RANB9_HUMAN
ID RANB9_HUMAN Reviewed; 729 AA.
AC Q96S59; A0PJA2; B2R8E1; O94764; Q6P3T7; Q7LBR2; Q7Z7F9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Ran-binding protein 9;
DE Short=RanBP9;
DE AltName: Full=BPM-L;
DE AltName: Full=BPM90;
DE AltName: Full=Ran-binding protein M;
DE Short=RanBPM {ECO:0000303|PubMed:11470507, ECO:0000303|PubMed:17467196};
DE AltName: Full=RanBP7;
GN Name=RANBP9; Synonyms=RANBPM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH RAN.
RX PubMed=11470507; DOI=10.1016/s0378-1119(01)00553-4;
RA Nishitani H., Hirose E., Uchimura Y., Nakamura M., Umeda M., Nishii K.,
RA Mori N., Nishimoto T.;
RT "Full-sized RanBPM cDNA encodes a protein possessing a long stretch of
RT proline and glutamine within the N-terminal region, comprising a large
RT protein complex.";
RL Gene 272:25-33(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lymph, Spinal ganglion, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 85-729 (ISOFORM 1), AND INTERACTION WITH RAN.
RX PubMed=9817760; DOI=10.1083/jcb.143.4.1041;
RA Nakamura M., Masuda H., Horii J., Kuma K., Yokoyama N., Ohba T.,
RA Nishitani H., Miyata T., Tanaka M., Nishimoto T.;
RT "When overexpressed, a novel centrosomal protein, RanBPM, causes ectopic
RT microtubule nucleation similar to gamma-tubulin.";
RL J. Cell Biol. 143:1041-1052(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 136-729 (ISOFORM 1), INTERACTION WITH HIPK2,
RP AND SUBCELLULAR LOCATION.
RX PubMed=12220523; DOI=10.1016/s0006-291x(02)02020-x;
RA Wang Y., Marion Schneider E., Li X., Duttenhoefer I., Debatin K.-M.,
RA Hug H.;
RT "HIPK2 associates with RanBPM.";
RL Biochem. Biophys. Res. Commun. 297:148-153(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 148-729 (ISOFORM 1), FUNCTION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH AR.
RC TISSUE=Prostate;
RX PubMed=12361945; DOI=10.1074/jbc.m209741200;
RA Rao M.A., Cheng H., Quayle A.N., Nishitani H., Nelson C.C., Rennie P.S.;
RT "RanBPM, a nuclear protein that interacts with and regulates
RT transcriptional activity of androgen receptor and glucocorticoid
RT receptor.";
RL J. Biol. Chem. 277:48020-48027(2002).
RN [8]
RP INTERACTION WITH USP11, AND UBIQUITINATION.
RX PubMed=12084015; DOI=10.1042/bj20011851;
RA Ideguchi H., Ueda A., Tanaka M., Yang J., Tsuji T., Ohno S., Hagiwara E.,
RA Aoki A., Ishigatsubo Y.;
RT "Structural and functional characterization of the USP11 deubiquitinating
RT enzyme, which interacts with the RanGTP-associated protein RanBPM.";
RL Biochem. J. 367:87-95(2002).
RN [9]
RP INTERACTION WITH S100A7.
RX PubMed=12421467; DOI=10.1186/1471-2407-2-28;
RA Emberley E.D., Gietz R.D., Campbell J.D., Hayglass K.T., Murphy L.C.,
RA Watson P.H.;
RT "RanBPM interacts with psoriasin in vitro and their expression correlates
RT with specific clinical features in vivo in breast cancer.";
RL BMC Cancer 2:28-28(2002).
RN [10]
RP FUNCTION IN RAS SIGNALING, INTERACTION WITH MET AND SOS, AND TISSUE
RP SPECIFICITY.
