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Protein

Ras-related protein Ral-A

Gene

RALA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Plays a role in the early stages of cytokinesis and is required to tether the exocyst to the cytokinetic furrow. The RALA-exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling. Key regulator of LPAR1 signaling and competes with ADRBK1 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells.3 Publications

Enzyme regulationi

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).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi24 – 296GTP2 Publications
Nucleotide bindingi40 – 467GTP2 Publications
Nucleotide bindingi127 – 1304GTP2 Publications

GO - Molecular functioni

  • ATPase binding Source: UniProtKB
  • Edg-2 lysophosphatidic acid receptor binding Source: UniProtKB
  • GDP binding Source: UniProtKB
  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB
  • myosin binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton reorganization Source: BHF-UCL
  • chemotaxis Source: ProtInc
  • cytokinesis Source: UniProtKB
  • exocytosis Source: UniProtKB-KW
  • membrane organization Source: Reactome
  • membrane raft localization Source: UniProtKB
  • neural tube closure Source: Ensembl
  • neurotrophin TRK receptor signaling pathway Source: Reactome
  • positive regulation of filopodium assembly Source: BHF-UCL
  • Ras protein signal transduction Source: Reactome
  • regulation of exocytosis Source: UniProtKB
  • signal transduction Source: ProtInc
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Exocytosis, Host-virus interaction

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_12065. p38MAPK events.
REACT_147867. Translocation of GLUT4 to the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Ral-A
Gene namesi
Name:RALA
Synonyms:RAL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:9839. RALA.

Subcellular locationi

  • Cell surface
  • Cell membrane; Lipid-anchor; Cytoplasmic side
  • Cleavage furrow
  • Midbody

  • Note: Prior to LPA treatment found predominantly at the cell surface and in the presence of LPA colocalizes with LPAR1 and LPAR2 in the endocytic vesicles. During early cytokinesis localizes at the cleavage furrow membrane. Colocalizes with EXOC2 at the early midbody ring and persists there till maturation of the midbody.

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • cleavage furrow Source: UniProtKB
  • cytoplasmic vesicle membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • midbody Source: UniProtKB-SubCell
  • myelin sheath Source: Ensembl
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471K → E: Strongly reduces interaction with EXOC8. 1 Publication
Mutagenesisi47 – 471K → I: No effect on interaction with EXOC8. 1 Publication
Mutagenesisi48 – 481A → W: Strongly reduces interaction with EXOC8. 1 Publication
Mutagenesisi50 – 501S → W: Strongly reduces interaction with EXOC8. 1 Publication
Mutagenesisi52 – 521R → A: Strongly reduces interaction with EXOC8. 1 Publication
Mutagenesisi52 – 521R → W: No effect on interaction with EXOC8. 1 Publication
Mutagenesisi81 – 811N → A: No effect on interaction with EXOC8. 1 Publication
Mutagenesisi81 – 811N → R: Strongly reduces interaction with EXOC8. 1 Publication
Mutagenesisi203 – 2031C → S: Loss of geranylgeranylation and membrane localization. 1 Publication
Mutagenesisi206 – 2061L → 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. 1 Publication

Organism-specific databases

PharmGKBiPA34197.

Polymorphism and mutation databases

BioMutaiRALA.
DMDMi131834.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203Ras-related protein Ral-APRO_0000082693Add
BLAST
Propeptidei204 – 2063Removed in mature formBy similarityPRO_0000281344

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031Cysteine methyl esterBy similarity
Lipidationi203 – 2031S-geranylgeranyl cysteine2 Publications

Post-translational modificationi

Prenylation is essential for membrane localization. The geranylgeranylated form and the farnesylated mutant does not undergo alternative prenylation in response to geranylgeranyltransferase I inhibitors (GGTIs) and farnesyltransferase I inhibitors (FTIs).2 Publications

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP11233.
PaxDbiP11233.
PRIDEiP11233.

PTM databases

PhosphoSiteiP11233.

Expressioni

Inductioni

Activated in an LPA-dependent manner by LPAR1 and in an LPA-independent manner by LPAR2.1 Publication

Gene expression databases

BgeeiP11233.
CleanExiHS_RALA.
ExpressionAtlasiP11233. baseline and differential.
GenevisibleiP11233. HS.

Organism-specific databases

HPAiHPA065232.

Interactioni

Subunit structurei

Interacts with RALBP1 via its effector domain. Interacts with EXOC8 and EXOC2. EXOC2 and EXOC8 have overlapping binding sites and compete for RALA binding. Interacts with Clostridium exoenzyme C3. Interacts with RALGPS1. Interacts with LPAR1 and LPAR2. Interacts with ADRBK1 in response to LPAR1 activation. RALA and ADRBK1 mutually inhibit each other's binding to LPAR1.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Exoc2O549212EBI-1036803,EBI-1036795From a different organism.
PPP2R1BP301546EBI-1036803,EBI-357094

Protein-protein interaction databases

BioGridi111834. 44 interactions.
IntActiP11233. 10 interactions.
MINTiMINT-238571.
STRINGi9606.ENSP00000005257.

