ID MSI1H_MOUSE Reviewed; 362 AA. AC Q61474; Q8BNC7; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-SEP-2015, entry version 116. DE RecName: Full=RNA-binding protein Musashi homolog 1; DE Short=Musashi-1; GN Name=Msi1; Synonyms=Msi1h; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, AND TISSUE RP SPECIFICITY. RC STRAIN=ICR; TISSUE=Cerebellum; RX PubMed=8660864; DOI=10.1006/dbio.1996.0130; RA Sakakibara S., Imai T., Hamaguchi K., Okabe M., Aruga J., Nakajima K., RA Yasutomi D., Nagata T., Kurihara Y., Uesugi S., Miyata T., Ogawa M., RA Mikoshiba K., Okano H.; RT "Mouse-Musashi-1, a neural RNA-binding protein highly enriched in the RT mammalian CNS stem cell."; RL Dev. Biol. 176:230-242(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP FUNCTION, AND MUTAGENESIS OF PHE-63; PHE-65 AND PHE-68. RX PubMed=11359897; DOI=10.1128/MCB.21.12.3888-3900.2001; RA Imai T., Tokunaga A., Yoshida T., Hashimoto M., Mikoshiba K., RA Weinmaster G., Nakafuku M., Okano H.; RT "The neural RNA-binding protein Musashi1 translationally regulates RT mammalian numb gene expression by interacting with its mRNA."; RL Mol. Cell. Biol. 21:3888-3900(2001). RN [4] RP FUNCTION. RX PubMed=12407178; DOI=10.1073/pnas.232087499; RA Sakakibara S., Nakamura Y., Yoshida T., Shibata S., Koike M., RA Takano H., Ueda S., Uchiyama Y., Noda T., Okano H.; RT "RNA-binding protein Musashi family: roles for CNS stem cells and a RT subpopulation of ependymal cells revealed by targeted disruption and RT antisense ablation."; RL Proc. Natl. Acad. Sci. U.S.A. 99:15194-15199(2002). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 RT expression."; RL Cell 143:1174-1189(2010). RN [6] RP STRUCTURE BY NMR OF 110-184, AND INTERACTION WITH RNA. RX PubMed=10080895; DOI=10.1006/jmbi.1999.2596; RA Nagata T., Kanno R., Kurihara Y., Uesugi S., Imai T., Sakakibara S., RA Okano H., Katahira M.; RT "Structure, backbone dynamics and interactions with RNA of the C- RT terminal RNA-binding domain of a mouse neural RNA-binding protein, RT Musashi1."; RL J. Mol. Biol. 287:315-330(1999). RN [7] RP STRUCTURE BY NMR OF 20-96, AND INTERACTION WITH RNA. RX PubMed=12907678; DOI=10.1074/jbc.M306210200; RA Miyanoiri Y., Kobayashi H., Imai T., Watanabe M., Nagata T., RA Uesugi S., Okano H., Katahira M.; RT "Origin of higher affinity to RNA of the N-terminal RNA-binding domain RT than that of the C-terminal one of a mouse neural protein, musashi1, RT as revealed by comparison of their structures, modes of interaction, RT surface electrostatic potentials, and backbone dynamics."; RL J. Biol. Chem. 278:41309-41315(2003). CC -!- FUNCTION: RNA binding protein that regulates the expression of CC target mRNAs at the translation level. Regulates expression of the CC NOTCH1 antagonist NUMB. Binds RNA containing the sequence 5'- CC GUUAGUUAGUUAGUU-3' and other sequences containing the pattern 5'- CC [GA]U(1-3)AGU-3'. May play a role in the proliferation and CC maintenance of stem cells in the central nervous system. CC {ECO:0000269|PubMed:11359897, ECO:0000269|PubMed:12407178}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q61474-1; Sequence=Displayed; CC Name=2; CC IsoId=Q61474-2; Sequence=VSP_011166, VSP_011167; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Detected in olfactory bulb, brain stem, small CC intestine, and at low levels in brain cortex, hippocampus and CC ovary. Detected in neural progenitor cells, including neural stem CC cells. {ECO:0000269|PubMed:8660864}. CC -!- DEVELOPMENTAL STAGE: Highly expressed in embryonic brain at day CC 12. Expressed at intermediate levels during the rest of embryonic CC development and in newborns up to day 3. After this expression CC decreases and stabilizes at low levels of expression around day CC 13. CC -!- DOMAIN: The first RNA recognition motif binds more strongly to RNA CC compared to the second one. CC -!- SIMILARITY: Belongs to the Musashi family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains. CC {ECO:0000255|PROSITE-ProRule:PRU00176}. 