Q15311 (RBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RalA-binding protein 1
Short name=RalBP1

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

Gene names

Name:	RALBP1
Synonyms:	RLIP1, RLIP76

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin. Ref.1 Ref.6 Ref.7
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 CDK1 during mitosis. Interacts with EPN1, NUMB and TFAP2A during interphase and mitosis. Ref.1 Ref.5 Ref.6 Ref.8
Subcellular location	Membrane; Peripheral membrane protein Ref.7.
Tissue specificity	Expressed ubiquitously but at low levels. Shows a strong expression in the erythrocytes. Ref.7
Sequence similarities	Contains 1 Rho-GAP domain.

Ontologies

Keywords
Biological process	Transport
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chemotaxis Traceable author statement PubMed 10848592. Source: ProtInc positive regulation of Cdc42 GTPase activity Inferred from direct assay Ref.1. Source: UniProtKB small GTPase mediated signal transduction Inferred from physical interaction Ref.1. Source: UniProtKB transport Inferred from direct assay Ref.2Ref.7. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome membrane Inferred from direct assay Ref.2Ref.7. Source: UniProtKB
Molecular_function	ATPase activity, coupled to movement of substances Inferred from direct assay Ref.7. Source: UniProtKB Rac GTPase activator activity Inferred from direct assay Ref.1. 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 Ref.2

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

29

1

Phosphoserine By similarity

Modified residue

62

1

Phosphoserine Ref.10

Modified residue

92

1

Phosphoserine Ref.12 Ref.14

Modified residue

93

1

Phosphoserine Ref.12 Ref.14

Modified residue

463

1

Phosphoserine Ref.16

Natural variations

Natural variant

617

1

A → V.
Corresponds to variant rs35867116 [ dbSNP | Ensembl ].

VAR_049147

Secondary structure

1

.

.

.

.

.

655

Helix Strand Turn

Details...

Helix

395 – 414

20

Helix

424 – 444

21

Sequences

	Sequence		Length	Mass (Da)
	Q15311 [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, PROTEIN SEQUENCE OF 2-15; 409-438 AND 472-486. Tissue: Bone marrow.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[5]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH REPS2. Tissue: Brain.
[6]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CCNB1; CDK1; EPN1; NUMB AND TFAP2A.
[7]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DAB2IP.
[9]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L42542 mRNA. Translation: AAB00103.1.
CH471113 Genomic DNA. Translation: EAX01601.1.
CH471113 Genomic DNA. Translation: EAX01602.1.
CH471113 Genomic DNA. Translation: EAX01604.1.
CH471113 Genomic DNA. Translation: EAX01605.1.
BC013126 mRNA. Translation: AAH13126.1.

IPI

IPI00009544.

PIR

F59435.

RefSeq

NP_006779.1. NM_006788.3.

UniGene

Hs.528993.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KWH	NMR	-	A	393-446	[»]
2KWI	NMR	-	B	393-446	[»]

ProteinModelPortal

Q15311.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15311. 4 interactions.

MINT

MINT-140436.

STRING

9606.ENSP00000019317.

Protein family/group databases

TCDB

9.A.1.1.1. non ABC multidrug exporter (N-MDE) family.

PTM databases

PhosphoSite

Q15311.

Polymorphism databases

DMDM

34098413.

Proteomic databases

PaxDb

Q15311.

PeptideAtlas

Q15311.

PRIDE

Q15311.

Protocols and materials databases

DNASU

10928.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000019317; ENSP00000019317; ENSG00000017797.
ENST00000383432; ENSP00000372924; ENSG00000017797.

GeneID

10928.

KEGG

hsa:10928.

UCSC

uc002kob.3. human.

Organism-specific databases

CTD

10928.

GeneCards

GC18P009465.

HGNC

HGNC:9841. RALBP1.

HPA

CAB046010.
HPA046651.

MIM

605801. gene.

neXtProt

NX_Q15311.

PharmGKB

PA34199.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG295787.

HOGENOM

HOG000007929.

HOVERGEN

HBG044496.

InParanoid

Q15311.

KO

K08773.

OMA

ETQAGIK.

OrthoDB

EOG41RPTW.

PhylomeDB

Q15311.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q15311.

Bgee

Q15311.

CleanEx

HS_RALBP1.

Genevestigator

Q15311.

GermOnline

ENSG00000017797. Homo sapiens.

Family and domain databases

Gene3D

1.10.555.10. 1 hit.

InterPro

IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]

Pfam

PF00620. RhoGAP. 1 hit.
[Graphical view]

SMART

SM00324. RhoGAP. 1 hit.
[Graphical view]

SUPFAM

SSF48350. Rho_GAP. 1 hit.

PROSITE

PS50238. RHOGAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RALBP1. human.

EvolutionaryTrace

Q15311.

GenomeRNAi

10928.

NextBio

41515.

SOURCE

Search...

Entry information

Entry name

RBP1_HUMAN

Accession

Primary (citable) accession number: Q15311
Secondary accession number(s): D3DUI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.