Structurei

Secondary structure

1
206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 207Combined sources
Helixi27 – 3610Combined sources
Beta strandi49 – 579Combined sources
Beta strandi60 – 689Combined sources
Helixi76 – 8510Combined sources
Beta strandi87 – 948Combined sources
Helixi98 – 11518Combined sources
Beta strandi122 – 1276Combined sources
Helixi129 – 1346Combined sources
Helixi139 – 14810Combined sources
Beta strandi152 – 1554Combined sources
Turni158 – 1603Combined sources
Helixi164 – 18017Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UADX-ray2.10A/B9-183[»]
1ZC3X-ray2.00A/C9-183[»]
1ZC4X-ray2.50A/C9-183[»]
2A78X-ray1.81A9-183[»]
2A9KX-ray1.73A9-183[»]
2BOVX-ray2.66A1-206[»]
DisProtiDP00581.
ProteinModelPortaliP11233.
SMRiP11233. Positions 13-182.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11233.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi43 – 519Effector region

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00780000121849.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP11233.
KOiK07834.
OMAiFAATTEF.
OrthoDBiEOG7QVM41.
PhylomeDBiP11233.
TreeFamiTF312796.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR028412. Ral.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PTHR24070:SF174. PTHR24070:SF174. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11233-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAANKPKGQN SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS
60 70 80 90 100
YRKKVVLDGE EVQIDILDTA GQEDYAAIRD NYFRSGEGFL CVFSITEMES
110 120 130 140 150
FAATADFREQ ILRVKEDENV PFLLVGNKSD LEDKRQVSVE EAKNRAEQWN
160 170 180 190 200
VNYVETSAKT RANVDKVFFD LMREIRARKM EDSKEKNGKK KRKSLAKRIR

ERCCIL
Length:206
Mass (Da):23,567
Last modified:July 1, 1989 - v1
Checksum:i6974341EA18C1975
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 22MA → MVDYL (PubMed:2550440).Curated
Sequence conflicti1 – 22MA → MVDYL (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15014 mRNA. Translation: CAA33118.1.
M29893 mRNA. Translation: AAA36542.1.
AF493910 mRNA. Translation: AAM12624.1.
AC004837 Genomic DNA. No translation available.
CH236951 Genomic DNA. Translation: EAL23994.1.
CH471073 Genomic DNA. Translation: EAW94123.1.
BC039858 mRNA. Translation: AAH39858.1.
CCDSiCCDS5460.1.
PIRiS04596. TVHUAA.
RefSeqiNP_005393.2. NM_005402.3.
XP_006715825.1. XM_006715762.2.
XP_011513768.1. XM_011515466.1.
UniGeneiHs.6906.

Genome annotation databases

EnsembliENST00000005257; ENSP00000005257; ENSG00000006451.
GeneIDi5898.
KEGGihsa:5898.
UCSCiuc003thd.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15014 mRNA. Translation: CAA33118.1.
M29893 mRNA. Translation: AAA36542.1.
AF493910 mRNA. Translation: AAM12624.1.
AC004837 Genomic DNA. No translation available.
CH236951 Genomic DNA. Translation: EAL23994.1.
CH471073 Genomic DNA. Translation: EAW94123.1.
BC039858 mRNA. Translation: AAH39858.1.
CCDSiCCDS5460.1.
PIRiS04596. TVHUAA.
RefSeqiNP_005393.2. NM_005402.3.
XP_006715825.1. XM_006715762.2.
XP_011513768.1. XM_011515466.1.
UniGeneiHs.6906.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UADX-ray2.10A/B9-183[»]
1ZC3X-ray2.00A/C9-183[»]
1ZC4X-ray2.50A/C9-183[»]
2A78X-ray1.81A9-183[»]
2A9KX-ray1.73A9-183[»]
2BOVX-ray2.66A1-206[»]
DisProtiDP00581.
ProteinModelPortaliP11233.
SMRiP11233. Positions 13-182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111834. 44 interactions.
IntActiP11233. 10 interactions.
MINTiMINT-238571.
STRINGi9606.ENSP00000005257.

PTM databases

PhosphoSiteiP11233.

Polymorphism and mutation databases

BioMutaiRALA.
DMDMi131834.

Proteomic databases

MaxQBiP11233.
PaxDbiP11233.
PRIDEiP11233.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000005257; ENSP00000005257; ENSG00000006451.
GeneIDi5898.
KEGGihsa:5898.
UCSCiuc003thd.3. human.

