Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ras-related protein Ral-A

 RALA_HUMAN              Reviewed;         206 AA.
P11233; A4D1W3;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
18-JUL-2018, entry version 198.
RecName: Full=Ras-related protein Ral-A;
Flags: Precursor;
Name=RALA; Synonyms=RAL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2662142; DOI=10.1093/nar/17.11.4380;
Chardin P., Tavitian A.;
"Coding sequences of human ralA and ralB cDNAs.";
Nucleic Acids Res. 17:4380-4380(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Platelet;
PubMed=2550440;
Polakis P.G., Weber R.F., Nevins B., Didsbury J.R., Evans T.,
Snyderman R.;
"Identification of the ral and rac1 gene products, low molecular mass
GTP-binding proteins from human platelets.";
J. Biol. Chem. 264:16383-16389(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
ISOPRENYLATION AT CYS-203.
PubMed=1903399;
Kinsella B.T., Erdman R.A., Maltese W.A.;
"Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins
encoded by rac1, rac2, and ralA.";
J. Biol. Chem. 266:9786-9794(1991).
[9]
INTERACTION WITH RALBP1.
PubMed=7673236; DOI=10.1074/jbc.270.38.22473;
Jullien-Flores V., Dorseuil O., Romero F., Letourneur F.,
Saragosti S., Berger R., Tavitian A., Gacon G., Camonis J.H.;
"Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with
CDC42/Rac GTPase-activating protein activity.";
J. Biol. Chem. 270:22473-22477(1995).
[10]
INTERACTION WITH RALGPS1.
PubMed=10747847; DOI=10.1074/jbc.C000085200;
Rebhun J.F., Chen H., Quilliam L.A.;
"Identification and characterization of a new family of guanine
nucleotide exchange factors for the ras-related GTPase Ral.";
J. Biol. Chem. 275:13406-13410(2000).
[11]
INTERACTION WITH EXOC8.
PubMed=14525976; DOI=10.1074/jbc.M308702200;
Moskalenko S., Tong C., Rosse C., Mirey G., Formstecher E., Daviet L.,
Camonis J., White M.A.;
"Ral GTPases regulate exocyst assembly through dual subunit
interactions.";
J. Biol. Chem. 278:51743-51748(2003).
[12]
SUBCELLULAR LOCATION.
PubMed=16213214; DOI=10.1016/j.cell.2005.07.027;
Gromley A., Yeaman C., Rosa J., Redick S., Chen C.-T., Mirabelle S.,
Guha M., Sillibourne J., Doxsey S.J.;
"Centriolin anchoring of exocyst and SNARE complexes at the midbody is
required for secretory-vesicle-mediated abscission.";
Cell 123:75-87(2005).
[13]
SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-203, AND MUTAGENESIS OF
CYS-203 AND LEU-206.
PubMed=17875936; DOI=10.1128/MCB.00057-07;
Falsetti S.C., Wang D.A., Peng H., Carrico D., Cox A.D., Der C.J.,
Hamilton A.D., Sebti S.M.;
"Geranylgeranyltransferase I inhibitors target RalB to inhibit
anchorage-dependent growth and induce apoptosis and RalA to inhibit
anchorage-independent growth.";
Mol. Cell. Biol. 27:8003-8014(2007).
[14]
FUNCTION, INTERACTION WITH EXOC2 AND EXOC8, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 1-MET--SER-11; GLY-23; GLU-38; ALA-48; ASP-49 AND
GLN-72.
PubMed=18756269; DOI=10.1038/emboj.2008.166;
Cascone I., Selimoglu R., Ozdemir C., Del Nery E., Yeaman C.,
White M., Camonis J.;
"Distinct roles of RalA and RalB in the progression of cytokinesis are
supported by distinct RalGEFs.";
EMBO J. 27:2375-2387(2008).
[15]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH LPAR1;
LPAR2 AND GRK2.
PubMed=19306925; DOI=10.1016/j.cellsig.2009.03.011;
Aziziyeh A.I., Li T.T., Pape C., Pampillo M., Chidiac P.,
Possmayer F., Babwah A.V., Bhattacharya M.;
"Dual regulation of lysophosphatidic acid (LPA1) receptor signalling
by Ral and GRK.";
Cell. Signal. 21:1207-1217(2009).
