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Identification
HMDB Protein ID HMDBP08519
Secondary Accession Numbers
  • 14231
Name Ran-binding protein 9
Synonyms
  1. BPM-L
  2. BPM90
  3. Ran-binding protein M
  4. RanBP7
  5. RanBP9
  6. RanBPM
Gene Name RANBP9
Protein Type Unknown
Biological Properties
General Function Cell cycle control, cell division, chromosome partitioning
Specific Function May act as an adapter protein to couple membrane receptors to intracellular signaling pathways. May be involved in signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET signaling by recruiting Sos and activating the Ras pathway. Involved in activation of androgen and glucocorticoid receptor in the presence of their cognate hormones. Stabilizes TP73 isoform Alpha, probably by inhibiting its ubiquitination, and increases its proapoptotic activity. Inhibits the kinase activity of DYRK1A and DYRK1B. Inhibits FMR1 binding to RNA
Pathways Not Available
Reactions Not Available
GO Classification Not Available
Cellular Location
  1. Nucleus
  2. Cytoplasm
Gene Properties
Chromosome Location Chromosome:6
Locus 6p23
SNPs RANBP9
Gene Sequence
>2190 bp
ATGTCCGGGCAGCCGCCGCCGCCGCCGCCGCAGCAGCAGCAACAGCAGCAGCAGCTGTCG
CCGCCACCGCCGGCGGCCTTGGCCCCAGTCTCCGGAGTCGTCCTGCCGGCGCCCCCGGCC
GTCAGCGCCGGCTCTTCTCCGGCCGGCTCGCCCGGCGGCGGTGCGGGCGGCGAAGGCTTA
GGGGCCGCGGCGGCCGCCCTGCTCCTCCACCCTCCGCCGCCGCCGCCCCCGGCCACCGCG
GCCCCGCCGCCCCCGCCGCCGCCCCCGCCTCCCCCTGCCTCAGCGGCTGCCCCCGCCAGC
GGGCCGCCCGCTCCCCCGGGCCTTGCAGCGGGCCCCGGCCCGGCTGGAGGAGCCCCGACC
CCAGCTCTGGTGGCGGGCAGCAGCGCCGCGGCCCCCTTCCCTCACGGGGACTCGGCCCTG
AACGAGCAGGAGAAGGAGTTGCAGCGGCGGCTGAAGCGTCTCTACCCGGCCGTGGACGAA
CAAGAGACGCCGCTGCCTCGGTCCTGGAGCCCGAAGGACAAGTTCAGCTACATCGGCCTC
TCTCAGAACAACCTGCGGGTGCACTACAAAGGTCATGGCAAAACCCCAAAAGATGCCGCG
TCAGTTCGAGCCACGCATCCAATACCAGCAGCCTGTGGGATTTATTATTTTGAAGTAAAA
ATTGTCAGTAAGGGAAGAGATGGTTACATGGGAATTGGTCTTTCTGCTCAAGGTGTGAAC
ATGAATAGACTACCAGGTTGGGATAAGCATTCATATGGTTACCATGGGGATGATGGACAT
TCGTTTTGTTCTTCTGGAACTGGACAACCTTATGGACCAACTTTCACTACTGGTGATGTC
ATTGGCTGTTGTGTTAATCTTATCAACAATACCTGCTTTTACACCAAGAATGGACATAGT
TTAGGTATTGCTTTCACTGACCTACCGCCAAATTTGTATCCTACTGTGGGGCTTCAAACA
CCAGGAGAAGTGGTCGATGCCAATTTTGGGCAACATCCTTTCGTGTTTGATATAGAAGAC
TATATGCGGGAGTGGAGAACCAAAATCCAGGCACAGATAGATCGATTTCCTATCGGAGAT
CGAGAAGGAGAATGGCAGACCATGATACAAAAAATGGTTTCATCTTATTTAGTCCACCAT
GGGTACTGTGCCACAGCAGAGGCCTTTGCCAGATCTACAGACCAGACCGTTCTAGAAGAA
TTAGCTTCCATTAAGAATAGACAAAGAATTCAGAAATTGGTATTAGCAGGAAGAATGGGA
GAAGCCATTGAAACAACACAACAGTTATACCCAAGTTTACTTGAAAGAAATCCTAATCTC
CTTTTCACATTAAAAGTGCGTCAGTTTATAGAAATGGTGAATGGTACAGATAGTGAAGTA
CGATGTTTGGGAGGCCGAAGTCCAAAGTCTCAAGACAGTTATCCTGTTAGTCCTCGACCT
TTTAGTAGTCCAAGTATGAGCCCCAGCCATGGAATGAATATCCACAATTTAGCATCAGGC
