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P11234

- RALB_HUMAN

UniProt

P11234 - RALB_HUMAN

Protein

Ras-related protein Ral-B

Gene

RALB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells. Plays a role in the late stages of cytokinesis and is required for the abscission of the bridge joining the sister cells emerging from mitosis. Required for suppression of apoptosis.1 Publication

    Enzyme regulationi

    Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase-activating protein (GAP).

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi21 – 299GTP
    Nucleotide bindingi68 – 725GTP
    Nucleotide bindingi128 – 1314GTP
    Nucleotide bindingi158 – 1603GTP

    GO - Molecular functioni

    1. GTPase activity Source: UniProtKB
    2. GTP binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cytokinesis Source: UniProtKB
    3. neurotrophin TRK receptor signaling pathway Source: Reactome
    4. Ras protein signal transduction Source: Reactome
    5. regulation of exocyst assembly Source: UniProtKB
    6. regulation of exocyst localization Source: UniProtKB
    7. signal transduction Source: ProtInc

    Keywords - Biological processi

    Apoptosis, Cell cycle, Cell division

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_12065. p38MAPK events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related protein Ral-B
    Gene namesi
    Name:RALB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:9840. RALB.

    Subcellular locationi

    Cell membrane 2 Publications; Lipid-anchor 2 Publications; Cytoplasmic side 2 Publications
    Note: During late cytokinesis localizes at the midbody.

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. midbody Source: UniProtKB
    3. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi46 – 461T → A: Reduces the binding affinity to EXOC2 effector. 1 Publication
    Mutagenesisi46 – 461T → S: Reduces the binding affinity to EXOC2 effector. 1 Publication
    Mutagenesisi72 – 721Q → L: Loss of GTPase activity. 1 Publication
    Mutagenesisi203 – 2031C → S: Loss of geranylgeranylation and membrane localization. 1 Publication
    Mutagenesisi206 – 2061L → S: Converts geranyl-geranylation to farnesylation. No effect on membrane localization. Confers resistance to GGTI-induced pancreatic cancer cell apoptosis, but not to GGTI-dependent inhibition of anchorage-independent proliferation. 1 Publication

    Organism-specific databases

    PharmGKBiPA34198.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 203203Ras-related protein Ral-BPRO_0000082698Add
    BLAST
    Propeptidei204 – 2063Removed in mature formBy similarityPRO_0000281349

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei203 – 2031Cysteine methyl esterBy similarity
    Lipidationi203 – 2031S-geranylgeranyl cysteine1 Publication

    Post-translational modificationi

    Prenylation is essential for membrane localization. The geranylgeranylated form and the farnesylated mutant does not undergo alternative prenylation in response to geranylgeranyltransferase I inhibitors (GGTIs) and farnesyltransferase I inhibitors (FTIs).1 Publication

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiP11234.
    PaxDbiP11234.
    PRIDEiP11234.

    PTM databases

    PhosphoSiteiP11234.

    Expressioni

    Gene expression databases

    ArrayExpressiP11234.
    BgeeiP11234.
    CleanExiHS_RALB.
    GenevestigatoriP11234.

    Organism-specific databases

    HPAiCAB026010.

    Interactioni

    Subunit structurei

    Interacts with EXOC2 and EXOC8. Interacts with RALBP1 via its effector domain.4 Publications

    Protein-protein interaction databases

    BioGridi111835. 16 interactions.
    IntActiP11234. 11 interactions.
    MINTiMINT-5000915.
    STRINGi9606.ENSP00000272519.

    Structurei

    Secondary structure

    1
    206
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni10 – 123
    Beta strandi14 – 2512
    Helixi27 – 3610
    Beta strandi51 – 566
    Beta strandi61 – 688
    Beta strandi74 – 774
    Helixi78 – 847
    Beta strandi87 – 9610
    Helixi98 – 11417
    Beta strandi117 – 1193
    Beta strandi123 – 1286
    Helixi140 – 1489
    Turni149 – 1513
    Beta strandi154 – 1563
    Turni159 – 1613
    Helixi165 – 17915
    Turni180 – 1823

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KE5NMR-A12-185[»]
    2KWINMR-A8-185[»]
    ProteinModelPortaliP11234.
    SMRiP11234. Positions 8-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11234.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi43 – 519Effector region