[16]
FUNCTION.
PubMed=20005108; DOI=10.1016/j.cub.2009.11.016;
Balasubramanian N., Meier J.A., Scott D.W., Norambuena A., White M.A.,
Schwartz M.A.;
"RalA-exocyst complex regulates integrin-dependent membrane raft
exocytosis and growth signaling.";
Curr. Biol. 20:75-79(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[19]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 9-183 IN COMPLEX WITH EXOC8
AND GTP ANALOG, INTERACTION WITH EXOC2, AND MUTAGENESIS OF LYS-47;
ALA-48; SER-50; ARG-52 AND ASN-81.
PubMed=15920473; DOI=10.1038/sj.emboj.7600699;
Jin R., Junutula J.R., Matern H.T., Ervin K.E., Scheller R.H.,
Brunger A.T.;
"Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the
RalA GTPase.";
EMBO J. 24:2064-2074(2005).
[20]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 9-183 IN COMPLEX WITH GTP AND
CLOSTRIDIUM EXOENZYME C3.
PubMed=16177825; DOI=10.1038/sj.emboj.7600813;
Pautsch A., Vogelsgesang M., Traenkle J., Herrmann C., Aktories K.;
"Crystal structure of the C3bot-RalA complex reveals a novel type of
action of a bacterial exoenzyme.";
EMBO J. 24:3670-3680(2005).
[21]
X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) IN COMPLEX WITH GTP AND
CLOSTRIDIUM EXOENZYME C3.
PubMed=15809419; DOI=10.1073/pnas.0501525102;
Holbourn K.P., Sutton J.M., Evans H.R., Shone C.C., Acharya K.R.;
"Molecular recognition of an ADP-ribosylating Clostridium botulinum C3
exoenzyme by RalA GTPase.";
Proc. Natl. Acad. Sci. U.S.A. 102:5357-5362(2005).
-!- FUNCTION: Multifunctional GTPase involved in a variety of cellular
processes including gene expression, cell migration, cell
proliferation, oncogenic transformation and membrane trafficking.
Accomplishes its multiple functions by interacting with distinct
downstream effectors. Acts as a GTP sensor for GTP-dependent
exocytosis of dense core vesicles. The RALA-exocyst complex
regulates integrin-dependent membrane raft exocytosis and growth
signaling (PubMed:20005108). Key regulator of LPAR1 signaling and
competes with GRK2 for binding to LPAR1 thus affecting the
signaling properties of the receptor. Required for anchorage-
independent proliferation of transformed cells (PubMed:19306925).
During mitosis, supports the stabilization and elongation of the
intracellular bridge between dividing cells. Cooperates with EXOC2
to recruit other components of the exocyst to the early midbody
(PubMed:18756269). {ECO:0000269|PubMed:18756269,
ECO:0000269|PubMed:19306925, ECO:0000269|PubMed:20005108}.
-!- ENZYME REGULATION: Alternates between an inactive form bound to
GDP and an active form bound to GTP. Activated by a guanine
nucleotide-exchange factor (GEF) and inactivated by a GTPase-
activating protein (GAP).
-!- SUBUNIT: Interacts (via effector domain) with RALBP1
(PubMed:7673236). Interacts with EXOC2/Sec5 and EXOC8/Exo84;
binding to EXOC2 and EXOC8 is mutually exclusive (PubMed:14525976,
PubMed:18756269, PubMed:15920473). Interacts with Clostridium
exoenzyme C3 (PubMed:16177825, PubMed:15809419). Interacts with
RALGPS1 (PubMed:10747847). Interacts with LPAR1 and LPAR2.
Interacts with GRK2 in response to LPAR1 activation. RALA and GRK2
binding to LPAR1 is mutually exclusive (PubMed:19306925).
Interacts with CDC42 (By similarity).
{ECO:0000250|UniProtKB:P63322, ECO:0000269|PubMed:10747847,
ECO:0000269|PubMed:14525976, ECO:0000269|PubMed:15809419,
ECO:0000269|PubMed:15920473, ECO:0000269|PubMed:16177825,
ECO:0000269|PubMed:18756269, ECO:0000269|PubMed:19306925,
ECO:0000269|PubMed:7673236}.