Organism-specific databases

CTDi5898.
GeneCardsiGC07P039663.
HGNCiHGNC:9839. RALA.
HPAiHPA065232.
MIMi179550. gene.
neXtProtiNX_P11233.
PharmGKBiPA34197.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00780000121849.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP11233.
KOiK07834.
OMAiFAATTEF.
OrthoDBiEOG7QVM41.
PhylomeDBiP11233.
TreeFamiTF312796.

Enzyme and pathway databases

ReactomeiREACT_12065. p38MAPK events.
REACT_147867. Translocation of GLUT4 to the plasma membrane.

Miscellaneous databases

ChiTaRSiRALA. human.
EvolutionaryTraceiP11233.
GeneWikiiRALA.
GenomeRNAii5898.
NextBioi22942.
PROiP11233.
SOURCEiSearch...

Gene expression databases

BgeeiP11233.
CleanExiHS_RALA.
ExpressionAtlasiP11233. baseline and differential.
GenevisibleiP11233. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR028412. Ral.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PTHR24070:SF174. PTHR24070:SF174. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Coding sequences of human ralA and ralB cDNAs."
    Chardin P., Tavitian A.
    Nucleic Acids Res. 17:4380-4380(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Identification of the ral and rac1 gene products, low molecular mass GTP-binding proteins from human platelets."
    Polakis P.G., Weber R.F., Nevins B., Didsbury J.R., Evans T., Snyderman R.
    J. Biol. Chem. 264:16383-16389(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Platelet.
  3. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  4. "Human chromosome 7: DNA sequence and biology."
    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.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The DNA sequence of human chromosome 7."
    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.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye.
  8. "Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA."
    Kinsella B.T., Erdman R.A., Maltese W.A.
    J. Biol. Chem. 266:9786-9794(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-203.
  9. "Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity."
    Jullien-Flores V., Dorseuil O., Romero F., Letourneur F., Saragosti S., Berger R., Tavitian A., Gacon G., Camonis J.H.
    J. Biol. Chem. 270:22473-22477(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RALBP1.
  10. "Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral."
    Rebhun J.F., Chen H., Quilliam L.A.
    J. Biol. Chem. 275:13406-13410(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RALGPS1.
  11. "Ral GTPases regulate exocyst assembly through dual subunit interactions."
    Moskalenko S., Tong C., Rosse C., Mirey G., Formstecher E., Daviet L., Camonis J., White M.A.
    J. Biol. Chem. 278:51743-51748(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EXOC8.
  12. "Geranylgeranyltransferase I inhibitors target RalB to inhibit anchorage-dependent growth and induce apoptosis and RalA to inhibit anchorage-independent growth."
    Falsetti S.C., Wang D.A., Peng H., Carrico D., Cox A.D., Der C.J., Hamilton A.D., Sebti S.M.
    Mol. Cell. Biol. 27:8003-8014(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-203, MUTAGENESIS OF CYS-203 AND LEU-206.
  13. "Distinct roles of RalA and RalB in the progression of cytokinesis are supported by distinct RalGEFs."
    Cascone I., Selimoglu R., Ozdemir C., Del Nery E., Yeaman C., White M., Camonis J.
    EMBO J. 27:2375-2387(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. "Dual regulation of lysophosphatidic acid (LPA1) receptor signalling by Ral and GRK."
    Aziziyeh A.I., Li T.T., Pape C., Pampillo M., Chidiac P., Possmayer F., Babwah A.V., Bhattacharya M.
    Cell. Signal. 21:1207-1217(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH LPAR1; LPAR2 AND ADRBK1.
  15. "RalA-exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling."
    Balasubramanian N., Meier J.A., Scott D.W., Norambuena A., White M.A., Schwartz M.A.
    Curr. Biol. 20:75-79(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase."
    Jin R., Junutula J.R., Matern H.T., Ervin K.E., Scheller R.H., Brunger A.T.
    EMBO J. 24:2064-2074(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 9-183 IN COMPLEX WITH EXOC8 AND GTP ANALOG, INTERACTION WITH EXOC2, MUTAGENESIS OF LYS-47; ALA-48; SER-50; ARG-52 AND ASN-81.
  18. "Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme."
    Pautsch A., Vogelsgesang M., Traenkle J., Herrmann C., Aktories K.
    EMBO J. 24:3670-3680(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 9-183 IN COMPLEX WITH GTP AND CLOSTRIDIUM EXOENZYME C3.
  19. "Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase."
    Holbourn K.P., Sutton J.M., Evans H.R., Shone C.C., Acharya K.R.
    Proc. Natl. Acad. Sci. U.S.A. 102:5357-5362(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) IN COMPLEX WITH GTP AND CLOSTRIDIUM EXOENZYME C3.

Entry informationi

Entry nameiRALA_HUMAN
AccessioniPrimary (citable) accession number: P11233
Secondary accession number(s): A4D1W3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 22, 2015
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.