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 27-MAR-2024, entry version 191. 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="https://atlasgeneticsoncology.org/gene/42040/RANBP9"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. 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 EMDB; EMD-12564; -. DR SMR; Q96S59; -. DR BioGRID; 115359; 442. DR ComplexPortal; CPX-7901; GID E3 ubiquitin ligase complex, RMND5B-RANBP9 variant. DR ComplexPortal; CPX-876; GID E3 ubiquitin ligase complex, RMND5A-RANBP9 variant. DR CORUM; Q96S59; -. DR IntAct; Q96S59; 86. 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; 9606-ENSP00000011619; -. DR PeptideAtlas; Q96S59; -. DR ProteomicsDB; 3415; -. DR ProteomicsDB; 78074; -. [Q96S59-1] DR ProteomicsDB; 78075; -. [Q96S59-2] DR Pumba; Q96S59; -. DR Antibodypedia; 24991; 310 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 AGR; HGNC:13727; -. 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; YGQQLRM; -. DR OrthoDB; 38145at2759; -. 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; 54 hits in 1161 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 208 other cell types or tissues. DR ExpressionAtlas; Q96S59; baseline and differential. 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: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 IDEAL; IID00733; -. 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 PANTHER; PTHR12864; RAN BINDING PROTEIN 9-RELATED; 1. DR PANTHER; PTHR12864:SF56; RAN-BINDING PROTEIN 9; 1. DR Pfam; PF10607; CTLH; 2. 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; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1. DR PROSITE; PS50188; B302_SPRY; 1. DR PROSITE; PS50897; CTLH; 1. DR PROSITE; PS50896; LISH; 1. DR Genevisible; Q96S59; HS. 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 //