RX PubMed=12147692; DOI=10.1074/jbc.m205111200;
RA Wang D., Li Z., Messing E.M., Wu G.;
RT "Activation of Ras/Erk pathway by a novel MET-interacting protein RanBPM.";
RL J. Biol. Chem. 277:36216-36222(2002).
RN [11]
RP INTERACTION WITH CALB1.
RX PubMed=12684061; DOI=10.1016/s0006-291x(03)00499-6;
RA Lutz W., Frank E.M., Craig T.A., Thompson R., Venters R.A., Kojetin D.,
RA Cavanagh J., Kumar R.;
RT "Calbindin D28K interacts with Ran-binding protein M: identification of
RT interacting domains by NMR spectroscopy.";
RL Biochem. Biophys. Res. Commun. 303:1186-1192(2003).
RN [12]
RP INTERACTION WITH CDC2L1, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=14511641; DOI=10.1016/j.bbrc.2003.08.116;
RA Mikolajczyk M., Shi J., Vaillancourt R.R., Sachs N.A., Nelson M.;
RT "The cyclin-dependent kinase 11(p46) isoform interacts with RanBPM.";
RL Biochem. Biophys. Res. Commun. 310:14-18(2003).
RN [13]
RP INTERACTION WITH MKLN1 AND GID8, AND IDENTIFICATION IN A COMPLEX WITH MKLN1
RP AND GID8.
RX PubMed=12559565; DOI=10.1016/s0378-1119(02)01153-8;
RA Umeda M., Nishitani H., Nishimoto T.;
RT "A novel nuclear protein, Twa1, and Muskelin comprise a complex with
RT RanBPM.";
RL Gene 303:47-54(2003).
RN [14]
RP FUNCTION, INTERACTION WITH DYRK1A AND DYRK1B, AND IDENTIFICATION IN A
RP COMPLEX WITH RAN; DYRK1B AND COPS5.
RX PubMed=14500717; DOI=10.1074/jbc.m307556200;
RA Zou Y., Lim S., Lee K., Deng X., Friedman E.;
RT "Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell
RT migration and is negatively regulated by the Met adaptor Ran-binding
RT protein M.";
RL J. Biol. Chem. 278:49573-49581(2003).
RN [15]
RP INTERACTION WITH RAN AND MET.
RX PubMed=14684163; DOI=10.1016/j.bbrc.2003.11.124;
RA Wang D., Li Z., Schoen S.R., Messing E.M., Wu G.;
RT "A novel MET-interacting protein shares high sequence similarity with
RT RanBPM, but fails to stimulate MET-induced Ras/Erk signaling.";
RL Biochem. Biophys. Res. Commun. 313:320-326(2004).
RN [16]
RP FUNCTION, INTERACTION WITH ITGB1 AND ITGB2, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION.
RX PubMed=14722085; DOI=10.1074/jbc.m313515200;
RA Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S.,
RA Fabbri M., Pardi R., Bianchi E.;
RT "RanBPM is a phosphoprotein that associates with the plasma membrane and
RT interacts with the integrin LFA-1.";
RL J. Biol. Chem. 279:13027-13034(2004).
RN [17]
RP FUNCTION, INTERACTION WITH FMR1, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15381419; DOI=10.1016/j.jmb.2004.08.024;
RA Menon R.P., Gibson T.J., Pastore A.;
RT "The C-terminus of fragile X mental retardation protein interacts with the
RT multi-domain Ran-binding protein in the microtubule-organising centre.";
RL J. Mol. Biol. 343:43-53(2004).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TP73.
RX PubMed=15558019; DOI=10.1038/sj.onc.1208257;
RA Kramer S., Ozaki T., Miyazaki K., Kato C., Hanamoto T., Nakagawara A.;
RT "Protein stability and function of p73 are modulated by a physical
RT interaction with RanBPM in mammalian cultured cells.";
RL Oncogene 24:938-944(2005).
