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RALBP1 (human)

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: GTPase activating protein, misc. 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; 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®

Select Structure to View Below RALBP1 2KWH - A=393-446 (human) 2KWI - B=393-446 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 2KWH 2KWI  |  Phospho3D  |  DISEASE  |  Source  |  InnateDB  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Sites Implicated In
activation: 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

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		S13-p	LPPTSSPsEHRRVEH
0	1		S22	HRRVEHGSGLtRtPs
0	3		T25-p	VEHGSGLtRtPssEE
0	38		T27-p	HGSGLtRtPssEEIs
0	481		S29-p	SGLtRtPssEEIsPt
0	78		S30-p	GLtRtPssEEIsPtK
0	46		S34-p	tPssEEIsPtKFPGL
0	3		T36-p	ssEEIsPtKFPGLYR
0	38		S48-p	LYRTGEPsPPHDILH
0	2		V60	ILHEPPDVVsDDEKD
0	36		S62-p	HEPPDVVsDDEKDHG
0	1		T82	FKKKEKRTEGYAAFQ
0	1		Y85	KEKRTEGYAAFQEDs
0	15		S92-p	YAAFQEDssGDEAEs
0	16		S93-p	AAFQEDssGDEAEsP
0	2		S99-p	ssGDEAEsPSKMKRS
0	1		K107-a	PSKMKRSkGIHVFkK
0	1		K113-a	SkGIHVFkKPsFskK
0	5		S116-p	IHVFkKPsFskKKEK
1	2		S118-p	VFkKPsFskKKEKDF
0	1		K119-a	FkKPsFskKKEKDFK
0	1		K152-u	KHKEKKSkDLTAADV
0	7		K187-u	QIDVPNLkPIFGIPL
0	1		S252-p	AAYDREEstNLEDYE
0	1		T253-p	AYDREEstNLEDYEP
1	0		T297-p	ACGRTTEtEKVQEFQ
1	0		S353-p	LSPTVQIsNRVLYVF
0	1		K454-u	KRQECETkIAQEIAs
0	1		S461-p	kIAQEIAsLsKEDVS
0	11		S463-p	AQEIAsLsKEDVSkE
0	1		K469-u	LsKEDVSkEEMNENE
1	0		S509-p	FLRRQIAsEKEEIER
0	3		S645-p	GKEPAKPsPSRDRKE

	mouse
S13	LPPSSSPSEHRRAEH
S22-p	HRRAEHGsGLtRtPs
T25-p	AEHGsGLtRtPssEE
T27-p	HGsGLtRtPssEEIs
S29-p	sGLtRtPssEEIsPt
S30-p	GLtRtPssEEIsPtK
S34-p	tPssEEIsPtKFPGL
T36-p	ssEEIsPtKFPGLYR
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-a	PSKVKRSkGIHVFkK
K113-a	SkGIHVFkKPsFSkK
S116-p	IHVFkKPsFSkKKEK
S118	VFkKPsFSkKKEKDF
K119-a	FkKPsFSkKKEKDFK
K152	KHKEKKSKDLTAADV
K187-u	QMDAPSVkPIFGVPL
S252	AAYDREESPNLEEYE
P253	AYDREESPNLEEYEP
M297	ACGKTTEMEKVQEFQ
S353	LSPTVQISNRVLYVL
K454	KRQECETKIAQEIAS
S461	KIAQEIASLsKEDVS
S463-p	AQEIASLsKEDVSKE
K469	LsKEDVSKEEMNENE
S509	FLRRQIASEKEEIDR
S638	AKEQAKASPSKDRKE

	rat
S13	LPPTSSPSEHRRAEH
S22	HRRAEHGSGLTRTPs
T25	AEHGSGLTRTPssEE
T27	HGSGLTRTPssEEIS
S29-p	SGLTRTPssEEISPT
S30-p	GLTRTPssEEISPTK
S34	TPssEEISPTKFPEL
T36	ssEEISPTKFPELYR
S48	LYRTGEPSPPHDILH
I60	ILHEPPDIVSDDEKD
S62	HEPPDIVSDDEKDHG
T82	FKKKEKRTEGYVAFQ
Y85	KEKRTEGYVAFQEDS
S92	YVAFQEDSSGDEAES
S93	VAFQEDSSGDEAESP
S99	SSGDEAESPSKMKRS
K107	PSKMKRSKGIHVFKK
K113	SKGIHVFKKPSFSKK
S116	IHVFKKPSFSKKKEK
S118	VFKKPSFSKKKEKDF
K119	FKKPSFSKKKEKDFK
K152	KHKEKKCKDFTAADV
R187	QTDAPSLRPIFGAPF
S252	AAYDREESPNLEEYE
P253	AYDREESPNLEEYEP
V297	ACGRTTEVEKVQEFQ
S353	LSPTVQISNRVLYVL
K454	KRQECETKIAQEIAS
S461	KIAQEIASLSKEDVS
S463	AQEIASLSKEDVSKE
K469	LSKEDVSKEETNENE
S509	FLRRQIASEKEEIDR
S637	AKEQAKPSPSKDRKE

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