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Ras family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOVERGENiHBG009351.
    KOiK07835.
    PhylomeDBiP11234.
    TreeFamiTF312796.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR028412. Ral.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR020849. Small_GTPase_Ras.
    [Graphical view]
    PANTHERiPTHR24070. PTHR24070. 1 hit.
    PTHR24070:SF199. PTHR24070:SF199. 1 hit.
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00173. RAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51421. RAS. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P11234-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAANKSKGQS SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS    50
    YRKKVVLDGE EVQIDILDTA GQEDYAAIRD NYFRSGEGFL LVFSITEHES 100
    FTATAEFREQ ILRVKAEEDK IPLLVVGNKS DLEERRQVPV EEARSKAEEW 150
    GVQYVETSAK TRANVDKVFF DLMREIRTKK MSENKDKNGK KSSKNKKSFK 200
    ERCCLL 206
    Length:206
    Mass (Da):23,409
    Last modified:July 1, 1989 - v1
    Checksum:iE0AC95130FB6452C
    GO
    Isoform 2 (identifier: P11234-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MKQRQSALQWVICVSQPQKTSEM

    Note: No experimental confirmation available.

    Show »
    Length:228
    Mass (Da):25,967
    Checksum:iB36FAF7D688B0861
    GO
    Isoform 3 (identifier: P11234-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         36-37: YD → NVSKSLAYDKKKYTANKKVEGIL

    Note: No experimental confirmation available.

    Show »
    Length:227
    Mass (Da):25,710
    Checksum:i174A6FBCF109A103
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MKQRQSALQWVICVSQPQKT SEM in isoform 2. 1 PublicationVSP_055843
    Alternative sequencei36 – 372YD → NVSKSLAYDKKKYTANKKVE GIL in isoform 3. 1 PublicationVSP_055844

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15015 mRNA. Translation: CAA33119.1.
    M35416 mRNA. Translation: AAA60250.1.
    AF493911 mRNA. Translation: AAM12625.1.
    BT006953 mRNA. Translation: AAP35599.1.
    AK127675 mRNA. Translation: BAC87080.1.
    AK303214 mRNA. Translation: BAG64302.1.
    AK312453 mRNA. Translation: BAG35360.1.
    AC012363 Genomic DNA. Translation: AAY14800.1.
    CH471103 Genomic DNA. Translation: EAW95240.1.
    CH471103 Genomic DNA. Translation: EAW95242.1.
    BC018163 mRNA. Translation: AAH18163.1.
    CCDSiCCDS2131.1.
    PIRiS04597. TVHUAB.
    RefSeqiNP_002872.1. NM_002881.2.
    XP_005263784.1. XM_005263727.1.
    XP_005263785.1. XM_005263728.1.
    XP_005263786.1. XM_005263729.1.
    UniGeneiHs.469820.

    Genome annotation databases

    EnsembliENST00000272519; ENSP00000272519; ENSG00000144118. [P11234-1]
    ENST00000420510; ENSP00000414224; ENSG00000144118. [P11234-1]
    GeneIDi5899.
    KEGGihsa:5899.
    UCSCiuc002tmk.3. human.

    Polymorphism databases

    DMDMi131835.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15015 mRNA. Translation: CAA33119.1 .
    M35416 mRNA. Translation: AAA60250.1 .
    AF493911 mRNA. Translation: AAM12625.1 .
    BT006953 mRNA. Translation: AAP35599.1 .
    AK127675 mRNA. Translation: BAC87080.1 .
    AK303214 mRNA. Translation: BAG64302.1 .
    AK312453 mRNA. Translation: BAG35360.1 .
    AC012363 Genomic DNA. Translation: AAY14800.1 .
    CH471103 Genomic DNA. Translation: EAW95240.1 .
    CH471103 Genomic DNA. Translation: EAW95242.1 .
    BC018163 mRNA. Translation: AAH18163.1 .
    CCDSi CCDS2131.1.
    PIRi S04597. TVHUAB.
    RefSeqi NP_002872.1. NM_002881.2.
    XP_005263784.1. XM_005263727.1.
    XP_005263785.1. XM_005263728.1.
    XP_005263786.1. XM_005263729.1.
    UniGenei Hs.469820.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KE5 NMR - A 12-185 [» ]
    2KWI NMR - A 8-185 [» ]
    ProteinModelPortali P11234.
    SMRi P11234. Positions 8-185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111835. 16 interactions.
    IntActi P11234. 11 interactions.
    MINTi MINT-5000915.
    STRINGi 9606.ENSP00000272519.