-!- INTERACTION:
P62158:CALM3; NbExp=3; IntAct=EBI-1036803, EBI-397435;
O54921:Exoc2 (xeno); NbExp=2; IntAct=EBI-1036803, EBI-1036795;
P30154:PPP2R1B; NbExp=6; IntAct=EBI-1036803, EBI-357094;
Q15311:RALBP1; NbExp=4; IntAct=EBI-1036803, EBI-749285;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17875936,
ECO:0000269|PubMed:18756269, ECO:0000269|PubMed:19306925}; Lipid-
anchor {ECO:0000269|PubMed:17875936}; Cytoplasmic side. Cleavage
furrow {ECO:0000269|PubMed:18756269}. Midbody, Midbody ring
{ECO:0000269|PubMed:16213214}. Note=Predominantly at the cell
surface in the absence of LPA. In the presence of LPA, colocalizes
with LPAR1 and LPAR2 in endocytic vesicles (PubMed:19306925). May
colocalize with CNTRL/centriolin at the midbody ring
(PubMed:16213214). However, localization at the midbody at late
cytokinesis was not confirmed (PubMed:18756269).
{ECO:0000269|PubMed:16213214, ECO:0000269|PubMed:18756269,
ECO:0000269|PubMed:19306925}.
-!- INDUCTION: Activated in an LPA-dependent manner by LPAR1 and in an
LPA-independent manner by LPAR2. {ECO:0000269|PubMed:19306925}.
-!- PTM: Prenylation is essential for membrane localization. The
geranylgeranylated form and the farnesylated mutant do not undergo
alternative prenylation in response to geranylgeranyltransferase I
inhibitors (GGTIs) and farnesyltransferase I inhibitors (FTIs).
{ECO:0000269|PubMed:17875936, ECO:0000269|PubMed:1903399}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X15014; CAA33118.1; -; mRNA.
EMBL; M29893; AAA36542.1; -; mRNA.
EMBL; AF493910; AAM12624.1; -; mRNA.
EMBL; AC004837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236951; EAL23994.1; -; Genomic_DNA.
EMBL; CH471073; EAW94123.1; -; Genomic_DNA.
EMBL; BC039858; AAH39858.1; -; mRNA.
CCDS; CCDS5460.1; -.
PIR; S04596; TVHUAA.
RefSeq; NP_005393.2; NM_005402.3.
RefSeq; XP_006715825.1; XM_006715762.2.
RefSeq; XP_011513768.1; XM_011515466.1.
UniGene; Hs.6906; -.
PDB; 1UAD; X-ray; 2.10 A; A/B=9-183.
PDB; 1ZC3; X-ray; 2.00 A; A/C=9-183.
PDB; 1ZC4; X-ray; 2.50 A; A/C=9-183.
PDB; 2A78; X-ray; 1.81 A; A=9-183.
PDB; 2A9K; X-ray; 1.73 A; A=9-183.
PDB; 2BOV; X-ray; 2.66 A; A=1-206.
PDBsum; 1UAD; -.
PDBsum; 1ZC3; -.
PDBsum; 1ZC4; -.
PDBsum; 2A78; -.
PDBsum; 2A9K; -.
PDBsum; 2BOV; -.
DisProt; DP00581; -.
ProteinModelPortal; P11233; -.
SMR; P11233; -.
BioGrid; 111834; 71.
IntAct; P11233; 35.
MINT; P11233; -.
STRING; 9606.ENSP00000005257; -.
ChEMBL; CHEMBL3879855; -.
DrugBank; DB04315; Guanosine-5'-Diphosphate.
iPTMnet; P11233; -.
PhosphoSitePlus; P11233; -.
SwissPalm; P11233; -.
BioMuta; RALA; -.
DMDM; 131834; -.
EPD; P11233; -.
MaxQB; P11233; -.
PaxDb; P11233; -.
PeptideAtlas; P11233; -.
PRIDE; P11233; -.
ProteomicsDB; 52726; -.
Ensembl; ENST00000005257; ENSP00000005257; ENSG00000006451.
GeneID; 5898; -.
KEGG; hsa:5898; -.
UCSC; uc003thd.4; human.
CTD; 5898; -.
DisGeNET; 5898; -.