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; D49654; BAA08530.1; -; mRNA. DR EMBL; AK084019; BAC39099.1; -; mRNA. DR CCDS; CCDS19591.1; -. [Q61474-1] DR RefSeq; NP_032655.1; NM_008629.1. [Q61474-1] DR UniGene; Mm.391995; -. DR UniGene; Mm.5077; -. DR PDB; 1UAW; NMR; -; A=20-96. DR PDB; 2MSS; NMR; -; A=110-184. DR PDB; 2MST; NMR; -; A=110-184. DR PDB; 2RS2; NMR; -; A=20-103. DR PDBsum; 1UAW; -. DR PDBsum; 2MSS; -. DR PDBsum; 2MST; -. DR PDBsum; 2RS2; -. DR ProteinModelPortal; Q61474; -. DR SMR; Q61474; 18-187. DR IntAct; Q61474; 1. DR MINT; MINT-4102437; -. DR STRING; 10090.ENSMUSP00000120516; -. DR PhosphoSite; Q61474; -. DR MaxQB; Q61474; -. DR PaxDb; Q61474; -. DR PRIDE; Q61474; -. DR DNASU; 17690; -. DR Ensembl; ENSMUST00000150779; ENSMUSP00000120516; ENSMUSG00000054256. [Q61474-1] DR GeneID; 17690; -. DR KEGG; mmu:17690; -. DR UCSC; uc008zdu.1; mouse. [Q61474-2] DR UCSC; uc008zdv.1; mouse. [Q61474-1] DR CTD; 4440; -. DR MGI; MGI:107376; Msi1. DR eggNOG; COG0724; -. DR GeneTree; ENSGT00730000110584; -. DR HOVERGEN; HBG002295; -. DR InParanoid; Q61474; -. DR KO; K14411; -. DR OMA; HYFEQFG; -. DR OrthoDB; EOG715Q6V; -. DR PhylomeDB; Q61474; -. DR TreeFam; TF325419; -. DR EvolutionaryTrace; Q61474; -. DR NextBio; 292270; -. DR PRO; PR:Q61474; -. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; Q61474; -. DR CleanEx; MM_MSI1; -. DR ExpressionAtlas; Q61474; baseline and differential. DR Genevisible; Q61474; MM. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005844; C:polysome; IDA:MGI. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0044822; F:poly(A) RNA binding; ISO:MGI. DR GO; GO:0008266; F:poly(U) RNA binding; IDA:MGI. DR GO; GO:0003727; F:single-stranded RNA binding; IDA:MGI. DR Gene3D; 3.30.70.330; -; 2. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR000504; RRM_dom. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 2. DR PROSITE; PS50102; RRM; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Complete proteome; KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW RNA-binding. FT CHAIN 1 362 RNA-binding protein Musashi homolog 1. FT /FTId=PRO_0000081650. FT DOMAIN 20 110 RRM 1. {ECO:0000255|PROSITE- FT ProRule:PRU00176}. FT DOMAIN 109 186 RRM 2. {ECO:0000255|PROSITE- FT ProRule:PRU00176}. FT COMPBIAS 274 281 Poly-Ala. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000250|UniProtKB:O43347}. FT MOD_RES 191 191 Phosphoserine. FT {ECO:0000250|UniProtKB:O43347}. FT VAR_SEQ 1 21 Missing (in isoform 2). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_011166. FT VAR_SEQ 264 362 AIPLTAYGPMAAAAAAAAVVRGTGSHPWTMAPPPGSTPSRT FT GGFLGTTSPGPMAELYGAANQDSGVSSYISAASPAPSTGFG FT HSLGGPLIATAFTNGYH -> GQWLRFRASHRPRGEKGGER FT DCPLPRGEAGRTTVPGHWPVSSATWPSRVGREAKPGRRR FT (in isoform 2). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_011167. FT MUTAGEN 63 63 F->L: Abolishes RNA binding; when FT associated with L-65 and L-68. FT {ECO:0000269|PubMed:11359897}. FT MUTAGEN 65 65 F->L: Abolishes RNA binding; when FT associated with L-63 and L-68. FT {ECO:0000269|PubMed:11359897}. FT MUTAGEN 68 68 F->L: Abolishes RNA binding; when FT associated with L-63 and L-65. FT {ECO:0000269|PubMed:11359897}. FT STRAND 22 26 {ECO:0000244|PDB:1UAW}. FT HELIX 34 40 {ECO:0000244|PDB:1UAW}. FT TURN 41 43 {ECO:0000244|PDB:1UAW}. FT STRAND 49 52 {ECO:0000244|PDB:1UAW}. FT STRAND 57 59 {ECO:0000244|PDB:1UAW}. FT STRAND 61 66 {ECO:0000244|PDB:1UAW}. FT HELIX 73 79 {ECO:0000244|PDB:1UAW}. FT TURN 80 82 {ECO:0000244|PDB:1UAW}. FT STRAND 83 85 {ECO:0000244|PDB:2RS2}. FT STRAND 91 94 {ECO:0000244|PDB:1UAW}. FT STRAND 111 114 {ECO:0000244|PDB:2MSS}. FT HELIX 122 130 {ECO:0000244|PDB:2MSS}. FT STRAND 136 138 {ECO:0000244|PDB:2MSS}. FT STRAND 144 146 {ECO:0000244|PDB:2MSS}. FT STRAND 151 156 {ECO:0000244|PDB:2MSS}. FT HELIX 160 167 {ECO:0000244|PDB:2MSS}. FT STRAND 168 170 {ECO:0000244|PDB:2MSS}. FT STRAND 174 176 {ECO:0000244|PDB:2MSS}. FT STRAND 180 182 {ECO:0000244|PDB:2MSS}. SQ SEQUENCE 362 AA; 39119 MW; 75C316BB384AE211 CRC64; METDAPQPGL ASPDSPHDPC KMFIGGLSWQ TTQEGLREYF GQFGEVKECL VMRDPLTKRS RGFGFVTFMD QAGVDKVLAQ SRHELDSKTI DPKVAFPRRA QPKMVTRTKK IFVGGLSVNT TVEDVKHYFE QFGKVDDAML MFDKTTNRHR GFGFVTFESE DIVEKVCEIH FHEINNKMVE CKKAQPKEVM SPTGSARGRS RVMPYGMDAF MLGIGMLGYP GFQATTYASR SYTGLAPGYT YQFPEFRVER SPLPSAPVLP ELTAIPLTAY GPMAAAAAAA AVVRGTGSHP WTMAPPPGST PSRTGGFLGT TSPGPMAELY GAANQDSGVS SYISAASPAP STGFGHSLGG PLIATAFTNG YH //