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UniProtKB/Swiss-Prot entry P11233


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RALA_HUMAN
Primary accession number P11233
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 1, 1989 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 101)
Name and origin of the protein
Protein name Ras-related protein Ral-A [Precursor]
Synonyms None
Gene name
Name: RALA
Synonyms: RAL
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/17.11.4380; PubMed=2662142 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
ISOPRENYLATION AT CYS-203.
PubMed=1903399 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
INTERACTION WITH RALBP1.
DOI=10.1074/jbc.270.38.22473; PubMed=7673236 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
INTERACTION WITH RALGPS1.
DOI=10.1074/jbc.C000085200; PubMed=10747847 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
INTERACTION WITH EXOC8.
DOI=10.1074/jbc.M308702200; PubMed=14525976 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[11]
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.
DOI=10.1038/sj.emboj.7600699; PubMed=15920473 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 9-183 IN COMPLEX WITH GTP AND CLOSTRIDIUM EXOENZYME C3.
DOI=10.1038/sj.emboj.7600813; PubMed=16177825 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) IN COMPLEX WITH GTP AND CLOSTRIDIUM EXOENZYME C3.
DOI=10.1073/pnas.0501525102; PubMed=15809419 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X15014; CAA33118.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29893; AAA36542.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF493910; AAM12624.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004837; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC039858; AAH39858.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00217519; -.
PIR S04596; TVHUAA.
RefSeq NP_005393.2; -.
UniGene Hs.6906
3D structure databases
PDB
1UAD; X-ray; 2.10 A; A/B=9-183.[ExPASy / RCSB / EBI]
1ZC3; X-ray; 2.00 A; A/C=9-183.[ExPASy / RCSB / EBI]
1ZC4; X-ray; 2.50 A; A/C=9-183.[ExPASy / RCSB / EBI]
2A78; X-ray; 1.81 A; A=9-183.[ExPASy / RCSB / EBI]
2A9K; X-ray; 1.73 A; A=9-183.[ExPASy / RCSB / EBI]
2BOV; X-ray; 2.66 A; A=1-206.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1UAD; -.
1ZC3; -.
1ZC4; -.
2A78; -.
2A9K; -.
2BOV; -.
ModBase P11233.
Protein-protein interaction databases
IntAct P11233; 3.
PTM databases
PhosphoSite P11233; -.
Enzyme and pathway databases
Pathway_Interaction_DB arf6_traffickingpathway; Arf6 trafficking events.
foxopathway; FoxO family signaling.
p38alphabetapathway; Regulation of p38-alpha and p38-beta.
Reactome REACT_11061; Signalling by NGF.
Organism-specific databases
GeneCards GC07P039630; -.
H-InvDB HIX0006618; -.
HGNC HGNC:9839; RALA.
GenAtlas RALA.
MIM 179550; gene. [NCBI / EBI]
PharmGKB PA34197; -.
Gene expression databases
ArrayExpress P11233; -.
Bgee P11233; -.
CleanEx HS_RALA; -.
GermOnline ENSG00000006451; Homo sapiens.
Ontologies
GO
GO:0005622; Cellular component: intracellular (inferred from electronic annotation from InterPro).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005525; Molecular function: GTP binding (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0031532; Biological process: actin cytoskeleton reorganization (inferred from direct assay from UniProtKB).
GO:0006935; Biological process: chemotaxis (traceable author statement from ProtInc).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0051491; Biological process: positive regulation of filopodium assembly (inferred from direct assay from UniProtKB).
GO:0007265; Biological process: Ras protein signal transduction (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR003577; GTPase_Ras.
IPR013753; Ras.
IPR001806; Ras_GTPase.
IPR015591; Ras_Ral_related.
IPR005225; Small_GTP_bd.
Graphical view of domain structure.
PANTHER PTHR11708:SF124; Ras_Ral_related; 1.
Pfam PF00071; Ras; 1.
Pfam graphical view of domain structure.
PRINTS PR00449; RASTRNSFRMNG.
SMART SM00173; RAS; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00231; small_GTP; 1.
PROSITE PS51421; RAS; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P11233; -.
Genome annotation databases
Ensembl ENSG00000006451; Homo sapiens. [Contig view]
GeneID 5898; -.
KEGG hsa:5898; -.
Phylogenomic databases
HOGENOM P11233; -.
HOVERGEN P11233; -.
OMA P11233; AKPKGQN.
Other
NextBio 22942; -.
SOURCE RALA; Homo sapiens.
ProtoNet P11233.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell membrane; GTP-binding; Host-virus interaction; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   203  203     Ras-related protein Ral-A. PRO_0000082693
PROPEP   204   206  3     Removed in mature form (By similarity). PRO_0000281344
NP_BIND   24    29  6     GTP. 
NP_BIND   40    46  7     GTP. 
NP_BIND   127   130  4     GTP. 
MOTIF   43    51  9     Effector region (By similarity). 
MOD_RES   203   203        Cysteine methyl ester (Probable). 
LIPID   203   203        S-geranylgeranyl cysteine. 
MUTAGEN   47    47        K->E: Strongly reduces interaction with EXOC8. 
MUTAGEN   47    47        K->I: No effect on interaction with EXOC8. 
MUTAGEN   48    48        A->W: Strongly reduces interaction with EXOC8. 
MUTAGEN   50    50        S->W: Strongly reduces interaction with EXOC8. 
MUTAGEN   52    52        R->A: Strongly reduces interaction with EXOC8. 
MUTAGEN   52    52        R->W: No effect on interaction with EXOC8. 
MUTAGEN   81    81        N->A: No effect on interaction with EXOC8. 
MUTAGEN   81    81        N->R: Strongly reduces interaction with EXOC8. 
CONFLICT   1     2        MA -> MVDYL (in Ref. 2 and 3). 
STRAND   14    20  7      
HELIX   27    36  10      
STRAND   47    57  11      
STRAND   60    69  10      
HELIX   77    85  9      
STRAND   87    94  8      
HELIX   98   115  18      
STRAND   120   127  8      
HELIX   132   134  3      
HELIX   139   149  11      
STRAND   152   155  4      
TURN   158   160  3      
HELIX   164   181  18      
Sequence information
Length: 206 AA [This is the length of the unprocessed precursor] Molecular weight: 23567 Da [This is the MW of the unprocessed precursor] CRC64: 6974341EA18C1975 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAANKPKGQN SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE 

        70         80         90        100        110        120 
EVQIDILDTA GQEDYAAIRD NYFRSGEGFL CVFSITEMES FAATADFREQ ILRVKEDENV 

       130        140        150        160        170        180 
PFLLVGNKSD LEDKRQVSVE EAKNRAEQWN VNYVETSAKT RANVDKVFFD LMREIRARKM 

       190        200 
EDSKEKNGKK KRKSLAKRIR ERCCIL 

P11233 in FASTA format

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