Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Ras-related protein Ral-A  

UniProtKB / Swiss-Prot ID :  RALA_HUMAN

Gene Name (Synonyms) : 
RALA, RAL  

Species :  Homo sapiens (Human). 

Subcellular Localization :  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 co-localizes with LPAR1 and LPAR2 in the endocytic vesicles. During earl 

Protein Function :  Multifuntional 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. 

Protein Sequence MAANKPKGQNSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTA...
Predicted Secondary Structure CCCCCCCCCCCCCEEEEEEEECCCCCHHHHHHHHHCCCCCCCCCCCCEEEEEEEEEECCEEEEEEEEECC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
11PhosphoserineKGQNSLALH
CCCCCCCEE
13.71HPRD
Link
43PhosphotyrosineFVEDYEPTK
CCCCCCCCC
15.42Phosphositeplus
Link
159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ETSAKTRAN
EEECCCCCC
38.01Phosphositeplus
Link
183DePhosphoserineKMEDSKEKN
HCCCCCCCC
29.43HPRD
Link-
183PhosphoserineKMEDSKEKN
HCCCCCCCC
29.43HPRD
Link-
183PhosphoserineKMEDSKEKN
HCCCCCCCC
29.43Phosphositeplus
Link-
194DePhosphoserineKKRKSLAKR
CCCCCCCCH
37.28HPRD
Link-
194PhosphoserineKKRKSLAKR
CCCCCCCCH
37.28Phosphositeplus
Link-
203Cysteine methyl ester.IRERCCIL
HCCCCCCC
1.13UniProtKB
Link-
203S-geranylgeranyl cysteine.IRERCCIL
HCCCCCCC
1.13UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
2AAB_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
EBI-1266564
EBI-1266554
EBI-1
intact17540176
17540176
17540176
17540176
17540176
17540176
ARF1_HUMANin vivoHPRD:01549HPRD12509462
9688545
RBP1_HUMANENSP00000005257STRING
DBPA_HUMANENSP00000005257STRING
EXOC2_HUMANENSP00000005257STRING
CALM_HUMANENSP00000005257STRING
RASA1_HUMANENSP00000005257STRING
EXC6B_HUMANENSP00000005257STRING
AMRP_HUMANENSP00000005257STRING
AMRP_HUMANENSP00000005257STRING
AMRP_HUMANENSP00000005257STRING
ABCE1_HUMANENSP00000005257STRING
ARF6_HUMANENSP00000005257STRING
PLD1_HUMANENSP00000005257STRING
REPS2_HUMANENSP00000005257STRING
EXOC8_HUMANENSP00000005257STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Prenylation
ReferencePubMed
"Geranylgeranyltransferase I inhibitors target RalB to inhibitanchorage-dependent growth and induce apoptosis and RalA to inhibitanchorage-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).
Cited for: SUBCELLULAR LOCATION, ISOPRENYLATION, ISOPRENYLATION AT CYS-203, ANDMUTAGENESIS OF CYS-203 AND LEU-206.
"Carboxyl-terminal isoprenylation of ras-related GTP-binding proteinsencoded by rac1, rac2, and ralA.";
Kinsella B.T., Erdman R.A., Maltese W.A.;
J. Biol. Chem. 266:9786-9794(1991).
Cited for: ISOPRENYLATION AT CYS-203.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures