RALGDS

Protein-coding gene in the species Homo sapiens

RALGDS
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1RAX, 2B3A, 2RGF, 3KH0

Identifiers
AliasesRALGDS, RGDS, RGF, RalGEF, ral guanine nucleotide dissociation stimulator
External IDsOMIM: 601619; MGI: 107485; HomoloGene: 4562; GeneCards: RALGDS; OMA:RALGDS - orthologs
Gene location (Human)
Chromosome 9 (human)
Chr.Chromosome 9 (human)[1]
Chromosome 9 (human)
Genomic location for RALGDS
Genomic location for RALGDS
Band9q34.13-q34.2Start133,097,720 bp[1]
End133,149,334 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for RALGDS
Genomic location for RALGDS
Band2|2 A3Start28,403,137 bp[2]
End28,443,093 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right hemisphere of cerebellum

  • pituitary gland

  • anterior pituitary

  • C1 segment

  • skin of abdomen

  • skin of leg

  • substantia nigra

  • granulocyte

  • amygdala

  • caudate nucleus
Top expressed in
  • lactiferous gland

  • entorhinal cortex

  • perirhinal cortex

  • CA3 field

  • genital tubercle

  • spermatid

  • primary visual cortex

  • superior frontal gyrus

  • lip

  • ventricular zone
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • protein binding
  • guanyl-nucleotide exchange factor activity
  • GTPase regulator activity
Cellular component
  • cytosol
  • brush border
  • cytoplasm
  • nucleus
Biological process
  • small GTPase mediated signal transduction
  • Ras protein signal transduction
  • signal transduction
  • regulation of catalytic activity
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5900

19730

Ensembl

ENSG00000160271

ENSMUSG00000026821

UniProt

Q12967

Q03385

RefSeq (mRNA)

NM_006266
NM_001042368
NM_001271774
NM_001271775
NM_001271776

NM_001145834
NM_001145835
NM_001145836
NM_009058

RefSeq (protein)

NP_001035827
NP_001258703
NP_001258704
NP_001258705
NP_006257

NP_001139306
NP_001139307
NP_001139308
NP_033084

Location (UCSC)Chr 9: 133.1 – 133.15 MbChr 2: 28.4 – 28.44 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ral guanine nucleotide dissociation stimulator is a protein that is encoded by the RALGDS gene in humans.[5][6]

Interactions

RALGDS has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000160271 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026821 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Hofer F, Fields S, Schneider C, Martin GS (December 1994). "Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator". Proc Natl Acad Sci U S A. 91 (23): 11089–93. Bibcode:1994PNAS...9111089H. doi:10.1073/pnas.91.23.11089. PMC 45172. PMID 7972015.
  6. ^ "Entrez Gene: RALGDS ral guanine nucleotide dissociation stimulator".
  7. ^ a b Bhattacharya M, Anborgh PH, Babwah AV, Dale LB, Dobransky T, Benovic JL, Feldman RD, Verdi JM, Rylett RJ, Ferguson SS (August 2002). "Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization". Nat. Cell Biol. 4 (8): 547–55. doi:10.1038/ncb821. PMID 12105416. S2CID 20784208.
  8. ^ a b c d Spaargaren M, Bischoff JR (December 1994). "Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap". Proc. Natl. Acad. Sci. U.S.A. 91 (26): 12609–13. Bibcode:1994PNAS...9112609S. doi:10.1073/pnas.91.26.12609. PMC 45488. PMID 7809086.
  9. ^ a b Boettner B, Govek EE, Cross J, Van Aelst L (August 2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proc. Natl. Acad. Sci. U.S.A. 97 (16): 9064–9. Bibcode:2000PNAS...97.9064B. doi:10.1073/pnas.97.16.9064. PMC 16822. PMID 10922060.
  10. ^ a b Li W, Han M, Guan KL (April 2000). "The leucine-rich repeat protein SUR-8 enhances MAP kinase activation and forms a complex with Ras and Raf". Genes Dev. 14 (8): 895–900. doi:10.1101/gad.14.8.895. PMC 316541. PMID 10783161.
  11. ^ Mitin NY, Ramocki MB, Zullo AJ, Der CJ, Konieczny SF, Taparowsky EJ (May 2004). "Identification and characterization of rain, a novel Ras-interacting protein with a unique subcellular localization". J. Biol. Chem. 279 (21): 22353–61. doi:10.1074/jbc.M312867200. PMID 15031288.
  12. ^ Miller MJ, Prigent S, Kupperman E, Rioux L, Park SH, Feramisco JR, White MA, Rutkowski JL, Meinkoth JL (February 1997). "RalGDS functions in Ras- and cAMP-mediated growth stimulation". J. Biol. Chem. 272 (9): 5600–5. doi:10.1074/jbc.272.9.5600. PMID 9038168.
  13. ^ Rodriguez-Viciana P, Warne PH, Khwaja A, Marte BM, Pappin D, Das P, Waterfield MD, Ridley A, Downward J (May 1997). "Role of phosphoinositide 3-OH kinase in cell transformation and control of the actin cytoskeleton by Ras". Cell. 89 (3): 457–67. doi:10.1016/s0092-8674(00)80226-3. PMID 9150145. S2CID 14459536.
  14. ^ Stang S, Bottorff D, Stone JC (June 1997). "Interaction of activated Ras with Raf-1 alone may be sufficient for transformation of rat2 cells". Mol. Cell. Biol. 17 (6): 3047–55. doi:10.1128/MCB.17.6.3047. PMC 232157. PMID 9154803.
  15. ^ Kimmelman A, Tolkacheva T, Lorenzi MV, Osada M, Chan AM (November 1997). "Identification and characterization of R-ras3: a novel member of the RAS gene family with a non-ubiquitous pattern of tissue distribution". Oncogene. 15 (22): 2675–85. doi:10.1038/sj.onc.1201674. PMID 9400994.
  16. ^ Ehrhardt GR, Leslie KB, Lee F, Wieler JS, Schrader JW (October 1999). "M-Ras, a widely expressed 29-kD homologue of p21 Ras: expression of a constitutively active mutant results in factor-independent growth of an interleukin-3-dependent cell line". Blood. 94 (7): 2433–44. doi:10.1182/blood.V94.7.2433.419k31_2433_2444. PMID 10498616. S2CID 40024826.
  17. ^ a b Nancy V, Wolthuis RM, de Tand MF, Janoueix-Lerosey I, Bos JL, de Gunzburg J (March 1999). "Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2". J. Biol. Chem. 274 (13): 8737–45. doi:10.1074/jbc.274.13.8737. PMID 10085114.

