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Q15311 (RBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length655 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 Ref.18

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 processTransport
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   Molecular functionGTPase activation
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.2Ref.7. Source: GOC

chemotaxis

Traceable author statement PubMed 10848592. Source: ProtInc

positive regulation of Cdc42 GTPase activity

Inferred from direct assay Ref.1. Source: UniProtKB

positive regulation of Rac GTPase activity

Inferred from direct assay Ref.1. Source: GOC

regulation of GTPase activity

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement Ref.1. Source: ProtInc

small GTPase mediated signal transduction

Inferred from physical interaction Ref.1. Source: UniProtKB

transport

Inferred from direct assay Ref.2Ref.7. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

membrane

Inferred from direct assay Ref.2Ref.7. Source: UniProtKB

   Molecular_functionATPase activity

Inferred from direct assay Ref.2. Source: UniProtKB

ATPase activity, coupled to movement of substances

Inferred from direct assay Ref.7. Source: UniProtKB

GTPase activator activity

Inferred from direct assay Ref.1. Source: UniProtKB

Rac GTPase activator activity

Inferred from direct assay Ref.1. Source: UniProtKB

Rac GTPase binding

Inferred from physical interaction Ref.1. Source: UniProtKB

Ral GTPase binding

Inferred from physical interaction Ref.1PubMed 9753634. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CCL20P785562EBI-749285,EBI-3913209
TAX1BP1Q86VP13EBI-749285,EBI-529518

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.13
Chain2 – 655654RalA-binding protein 1
PRO_0000056733

Regions

Domain192 – 380189Rho-GAP
Region403 – 49997Interacts with RalA
Compositional bias164 – 1718Poly-Lys

Amino acid modifications

Modified residue21N-acetylthreonine Ref.13
Modified residue291Phosphoserine By similarity
Modified residue621Phosphoserine Ref.10
Modified residue921Phosphoserine Ref.12 Ref.15
Modified residue931Phosphoserine Ref.12 Ref.15
Modified residue4631Phosphoserine Ref.17

Natural variations

Natural variant6171A → V.
Corresponds to variant rs35867116 [ dbSNP | Ensembl ].
VAR_049147

Secondary structure

.................................. 655
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15311 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: EC6F75329FD8D062

FASTA65576,063
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[14]"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].
[15]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"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].
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"The RalB-RLIP76 complex reveals a novel mode of ral-effector interaction."
Fenwick R.B., Campbell L.J., Rajasekar K., Prasannan S., Nietlispach D., Camonis J., Owen D., Mott H.R.
Structure 18:985-995(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 393-446 IN COMPLEX WITH RALB, INTERACTION WITH RALB.
+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.
CCDSCCDS11845.1.
PIRF59435.
RefSeqNP_006779.1. NM_006788.3.
XP_006722358.1. XM_006722295.1.
XP_006722359.1. XM_006722296.1.
UniGeneHs.528993.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KWHNMR-A393-446[»]
2KWINMR-B393-446[»]
2MBGNMR-A184-446[»]
ProteinModelPortalQ15311.
SMRQ15311. Positions 183-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116131. 22 interactions.
IntActQ15311. 8 interactions.
MINTMINT-140436.
STRING9606.ENSP00000019317.

Protein family/group databases

TCDB9.A.1.1.1. the non abc multidrug exporter (n-mde) family.

PTM databases

PhosphoSiteQ15311.

Polymorphism databases

DMDM34098413.

Proteomic databases

MaxQBQ15311.
PaxDbQ15311.
PeptideAtlasQ15311.
PRIDEQ15311.

Protocols and materials databases

DNASU10928.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000019317; ENSP00000019317; ENSG00000017797.
ENST00000383432; ENSP00000372924; ENSG00000017797.
GeneID10928.
KEGGhsa:10928.
UCSCuc002kob.3. human.

Organism-specific databases

CTD10928.
GeneCardsGC18P009465.
HGNCHGNC:9841. RALBP1.
HPACAB046010.
HPA046651.
HPA054654.
MIM605801. gene.
neXtProtNX_Q15311.
PharmGKBPA34199.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295787.
HOGENOMHOG000007929.
HOVERGENHBG044496.
InParanoidQ15311.
KOK08773.
OMATMMYDGV.
OrthoDBEOG7V49ZT.
PhylomeDBQ15311.
TreeFamTF315411.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ15311.

Gene expression databases

ArrayExpressQ15311.
BgeeQ15311.
CleanExHS_RALBP1.
GenevestigatorQ15311.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
InterProIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamPF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTSM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
PROSITEPS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRALBP1. human.
EvolutionaryTraceQ15311.
GeneWikiRALBP1.
GenomeRNAi10928.
NextBio41515.
PROQ15311.
SOURCESearch...

Entry information

Entry nameRBP1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM