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Q15311

- RBP1_HUMAN

UniProt

Q15311 - RBP1_HUMAN

Protein

RalA-binding protein 1

Gene

RALBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.3 Publications

    GO - Molecular functioni

    1. ATPase activity Source: UniProtKB
    2. ATPase activity, coupled to movement of substances Source: UniProtKB
    3. GTPase activator activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. Rac GTPase activator activity Source: UniProtKB
    6. Rac GTPase binding Source: UniProtKB
    7. Ral GTPase binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. chemotaxis Source: ProtInc
    3. positive regulation of Cdc42 GTPase activity Source: UniProtKB
    4. positive regulation of Rac GTPase activity Source: GOC
    5. regulation of GTPase activity Source: UniProtKB
    6. regulation of small GTPase mediated signal transduction Source: Reactome
    7. signal transduction Source: ProtInc
    8. small GTPase mediated signal transduction Source: UniProtKB
    9. transport Source: UniProtKB

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Biological processi

    Transport

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    SignaLinkiQ15311.

    Protein family/group databases

    TCDBi9.A.1.1.1. the non abc multidrug exporter (n-mde) family.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:RALBP1
    Synonyms:RLIP1, RLIP76
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:9841. RALBP1.

    Subcellular locationi

    Membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34199.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 655654RalA-binding protein 1PRO_0000056733Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication
    Modified residuei29 – 291PhosphoserineBy similarity
    Modified residuei62 – 621Phosphoserine1 Publication
    Modified residuei92 – 921Phosphoserine2 Publications
    Modified residuei93 – 931Phosphoserine2 Publications
    Modified residuei463 – 4631Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15311.
    PaxDbiQ15311.
    PeptideAtlasiQ15311.
    PRIDEiQ15311.

    PTM databases

    PhosphoSiteiQ15311.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously but at low levels. Shows a strong expression in the erythrocytes.1 Publication

    Gene expression databases

    ArrayExpressiQ15311.
    BgeeiQ15311.
    CleanExiHS_RALBP1.
    GenevestigatoriQ15311.

    Organism-specific databases

    HPAiCAB046010.
    HPA046651.
    HPA054654.

    Interactioni

    Subunit structurei

    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.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCL20P785562EBI-749285,EBI-3913209
    TAX1BP1Q86VP13EBI-749285,EBI-529518

    Protein-protein interaction databases

    BioGridi116131. 22 interactions.
    IntActiQ15311. 11 interactions.
    MINTiMINT-140436.
    STRINGi9606.ENSP00000019317.

    Structurei

    Secondary structure

    1
    655
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi184 – 1874
    Helixi194 – 2007
    Helixi211 – 22212
    Turni223 – 2253
    Turni228 – 2325
    Helixi237 – 24812
    Helixi255 – 2573
    Helixi260 – 27314
    Helixi280 – 29112
    Helixi296 – 30914
    Helixi312 – 33423
    Helixi339 – 35012
    Helixi354 – 36714
    Beta strandi384 – 3863
    Helixi395 – 41420
    Turni417 – 4193
    Helixi424 – 44421

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KWHNMR-A393-446[»]
    2KWINMR-B393-446[»]
    2MBGNMR-A184-446[»]
    ProteinModelPortaliQ15311.
    SMRiQ15311. Positions 183-446.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15311.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini192 – 380189Rho-GAPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni403 – 49997Interacts with RalAAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi164 – 1718Poly-Lys

