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P11233

- RALA_HUMAN

UniProt

P11233 - RALA_HUMAN

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Protein
Ras-related protein Ral-A
Gene
RALA, RAL
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 296GTP
Nucleotide bindingi40 – 467GTP
Nucleotide bindingi127 – 1304GTP

GO - Molecular functioni

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

GO - Biological processi

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

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
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203Ras-related protein Ral-A
PRO_0000082693Add
BLAST
Propeptidei204 – 2063Removed in mature form By similarity
PRO_0000281344

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031Cysteine methyl ester By 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).

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 LPAR1.5 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. 8 interactions.
MINTiMINT-238571.
STRINGi9606.ENSP00000005257.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP11233.

Family & Domainsi

Motif

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

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 22MA → MVDYL1 Publication
Sequence conflicti1 – 22MA → MVDYL1 Publication

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. 8 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

« 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: September 3, 2014
This is version 156 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

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