RANB3_MOUSE
ID RANB3_MOUSE Reviewed; 491 AA.
AC Q9CT10; A6H6I9; Q3TIS4; Q3U2G4; Q3UYG7;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Ran-binding protein 3;
DE Short=RanBP3;
GN Name=Ranbp3;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Liver, and Medulla oblongata;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-33; SER-40; SER-146
RP AND SER-257, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-33; SER-40; SER-146
RP AND SER-257, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9 AND LYS-21, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Acts as a cofactor for XPO1/CRM1-mediated nuclear export,
CC perhaps as export complex scaffolding protein. Bound to XPO1/CRM1,
CC stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound
CC GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to
CC CHC1/RCC1 and increases the guanine nucleotide exchange activity of
CC CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner.
CC Negative regulator of TGF-beta signaling through interaction with the
CC R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CHC1 in a Ran-stimulated manner. Interacts with
CC XPO1. Interacts (via its C-terminal R domain) with SMAD2
CC (dephosphorylated form via its MH1 and MH2 domains); the interaction
CC results in the nuclear export of SMAD2 and termination of the TGF-beta
CC signaling. Interacts (via its C-terminal R domain) with SMAD3
CC (dephosphorylated form via its MH1 domain); the interaction results in
CC the nuclear export of SMAD3 and termination of the TGF-beta signaling
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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DR EMBL; AK011541; BAB27684.1; -; mRNA.
DR EMBL; AK133949; BAE21946.1; -; mRNA.
DR EMBL; AK134696; BAE22245.1; -; mRNA.
DR EMBL; AK155301; BAE33176.1; -; mRNA.
DR EMBL; AK167731; BAE39772.1; -; mRNA.
DR EMBL; BC145892; AAI45893.1; -; mRNA.
DR EMBL; BC145894; AAI45895.1; -; mRNA.
DR CCDS; CCDS28911.1; -.
DR RefSeq; NP_082209.1; NM_027933.3.
DR AlphaFoldDB; Q9CT10; -.
DR SMR; Q9CT10; -.
DR BioGRID; 214944; 20.
DR IntAct; Q9CT10; 1.
DR MINT; Q9CT10; -.
DR STRING; 10090.ENSMUSP00000002445; -.
DR iPTMnet; Q9CT10; -.
DR PhosphoSitePlus; Q9CT10; -.
DR EPD; Q9CT10; -.
DR jPOST; Q9CT10; -.
DR MaxQB; Q9CT10; -.
DR PaxDb; Q9CT10; -.
DR PeptideAtlas; Q9CT10; -.
DR PRIDE; Q9CT10; -.
DR ProteomicsDB; 300351; -.
DR Antibodypedia; 24035; 268 antibodies from 29 providers.
DR DNASU; 71810; -.
DR Ensembl; ENSMUST00000002445; ENSMUSP00000002445; ENSMUSG00000002372.
DR GeneID; 71810; -.
DR KEGG; mmu:71810; -.
DR UCSC; uc008dct.2; mouse.
DR CTD; 8498; -.
DR MGI; MGI:1919060; Ranbp3.
DR VEuPathDB; HostDB:ENSMUSG00000002372; -.
DR eggNOG; KOG0866; Eukaryota.
DR GeneTree; ENSGT00940000158588; -.
DR HOGENOM; CLU_034909_1_0_1; -.
DR InParanoid; Q9CT10; -.
DR OrthoDB; 918488at2759; -.
DR PhylomeDB; Q9CT10; -.
DR TreeFam; TF313181; -.
DR BioGRID-ORCS; 71810; 14 hits in 74 CRISPR screens.
DR ChiTaRS; Ranbp3; mouse.
DR PRO; PR:Q9CT10; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9CT10; protein.
DR Bgee; ENSMUSG00000002372; Expressed in spermatocyte and 267 other tissues.
DR ExpressionAtlas; Q9CT10; baseline and differential.
DR Genevisible; Q9CT10; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0006611; P:protein export from nucleus; IBA:GO_Central.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR PANTHER; PTHR23138; PTHR23138; 2.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR PROSITE; PS50196; RANBD1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT CHAIN 2..491
FT /note="Ran-binding protein 3"
FT /id="PRO_0000097167"
FT DOMAIN 302..442
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 56
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6Z4"
FT CONFLICT 259
FT /note="P -> T (in Ref. 1; BAE39772)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="L -> P (in Ref. 1; BAB27684)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="T -> K (in Ref. 1; BAB27684)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="S -> P (in Ref. 1; BAB27684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 52573 MW; 6BEFB98D5B0B38B7 CRC64;
MADLANEEKP AVAPSVFVFQ KDKGQKRSAG SSSPEAGEDS DHEDGNYCPP VKRERTSSLT
HSEEKSSGFR LKPPTLIHGQ APSAGLPSQK PREQQRGVLR PAVLQAPQPK VLSQTVPSSG
TNGVSMPADC TGPATSVSPE NLTQRSPSES AEETHTLEEK VPQKTPHGTS EEGHCEEEQA
APQAFVFGQN LRDRVKLMNE NASVADVDSA AHPSSETPSA TNYFLQYISS SADNATHSAD
NSTKFVFGQN MSERVLSPPK LNEANSDTSR ETTHAQSGSE SSSQEAAPKK ESLAESAAAY
TKATAWTCLL EKVEVITGEE AESNVLQIQC KLFVFDKTSQ SWVERGRGLL RLNDMASTDD
GTLQSRLVMR TQGSLRLILN TKLWAQMQMD KASEKSIRIT ATDAEDQGVK VFLISASSKD
TGQLYAALHH RILALRSRAE QEQEAKAPPP EPGATRATEE EDSDEDAVLA PSGVTGAGTG
DEGDGQAPGS T
