RANB9_MOUSE
ID RANB9_MOUSE Reviewed; 653 AA.
AC P69566; P84500; Q3V136;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Ran-binding protein 9 {ECO:0000305};
DE Short=RanBP9;
DE AltName: Full=B-cell antigen receptor Ig beta-associated protein 1;
DE Short=IBAP-1;
DE AltName: Full=Ran-binding protein M;
DE Short=RanBPM;
GN Name=Ranbp9 {ECO:0000312|MGI:MGI:1928741}; Synonyms=Ranbpm;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DDX4, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=14648869; DOI=10.1002/mrd.20009;
RA Shibata N., Tsunekawa N., Okamoto-Ito S., Akasu R., Tokumasu A., Noce T.;
RT "Mouse RanBPM is a partner gene to a germline specific RNA helicase, mouse
RT vasa homolog protein.";
RL Mol. Reprod. Dev. 67:1-7(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Doi T., Watanabe T.;
RT "B cell antigen receptor Ig beta associated protein.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-653 (ISOFORM 1), AND INTERACTION WITH
RP NGFR.
RC TISSUE=Brain;
RX PubMed=12963025; DOI=10.1016/j.bbrc.2003.08.033;
RA Bai D., Chen H., Huang B.-R.;
RT "RanBPM is a novel binding protein for p75NTR.";
RL Biochem. Biophys. Res. Commun. 309:552-557(2003).
RN [5]
RP TISSUE SPECIFICITY.
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 [6]
RP INTERACTION WITH MKLN1, AND SUBCELLULAR LOCATION.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402 AND SER-412, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH TEX19.1.
RX PubMed=28254886; DOI=10.1242/jcs.188763;
RA Tarabay Y., Achour M., Teletin M., Ye T., Teissandier A., Mark M.,
RA Bourc'his D., Viville S.;
RT "Tex19 paralogs are new members of the piRNA pathway controlling
RT retrotransposon suppression.";
RL J. Cell Sci. 130:1463-1474(2017).
CC -!- FUNCTION: May act as scaffolding protein, and as adapter protein to
CC couple membrane receptors to intracellular signaling pathways. Acts as
CC a mediator of cell spreading and actin cytoskeleton rearrangement. Core
CC component of the CTLH E3 ubiquitin-protein ligase complex that
CC selectively accepts ubiquitin from UBE2H and mediates ubiquitination
CC and subsequent proteasomal degradation of the transcription factor
CC HBP1. May be involved in signaling of ITGB2/LFA-1 and other integrins.
CC Enhances HGF-MET signaling by recruiting Sos and activating the Ras
CC pathway. Enhances dihydrotestosterone-induced transactivation activity
CC of AR, as well as dexamethasone-induced transactivation activity of
CC NR3C1, but not affect estrogen-induced transactivation. Stabilizes TP73
CC isoform Alpha, probably by inhibiting its ubiquitination, and increases
CC its proapoptotic activity. Inhibits the kinase activity of DYRK1A and
CC DYRK1B. Inhibits FMR1 binding to RNA. {ECO:0000250|UniProtKB:Q96S59}.
CC -!- SUBUNIT: Part of a complex consisting of RANBP9, MKLN1 and GID8.
CC Identified in the CTLH complex that contains GID4, RANBP9 and/or
CC RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B),
CC GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or
CC alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or
CC RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5
CC have ancillary roles. Interacts with GTP-bound Ran, AR, CDC2L1/p110C,
CC CALB1, S100A7, USP11, SOS1 or SOS2, GID8, and FMR1. Interacts with the
CC Dyrk kinases HIPK2, DYRK1A, and DYRK1B. Interacts with TP73 isoform
CC Alpha but not with TP53. Interacts with the HGF receptor MET and the
CC integrins ITGB1 and ITGB2, but not with ITGAL. Part of a complex
CC consisting of RANBP9, RAN, DYRK1B and COPS5. Directly interacts with
CC RANBP10. Interacts with YPEL5 (By similarity). Interacts with MKLN1
CC (PubMed:18710924). Interacts with DDX4 (PubMed:14648869). Interacts
CC with NGFR (PubMed:12963025). Interacts with Tex19.1 and, probably,
CC Tex19.2 (PubMed:28254886). {ECO:0000250|UniProtKB:Q96S59,
CC ECO:0000269|PubMed:12963025, ECO:0000269|PubMed:14648869,
CC ECO:0000269|PubMed:18710924, ECO:0000269|PubMed:28254886}.
CC -!- INTERACTION:
CC P69566; Q9JI18: Lrp1b; NbExp=2; IntAct=EBI-772305, EBI-8294317;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18710924}. Cell
CC membrane {ECO:0000305|PubMed:18710924}; Peripheral membrane protein
CC {ECO:0000305|PubMed:18710924}; Cytoplasmic side
CC {ECO:0000305|PubMed:18710924}. Nucleus {ECO:0000269|PubMed:18710924}.
CC Note=Predominantly cytoplasmic (PubMed:18710924). A phosphorylated form
CC is associated with the plasma membrane (By similarity). Perinuclear in
CC spermatids (PubMed:14648869). {ECO:0000250|UniProtKB:Q96S59,
CC ECO:0000269|PubMed:14648869, ECO:0000269|PubMed:18710924}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P69566-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P69566-2; Sequence=VSP_028266, VSP_028267;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC maturating spermatocytes. {ECO:0000269|PubMed:14648869,
CC ECO:0000269|PubMed:14722085}.
