Q15311 (RBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 115.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
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| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| 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 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 | |
| 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 activityInferred from direct assay Ref.1. Source: UniProtKB small GTPase mediated signal transductionInferred from physical interaction Ref.1. Source: UniProtKB transportInferred from direct assay Ref.2Ref.7. Source: UniProtKB |
| Cellular_component | cytosol Traceable author statement. Source: Reactome membraneInferred 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 activityInferred 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 | |||||||||||||
Helix Strand Turn | |||||||||||||
| Helix | 395 – 414 | 20 | |||||||||||
| Helix | 424 – 444 | 21 | |||||||||||
Sequences
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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. 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 |
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| 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 |
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| 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. | ||||||||
Relevant documents
| Human chromosome 18 Human chromosome 18: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
