=1-167.
PDB; 4HDQ; X-ray; 1.95 A; B=1-167.
PDB; 4M8N; X-ray; 3.29 A; E/F/G/H=1-166.
PDB; 4MGI; X-ray; 2.80 A; R=1-167.
PDB; 4MGK; X-ray; 2.70 A; R=1-167.
PDB; 4MGY; X-ray; 2.60 A; R=1-167.
PDB; 4MGZ; X-ray; 3.00 A; R=1-167.
PDB; 4MH0; X-ray; 2.40 A; R=1-167.
PDB; 5KHO; X-ray; 2.78 A; C/D=1-167.
PDB; 6AXF; X-ray; 3.10 A; B/D/F/H/J/L/N/P=1-167.
PDB; 6BA6; NMR; -; B=1-167.
PDBsum; 3BRW; -.
PDBsum; 3CF6; -.
PDBsum; 4DXA; -.
PDBsum; 4HDO; -.
PDBsum; 4HDQ; -.
PDBsum; 4M8N; -.
PDBsum; 4MGI; -.
PDBsum; 4MGK; -.
PDBsum; 4MGY; -.
PDBsum; 4MGZ; -.
PDBsum; 4MH0; -.
PDBsum; 5KHO; -.
PDBsum; 6AXF; -.
PDBsum; 6BA6; -.
ProteinModelPortal; P61224; -.
SMR; P61224; -.
BioGrid; 111843; 76.
DIP; DIP-35407N; -.
IntAct; P61224; 56.
MINT; P61224; -.
STRING; 9606.ENSP00000250559; -.
iPTMnet; P61224; -.
PhosphoSitePlus; P61224; -.
SwissPalm; P61224; -.
BioMuta; RAP1B; -.
DMDM; 47117723; -.
OGP; P09526; -.
EPD; P61224; -.
MaxQB; P61224; -.
PaxDb; P61224; -.
PeptideAtlas; P61224; -.
PRIDE; P61224; -.
ProteomicsDB; 57277; -.
TopDownProteomics; P61224-1; -. [P61224-1]
TopDownProteomics; P61224-2; -. [P61224-2]
DNASU; 5908; -.
Ensembl; ENST00000250559; ENSP00000250559; ENSG00000127314. [P61224-1]
Ensembl; ENST00000341355; ENSP00000441275; ENSG00000127314. [P61224-1]
Ensembl; ENST00000393436; ENSP00000377085; ENSG00000127314. [P61224-1]
Ensembl; ENST00000450214; ENSP00000399986; ENSG00000127314. [P61224-4]
Ensembl; ENST00000537460; ENSP00000439966; ENSG00000127314. [P61224-1]
Ensembl; ENST00000539091; ENSP00000444830; ENSG00000127314. [P61224-4]
Ensembl; ENST00000540209; ENSP00000446318; ENSG00000127314. [P61224-3]
Ensembl; ENST00000542145; ENSP00000440014; ENSG00000127314. [P61224-2]
GeneID; 5908; -.
KEGG; hsa:5908; -.
UCSC; uc001sub.5; human. [P61224-1]
CTD; 5908; -.
DisGeNET; 5908; -.
EuPathDB; HostDB:ENSG00000127314.17; -.
GeneCards; RAP1B; -.
H-InvDB; HIX0032084; -.
HGNC; HGNC:9857; RAP1B.
MalaCards; RAP1B; -.
MIM; 179530; gene.
neXtProt; NX_P61224; -.
OpenTargets; ENSG00000127314; -.
PharmGKB; PA34219; -.
eggNOG; KOG0395; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00860000133678; -.
HOGENOM; HOG000233973; -.
HOVERGEN; HBG009351; -.
InParanoid; P61224; -.
KO; K07836; -.
OMA; WGNAPYY; -.
OrthoDB; EOG091G0OOG; -.
PhylomeDB; P61224; -.
TreeFam; TF313014; -.
Reactome; R-HSA-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-HSA-392517; Rap1 signalling.
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
Reactome; R-HSA-8875555; MET activates RAP1 and RAC1.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
SignaLink; P61224; -.
SIGNOR; P61224; -.
ChiTaRS; RAP1B; human.
EvolutionaryTrace; P61224; -.
GeneWiki; RAP1B; -.
GenomeRNAi; 5908; -.
PRO; PR:P61224; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000127314; -.
CleanEx; HS_RAP1B; -.
ExpressionAtlas; P61224; baseline and differential.
Genevisible; P61224; HS.
GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005622; C:intracellular; IDA:LIFEdb.
GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
GO; GO:0016020; C:membrane; TAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0097211; P:cellular response to gonadotropin-releasing hormone; IEA:Ensembl.
GO; GO:0061028; P:establishment of endothelial barrier; IMP:UniProtKB.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0032486; P:Rap protein signal transduction; IMP:UniProtKB.
