Reviewed,
UniProtKB/Swiss-Prot Q15311 (RBP1_HUMAN)
Last modified
February 9, 2010.
Version 84.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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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 |
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| Organism | Homo sapiens (Human) [Complete 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 CDC2 to switch off endocytosis, One of its substrates would be EPN1/Epsin. Ref.1 Ref.5 Ref.6 |
| 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. Ref.1 Ref.5 Ref.4 Ref.7 |
| Subcellular location | |
| Tissue specificity | Expressed ubiquitously but at low levels. Shows a strong expression in the erythrocytes. Ref.6 |
| Sequence similarities | Contains 1 Rho-GAP domain. |
Ontologies
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 | 11 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 27 | 1 | Phosphothreonine Ref.9 | ||||||
| Modified residue | 29 | 1 | Phosphoserine Ref.13 Ref.9 | ||||||
| Modified residue | 30 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 34 | 1 | Phosphoserine Ref.13 Ref.10 | ||||||
| Modified residue | 62 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 92 | 1 | Phosphoserine Ref.13 Ref.8 Ref.11 Ref.15 | ||||||
| Modified residue | 93 | 1 | Phosphoserine Ref.13 Ref.8 Ref.11 Ref.15 | ||||||
| Modified residue | 270 | 1 | Phosphotyrosine Ref.13 | ||||||
| Modified residue | 280 | 1 | Phosphothreonine Ref.13 | ||||||
| Modified residue | 463 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 645 | 1 | Phosphoserine | ||||||
Natural variations | |||||||||
| Natural variant | 617 | 1 | A → V: dbSNP rs35867116. | VAR_049147 | |||||
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: 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. |
| [12] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-29; SER-30; SER-34; SER-92; SER-93; TYR-270; THR-280 AND SER-463, MASS SPECTROMETRY. |
| [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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-92; SER-93 AND SER-645, MASS SPECTROMETRY. |
| [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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, MASS SPECTROMETRY. Tissue: T-cell. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L42542 mRNA. Translation: AAB00103.1. BC013126 mRNA. Translation: AAH13126.1. |
| IPI | IPI00009544. |
| PIR | F59435. |
| RefSeq | NP_006779.1. |
| UniGene | Hs.528993 Hs.719181 |
3D structure databases | |
| SMR | Q15311. Positions 184-352. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q15311. 3 interactions. |
| STRING | Q15311. |
Protein family/group databases | |
| TCDB | 9.A.1.1.1. non ABC multidrug exporter (N-MDE) family. |
PTM databases | |
| PhosphoSite | Q15311. |
Proteomic databases | |
| PeptideAtlas | Q15311. |
| PRIDE | Q15311. |
Genome annotation databases | |
| Ensembl | ENST00000019317; ENSP00000019317; ENSG00000017797; Homo sapiens. [Genome view] ENST00000383432; ENSP00000372924; ENSG00000017797; Homo sapiens. [Genome view] |
| GeneID | 10928. |
| KEGG | hsa:10928. |
| UCSC | uc002kob.1. human. |
Organism-specific databases | |
| CTD | 10928. |
| GeneCards | GC18P009465. |
| H-InvDB | HIX0014325. |
| HGNC | HGNC:9841. RALBP1. |
| MIM | 605801. gene. |
| PharmGKB | PA34199. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG10919. |
| HOGENOM | HBG713891. |
| HOVERGEN | Q15311. |
| InParanoid | Q15311. |
| OMA | TQAGIKE. |
| OrthoDB | EOG94BDMF. |
| PhylomeDB | Q15311. |
Enzyme and pathway databases | |
| Reactome | REACT_11044. Signaling by Rho GTPases. |
Gene expression databases | |
| ArrayExpress | Q15311. |
| Bgee | Q15311. |
| CleanEx | HS_RALBP1. |
| Genevestigator | Q15311. |
| GermOnline | ENSG00000017797. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR008936. Rho_GTPase_activation_prot. 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 |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| 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 |
| SIMILARITY comments Index of protein domains and families |

Clusters with


