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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. 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).3 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi24 – 29GTP2 Publications6
Nucleotide bindingi40 – 46GTP2 Publications7
Nucleotide bindingi127 – 130GTP2 Publications4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell cycle, Cell division, Exocytosis
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-171007 p38MAPK events
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P11233

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ras-related protein Ral-A
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RALA
Synonyms:RAL
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000006451.7

Human Gene Nomenclature Database

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HGNCi
HGNC:9839 RALA

Online Mendelian Inheritance in Man (OMIM)

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MIMi
179550 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P11233

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1 – 11Missing : Impaired cytokinesis, as shown by increased number of binucleate cells. Impaired cytokinesis; when associated with L-72. 1 PublicationAdd BLAST11
Mutagenesisi23G → 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. 1 Publication1
Mutagenesisi38E → 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. 1 Publication1
Mutagenesisi47K → E: Strongly reduces interaction with EXOC8. 1 Publication1
Mutagenesisi47K → I: No effect on interaction with EXOC8. 1 Publication1
Mutagenesisi48A → 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. 1 Publication1
Mutagenesisi48A → W: Strongly reduces interaction with EXOC8. 1 Publication1
Mutagenesisi49D → E: No effect on cytokinesis; when associated with L-72. 1 Publication1
Mutagenesisi49D → N: No effect on cytokinesis. Impaired cytokinesis, as shown by increased number of binucleate cells; when associated with L-72. 1 Publication1
Mutagenesisi50S → W: Strongly reduces interaction with EXOC8. 1 Publication1
Mutagenesisi52R → A: Strongly reduces interaction with EXOC8. 1 Publication1
Mutagenesisi52R → W: No effect on interaction with EXOC8. 1 Publication1
Mutagenesisi72Q → 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. 1 Publication1
Mutagenesisi81N → A: No effect on interaction with EXOC8. 1 Publication1
Mutagenesisi81N → R: Strongly reduces interaction with EXOC8. 1 Publication1
Mutagenesisi203C → S: Loss of geranylgeranylation and membrane localization. 1 Publication1
Mutagenesisi206L → 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 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
5898

Open Targets

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OpenTargetsi
ENSG00000006451

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34197

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3879855

Drug and drug target database

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DrugBanki
DB04315 Guanosine-5'-Diphosphate

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RALA

Domain mapping of disease mutations (DMDM)

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DMDMi
131834

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000826931 – 203Ras-related protein Ral-AAdd BLAST203
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000281344204 – 206Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei203Cysteine methyl esterBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi203S-geranylgeranyl cysteine2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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).2 Publications

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P11233

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P11233

MaxQB - The MaxQuant DataBase

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MaxQBi
P11233

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P11233

PeptideAtlas

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PeptideAtlasi
P11233

PRoteomics IDEntifications database

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PRIDEi
P11233

ProteomicsDB human proteome resource

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ProteomicsDBi
52726

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P11233

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P11233

SwissPalm database of S-palmitoylation events

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SwissPalmi
P11233

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000006451 Expressed in 228 organ(s), highest expression level in forebrain

CleanEx database of gene expression profiles

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CleanExi
HS_RALA

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P11233 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P11233 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA065232

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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).By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111834, 71 interactors

Protein interaction database and analysis system

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IntActi
P11233, 34 interactors

Molecular INTeraction database

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MINTi
P11233

STRING: functional protein association networks

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STRINGi
9606.ENSP00000005257

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1206
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]

Database of protein disorder

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DisProti
DP00581

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P11233

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P11233

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P11233

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi43 – 51Effector region9

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0395 Eukaryota
COG1100 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155142

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233973

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG009351

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P11233

KEGG Orthology (KO)

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KOi
K07834

Identification of Orthologs from Complete Genome Data

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OMAi
QSRAQQW

Database of Orthologous Groups

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OrthoDBi
1259506at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P11233

TreeFam database of animal gene trees

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TreeFami
TF312796

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR027417 P-loop_NTPase
IPR028412 Ral
IPR005225 Small_GTP-bd_dom
IPR001806 Small_GTPase
IPR020849 Small_GTPase_Ras-type

The PANTHER Classification System

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PANTHERi
PTHR24070 PTHR24070, 1 hit
PTHR24070:SF174 PTHR24070:SF174, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00071 Ras, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00231 small_GTP, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51421 RAS, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6974341EA18C1975
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7C3P7H7C3P7_HUMAN
Ras-related protein Ral-A
RALA
164Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JPE8C9JPE8_HUMAN
Ras-related protein Ral-A
RALA
101Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti1 – 2MA → MVDYL in AAA36542 (PubMed:2550440).Curated2
Sequence conflicti1 – 2MA → MVDYL in AAM12624 (Ref. 3) Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS5460.1

Protein sequence database of the Protein Information Resource

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PIRi
S04596 TVHUAA

NCBI Reference Sequences

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RefSeqi
NP_005393.2, NM_005402.3
XP_006715825.1, XM_006715762.2
XP_011513768.1, XM_011515466.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.6906

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000005257; ENSP00000005257; ENSG00000006451

Database of genes from NCBI RefSeq genomes

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GeneIDi
5898

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5898

UCSC genome browser

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UCSCi
uc003thd.4 human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111834, 71 interactors
IntActiP11233, 34 interactors
MINTiP11233
STRINGi9606.ENSP00000005257

Chemistry databases

ChEMBLiCHEMBL3879855
DrugBankiDB04315 Guanosine-5'-Diphosphate

PTM databases

iPTMnetiP11233
PhosphoSitePlusiP11233
SwissPalmiP11233

Polymorphism and mutation databases

BioMutaiRALA
DMDMi131834

Proteomic databases

EPDiP11233
jPOSTiP11233
MaxQBiP11233
PaxDbiP11233
PeptideAtlasiP11233
PRIDEiP11233
ProteomicsDBi52726

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000005257; ENSP00000005257; ENSG00000006451
GeneIDi5898
KEGGihsa:5898
UCSCiuc003thd.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5898
DisGeNETi5898
EuPathDBiHostDB:ENSG00000006451.7

GeneCards: human genes, protein and diseases

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GeneCardsi
RALA
HGNCiHGNC:9839 RALA
HPAiHPA065232
MIMi179550 gene
neXtProtiNX_P11233
OpenTargetsiENSG00000006451
PharmGKBiPA34197

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0395 Eukaryota
COG1100 LUCA
GeneTreeiENSGT00940000155142
HOGENOMiHOG000233973
HOVERGENiHBG009351
InParanoidiP11233
KOiK07834
OMAiQSRAQQW
OrthoDBi1259506at2759
PhylomeDBiP11233
TreeFamiTF312796

Enzyme and pathway databases

ReactomeiR-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-171007 p38MAPK events
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation
SIGNORiP11233

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
RALA human
EvolutionaryTraceiP11233

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
RALA

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
5898

Protein Ontology

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PROi
PR:P11233

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000006451 Expressed in 228 organ(s), highest expression level in forebrain
CleanExiHS_RALA
ExpressionAtlasiP11233 baseline and differential
GenevisibleiP11233 HS

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR028412 Ral
IPR005225 Small_GTP-bd_dom
IPR001806 Small_GTPase
IPR020849 Small_GTPase_Ras-type
PANTHERiPTHR24070 PTHR24070, 1 hit
PTHR24070:SF174 PTHR24070:SF174, 1 hit
PfamiView protein in Pfam
PF00071 Ras, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00231 small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS51421 RAS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRALA_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P11233
Secondary accession number(s): A4D1W3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 16, 2019
This is version 201 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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