RANGAP1

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Ran GTPase activating protein 1
Protein RANGAP1 PDB 1z5s.png
PDB rendering based on 1z5s.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols RANGAP1 ; Fug1; RANGAP; SD
External IDs OMIM602362 MGI103071 HomoloGene55700 GeneCards: RANGAP1 Gene
RNA expression pattern
PBB GE RANGAP1 212125 at tn.png
PBB GE RANGAP1 212127 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5905 19387
Ensembl ENSG00000100401 ENSMUSG00000022391
UniProt P46060 P46061
RefSeq (mRNA) NM_001278651 NM_001146174
RefSeq (protein) NP_001265580 NP_001139646
Location (UCSC) Chr 22:
41.64 – 41.68 Mb
Chr 15:
81.7 – 81.73 Mb
PubMed search [1] [2]
For more details on RanGAP proteins in non-human species, see RanGAP.

Ran GTPase-activating protein 1 is an enzyme that in humans is encoded by the RANGAP1 gene.[1][2]

RanGAP1, is a homodimeric 65-kD polypeptide that specifically induces the GTPase activity of RAN, but not of RAS by over 1,000-fold. RanGAP1 is the immediate antagonist of RCC1, a regulator molecule that keeps RAN in the active, GTP-bound state. The RANGAP1 gene encodes a 587-amino acid polypeptide. The sequence is unrelated to that of GTPase activators for other RAS-related proteins, but is 88% identical to Fug1, the murine homolog of yeast Rna1p. RanGAP1 and RCC1 control RAN-dependent transport between the nucleus and cytoplasm. RanGAP1 is a key regulator of the RAN GTP/GDP cycle.[2]

Interactions[edit]

RanGAP1 is a trafficking protein which helps transport other proteins from the cytoplasm to the nucleus. Small ubiqutin-related modifier needs to be associated with it before it can be localized at the nuclear pore Hochstrasser, M. (2000), "All in the Ubiquitin Family", Science, vol. 289, no. 5479, pp. 563–564. RANGAP1 has been shown to interact with Ran (biology)[3][4][5] and UBE2I.[6][7][8]

References[edit]

  1. ^ Bischoff FR, Krebber H, Kempf T, Hermes I, Ponstingl H (Apr 1995). "Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport". Proc Natl Acad Sci U S A 92 (5): 1749–53. doi:10.1073/pnas.92.5.1749. PMC 42597. PMID 7878053. 
  2. ^ a b "Entrez Gene: RANGAP1 Ran GTPase activating protein 1". 
  3. ^ Hillig, R C; Renault L; Vetter I R; Drell T; Wittinghofer A; Becker J (Jun 1999). "The crystal structure of rna1p: a new fold for a GTPase-activating protein". Mol. Cell (UNITED STATES) 3 (6): 781–91. doi:10.1016/S1097-2765(01)80010-1. ISSN 1097-2765. PMID 10394366. 
  4. ^ Becker, J; Melchior F; Gerke V; Bischoff F R; Ponstingl H; Wittinghofer A (May 1995). "RNA1 encodes a GTPase-activating protein specific for Gsp1p, the Ran/TC4 homologue of Saccharomyces cerevisiae". J. Biol. Chem. (UNITED STATES) 270 (20): 11860–5. doi:10.1074/jbc.270.20.11860. ISSN 0021-9258. PMID 7744835. 
  5. ^ Bischoff, F R; Klebe C; Kretschmer J; Wittinghofer A; Ponstingl H (Mar 1994). "RanGAP1 induces GTPase activity of nuclear Ras-related Ran". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 91 (7): 2587–91. doi:10.1073/pnas.91.7.2587. ISSN 0027-8424. PMC 43414. PMID 8146159. 
  6. ^ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. (England) 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. 
  7. ^ Tatham, Michael H; Kim Suhkmann; Yu Bin; Jaffray Ellis; Song Jing; Zheng Jian; Rodriguez Manuel S; Hay Ronald T; Chen Yuan (Aug 2003). "Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation". Biochemistry (United States) 42 (33): 9959–69. doi:10.1021/bi0345283. ISSN 0006-2960. PMID 12924945. 
  8. ^ Knipscheer, Puck; Flotho Annette; Klug Helene; Olsen Jesper V; van Dijk Willem J; Fish Alexander; Johnson Erica S; Mann Matthias; Sixma Titia K; Pichler Andrea (Aug 2008). "Ubc9 sumoylation regulates SUMO target discrimination". Mol. Cell (United States) 31 (3): 371–82. doi:10.1016/j.molcel.2008.05.022. PMID 18691969. 

Further reading[edit]