GO; GO:1901888; P:regulation of cell junction assembly; IMP:UniProtKB.
GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
GO; GO:0009743; P:response to carbohydrate; IEA:Ensembl.
CDD; cd04175; Rap1; 1.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR038851; Rap1.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras-type.
PANTHER; PTHR24070; PTHR24070; 1.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51421; RAS; 1.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Alternative splicing; Cell junction;
Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; GTP-binding; Lipoprotein; Membrane;
Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
Reference proteome.
CHAIN 1 181 Ras-related protein Rap-1b.
/FTId=PRO_0000030209.
PROPEP 182 184 Removed in mature form.
/FTId=PRO_0000030210.
NP_BIND 10 18 GTP. {ECO:0000269|PubMed:18309292,
ECO:0000269|PubMed:22577140}.
NP_BIND 57 61 GTP. {ECO:0000269|PubMed:18309292,
ECO:0000269|PubMed:22577140}.
NP_BIND 116 119 GTP. {ECO:0000269|PubMed:18309292,
ECO:0000269|PubMed:22577140}.
NP_BIND 147 149 GTP. {ECO:0000269|PubMed:18309292,
ECO:0000269|PubMed:22577140}.
REGION 25 67 Interaction with KRIT1.
{ECO:0000269|PubMed:22577140}.
MOTIF 32 40 Effector region. {ECO:0000305}.
MOD_RES 39 39 ADP-ribosylserine; by botulinum toxin.
{ECO:0000305|PubMed:3141412}.
MOD_RES 179 179 Phosphoserine; by PKA.
{ECO:0000269|PubMed:8463283}.
MOD_RES 181 181 Cysteine methyl ester.
{ECO:0000269|PubMed:2123345}.
LIPID 181 181 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:2123345}.
VAR_SEQ 20 61 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045303.
VAR_SEQ 43 61 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045304.
VAR_SEQ 62 108 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045305.
MUTAGEN 12 12 G->V: Constitutively activated.
MUTAGEN 25 25 Q->A: Impairs interaction with KRIT1.
MUTAGEN 32 32 Y->A: 25-fold reduction in RAP1GAP-
stimulated GTPase activity.
{ECO:0000269|PubMed:18309292}.
MUTAGEN 32 32 Y->F: 2-fold reduction in RAP1GAP-
stimulated GTPase activity.
{ECO:0000269|PubMed:18309292}.
MUTAGEN 37 37 E->A: Strong reduction in nucleotide
exchange with EPAC2.
{ECO:0000269|PubMed:18660803}.
MUTAGEN 38 38 D->A: Impairs interaction with KRIT1.
MUTAGEN 63 63 Q->E: Abolishes complex formation with
RAP1GAP. Loss GTPase activity.
{ECO:0000269|PubMed:18309292}.
MUTAGEN 64 64 F->A: Abolishes complex formation with
RAP1GAP. Loss GTPase activity.
{ECO:0000269|PubMed:18309292}.
MUTAGEN 179 179 S->A: Abolishes phosphorylation by PKA.
{ECO:0000269|PubMed:8463283}.
CONFLICT 8 8 V -> F (in Ref. 11; AAH95467).
{ECO:0000305}.
CONFLICT 16 16 K -> N (in Ref. 11; AAH78173).
{ECO:0000305}.
STRAND 2 9 {ECO:0000244|PDB:4HDO}.
HELIX 12 14 {ECO:0000244|PDB:6AXF}.
HELIX 16 25 {ECO:0000244|PDB:4HDO}.
TURN 27 29 {ECO:0000244|PDB:3CF6}.
STRAND 36 46 {ECO:0000244|PDB:4HDO}.
STRAND 49 58 {ECO:0000244|PDB:4HDO}.
STRAND 60 62 {ECO:0000244|PDB:4DXA}.
STRAND 63 65 {ECO:0000244|PDB:4M8N}.
HELIX 68 74 {ECO:0000244|PDB:4HDO}.
STRAND 76 83 {ECO:0000244|PDB:4HDO}.
HELIX 87 91 {ECO:0000244|PDB:4HDO}.
HELIX 93 104 {ECO:0000244|PDB:4HDO}.
STRAND 105 107 {ECO:0000244|PDB:3BRW}.
STRAND 111 116 {ECO:0000244|PDB:4HDO}.
HELIX 118 120 {ECO:0000244|PDB:6BA6}.
HELIX 121 123 {ECO:0000244|PDB:4HDO}.
HELIX 128 137 {ECO:0000244|PDB:4HDO}.
STRAND 142 145 {ECO:0000244|PDB:4HDO}.
TURN 148 151 {ECO:0000244|PDB:4HDO}.
HELIX 154 166 {ECO:0000244|PDB:4HDO}.
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


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