CC -!- DOMAIN: The SPRY domain mediates the interaction with MET, AR, and
CC CDC2L1. {ECO:0000250|UniProtKB:Q96S59}.
CC -!- PTM: Phosphorylated in response to stress.
CC {ECO:0000250|UniProtKB:Q96S59}.
CC -!- PTM: Ubiquitinated. Polyubiquitination targets the protein for rapid
CC degradation via the ubiquitin system (By similarity).
CC {ECO:0000250|UniProtKB:Q96S59}.
CC -!- SIMILARITY: Belongs to the RANBP9/10 family. {ECO:0000305}.
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DR EMBL; AF006465; AAD01272.1; -; mRNA.
DR EMBL; AK132714; BAE21317.1; -; mRNA.
DR PIR; JC8013; JC8013.
DR RefSeq; NP_064314.2; NM_019930.2.
DR AlphaFoldDB; P69566; -.
DR SMR; P69566; -.
DR BioGRID; 208133; 14.
DR IntAct; P69566; 8.
DR MINT; P69566; -.
DR STRING; 10090.ENSMUSP00000130636; -.
DR iPTMnet; P69566; -.
DR PhosphoSitePlus; P69566; -.
DR EPD; P69566; -.
DR MaxQB; P69566; -.
DR PaxDb; P69566; -.
DR PeptideAtlas; P69566; -.
DR PRIDE; P69566; -.
DR ProteomicsDB; 255093; -. [P69566-1]
DR ProteomicsDB; 255094; -. [P69566-2]
DR Antibodypedia; 24991; 274 antibodies from 35 providers.
DR DNASU; 56705; -.
DR Ensembl; ENSMUST00000222651; ENSMUSP00000152620; ENSMUSG00000038546. [P69566-2]
DR GeneID; 56705; -.
DR KEGG; mmu:56705; -.
DR CTD; 10048; -.
DR MGI; MGI:1928741; Ranbp9.
DR VEuPathDB; HostDB:ENSMUSG00000038546; -.
DR eggNOG; KOG1477; Eukaryota.
DR GeneTree; ENSGT00940000157305; -.
DR InParanoid; P69566; -.
DR OrthoDB; 1106989at2759; -.
DR PhylomeDB; P69566; -.
DR Reactome; R-MMU-373760; L1CAM interactions.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-8851805; MET activates RAS signaling.
DR BioGRID-ORCS; 56705; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ranbp9; mouse.
DR PRO; PR:P69566; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P69566; protein.
DR Bgee; ENSMUSG00000038546; Expressed in animal zygote and 243 other tissues.
DR ExpressionAtlas; P69566; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
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:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:1902993; P:positive regulation of amyloid precursor protein catabolic process; ISO:MGI.
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 Acetylation; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..653
FT /note="Ran-binding protein 9"
FT /id="PRO_0000097170"
FT DOMAIN 72..259
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 290..322
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 328..385
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..332
FT /note="Interaction with CALB1"
FT /evidence="ECO:0000250"
FT REGION 386..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..653
FT /note="Interaction with FMR1"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..26
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 330
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96S59"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..107
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028266"
FT VAR_SEQ 108..115
FT /note="NNLRVHYK -> MWESSWVL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028267"
FT CONFLICT 92
FT /note="R -> P (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 653 AA; 71012 MW; BE810E69B238BBD5 CRC64;
MSGQPPPPPP QQQPPPPPPP ASAAAPATAP PGLAVGPGPA AGVPVPGLAA GSSAAAPFPH
GDSALNEQEK ELQRRLKRLY PAVDEQETPL PRSWSPKDKF SYIGLSQNNL RVHYKGHGKT
PKDAASVRAT HPIPAACGIY YFEVKIVSKG RDGYMGIGLS AQGVNMNRLP GWDKHSYGYH
GDDGHSFCSS GTGQPYGPTF TTGDVIGCCV NLINNTCFYT KNGHSLGIAF TDLPPNLYPT
VGLQTPGEVV DANFGQHPFV FDIEDYMREW RTKIQAQIDR FPIGDREGEW QTMIQKMVSS
YLVHHGYCAT AEAFARSTDQ TVLEELASIK NRQRIQKLVL AGRMGEAIET TQQLYPSLLE
RNPNLLFTLK VRQFIEMVNG TDSEVRCLGG RSPKSQDSYP VSPRPFSSPS MSPSHGMSIH
SLAPGKSSTA HFSGFESCSN GVISNKAHQS YCHSKHQLSS LTVPELNSLN VSRSQQVNNF
TSNDVDMETD HYSNGVGETS SNGFLNGSSK HDHEMEDCDT EMEVDCSQLR RQLCGGSQAA
IERMIHFGRE LQAMSEQLRR ECGKNTANKK MLKDAFSLLA YSDPWNSPVG NQLDPIQREP
VCSALNSAIL ETHNLPKQPP LALAMGQATQ CLGLMARSGV GSCAFATVED YLH
