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P11233

- RALA_HUMAN

UniProt

P11233 - RALA_HUMAN

Protein

Ras-related protein Ral-A

Gene

RALA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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

    1. Edg-2 lysophosphatidic acid receptor binding Source: UniProtKB
    2. GTPase activity Source: InterPro
    3. GTP binding Source: ProtInc
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: BHF-UCL
    2. chemotaxis Source: ProtInc
    3. cytokinesis Source: UniProtKB
    4. exocytosis Source: UniProtKB-KW
    5. membrane organization Source: Reactome
    6. membrane raft localization Source: UniProtKB
    7. neurotrophin TRK receptor signaling pathway Source: Reactome
    8. positive regulation of filopodium assembly Source: BHF-UCL
    9. Ras protein signal transduction Source: Reactome
    10. regulation of exocytosis Source: UniProtKB
    11. signal transduction Source: ProtInc
    12. viral process Source: UniProtKB-KW

    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: 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

    1. cell surface Source: UniProtKB
    2. cleavage furrow Source: UniProtKB
    3. cytoplasmic vesicle membrane Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. midbody Source: UniProtKB-SubCell
    6. plasma membrane Source: UniProtKB

    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.

    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

    ArrayExpressiP11233.
    BgeeiP11233.
    CleanExiHS_RALA.
    GenevestigatoriP11233.

    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. 43 interactions.
    IntActiP11233. 9 interactions.
    MINTiMINT-238571.
    STRINGi9606.ENSP00000005257.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000233973.
    HOVERGENiHBG009351.
    InParanoidiP11233.
    KOiK07834.
    OMAiDRCKKRR.
    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

    MAANKPKGQN SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS    50
    YRKKVVLDGE EVQIDILDTA GQEDYAAIRD NYFRSGEGFL CVFSITEMES 100
    FAATADFREQ ILRVKEDENV PFLLVGNKSD LEDKRQVSVE EAKNRAEQWN 150
    VNYVETSAKT RANVDKVFFD LMREIRARKM EDSKEKNGKK KRKSLAKRIR 200
    ERCCIL 206
    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 → MVDYL1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_006715762.1.
    XP_006715826.1. XM_006715763.1.
    UniGeneiHs.6906.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi131834.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS5460.1.
    PIRi S04596. TVHUAA.
    RefSeqi NP_005393.2. NM_005402.3.
    XP_006715825.1. XM_006715762.1.
    XP_006715826.1. XM_006715763.1.
    UniGenei Hs.6906.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UAD X-ray 2.10 A/B 9-183 [» ]
    1ZC3 X-ray 2.00 A/C 9-183 [» ]
    1ZC4 X-ray 2.50 A/C 9-183 [» ]
    2A78 X-ray 1.81 A 9-183 [» ]
    2A9K X-ray 1.73 A 9-183 [» ]
    2BOV X-ray 2.66 A 1-206 [» ]
    DisProti DP00581.
    ProteinModelPortali P11233.
    SMRi P11233. Positions 13-182.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111834. 43 interactions.
    IntActi P11233. 9 interactions.
    MINTi MINT-238571.
    STRINGi 9606.ENSP00000005257.

    PTM databases

    PhosphoSitei P11233.

    Polymorphism databases

    DMDMi 131834.

    Proteomic databases

    MaxQBi P11233.
    PaxDbi P11233.
    PRIDEi P11233.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000005257 ; ENSP00000005257 ; ENSG00000006451 .
    GeneIDi 5898.
    KEGGi hsa:5898.
    UCSCi uc003thd.3. human.

    Organism-specific databases

    CTDi 5898.
    GeneCardsi GC07P039663.
    HGNCi HGNC:9839. RALA.
    MIMi 179550. gene.
    neXtProti NX_P11233.
    PharmGKBi PA34197.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233973.
    HOVERGENi HBG009351.
    InParanoidi P11233.
    KOi K07834.
    OMAi DRCKKRR.
    OrthoDBi EOG7QVM41.
    PhylomeDBi P11233.
    TreeFami TF312796.

    Enzyme and pathway databases

    Reactomei REACT_12065. p38MAPK events.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.

    Miscellaneous databases

    ChiTaRSi Rala. human.
    EvolutionaryTracei P11233.
    GeneWikii RALA.
    GenomeRNAii 5898.
    NextBioi 22942.
    PROi P11233.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11233.
    Bgeei P11233.
    CleanExi HS_RALA.
    Genevestigatori P11233.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR028412. Ral.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR020849. Small_GTPase_Ras.
    [Graphical view ]
    PANTHERi PTHR24070. PTHR24070. 1 hit.
    PTHR24070:SF174. PTHR24070:SF174. 1 hit.
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00173. RAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51421. RAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 157 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