Reviewed, UniProtKB/Swiss-Prot Q15311 (RBP1_HUMAN)

Names and origin

Protein names

Recommended name:
    RalA-binding protein 1
      Short name=RalBP1
Alternative name(s):
    Ral-interacting protein 1
    76 kDa Ral-interacting protein
    Dinitrophenyl S-glutathione ATPase
      Short name=DNP-SG ATPase

Gene names

Name:	RALBP1
Synonyms:	RLIP1, RLIP76

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	655 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 CDC2 to switch off endocytosis, One of its substrates would be EPN1/Epsin.
Subunit structure	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 CDC2 during mitosis. Interacts with EPN1, NUMB and TFAP2A during interphase and mitosis.
Subcellular location	Membrane; Peripheral membrane protein.
Tissue specificity	Expressed ubiquitously but at low levels. Shows a strong expression in the erythrocytes.
Sequence similarities	Contains 1 Rho-GAP domain.

Ontologies

Keywords
Biological process	Transport
Cellular component	Membrane
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	chemotaxis Traceable author statement. Source: ProtInc positive regulation of Cdc42 GTPase activity Ref.1 Inferred from direct assay. Source: UniProtKB transport Ref.2 Ref.6 Inferred from direct assay. Source: UniProtKB
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro membrane Ref.2 Ref.6 Inferred from direct assay. Source: UniProtKB
Molecular function	ATPase activity, coupled to movement of substances Ref.6 Inferred from direct assay. Source: UniProtKB Rac GTPase activator activity Ref.1 Inferred from direct assay. Source: UniProtKB Rac GTPase binding Ref.1 Inferred from physical interaction. Source: UniProtKB Ral GTPase binding Ref.1 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 655	654	RalA-binding protein 1		PRO_0000056733
Regions
	Domain	192 – 380	189	Rho-GAP
	Region	403 – 499	97	Interacts with RalA
	Compositional bias	164 – 171	8	Poly-Lys
Amino acid modifications
	Modified residue	27	1	Phosphothreonine
	Modified residue	29	1	Phosphoserine
	Modified residue	34	1	Phosphoserine
	Modified residue	62	1	Phosphoserine
	Modified residue	92	1	Phosphoserine
	Modified residue	93	1	Phosphoserine

