Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
RalB (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
RalB 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. Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells. Plays a role in the late stages of cytokinesis and is required for the abscission of the bridge joining the sister cells emerging from mitosis. Required for suppression of apoptosis. Interacts with EXOC2 and EXOC8. Interacts with RALBP1 via its effector domain. 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, Ras; G protein, monomeric; G protein
Cellular Component: plasma membrane; midbody
Molecular Function: GTPase activity; protein binding; GTP binding
Biological Process: regulation of exocyst localization; nerve growth factor receptor signaling pathway; GTP catabolic process; apoptosis; regulation of exocyst assembly; Ras protein signal transduction; cytokinesis; signal transduction
Reference #:  P11234 (UniProtKB)
Alt. Names/Synonyms: GTP binding protein; GTP binding protein); RALB; RAS-like protein B; Ras-related protein Ral-B; v-ral simian leukemia viral oncogene homolog B (ras related
Gene Symbols: RALB
Molecular weight: 23,409 Da
Basal Isoelectric point: 6.24  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RalB

Protein Structure Not Found.


STRING  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
carcinogenesis, altered: S198‑p
cell growth, altered: S198‑p
cell motility, altered: S198‑p
cytoskeletal reorganization: S198‑p
intracellular localization: S198‑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 3 S22-p HKVIMVGsGGVGKSA
0 6 Y43-p YDEFVEDyEPTKADS
0 1 Y51-p EPTKADSyRKKVVLD
0 10 Y75-p DTAGQEDyAAIRDNY
0 1 S85-p IRDNYFRsGEGFLLV
0 1 T104-p EHESFTAtAEFREQI
0 1 K160 QYVETSAKTRANVDK
0 1 K179-ac LMREIRTkkMSENKD
0 1 K180-ac MREIRTkkMSENKDK
0 1 K190-ac ENKDKNGkKSSKNKK
1 0 S198-p KSSKNKKsFKERCCL
  mouse

 
S22 HKVIMVGSGGVGKSA
Y43 YDEFVEDYEPTKADS
Y51 EPTKADSYRKKVVLD
Y75 DTAGQEDYAAIRDNY
S85 IRDNYFRSGEGFLLV
T104 EHESFTATAEFREQI
K160-ub QYVETSAkTRANVDK
K179 LMREIRAKKMSENKD
K180 MREIRAKKMSENKDK
R190 ENKDKNGRKSSKSKK
S198 KSSKSKKSFKERCCL
  rat

 
S22 HKVIMVGSGGVGKSA
Y43 YDEFVEDYEPTKADS
Y51 EPTKADSYRKKVVLD
Y75 DTAGQEDYAAIRDNY
S85 IRDNYFRSGEGFLLV
T104 EHESFTATAEFREQI
K160 QYVETSAKTRANVDk
K179 LMREIRAKKMSENKD
K180 MREIRAKKMSENKDK
R190 ENKDKNGRKSGKSKK
S198 KSGKSKKSFKERCCL
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.