EuPathDB; HostDB:ENSG00000006451.7; -.
GeneCards; RALA; -.
HGNC; HGNC:9839; RALA.
HPA; HPA065232; -.
MIM; 179550; gene.
neXtProt; NX_P11233; -.
OpenTargets; ENSG00000006451; -.
PharmGKB; PA34197; -.
eggNOG; KOG0395; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00860000133672; -.
HOGENOM; HOG000233973; -.
HOVERGEN; HBG009351; -.
InParanoid; P11233; -.
KO; K07834; -.
OMA; QSRAQQW; -.
OrthoDB; EOG091G0UAU; -.
PhylomeDB; P11233; -.
TreeFam; TF312796; -.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-171007; p38MAPK events.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
SIGNOR; P11233; -.
ChiTaRS; RALA; human.
EvolutionaryTrace; P11233; -.
GeneWiki; RALA; -.
GenomeRNAi; 5898; -.
PRO; PR:P11233; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000006451; -.
CleanEx; HS_RALA; -.
ExpressionAtlas; P11233; baseline and differential.
Genevisible; P11233; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
GO; GO:0031755; F:Edg-2 lysophosphatidic acid receptor binding; IDA:UniProtKB.
GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0017022; F:myosin binding; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:BHF-UCL.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0051665; P:membrane raft localization; IDA:UniProtKB.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:BHF-UCL.
GO; GO:0007265; P:Ras protein signal transduction; IEA:InterPro.
GO; GO:0017157; P:regulation of exocytosis; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR028412; Ral.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras-type.
PANTHER; PTHR24070; PTHR24070; 1.
PANTHER; PTHR24070:SF174; PTHR24070:SF174; 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; Cell cycle; Cell division; Cell membrane;
Complete proteome; Exocytosis; GTP-binding; Lipoprotein; Membrane;
Methylation; Nucleotide-binding; Prenylation; Reference proteome.
CHAIN 1 203 Ras-related protein Ral-A.
/FTId=PRO_0000082693.
PROPEP 204 206 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000281344.
NP_BIND 24 29 GTP. {ECO:0000269|PubMed:15809419,
ECO:0000269|PubMed:16177825}.
NP_BIND 40 46 GTP. {ECO:0000269|PubMed:15809419,
ECO:0000269|PubMed:16177825}.
NP_BIND 127 130 GTP. {ECO:0000269|PubMed:15809419,
ECO:0000269|PubMed:16177825}.
MOTIF 43 51 Effector region.
MOD_RES 203 203 Cysteine methyl ester. {ECO:0000250}.
LIPID 203 203 S-geranylgeranyl cysteine.
{ECO:0000269|PubMed:17875936,
ECO:0000269|PubMed:1903399}.
MUTAGEN 1 11 Missing: Impaired cytokinesis, as shown
by increased number of binucleate cells.
Impaired cytokinesis; when associated
with L-72. {ECO:0000269|PubMed:18756269}.
MUTAGEN 23 23 G->V: Impaired cytokinesis, as shown by
increased number of binucleate cells. No
effect on interaction with EXOC2 and
EXOC8. No effect on cytokinesis; when
associated with R-38 or W-48. Decreased
interaction with EXOC2 and EXOC8; when
associated with R-38 or W-48.
{ECO:0000269|PubMed:18756269}.
MUTAGEN 38 38 E->R: Impaired cytokinesis, as shown by
increased number of binucleate cells. No
effect on cytokinesis; when associated
with V-23. Decreased interaction with
EXOC2 and EXOC8; when associated with V-
23. {ECO:0000269|PubMed:18756269}.
MUTAGEN 47 47 K->E: Strongly reduces interaction with
EXOC8. {ECO:0000269|PubMed:15920473}.
MUTAGEN 47 47 K->I: No effect on interaction with
EXOC8. {ECO:0000269|PubMed:15920473}.
MUTAGEN 48 48 A->W: Impaired cytokinesis, as shown by
increased number of binucleate cells. No
effect on cytokinesis; when associated
with V-23. Decreased interaction with
EXOC2 and EXOC8; when associated with V-
23. {ECO:0000269|PubMed:18756269}.
MUTAGEN 48 48 A->W: Strongly reduces interaction with
EXOC8. {ECO:0000269|PubMed:15920473}.