AAAGGAAGCACCGCACATTTTTCAGGTTTTGAAAGTTGTAGTAATGGTGTAATATCAAAT
AAAGCACATCAATCATATTGCCATAGTAATAAACACCAGTCATCCAACTTGAATGTACCA
GAACTAAACAGTATAAATATGTCAAGATCACAGCAAGTTAATAACTTCACCAGTAATGAT
GTAGACATGGAAACAGATCACTACTCCAATGGAGTTGGAGAAACTTCATCCAATGGTTTC
CTAAATGGTAGCTCTAAACATGACCACGAAATGGAAGATTGTGACACCGAAATGGAAGTT
GATTCAAGTCAGTTGAGACGCCAGTTGTGTGGAGGAAGTCAGGCCGCCATAGAAAGAATG
ATCCACTTTGGACGAGAGCTGCAAGCAATGAGTGAACAGCTAAGGAGAGACTGTGGCAAG
AACACTGCAAACAAAAAAATGTTGAAGGATGCATTCAGTCTACTAGCATATTCAGATCCC
TGGAACAGCCCAGTTGGAAATCAGCTTGACCCGATTCAGAGAGAACCTGTGTGCTCAGCT
CTTAACAGTGCAATATTAGAAACCCACAATCTGCCAAAGCAACCTCCACTTGCCCTAGCA
ATGGGACAGGCCACACAATGTCTAGGACTGATGGCTCGATCAGGAATTGGATCCTGCGCA
TTTGCCACAGTGGAAGACTACCTACATTAG
Protein Properties
Number of Residues 729
Molecular Weight 77846.7
Theoretical pI 6.78
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Ran-binding protein 9
MSGQPPPPPPQQQQQQQQLSPPPPAALAPVSGVVLPAPPAVSAGSSPAGSPGGGAGGEGL
GAAAAALLLHPPPPPPPATAAPPPPPPPPPPPASAAAPASGPPAPPGLAAGPGPAGGAPT
PALVAGSSAAAPFPHGDSALNEQEKELQRRLKRLYPAVDEQETPLPRSWSPKDKFSYIGL
SQNNLRVHYKGHGKTPKDAASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVN
MNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHS
LGIAFTDLPPNLYPTVGLQTPGEVVDANFGQHPFVFDIEDYMREWRTKIQAQIDRFPIGD
REGEWQTMIQKMVSSYLVHHGYCATAEAFARSTDQTVLEELASIKNRQRIQKLVLAGRMG
EAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSEVRCLGGRSPKSQDSYPVSPRP
FSSPSMSPSHGMNIHNLASGKGSTAHFSGFESCSNGVISNKAHQSYCHSNKHQSSNLNVP
ELNSINMSRSQQVNNFTSNDVDMETDHYSNGVGETSSNGFLNGSSKHDHEMEDCDTEMEV
DSSQLRRQLCGGSQAAIERMIHFGRELQAMSEQLRRDCGKNTANKKMLKDAFSLLAYSDP
WNSPVGNQLDPIQREPVCSALNSAILETHNLPKQPPLALAMGQATQCLGLMARSGIGSCA
FATVEDYLH
GenBank ID Protein 39812378
UniProtKB/Swiss-Prot ID Q96S59
UniProtKB/Swiss-Prot Entry Name RANB9_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_005493.2
GeneCard ID RANBP9
GenAtlas ID RANBP9
HGNC ID HGNC:13727
References
General References
  1. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed:14574404 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. 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. [PubMed:19608861 ]
  4. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed:17525332 ]
  5. Zou Y, Lim S, Lee K, Deng X, Friedman E: Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M. J Biol Chem. 2003 Dec 5;278(49):49573-81. Epub 2003 Sep 18. [PubMed:14500717 ]
  6. Wang D, Li Z, Messing EM, Wu G: Activation of Ras/Erk pathway by a novel MET-interacting protein RanBPM. J Biol Chem. 2002 Sep 27;277(39):36216-22. Epub 2002 Jul 29. [PubMed:12147692 ]
  7. Wang D, Li Z, Schoen SR, Messing EM, Wu G: A novel MET-interacting protein shares high sequence similarity with RanBPM, but fails to stimulate MET-induced Ras/Erk signaling. Biochem Biophys Res Commun. 2004 Jan 9;313(2):320-6. [PubMed:14684163 ]