Further reading

  • Spaargaren M, Bischoff JR (1995). "Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap". Proc. Natl. Acad. Sci. U.S.A. 91 (26): 12609–13. Bibcode:1994PNAS...9112609S. doi:10.1073/pnas.91.26.12609. PMC 45488. PMID 7809086.
  • Albright CF, Giddings BW, Liu J, Vito M, Weinberg RA (1993). "Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase". EMBO J. 12 (1): 339–47. doi:10.1002/j.1460-2075.1993.tb05662.x. PMC 413211. PMID 8094051.
  • Urano T, Emkey R, Feig LA (1996). "Ral-GTPases mediate a distinct downstream signaling pathway from Ras that facilitates cellular transformation". EMBO J. 15 (4): 810–6. doi:10.1002/j.1460-2075.1996.tb00416.x. PMC 450279. PMID 8631302.
  • Miller MJ, Prigent S, Kupperman E, Rioux L, Park SH, Feramisco JR, White MA, Rutkowski JL, Meinkoth JL (1997). "RalGDS functions in Ras- and cAMP-mediated growth stimulation". J. Biol. Chem. 272 (9): 5600–5. doi:10.1074/jbc.272.9.5600. PMID 9038168.
  • Fukunaga R, Hunter T (1997). "MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates". EMBO J. 16 (8): 1921–33. doi:10.1093/emboj/16.8.1921. PMC 1169795. PMID 9155018.
  • Geyer M, Herrmann C, Wohlgemuth S, Wittinghofer A, Kalbitzer HR (1997). "Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling". Nat. Struct. Biol. 4 (9): 694–9. doi:10.1038/nsb0997-694. hdl:11858/00-001M-0000-0024-AF7E-E. PMID 9302994. S2CID 3189922.
  • Humphrey D, Kwiatkowska J, Henske EP, Haines JL, Halley D, van Slegtenhorst M, Kwiatkowski DJ (1997). "Cloning and evaluation of RALGDS as a candidate for the tuberous sclerosis gene TSC1". Ann. Hum. Genet. 61 (Pt 4): 299–305. doi:10.1046/j.1469-1809.1997.6140299.x. PMID 9365783. S2CID 20453717.
  • Kimmelman A, Tolkacheva T, Lorenzi MV, Osada M, Chan AM (1998). "Identification and characterization of R-ras3: a novel member of the RAS gene family with a non-ubiquitous pattern of tissue distribution". Oncogene. 15 (22): 2675–85. doi:10.1038/sj.onc.1201674. PMID 9400994.
  • Shirouzu M, Morinaka K, Koyama S, Hu CD, Hori-Tamura N, Okada T, Kariya K, Kataoka T, Kikuchi A, Yokoyama S (1998). "Interactions of the amino acid residue at position 31 of the c-Ha-Ras protein with Raf-1 and RalGDS". J. Biol. Chem. 273 (13): 7737–42. doi:10.1074/jbc.273.13.7737. PMID 9516482.
  • Okada S, Matsuda M, Anafi M, Pawson T, Pessin JE (1998). "Insulin regulates the dynamic balance between Ras and Rap1 signaling by coordinating the assembly states of the Grb2-SOS and CrkII-C3G complexes". EMBO J. 17 (9): 2554–65. doi:10.1093/emboj/17.9.2554. PMC 1170597. PMID 9564038.
  • Nancy V, Wolthuis RM, de Tand MF, Janoueix-Lerosey I, Bos JL, de Gunzburg J (1999). "Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2". J. Biol. Chem. 274 (13): 8737–45. doi:10.1074/jbc.274.13.8737. PMID 10085114.