RN [19]
RP IDENTIFICATION IN THE CTLH COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=17467196; DOI=10.1016/j.gene.2007.02.032;
RA Kobayashi N., Yang J., Ueda A., Suzuki T., Tomaru K., Takeno M., Okuda K.,
RA Ishigatsubo Y.;
RT "RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat proteins
RT ARMC8alpha and ARMC8beta are components of the CTLH complex.";
RL Gene 396:236-247(2007).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [21]
RP FUNCTION, INTERACTION WITH RANBP10, AND SUBCELLULAR LOCATION.
RX PubMed=18222118; DOI=10.1016/j.bbrc.2008.01.072;
RA Harada N., Yokoyama T., Yamaji R., Nakano Y., Inui H.;
RT "RanBP10 acts as a novel coactivator for the androgen receptor.";
RL Biochem. Biophys. Res. Commun. 368:121-125(2008).
RN [22]
RP FUNCTION, AND INTERACTION WITH MKLN1.
RX PubMed=18710924; DOI=10.1083/jcb.200801133;
RA Valiyaveettil M., Bentley A.A., Gursahaney P., Hussien R., Chakravarti R.,
RA Kureishy N., Prag S., Adams J.C.;
RT "Novel role of the muskelin-RanBP9 complex as a nucleocytoplasmic mediator
RT of cell morphology regulation.";
RL J. Cell Biol. 182:727-739(2008).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-405, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [25]
RP INTERACTION WITH YPEL5.
RX PubMed=20580816; DOI=10.1016/j.ygeno.2010.05.003;
RA Hosono K., Noda S., Shimizu A., Nakanishi N., Ohtsubo M., Shimizu N.,
RA Minoshima S.;
RT "YPEL5 protein of the YPEL gene family is involved in the cell cycle
RT progression by interacting with two distinct proteins RanBPM and RanBP10.";
RL Genomics 96:102-111(2010).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [29]
RP SUBCELLULAR LOCATION.
RX PubMed=24143168; DOI=10.1371/journal.pone.0075217;
RA Francis O., Han F., Adams J.C.;
RT "Molecular phylogeny of a RING E3 ubiquitin ligase, conserved in eukaryotic
RT cells and dominated by homologous components, the muskelin/RanBPM/CTLH
RT complex.";
RL PLoS ONE 8:E75217-E75217(2013).
RN [30]
RP FUNCTION, IDENTIFICATION IN THE CTLH COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=29911972; DOI=10.7554/elife.35528;
RA Lampert F., Stafa D., Goga A., Soste M.V., Gilberto S., Olieric N.,
RA Picotti P., Stoffel M., Peter M.;
RT "The multi-subunit GID/CTLH E3 ligase promotes proliferation and targets
RT the transcription factor Hbp1 for degradation.";
RL Elife 7:0-0(2018).
RN [31] {ECO:0007744|PDB:5JI7, ECO:0007744|PDB:5JI9, ECO:0007744|PDB:5JIU}
RP X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) OF 108-350 IN COMPLEX WITH DDX4
RP PEPTIDE, AND INTERACTION WITH DDX4.
RX PubMed=27622290; DOI=10.1016/j.jmb.2016.09.004;
RA Hong S.K., Kim K.H., Song E.J., Kim E.E.;
RT "Structural Basis for the Interaction between the IUS-SPRY Domain of RanBPM
RT and DDX-4 in Germ Cell Development.";
RL J. Mol. Biol. 428:4330-4344(2016).
CC -!- FUNCTION: May act as scaffolding protein, and as adapter protein to
CC couple membrane receptors to intracellular signaling pathways
CC (Probable). Acts as a mediator of cell spreading and actin cytoskeleton
CC rearrangement (PubMed:18710924). Core component of the CTLH E3
CC ubiquitin-protein ligase complex that selectively accepts ubiquitin
CC from UBE2H and mediates ubiquitination and subsequent proteasomal
CC degradation of the transcription factor HBP1 (PubMed:29911972). May be
CC involved in signaling of ITGB2/LFA-1 and other integrins
CC (PubMed:14722085). Enhances HGF-MET signaling by recruiting Sos and
CC activating the Ras pathway (PubMed:12147692). Enhances
CC dihydrotestosterone-induced transactivation activity of AR, as well as
CC dexamethasone-induced transactivation activity of NR3C1, but not affect
CC estrogen-induced transactivation (PubMed:12361945, PubMed:18222118).