MUTAGEN 49 49 D->E: No effect on cytokinesis; when
associated with L-72.
{ECO:0000269|PubMed:18756269}.
MUTAGEN 49 49 D->N: No effect on cytokinesis. Impaired
cytokinesis, as shown by increased number
of binucleate cells; when associated with
L-72. {ECO:0000269|PubMed:18756269}.
MUTAGEN 50 50 S->W: Strongly reduces interaction with
EXOC8. {ECO:0000269|PubMed:15920473}.
MUTAGEN 52 52 R->A: Strongly reduces interaction with
EXOC8. {ECO:0000269|PubMed:15920473}.
MUTAGEN 52 52 R->W: No effect on interaction with
EXOC8. {ECO:0000269|PubMed:15920473}.
MUTAGEN 72 72 Q->L: Impaired cytokinesis, as shown by
increased number of binucleate cells.
Impaired cytokinesis; when associated
with N-49 or 1-M--S-11. No effect on
cytokinesis; when associated with E-49.
{ECO:0000269|PubMed:18756269}.
MUTAGEN 81 81 N->A: No effect on interaction with
EXOC8. {ECO:0000269|PubMed:15920473}.
MUTAGEN 81 81 N->R: Strongly reduces interaction with
EXOC8. {ECO:0000269|PubMed:15920473}.
MUTAGEN 203 203 C->S: Loss of geranylgeranylation and
membrane localization.
{ECO:0000269|PubMed:17875936}.
MUTAGEN 206 206 L->S: Converts geranyl-geranylation to
farnesylation. No effect on membrane
localization. Fails to deflect GGTI-
induced apoptosis of adherent cell
cultures, but rescues anchorage-
independent cell proliferation.
{ECO:0000269|PubMed:17875936}.
CONFLICT 1 2 MA -> MVDYL (in Ref. 2; AAA36542 and 3;
AAM12624). {ECO:0000305}.
STRAND 14 20 {ECO:0000244|PDB:2A9K}.
HELIX 27 36 {ECO:0000244|PDB:2A9K}.
STRAND 49 57 {ECO:0000244|PDB:2A9K}.
STRAND 60 68 {ECO:0000244|PDB:2A9K}.
HELIX 76 85 {ECO:0000244|PDB:2A9K}.
STRAND 87 94 {ECO:0000244|PDB:2A9K}.
HELIX 98 115 {ECO:0000244|PDB:2A9K}.
STRAND 122 127 {ECO:0000244|PDB:2A9K}.
HELIX 129 134 {ECO:0000244|PDB:2A9K}.
HELIX 139 148 {ECO:0000244|PDB:2A9K}.
STRAND 152 155 {ECO:0000244|PDB:2A9K}.
TURN 158 160 {ECO:0000244|PDB:2A9K}.
HELIX 164 180 {ECO:0000244|PDB:2A9K}.
SEQUENCE 206 AA; 23567 MW; 6974341EA18C1975 CRC64;
MAANKPKGQN SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE
EVQIDILDTA GQEDYAAIRD NYFRSGEGFL CVFSITEMES FAATADFREQ ILRVKEDENV
PFLLVGNKSD LEDKRQVSVE EAKNRAEQWN VNYVETSAKT RANVDKVFFD LMREIRARKM
EDSKEKNGKK KRKSLAKRIR ERCCIL


Related products :

Catalog number Product name Quantity
EIAAB33506 Mouse,Mus musculus,Rab34,Rab39,Rah,Rah1,Ras-related homolog,Ras-related protein Rab-34,Ras-related protein Rab-39,Ras-related protein Rah
18-003-43154 SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related - SMARCE1-related protein; HMG domain protein HMG20B; Structural DNA-binding protein BRAF35; BRCA2 0.05 mg Aff Pur
EIAAB30633 Homo sapiens,Human,Peroxin-5-related protein,Peroxisome biogenesis factor 5-like,PEX2-related protein,PEX5L,PEX5-like protein,PEX5R,PEX5-related protein,Pex5Rp,PXR2
EIAAB33504 Homo sapiens,Human,RAB34,RAB39,RAH,Ras-related protein Rab-34,Ras-related protein Rab-39,Ras-related protein Rah
EIAAB33569 Rab7,Rab7a,Ras-related protein BRL-RAS,Ras-related protein p23,Ras-related protein Rab-7a,Rat,Rattus norvegicus