  • Ehrhardt GR, Leslie KB, Lee F, Wieler JS, Schrader JW (1999). "M-Ras, a widely expressed 29-kD homologue of p21 Ras: expression of a constitutively active mutant results in factor-independent growth of an interleukin-3-dependent cell line". Blood. 94 (7): 2433–44. doi:10.1182/blood.V94.7.2433.419k31_2433_2444. PMID 10498616. S2CID 40024826.
  • Shao H, Kadono-Okuda K, Finlin BS, Andres DA (1999). "Biochemical characterization of the Ras-related GTPases Rit and Rin". Arch. Biochem. Biophys. 371 (2): 207–19. doi:10.1006/abbi.1999.1448. PMID 10545207.
  • Zheng Q, Yu L, Zhao Y, Sun X, Dai F, Hu P, Fu Q, Geng Z (2000). "[Refined chromosome assignment of human novel H-RalGDS gene on chromosome 9q34.1 by using radiation hybrid genebridge 4 panel]". Zhonghua Yi Xue Yi Chuan Xue Za Zhi. 17 (1): 1–5. PMID 10653898.
  • Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O (2000). "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (1): 65–73. doi:10.1093/dnares/7.1.65. PMID 10718198.
  • Zheng Q, Yu L, Zhao Y, Zhang H, Fu Q, Mao N, Hu P, Geng Z, Zhao S (2001). "Structure characterization of human RalGDS gene, and the identification of its novel variant". Mol. Biol. Rep. 27 (4): 209–16. doi:10.1023/A:1011043122220. PMID 11455956. S2CID 7866224.
  • Murphy GA, Graham SM, Morita S, Reks SE, Rogers-Graham K, Vojtek A, Kelley GG, Der CJ (2002). "Involvement of phosphatidylinositol 3-kinase, but not RalGDS, in TC21/R-Ras2-mediated transformation". J. Biol. Chem. 277 (12): 9966–75. doi:10.1074/jbc.M109059200. PMID 11788587.
  • Ramírez de Molina A, Penalva V, Lucas L, Lacal JC (2002). "Regulation of choline kinase activity by Ras proteins involves Ral-GDS and PI3K". Oncogene. 21 (6): 937–46. doi:10.1038/sj.onc.1205144. PMID 11840339. S2CID 20848629.
  • Tian X, Rusanescu G, Hou W, Schaffhausen B, Feig LA (2002). "PDK1 mediates growth factor-induced Ral-GEF activation by a kinase-independent mechanism". EMBO J. 21 (6): 1327–38. doi:10.1093/emboj/21.6.1327. PMC 125928. PMID 11889038.
  • v
  • t
  • e
  • 1lfd: CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN COMPLEXED WITH THE RAS-INTERACTING DOMAIN OF RALGDS
    1lfd: CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN COMPLEXED WITH THE RAS-INTERACTING DOMAIN OF RALGDS
  • 1lxd: CRYSTAL STRUCTURE OF THE RAS INTERACTING DOMAIN OF RALGDS, A GUANINE NUCLEOTIDE DISSOCIATION STIMULATOR OF RAL PROTEIN
    1lxd: CRYSTAL STRUCTURE OF THE RAS INTERACTING DOMAIN OF RALGDS, A GUANINE NUCLEOTIDE DISSOCIATION STIMULATOR OF RAL PROTEIN
  • 1rax: RA-DOMAIN OF RAL GUANOSINE-NUCLEOTIDE DISSOCIATION STIMULATOR
    1rax: RA-DOMAIN OF RAL GUANOSINE-NUCLEOTIDE DISSOCIATION STIMULATOR
  • 2b3a: Solution structure of the Ras-binding domain of the Ral Guanosine Dissociation Stimulator
    2b3a: Solution structure of the Ras-binding domain of the Ral Guanosine Dissociation Stimulator
  • 2rgf: RBD OF RAL GUANOSINE-NUCLEOTIDE EXCHANGE FACTOR (PROTEIN), NMR, 10 STRUCTURES
    2rgf: RBD OF RAL GUANOSINE-NUCLEOTIDE EXCHANGE FACTOR (PROTEIN), NMR, 10 STRUCTURES