CC Stabilizes TP73 isoform Alpha, probably by inhibiting its
CC ubiquitination, and increases its proapoptotic activity
CC (PubMed:15558019). Inhibits the kinase activity of DYRK1A and DYRK1B.
CC Inhibits FMR1 binding to RNA. {ECO:0000269|PubMed:12147692,
CC ECO:0000269|PubMed:12361945, ECO:0000269|PubMed:14500717,
CC ECO:0000269|PubMed:14722085, ECO:0000269|PubMed:15381419,
CC ECO:0000269|PubMed:15558019, ECO:0000269|PubMed:18222118,
CC ECO:0000269|PubMed:18710924, ECO:0000269|PubMed:29911972, ECO:0000305}.
CC -!- SUBUNIT: Part of a complex consisting of RANBP9, MKLN1 and GID8
CC (PubMed:12559565). Identified in the CTLH complex that contains GID4,
CC RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its
CC paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5 (PubMed:17467196,
CC PubMed:29911972). Within this complex, MAEA, RMND5A (or alternatively
CC its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the
CC catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles
CC (PubMed:29911972). Interacts with GTP-bound Ran, AR, CDC2L1/p110C,
CC CALB1, S100A7, USP11, MKLN1, SOS1 or SOS2, GID8, and FMR1
CC (PubMed:11470507, PubMed:9817760, PubMed:12361945, PubMed:12084015,
CC PubMed:12421467, PubMed:12147692, PubMed:12684061, PubMed:14511641,
CC PubMed:14684163, PubMed:15381419, PubMed:18710924). Interacts with the
CC Dyrk kinases HIPK2, DYRK1A, and DYRK1B (PubMed:12220523,
CC PubMed:14500717). Interacts with TP73 isoform Alpha but not with TP53
CC (PubMed:15558019). Interacts with the HGF receptor MET and the
CC integrins ITGB1 and ITGB2, but not with ITGAL (PubMed:14722085). Part
CC of a complex consisting of RANBP9, RAN, DYRK1B and COPS5
CC (PubMed:14500717). Directly interacts with RANBP10 (PubMed:18222118).
CC Interacts with YPEL5 (PubMed:20580816). Interacts with DDX4
CC (PubMed:27622290). Interacts with NGFR (By similarity). Interacts with
CC TEX19 (By similarity). {ECO:0000250|UniProtKB:P69566,
CC ECO:0000269|PubMed:11470507, ECO:0000269|PubMed:12084015,
CC ECO:0000269|PubMed:12147692, ECO:0000269|PubMed:12220523,
CC ECO:0000269|PubMed:12361945, ECO:0000269|PubMed:12421467,
CC ECO:0000269|PubMed:12559565, ECO:0000269|PubMed:12684061,
CC ECO:0000269|PubMed:14500717, ECO:0000269|PubMed:14511641,
CC ECO:0000269|PubMed:14684163, ECO:0000269|PubMed:14722085,
CC ECO:0000269|PubMed:15381419, ECO:0000269|PubMed:15558019,
CC ECO:0000269|PubMed:17467196, ECO:0000269|PubMed:18222118,
CC ECO:0000269|PubMed:18710924, ECO:0000269|PubMed:20580816,
CC ECO:0000269|PubMed:27622290, ECO:0000269|PubMed:29911972,
CC ECO:0000269|PubMed:9817760}.
