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Protein Page:
RalA (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RalA 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. 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. Activated in an LPA-dependent manner by LPAR1 and in an LPA-independent manner by LPAR2. Alternate 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). Belongs to the small GTPase superfamily. Ras family. Note: This description may include information from UniProtKB.
Protein type: G protein, monomeric; Motility/polarity/chemotaxis; G protein, monomeric, Ras; G protein
Cellular Component: cytoplasmic vesicle membrane; cell surface; endocytic vesicle; plasma membrane; midbody; cleavage furrow
Molecular Function: GTPase activity; protein binding; GTP binding; Edg-2 lysophosphatidic acid receptor binding
Biological Process: regulation of exocytosis; positive regulation of filopodium formation; exocytosis; lipid raft localization; nerve growth factor receptor signaling pathway; viral reproduction; GTP catabolic process; Ras protein signal transduction; actin cytoskeleton reorganization; cytokinesis; chemotaxis; signal transduction
Reference #:  P11233 (UniProtKB)
Alt. Names/Synonyms: MGC48949; RAL; RALA; Ras family small GTP binding protein RALA; ras related v-ral simian leukemia viral oncogene homolog A; RAS-like protein A; Ras-related protein Ral-A; v-ral simian leukemia viral oncogene homolog A (ras related)
Gene Symbols: RALA
Molecular weight: 23,567 Da
Basal Isoelectric point: 6.66  Predict pI for various phosphorylation states
CST Pathways:  Adherens Junction Dynamics
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RalA

Protein Structure Not Found.


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Sites Implicated In
cell growth, altered: S194‑p
cytoskeletal reorganization: S194‑p
intracellular localization: S194‑p
molecular association, regulation: S194‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K7 _MAANKPKGQNsLAL
0 1 S11-p NKPKGQNsLALHKVI
0 6 Y43-p YDEFVEDyEPTKADS
0 1 Y51-p EPTKADSyRKKVVLD
0 10 Y75-p DTAGQEDyAAIRDNY
0 1 K134 NKSDLEDKRQVSVEE
0 2 K143-ub QVSVEEAkNRAEQWN
0 1 Y153-p AEQWNVNyVETSAkT
0 5 K159-ub NyVETSAkTRANVDK
1 0 S183-p RARKMEDsKEKNGKK
0 1 K184 ARKMEDsKEKNGKKK
0 1 K189 DsKEKNGKKKRKsLA
3 1 S194-p NGKKKRKsLAKRIRE
  mouse

 
K7-ub _MAANKPkGQNsLAL
S11-p NKPkGQNsLALHKVI
Y43 YDEFVEDYEPTKADS
Y51 EPTKADSYRKKVVLD
Y75 DTAGQEDYAAIRDNY
K134-ub NKSDLEDkRQVSVEE
K143-ub QVSVEEAkNRADQWN
Y153 ADQWNVNYVETSAkT
K159-ub NYVETSAkTRANVDK
S183 RARKMEDSkEKNGkK
K184-ac ARKMEDSkEKNGkKK
K189-ac DSkEKNGkKKRKSLA
S194 NGkKKRKSLAKRIRE
  rat

 
K7 _MAANKPKGQNSLAL
S11 NKPKGQNSLALHKVI
Y43 YDEFVEDYEPTKADS
Y51 EPTKADSYRKKVVLD
Y75 DTAGQEDYAAIRDNY
K134 NKSDLEDKRQVSVEE
K143 QVSVEEAKNRADQWN
Y153 ADQWNVNYVETSAKT
K159 NYVETSAKTRANVDK
S183 RARKMEDSKEKNGKK
K184 ARKMEDSKEKNGKKK
K189 DSKEKNGKKKRKSLA
S194 NGKKKRKSLAKRIRE
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