    Sequence similaritiesi

    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG295787.
    HOGENOMiHOG000007929.
    HOVERGENiHBG044496.
    InParanoidiQ15311.
    KOiK08773.
    OMAiTMMYDGV.
    OrthoDBiEOG7V49ZT.
    PhylomeDBiQ15311.
    TreeFamiTF315411.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    InterProiIPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view]
    PfamiPF00620. RhoGAP. 1 hit.
    [Graphical view]
    SMARTiSM00324. RhoGAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    PROSITEiPS50238. RHOGAP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q15311-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTECFLPPTS SPSEHRRVEH GSGLTRTPSS EEISPTKFPG LYRTGEPSPP    50
    HDILHEPPDV VSDDEKDHGK KKGKFKKKEK RTEGYAAFQE DSSGDEAESP 100
    SKMKRSKGIH VFKKPSFSKK KEKDFKIKEK PKEEKHKEEK HKEEKHKEKK 150
    SKDLTAADVV KQWKEKKKKK KPIQEPEVPQ IDVPNLKPIF GIPLADAVER 200
    TMMYDGIRLP AVFRECIDYV EKYGMKCEGI YRVSGIKSKV DELKAAYDRE 250
    ESTNLEDYEP NTVASLLKQY LRDLPENLLT KELMPRFEEA CGRTTETEKV 300
    QEFQRLLKEL PECNYLLISW LIVHMDHVIA KELETKMNIQ NISIVLSPTV 350
    QISNRVLYVF FTHVQELFGN VVLKQVMKPL RWSNMATMPT LPETQAGIKE 400
    EIRRQEFLLN CLHRDLQGGI KDLSKEERLW EVQRILTALK RKLREAKRQE 450
    CETKIAQEIA SLSKEDVSKE EMNENEEVIN ILLAQENEIL TEQEELLAME 500
    QFLRRQIASE KEEIERLRAE IAEIQSRQQH GRSETEEYSS ESESESEDEE 550
    ELQIILEDLQ RQNEELEIKN NHLNQAIHEE REAIIELRVQ LRLLQMQRAK 600
    AEQQAQEDEE PEWRGGAVQP PRDGVLEPKA AKEQPKAGKE PAKPSPSRDR 650
    KETSI 655
    Length:655
    Mass (Da):76,063
    Last modified:January 23, 2007 - v3
    Checksum:iEC6F75329FD8D062
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti617 – 6171A → V.
    Corresponds to variant rs35867116 [ dbSNP | Ensembl ].
    VAR_049147

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS11845.1.
    PIRiF59435.
    RefSeqiNP_006779.1. NM_006788.3.
    XP_006722358.1. XM_006722295.1.
    XP_006722359.1. XM_006722296.1.
    UniGeneiHs.528993.

    Genome annotation databases

    EnsembliENST00000019317; ENSP00000019317; ENSG00000017797.
    ENST00000383432; ENSP00000372924; ENSG00000017797.
    GeneIDi10928.
    KEGGihsa:10928.
    UCSCiuc002kob.3. human.

    Polymorphism databases

    DMDMi34098413.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS11845.1.
    PIRi F59435.
    RefSeqi NP_006779.1. NM_006788.3.
    XP_006722358.1. XM_006722295.1.
    XP_006722359.1. XM_006722296.1.
    UniGenei Hs.528993.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KWH NMR - A 393-446 [» ]
    2KWI NMR - B 393-446 [» ]
    2MBG NMR - A 184-446 [» ]
    ProteinModelPortali Q15311.
    SMRi Q15311. Positions 183-446.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116131. 22 interactions.
    IntActi Q15311. 11 interactions.
    MINTi MINT-140436.
    STRINGi 9606.ENSP00000019317.

    Protein family/group databases

    TCDBi 9.A.1.1.1. the non abc multidrug exporter (n-mde) family.

    PTM databases

    PhosphoSitei Q15311.

    Polymorphism databases

    DMDMi 34098413.

    Proteomic databases

    MaxQBi Q15311.
    PaxDbi Q15311.
    PeptideAtlasi Q15311.
    PRIDEi Q15311.

    Protocols and materials databases

    DNASUi 10928.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000019317 ; ENSP00000019317 ; ENSG00000017797 .
    ENST00000383432 ; ENSP00000372924 ; ENSG00000017797 .
    GeneIDi 10928.
    KEGGi hsa:10928.
    UCSCi uc002kob.3. human.

    Organism-specific databases

    CTDi 10928.
    GeneCardsi GC18P009465.
    HGNCi HGNC:9841. RALBP1.
    HPAi CAB046010.
    HPA046651.
    HPA054654.
    MIMi 605801. gene.
    neXtProti NX_Q15311.
    PharmGKBi PA34199.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295787.
    HOGENOMi HOG000007929.
    HOVERGENi HBG044496.
    InParanoidi Q15311.
    KOi K08773.
    OMAi TMMYDGV.
    OrthoDBi EOG7V49ZT.
    PhylomeDBi Q15311.
    TreeFami TF315411.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    SignaLinki Q15311.

    Miscellaneous databases

    ChiTaRSi RALBP1. human.
    EvolutionaryTracei Q15311.
    GeneWikii RALBP1.
    GenomeRNAii 10928.
    NextBioi 41515.
    PROi Q15311.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15311.
    Bgeei Q15311.
    CleanExi HS_RALBP1.
    Genevestigatori Q15311.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    InterProi IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view ]
    Pfami PF00620. RhoGAP. 1 hit.
    [Graphical view ]
    SMARTi SM00324. RhoGAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    PROSITEi PS50238. RHOGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    12. 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. 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. 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.

    Entry informationi

    Entry nameiRBP1_HUMAN
    AccessioniPrimary (citable) accession number: Q15311
    Secondary accession number(s): D3DUI0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 15, 2003
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 129 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3