CC -!- INTERACTION:
CC Q96S59; P05067: APP; NbExp=3; IntAct=EBI-636085, EBI-77613;
CC Q96S59; Q9NRI5: DISC1; NbExp=7; IntAct=EBI-636085, EBI-529989;
CC Q96S59; Q9Y463: DYRK1B; NbExp=4; IntAct=EBI-636085, EBI-634187;
CC Q96S59; P49961: ENTPD1; NbExp=5; IntAct=EBI-636085, EBI-8074749;
CC Q96S59; P35372: OPRM1; NbExp=5; IntAct=EBI-636085, EBI-2624570;
CC Q96S59; P36873-2: PPP1CC; NbExp=3; IntAct=EBI-636085, EBI-3964623;
CC Q96S59; P31151: S100A7; NbExp=3; IntAct=EBI-636085, EBI-357520;
CC Q96S59; P31421: Grm2; Xeno; NbExp=4; IntAct=EBI-636085, EBI-7090147;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11470507,
CC ECO:0000269|PubMed:14511641, ECO:0000269|PubMed:15381419,
CC ECO:0000269|PubMed:15558019, ECO:0000269|PubMed:17467196,
CC ECO:0000269|PubMed:18222118, ECO:0000269|PubMed:24143168}. Nucleus
CC {ECO:0000269|PubMed:11470507, ECO:0000269|PubMed:14511641,
CC ECO:0000269|PubMed:15381419, ECO:0000269|PubMed:15558019,
CC ECO:0000269|PubMed:17467196, ECO:0000269|PubMed:18222118}. Cell
CC membrane {ECO:0000269|PubMed:14722085}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14722085}. Note=The unphosphorylated form is
CC predominantly cytoplasmic. A phosphorylated form is associated with the
CC plasma membrane. {ECO:0000269|PubMed:14722085}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96S59-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96S59-2; Sequence=VSP_013175;
CC Name=3;
CC IsoId=Q96S59-3; Sequence=VSP_056049;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC testes, placenta, heart, and muscle, and lowest levels in lung. Within
CC the brain, expressed predominantly by neurons in the gray matter of
CC cortex, the granular layer of cerebellum and the Purkinje cells.
CC {ECO:0000269|PubMed:12147692, ECO:0000269|PubMed:12361945,
CC ECO:0000269|PubMed:15381419}.
CC -!- DOMAIN: The SPRY domain mediates the interaction with MET, AR, and
CC CDC2L1.
CC -!- PTM: Phosphorylated in response to stress. Can be phosphorylated by the
CC cleaved p110 form of CDC2L1 (p110C). {ECO:0000269|PubMed:14511641,
CC ECO:0000269|PubMed:14722085}.
CC -!- PTM: Ubiquitinated. Polyubiquitination targets the protein for rapid
CC degradation via the ubiquitin system. Can be deubiquitinated by USP11.
CC {ECO:0000269|PubMed:12084015}.
CC -!- SIMILARITY: Belongs to the RANBP9/10 family. {ECO:0000305}.
CC -!- CAUTION: According to some authors RANBP9 is located in centrosomes and
CC involved in microtubule assembly. Other authors infirmed these results.
CC {ECO:0000305|PubMed:11470507, ECO:0000305|PubMed:9817760}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19886.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH52781.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAK15469.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA23216.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RANBP9ID42040ch6p23.html";
CC ---------------------------------------------------------------------------
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DR EMBL; AB055311; BAB62525.1; -; mRNA.
DR EMBL; AK313334; BAG36138.1; -; mRNA.
DR EMBL; AL441883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z93020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019886; AAH19886.1; ALT_SEQ; mRNA.
DR EMBL; BC052781; AAH52781.1; ALT_FRAME; mRNA.
DR EMBL; BC063849; AAH63849.1; -; mRNA.
DR EMBL; AB008515; BAA23216.1; ALT_INIT; mRNA.
DR EMBL; AF306510; AAK15469.1; ALT_INIT; mRNA.