    PTM databases

    PhosphoSitei P11234.

    Polymorphism databases

    DMDMi 131835.

    Proteomic databases

    MaxQBi P11234.
    PaxDbi P11234.
    PRIDEi P11234.

    Protocols and materials databases

    DNASUi 5899.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000272519 ; ENSP00000272519 ; ENSG00000144118 . [P11234-1 ]
    ENST00000420510 ; ENSP00000414224 ; ENSG00000144118 . [P11234-1 ]
    GeneIDi 5899.
    KEGGi hsa:5899.
    UCSCi uc002tmk.3. human.

    Organism-specific databases

    CTDi 5899.
    GeneCardsi GC02P120997.
    HGNCi HGNC:9840. RALB.
    HPAi CAB026010.
    MIMi 179551. gene.
    neXtProti NX_P11234.
    PharmGKBi PA34198.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOVERGENi HBG009351.
    KOi K07835.
    PhylomeDBi P11234.
    TreeFami TF312796.

    Enzyme and pathway databases

    Reactomei REACT_12065. p38MAPK events.

    Miscellaneous databases

    ChiTaRSi RALB. human.
    EvolutionaryTracei P11234.
    GeneWikii RALB.
    GenomeRNAii 5899.
    NextBioi 22946.
    PROi P11234.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11234.
    Bgeei P11234.
    CleanExi HS_RALB.
    Genevestigatori P11234.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR028412. Ral.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR020849. Small_GTPase_Ras.
    [Graphical view ]
    PANTHERi PTHR24070. PTHR24070. 1 hit.
    PTHR24070:SF199. PTHR24070:SF199. 1 hit.
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00173. RAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51421. RAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Coding sequences of human ralA and ralB cDNAs."
      Chardin P., Tavitian A.
      Nucleic Acids Res. 17:4380-4380(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Chromosomal localization and cDNA sequence of human ralB, a GTP binding protein."
      Hsieh C.-L., Swaroop A., Francke U.
      Somat. Cell Mol. Genet. 16:407-410(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Retina.
    3. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Caudate nucleus and Thymus.
    6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
      Tissue: Lung.
    9. "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: INTERACTION WITH RALBP1.
    10. "Ral GTPases regulate exocyst assembly through dual subunit interactions."
      Moskalenko S., Tong C., Rosse C., Mirey G., Formstecher E., Daviet L., Camonis J., White M.A.
      J. Biol. Chem. 278:51743-51748(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EXOC8.
    11. "Geranylgeranyltransferase I inhibitors target RalB to inhibit anchorage-dependent growth and induce apoptosis and RalA to inhibit anchorage-independent growth."
      Falsetti S.C., Wang D.A., Peng H., Carrico D., Cox A.D., Der C.J., Hamilton A.D., Sebti S.M.
      Mol. Cell. Biol. 27:8003-8014(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-203, MUTAGENESIS OF CYS-203 AND LEU-206.
    12. "Distinct roles of RalA and RalB in the progression of cytokinesis are supported by distinct RalGEFs."
      Cascone I., Selimoglu R., Ozdemir C., Del Nery E., Yeaman C., White M., Camonis J.
      EMBO J. 27:2375-2387(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Solution structure and dynamics of the small GTPase RalB in its active conformation: significance for effector protein binding."
      Fenwick R.B., Prasannan S., Campbell L.J., Nietlispach D., Evetts K.A., Camonis J., Mott H.R., Owen D.
      Biochemistry 48:2192-2206(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 12-185 IN COMPLEX WITH GTP ANALOG, INTERACTION WITH EXOC2, MUTAGENESIS OF THR-46 AND GLN-72.
    15. "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 8-185 IN COMPLEX WITH RALBP1, INTERACTION WITH RALBP1.

    Entry informationi

    Entry nameiRALB_HUMAN
    AccessioniPrimary (citable) accession number: P11234
    Secondary accession number(s): B4E040, Q53T32, Q6ZS74
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 155 of the entry and version 1 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, Reference proteome

    Documents

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

    External Data

    Dasty 3