  8. Mikolajczyk M, Shi J, Vaillancourt RR, Sachs NA, Nelson M: The cyclin-dependent kinase 11(p46) isoform interacts with RanBPM. Biochem Biophys Res Commun. 2003 Oct 10;310(1):14-8. [PubMed:14511641 ]
  9. Rao MA, Cheng H, Quayle AN, Nishitani H, Nelson CC, Rennie PS: RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor. J Biol Chem. 2002 Dec 13;277(50):48020-7. Epub 2002 Oct 1. [PubMed:12361945 ]
  10. Lutz W, Frank EM, Craig TA, Thompson R, Venters RA, Kojetin D, Cavanagh J, Kumar R: Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy. Biochem Biophys Res Commun. 2003 Apr 18;303(4):1186-92. [PubMed:12684061 ]
  11. Denti S, Sirri A, Cheli A, Rogge L, Innamorati G, Putignano S, Fabbri M, Pardi R, Bianchi E: RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1. J Biol Chem. 2004 Mar 26;279(13):13027-34. Epub 2004 Jan 13. [PubMed:14722085 ]
  12. Nishitani H, Hirose E, Uchimura Y, Nakamura M, Umeda M, Nishii K, Mori N, Nishimoto T: Full-sized RanBPM cDNA encodes a protein possessing a long stretch of proline and glutamine within the N-terminal region, comprising a large protein complex. Gene. 2001 Jul 11;272(1-2):25-33. [PubMed:11470507 ]
  13. Nakamura M, Masuda H, Horii J, Kuma Ki, Yokoyama N, Ohba T, Nishitani H, Miyata T, Tanaka M, Nishimoto T: When overexpressed, a novel centrosomal protein, RanBPM, causes ectopic microtubule nucleation similar to gamma-tubulin. J Cell Biol. 1998 Nov 16;143(4):1041-52. [PubMed:9817760 ]
  14. Wang Y, Marion Schneider E, Li X, Duttenhofer I, Debatin K, Hug H: HIPK2 associates with RanBPM. Biochem Biophys Res Commun. 2002 Sep 13;297(1):148-53. [PubMed:12220523 ]
  15. Ideguchi H, Ueda A, Tanaka M, Yang J, Tsuji T, Ohno S, Hagiwara E, Aoki A, Ishigatsubo Y: Structural and functional characterization of the USP11 deubiquitinating enzyme, which interacts with the RanGTP-associated protein RanBPM. Biochem J. 2002 Oct 1;367(Pt 1):87-95. [PubMed:12084015 ]
  16. Emberley ED, Gietz RD, Campbell JD, HayGlass KT, Murphy LC, Watson PH: RanBPM interacts with psoriasin in vitro and their expression correlates with specific clinical features in vivo in breast cancer. BMC Cancer. 2002 Nov 6;2:28. [PubMed:12421467 ]
  17. Umeda M, Nishitani H, Nishimoto T: A novel nuclear protein, Twa1, and Muskelin comprise a complex with RanBPM. Gene. 2003 Jan 16;303:47-54. [PubMed:12559565 ]
  18. Menon RP, Gibson TJ, Pastore A: The C terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre. J Mol Biol. 2004 Oct 8;343(1):43-53. [PubMed:15381419 ]
  19. Kramer S, Ozaki T, Miyazaki K, Kato C, Hanamoto T, Nakagawara A: Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells. Oncogene. 2005 Jan 27;24(5):938-44. [PubMed:15558019 ]