DR CCDS; CCDS4529.1; -. [Q96S59-1]
DR RefSeq; NP_005484.2; NM_005493.2. [Q96S59-1]
DR RefSeq; XP_006715008.1; XM_006714945.2. [Q96S59-3]
DR PDB; 5JI7; X-ray; 1.51 A; A=108-350.
DR PDB; 5JI9; X-ray; 2.50 A; A=108-350.
DR PDB; 5JIU; X-ray; 2.05 A; A/B=108-350.
DR PDB; 7NSC; EM; 3.30 A; A=1-729.
DR PDBsum; 5JI7; -.
DR PDBsum; 5JI9; -.
DR PDBsum; 5JIU; -.
DR PDBsum; 7NSC; -.
DR AlphaFoldDB; Q96S59; -.
DR SMR; Q96S59; -.
DR BioGRID; 115359; 291.
DR CORUM; Q96S59; -.
DR IntAct; Q96S59; 76.
DR MINT; Q96S59; -.
DR STRING; 9606.ENSP00000011619; -.
DR GlyGen; Q96S59; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96S59; -.
DR PhosphoSitePlus; Q96S59; -.
DR SwissPalm; Q96S59; -.
DR BioMuta; RANBP9; -.
DR DMDM; 61215334; -.
DR EPD; Q96S59; -.
DR jPOST; Q96S59; -.
DR MassIVE; Q96S59; -.
DR MaxQB; Q96S59; -.
DR PaxDb; Q96S59; -.
DR PeptideAtlas; Q96S59; -.
DR PRIDE; Q96S59; -.
DR ProteomicsDB; 3415; -.
DR ProteomicsDB; 78074; -. [Q96S59-1]
DR ProteomicsDB; 78075; -. [Q96S59-2]
DR Antibodypedia; 24991; 274 antibodies from 35 providers.
DR DNASU; 10048; -.
DR Ensembl; ENST00000011619.6; ENSP00000011619.3; ENSG00000010017.13. [Q96S59-1]
DR GeneID; 10048; -.
DR KEGG; hsa:10048; -.
DR MANE-Select; ENST00000011619.6; ENSP00000011619.3; NM_005493.3; NP_005484.2.
DR UCSC; uc003nbb.3; human. [Q96S59-1]
DR CTD; 10048; -.
DR DisGeNET; 10048; -.
DR GeneCards; RANBP9; -.
DR HGNC; HGNC:13727; RANBP9.
DR HPA; ENSG00000010017; Low tissue specificity.
DR MIM; 603854; gene.
DR neXtProt; NX_Q96S59; -.
DR OpenTargets; ENSG00000010017; -.
DR PharmGKB; PA34215; -.
DR VEuPathDB; HostDB:ENSG00000010017; -.
DR eggNOG; KOG1477; Eukaryota.
DR GeneTree; ENSGT00940000157305; -.
DR HOGENOM; CLU_009129_4_0_1; -.
DR InParanoid; Q96S59; -.
DR OMA; SNGYKCQ; -.
DR PhylomeDB; Q96S59; -.
DR TreeFam; TF331658; -.
DR PathwayCommons; Q96S59; -.
DR Reactome; R-HSA-373760; L1CAM interactions.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-8851805; MET activates RAS signaling.
DR SignaLink; Q96S59; -.
DR SIGNOR; Q96S59; -.
DR BioGRID-ORCS; 10048; 37 hits in 1085 CRISPR screens.
DR ChiTaRS; RANBP9; human.
DR GeneWiki; RANBP9; -.
DR GenomeRNAi; 10048; -.
DR Pharos; Q96S59; Tbio.
DR PRO; PR:Q96S59; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96S59; protein.
DR Bgee; ENSG00000010017; Expressed in sperm and 206 other tissues.
DR ExpressionAtlas; Q96S59; baseline and differential.
DR Genevisible; Q96S59; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; TAS:ProtInc.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:CACAO.
DR GO; GO:1902993; P:positive regulation of amyloid precursor protein catabolic process; ISS:ARUK-UCL.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR CDD; cd12909; SPRY_RanBP9_10; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035782; SPRY_RanBP9/10.
