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Protein Page:
RALBP1 (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
RALBP1 Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin. Interacts with the GTP-bound form of RALA, RALB, CDC42 and RAC1. Interacts with REPS1 and REPS2 and this does not affect the Ral-binding activity. Interacts with DAB2IP. Interacts with catalytically active CCNB1 and CDK1 during mitosis. Interacts with EPN1, NUMB and TFAP2A during interphase and mitosis. Expressed ubiquitously but at low levels. Shows a strong expression in the erythrocytes. Note: This description may include information from UniProtKB.
Protein type: GAPs; GAPs, Rac/Rho
Cellular Component: membrane; cytosol
Molecular Function: protein binding; ATPase activity, coupled to movement of substances; Rac GTPase activator activity; ATPase activity; Rac GTPase binding; Ral GTPase binding; GTPase activator activity
Biological Process: ATP catabolic process; regulation of small GTPase mediated signal transduction; regulation of GTPase activity; positive regulation of Cdc42 GTPase activity; transport; small GTPase mediated signal transduction; positive regulation of Rac GTPase activity; chemotaxis; signal transduction
Reference #:  Q15311 (UniProtKB)
Alt. Names/Synonyms: 76 kDa Ral-interacting protein; Dinitrophenyl S-glutathione ATPase; DNP-SG ATPase; Ral-interacting protein 1; ralA binding protein 1; RalA-binding protein 1; RALBP1; RBP1; RIP1; RLIP1; RLIP76
Gene Symbols: RALBP1
Molecular weight: 76,063 Da
Basal Isoelectric point: 5.68  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RALBP1

Protein Structure Not Found.


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Sites Implicated In
activity, induced: T297‑p, S509‑p
protein conformation: T297‑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 7 S11-p CFLPPTSsPsEHRRV
0 1 S13-p LPPTSsPsEHRRVEH
0 1 S22 HRRVEHGSGLtRtPs
0 3 T25-p VEHGSGLtRtPssEE
0 40 T27-p HGSGLtRtPssEEIs
0 514 S29-p SGLtRtPssEEIsPt
0 94 S30-p GLtRtPssEEIsPtK
0 67 S34-p tPssEEIsPtKFPGL
0 3 T36-p ssEEIsPtKFPGLYR
0 1 T44-p KFPGLYRtGEPsPPH
0 45 S48-p LYRtGEPsPPHDILH
0 2 V60 ILHEPPDVVsDDEKD
0 45 S62-p HEPPDVVsDDEKDHG
0 1 T82 FKKKEKRTEGyAAFQ
0 2 Y85-p KEKRTEGyAAFQEDs
0 24 S92-p yAAFQEDssGDEAEs
0 27 S93-p AAFQEDssGDEAEsP
0 3 S99-p ssGDEAEsPSKMKRS
0 1 K107 PSKMKRSKGIHVFKK
0 1 K113 SKGIHVFKKPsFsKK
0 6 S116-p IHVFKKPsFsKKKEK
1 2 S118-p VFKKPsFsKKKEKDF
0 1 K119 FKKPsFsKKKEKDFK
0 1 K152-ub KHKEKKSkDLTAADV
0 7 K187 QIDVPNLKPIFGIPL
0 1 Y219-p VFRECIDyVEKYGMK
0 1 S252-p AAYDREEstNLEDYE
0 1 T253-p AYDREEstNLEDYEP
0 1 Y270-p VASLLKQyLRDLPEN
0 1 T280-p DLPENLLtKELMPRF
1 0 T297-p ACGRTTEtEKVQEFQ
1 0 S353-p LSPTVQIsNRVLYVF
0 1 K454-ub KRQECETkIAQEIAs
0 3 S461-p kIAQEIAsLsKEDVS
0 17 S463-p AQEIAsLsKEDVSkE
0 1 K469-ub LsKEDVSkEEMNENE
1 0 S509-p FLRRQIAsEKEEIER
0 7 S645-p GKEPAKPsPSRDRKE
  mouse

 
S11 CFLPPSSSPSEHRRA
S13 LPPSSSPSEHRRAEH
S22-p HRRAEHGsGLtRtPs
T25-p AEHGsGLtRtPssEE
T27-p HGsGLtRtPssEEIs
S29-p sGLtRtPssEEIsPt
S30-p GLtRtPssEEIsPtK
S34-p tPssEEIsPtKFPGL
T36-p ssEEIsPtKFPGLYR
T44 KFPGLYRTGEPsPPH
S48-p LYRTGEPsPPHDVLH
T60-p VLHEPPDtVsDDDKD
S62-p HEPPDtVsDDDKDHG
T82-p FKKKEKRtEGyAAFQ
Y85-p KEKRtEGyAAFQEDs
S92-p yAAFQEDssGDEAEs
S93-p AAFQEDssGDEAEsP
S99-p ssGDEAEsPSKVKRS
K107-ac PSKVKRSkGIHVFkK
K113-ac SkGIHVFkKPsFSkK
S116-p IHVFkKPsFSkKKEK
S118 VFkKPsFSkKKEKDF
K119-ac FkKPsFSkKKEKDFK
K152 KHKEKKSKDLTAADV
K187-ub QMDAPSVkPIFGVPL
Y219 VFRECVDYMEKHGMK
S252 AAYDREESPNLEEYE
P253 AYDREESPNLEEYEP
Y270 VASLLKQYLRDLPEN
T280 DLPENLLTKELMPRF
M297 ACGKTTEMEKVQEFQ
S353 LSPTVQISNRVLYVL
K454 KRQECETKIAQEIAS
S461 KIAQEIASLsKEDVS
S463-p AQEIASLsKEDVSKE
K469 LsKEDVSKEEMNENE
S509 FLRRQIASEKEEIDR
S638 AKEQAKASPSKDRKE
  rat

 
S11 CFLPPTSSPSEHRRA
S13 LPPTSSPSEHRRAEH
S22 HRRAEHGSGLTRTPs
T25 AEHGSGLTRTPssEE
T27 HGSGLTRTPssEEIS
S29-p SGLTRTPssEEISPT
S30-p GLTRTPssEEISPTK
S34 TPssEEISPTKFPEL
T36 ssEEISPTKFPELYR
T44 KFPELYRTGEPsPPH
S48-p LYRTGEPsPPHDILH
I60 ILHEPPDIVsDDEKD
S62-p HEPPDIVsDDEKDHG
T82 FKKKEKRTEGYVAFQ
Y85 KEKRTEGYVAFQEDS
S92 YVAFQEDSsGDEAES
S93-p VAFQEDSsGDEAESP
S99 SsGDEAESPSKMKRS
K107 PSKMKRSKGIHVFKK
K113 SKGIHVFKKPSFSKK
S116 IHVFKKPSFSKKKEK
S118 VFKKPSFSKKKEKDF
K119 FKKPSFSKKKEKDFK
K152 KHKEKKCKDFTAADV
R187 QTDAPSLRPIFGAPF
Y219 VFRECVDYMEKHGMK
S252 AAYDREESPNLEEYE
P253 AYDREESPNLEEYEP
Y270 VASLLKQYLRDLPEN
T280 DLPENLLTKELMPRF
V297 ACGRTTEVEKVQEFQ
S353 LSPTVQISNRVLYVL
K454 KRQECETKIAQEIAS
S461 KIAQEIASLsKEDVS
S463-p AQEIASLsKEDVSKE
K469 LsKEDVSKEETNENE
S509 FLRRQIASEKEEIDR
S637 AKEQAKPSPSKDRKE
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