EIAAB32961 Parathion hydrolase-related protein,Phosphotriesterase-related protein,Pter,Rat,Rattus norvegicus,Resiniferotoxin-binding phosphotriesterase-related protein,Rpr-1
EIAAB30632 Mouse,Mus musculus,Peroxin-5-related protein,Pex2,PEX2-related protein,Pex5l,PEX5-like protein,Pex5r,PEX5-related protein,Pex5Rp,Pxr2
20-272-191608 Tyrosinase Related Protein 75 - Mouse monoclonal [3F388] to Tyrosinase Related Protein 75; EC 1.14.18.-; DHICA oxidase; Tyrosinase-related protein 1; TRP-1; TRP1; TRP; Catalase B; Glycoprotein 75; Mel 0.05 ml
EIAAB38042 Frizzled-related protein 1b,FRP1B,FRP-1b,Homo sapiens,Human,SARP3,SARP-3,Secreted apoptosis-related protein 3,Secreted frizzled-related protein 5,SFRP5,sFRP-5
EIAAB46352 Homo sapiens,Human,PP10631,WAS_WASL-interacting protein family member 2,WASP-interacting protein-related protein,WICH,WIP- and CR16-homologous protein,WIPF2,WIP-related protein,WIRE
EIAAB12793 ELK3,ETS domain-containing protein Elk-3,ETS-related protein ERP,ETS-related protein NET,Homo sapiens,Human,NET,SAP2,SAP-2,Serum response factor accessory protein 2,SRF accessory protein 2
EIAAB08778 COX7A2L,COX7AR,COX7a-related protein,COX7RP,Cytochrome c oxidase subunit 7A-related protein, mitochondrial,Cytochrome c oxidase subunit VIIa-related protein,EB1,Homo sapiens,Human
EIAAB29234 Homo sapiens,Human,KIAA0772,ORP2,ORP-2,OSBPL2,OSBP-related protein 2,Oxysterol-binding protein-related protein 2
EIAAB29227 Homo sapiens,Human,ORP10,ORP-10,OSBP9,OSBPL10,OSBP-related protein 10,Oxysterol-binding protein-related protein 10
EIAAB29244 Homo sapiens,Human,ORP9,ORP-9,OSBP4,OSBPL9,OSBP-related protein 9,Oxysterol-binding protein-related protein 9
EIAAB29228 Homo sapiens,Human,ORP11,ORP-11,OSBP12,OSBPL11,OSBP-related protein 11,Oxysterol-binding protein-related protein 11
EIAAB33753 C21KG,G-22K,GTP-binding protein smg p21A,Homo sapiens,Human,KREV1,RAP1A,Ras-related protein Krev-1,Ras-related protein Rap-1A
EIAAB29236 Homo sapiens,Human,KIAA0704,ORP3,ORP-3,OSBP3,OSBPL3,OSBP-related protein 3,Oxysterol-binding protein-related protein 3
EIAAB29242 Homo sapiens,Human,KIAA1451,ORP8,ORP-8,OSBP10,OSBPL8,OSBP-related protein 8,Oxysterol-binding protein-related protein 8
EIAAB29231 Homo sapiens,Human,ORP1,ORP-1,OSBP8,OSBPL1,OSBPL1A,OSBPL1B,OSBP-related protein 1,Oxysterol-binding protein-related protein 1
18-003-42229 Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 Polyclonal 0.1 mg Protein A
15-288-22161 Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 Polyclonal 0.05 mg
15-288-22161 Hairy_enhancer-of-split related with YRPW motif 1 - Hairy and enhancer of split-related protein 1; HESR-1; Cardiovascular helix-loop-helix factor 2; HES-related repressor protein 2; HERP2 Polyclonal 0.1 mg
EIAAB29240 Homo sapiens,Human,ORP6,ORP-6,OSBPL6,OSBP-related protein 6,Oxysterol-binding protein-related protein 6
EIAAB29241 Homo sapiens,Human,ORP7,ORP-7,OSBPL7,OSBP-related protein 7,Oxysterol-binding protein-related protein 7


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur