Ran-specific GTPase-activating protein

Details

Name
Ran-specific GTPase-activating protein
Synonyms
  • Ran-binding protein 1
  • RanBP1
Gene Name
RANBP1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0049671|Ran-specific GTPase-activating protein
MAAAKDTHEDHDTSTENTDESNHDPQFEPIVSLPEQEIKTLEEDEEELFKMRAKLFRFAS
ENDLPEWKERGTGDVKLLKHKEKGAIRLLMRRDKTLKICANHYITPMMELKPNAGSDRAW
VWNTHADFADECPKPELLAIRFLNAENAQKFKTKFEECRKEIEEREKKAGSGKNDHAEKV
AEKLEALSVKEETKEDAEEKQ
Number of residues
201
Molecular Weight
23309.92
Theoretical pI
Not Available
GO Classification
Functions
cadherin binding / GDP-dissociation inhibitor activity / GTPase activator activity / Ran GTPase binding
Processes
G1/S transition of mitotic cell cycle / positive regulation of mitotic centrosome separation / protein import into nucleus / RNA export from nucleus / signal transduction / spindle organization / ubiquitin-dependent protein catabolic process / viral process
Components
centrosome / cytoplasm / cytosol / nuclear envelope / nucleus
General Function
Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.
Specific Function
Cadherin binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0049672|Ran-specific GTPase-activating protein (RANBP1)
ATGGCGGCCGCCAAGGACACTCATGAGGACCATGATACTTCCACTGAGAATACAGACGAG
TCCAACCATGACCCTCAGTTTGAGCCAATAGTTTCTCTTCCTGAGCAAGAAATTAAAACA
CTGGAAGAAGATGAAGAGGAACTTTTTAAAATGCGGGCAAAACTGTTCCGATTTGCCTCT
GAGAACGATCTCCCAGAATGGAAGGAGCGAGGCACTGGTGACGTCAAGCTCCTGAAGCAC
AAGGAGAAAGGGGCCATCCGCCTCCTCATGCGGAGGGACAAGACCCTGAAGATCTGTGCC
AACCACTACATCACGCCGATGATGGAGCTGAAGCCCAACGCAGGTAGCGACCGTGCCTGG
GTCTGGAACACCCACGCTGACTTCGCCGACGAGTGCCCCAAGCCAGAGCTGCTGGCCATC
CGCTTCCTGAATGCTGAGAATGCACAGAAATTCAAAACAAAGTTTGAAGAATGCAGGAAA
GAGATCGAAGAGAGAGAAAAGAAAGCAGGATCAGGCAAAAATGATCATGCCGAAAAAGTG
GCGGAAAAGCTAGAAGCTCTCTCGGTGAAGGAGGAGACCAAGGAGGATGCTGAGGAGAAG
CAATAA
Chromosome Location
22
Locus
22q11.21
External Identifiers
ResourceLink
UniProtKB IDP43487
UniProtKB Entry NameRANG_HUMAN
HGNC IDHGNC:9847
General References
  1. Bischoff FR, Krebber H, Smirnova E, Dong W, Ponstingl H: Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1. EMBO J. 1995 Feb 15;14(4):705-15. [Article]
  2. Hayashi N, Yokoyama N, Seki T, Azuma Y, Ohba T, Nishimoto T: RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits RCC1 via Ran/TC4. Mol Gen Genet. 1995 Jun 25;247(6):661-9. [Article]
  3. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [Article]
  4. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [Article]
  5. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [Article]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
  7. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [Article]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [Article]
  9. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
  10. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  11. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. [Article]
  12. Zhou H, Di Palma S, Preisinger C, Peng M, Polat AN, Heck AJ, Mohammed S: Toward a comprehensive characterization of a human cancer cell phosphoproteome. J Proteome Res. 2013 Jan 4;12(1):260-71. doi: 10.1021/pr300630k. Epub 2012 Dec 18. [Article]
  13. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  14. Hendriks IA, D'Souza RC, Yang B, Verlaan-de Vries M, Mann M, Vertegaal AC: Uncovering global SUMOylation signaling networks in a site-specific manner. Nat Struct Mol Biol. 2014 Oct;21(10):927-36. doi: 10.1038/nsmb.2890. Epub 2014 Sep 14. [Article]
  15. Impens F, Radoshevich L, Cossart P, Ribet D: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli. Proc Natl Acad Sci U S A. 2014 Aug 26;111(34):12432-7. doi: 10.1073/pnas.1413825111. Epub 2014 Aug 11. [Article]
  16. Hendriks IA, Treffers LW, Verlaan-de Vries M, Olsen JV, Vertegaal AC: SUMO-2 Orchestrates Chromatin Modifiers in Response to DNA Damage. Cell Rep. 2015 Mar 10. pii: S2211-1247(15)00179-5. doi: 10.1016/j.celrep.2015.02.033. [Article]
  17. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB09130Copperapproved, investigationalunknownDetails
DB12695Phenethyl IsothiocyanateinvestigationalunknownDetails