DR Pfam; PF10607; CLTH; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..729
FT /note="Ran-binding protein 9"
FT /id="PRO_0000097169"
FT DOMAIN 147..334
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 365..397
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 403..460
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..407
FT /note="Interaction with CALB1"
FT /evidence="ECO:0000305"
FT REGION 461..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..729
FT /note="Interaction with FMR1"
FT /evidence="ECO:0000269|PubMed:15381419"
FT COMPBIAS 1..29
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 405
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69566"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..341
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013175"
FT VAR_SEQ 1..229
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056049"
FT CONFLICT 87
FT /note="P -> S (in Ref. 5; BAA23216)"
FT /evidence="ECO:0000305"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:5JI7"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:5JI7"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:5JI7"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:5JI7"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:5JI7"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:5JI7"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:5JI7"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:5JI7"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:5JI7"
FT STRAND 213..224
FT /evidence="ECO:0007829|PDB:5JI7"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:5JI7"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:5JI7"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:5JI7"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:5JI7"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:5JI7"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:5JI7"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:5JI7"
FT TURN 287..290
FT /evidence="ECO:0007829|PDB:5JI7"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:5JI7"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:5JI7"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:5JI7"
FT STRAND 323..332
FT /evidence="ECO:0007829|PDB:5JI7"
FT HELIX 338..343
FT /evidence="ECO:0007829|PDB:5JI7"
FT HELIX 364..379
FT /evidence="ECO:0007829|PDB:7NSC"
FT HELIX 383..387
FT /evidence="ECO:0007829|PDB:7NSC"
FT HELIX 696..712
FT /evidence="ECO:0007829|PDB:7NSC"
FT STRAND 713..715
FT /evidence="ECO:0007829|PDB:7NSC"
FT HELIX 717..721
FT /evidence="ECO:0007829|PDB:7NSC"
FT HELIX 724..727
FT /evidence="ECO:0007829|PDB:7NSC"
SQ SEQUENCE 729 AA; 77847 MW; 50DF1127B7FDA6C8 CRC64;
MSGQPPPPPP QQQQQQQQLS PPPPAALAPV SGVVLPAPPA VSAGSSPAGS PGGGAGGEGL
GAAAAALLLH PPPPPPPATA APPPPPPPPP PPASAAAPAS GPPAPPGLAA GPGPAGGAPT
PALVAGSSAA APFPHGDSAL NEQEKELQRR LKRLYPAVDE QETPLPRSWS PKDKFSYIGL
SQNNLRVHYK GHGKTPKDAA SVRATHPIPA ACGIYYFEVK IVSKGRDGYM GIGLSAQGVN
MNRLPGWDKH SYGYHGDDGH SFCSSGTGQP YGPTFTTGDV IGCCVNLINN TCFYTKNGHS
LGIAFTDLPP NLYPTVGLQT PGEVVDANFG QHPFVFDIED YMREWRTKIQ AQIDRFPIGD
REGEWQTMIQ KMVSSYLVHH GYCATAEAFA RSTDQTVLEE LASIKNRQRI QKLVLAGRMG
EAIETTQQLY PSLLERNPNL LFTLKVRQFI EMVNGTDSEV RCLGGRSPKS QDSYPVSPRP
FSSPSMSPSH GMNIHNLASG KGSTAHFSGF ESCSNGVISN KAHQSYCHSN KHQSSNLNVP
ELNSINMSRS QQVNNFTSND VDMETDHYSN GVGETSSNGF LNGSSKHDHE MEDCDTEMEV
DSSQLRRQLC GGSQAAIERM IHFGRELQAM SEQLRRDCGK NTANKKMLKD AFSLLAYSDP
WNSPVGNQLD PIQREPVCSA LNSAILETHN LPKQPPLALA MGQATQCLGL MARSGIGSCA
FATVEDYLH