Sequences

	Sequence		Length	Mass (Da)
	Q15311-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: EC6F75329FD8D062	FASTA	655	76,063
	10 20 30 40 50 60 MTECFLPPTS SPSEHRRVEH GSGLTRTPSS EEISPTKFPG LYRTGEPSPP HDILHEPPDV 70 80 90 100 110 120 VSDDEKDHGK KKGKFKKKEK RTEGYAAFQE DSSGDEAESP SKMKRSKGIH VFKKPSFSKK 130 140 150 160 170 180 KEKDFKIKEK PKEEKHKEEK HKEEKHKEKK SKDLTAADVV KQWKEKKKKK KPIQEPEVPQ 190 200 210 220 230 240 IDVPNLKPIF GIPLADAVER TMMYDGIRLP AVFRECIDYV EKYGMKCEGI YRVSGIKSKV 250 260 270 280 290 300 DELKAAYDRE ESTNLEDYEP NTVASLLKQY LRDLPENLLT KELMPRFEEA CGRTTETEKV 310 320 330 340 350 360 QEFQRLLKEL PECNYLLISW LIVHMDHVIA KELETKMNIQ NISIVLSPTV QISNRVLYVF 370 380 390 400 410 420 FTHVQELFGN VVLKQVMKPL RWSNMATMPT LPETQAGIKE EIRRQEFLLN CLHRDLQGGI 430 440 450 460 470 480 KDLSKEERLW EVQRILTALK RKLREAKRQE CETKIAQEIA SLSKEDVSKE EMNENEEVIN 490 500 510 520 530 540 ILLAQENEIL TEQEELLAME QFLRRQIASE KEEIERLRAE IAEIQSRQQH GRSETEEYSS 550 560 570 580 590 600 ESESESEDEE ELQIILEDLQ RQNEELEIKN NHLNQAIHEE REAIIELRVQ LRLLQMQRAK 610 620 630 640 650 AEQQAQEDEE PEWRGGAVQP PRDGVLEPKA AKEQPKAGKE PAKPSPSRDR KETSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity." Jullien-Flores V., Dorseuil O., Romero F., Letourneur F., Saragosti S., Berger R., Tavitian A., Gacon G., Camonis J.H. J. Biol. Chem. 270:22473-22477(1995) [PubMed: 7673236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RALA.
[2]	"Novel function of human RLIP76: ATP-dependent transport of glutathione conjugates and doxorubicin." Awasthi S., Cheng J., Singhal S.S., Saini M.K., Pandya U., Pikula S., Bandorowicz-Pikula J., Singh S.V., Zimniak P., Awasthi Y.C. Biochemistry 39:9327-9334(2000) [PubMed: 10924126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, PROTEIN SEQUENCE OF 2-15; 409-438 AND 472-486. Tissue: Bone marrow.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[4]	"Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral." Ikeda M., Ishida O., Hinoi T., Kishida S., Kikuchi A. J. Biol. Chem. 273:814-821(1998) [PubMed: 9422736] [Abstract] Cited for: INTERACTION WITH REPS2. Tissue: Brain.
[5]	"RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis." Rosse C., L'Hoste S., Offner N., Picard A., Camonis J. J. Biol. Chem. 278:30597-30604(2003) [PubMed: 12775724] [Abstract] Cited for: FUNCTION, INTERACTION WITH CCNB1; CDC2; EPN1; NUMB AND TFAP2A.
[6]	"RLIP76 is the major ATP-dependent transporter of glutathione-conjugates and doxorubicin in human erythrocytes." Sharma R., Singhal S.S., Cheng J., Yang Y., Sharma A., Zimniak P., Awasthi S., Awasthi Y.C. Arch. Biochem. Biophys. 391:171-179(2001) [PubMed: 11437348] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]	"AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation." Zhang H., Zhang R., Luo Y., D'Alessio A., Pober J.S., Min W. J. Biol. Chem. 279:44955-44965(2004) [PubMed: 15310755] [Abstract] Cited for: INTERACTION WITH DAB2IP.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27 AND SER-29, MASS SPECTROMETRY. Tissue: Platelet.
[10]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-62, MASS SPECTROMETRY.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42542 mRNA. Translation: AAB00103.1. BC013126 mRNA. Translation: AAH13126.1.
PIR	F59435.
RefSeq	NP_006779.1.
UniGene	Hs.528993
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15311.
PTM databases
PhosphoSite	Q15311.
Proteomic databases
PeptideAtlas	Q15311.
Genome annotation databases
Ensembl	ENSG00000017797. Homo sapiens. [Contig view]
GeneID	10928.
KEGG	hsa:10928.
Organism-specific databases
H-InvDB	HIX0014325.
HGNC	HGNC:9841. RALBP1.
MIM	605801. gene.
PharmGKB	PA34199.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	Q15311.
HOVERGEN	Q15311.
Enzyme and pathway databases
Reactome	REACT_11044. Signaling by Rho GTPases.
Gene expression databases
ArrayExpress	Q15311.
CleanEx	HS_RALBP1.
GermOnline	ENSG00000017797. Homo sapiens.
Family and domain databases
InterPro	IPR000198. RhoGAP. [Graphical view]
Gene3D	G3DSA:1.10.555.10. RhoGAP. 1 hit.
Pfam	PF00620. RhoGAP. 1 hit. [Graphical view]
SMART	SM00324. RhoGAP. 1 hit. [Graphical view]
PROSITE	PS50238. RHOGAP. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	41515.
SOURCE	Search...

Entry information

Entry name

RBP1_HUMAN

Accession

Primary (citable) accession number: Q15311

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 69 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)