MSI1H_MOUSE
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 03-AUG-2022, entry version 156.
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; 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), 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., 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 [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., Takano H.,
RA 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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16554442; DOI=10.1242/jcs.02852;
RA Ratti A., Fallini C., Cova L., Fantozzi R., Calzarossa C., Zennaro E.,
RA Pascale A., Quattrone A., Silani V.;
RT "A role for the ELAV RNA-binding proteins in neural stem cells:
RT stabilization of Msi1 mRNA.";
RL J. Cell Sci. 119:1442-1452(2006).
RN [6]
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 expression.";
RL Cell 143:1174-1189(2010).
RN [7]
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-terminal
RT RNA-binding domain of a mouse neural RNA-binding protein, Musashi1.";
RL J. Mol. Biol. 287:315-330(1999).
RN [8]
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., Uesugi S.,
RA Okano H., Katahira M.;
RT "Origin of higher affinity to RNA of the N-terminal RNA-binding domain than
RT that of the C-terminal one of a mouse neural protein, musashi1, as revealed
RT by comparison of their structures, modes of interaction, surface
RT electrostatic potentials, and backbone dynamics.";
RL J. Biol. Chem. 278:41309-41315(2003).
CC -!- FUNCTION: RNA binding protein that regulates the expression of target
CC mRNAs at the translation level. Regulates expression of the NOTCH1
CC antagonist NUMB. Binds RNA containing the sequence 5'-GUUAGUUAGUUAGUU-
CC 3' and other sequences containing the pattern 5'-[GA]U(1-3)AGU-3'. May
CC play a role in the proliferation and maintenance of stem cells in the
CC central nervous system. {ECO:0000269|PubMed:11359897,
CC ECO:0000269|PubMed:12407178}.
CC -!- INTERACTION:
CC Q61474; Q61474: Msi1; NbExp=2; IntAct=EBI-8327453, EBI-8327453;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16554442}. Nucleus
CC {ECO:0000269|PubMed:16554442}.
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 -!- TISSUE SPECIFICITY: Expressed in neural stem and progenitor cells (at
CC protein level) (PubMed:16554442). Detected in olfactory bulb, brain
CC stem, small intestine, and at low levels in brain cortex, hippocampus
CC and ovary (PubMed:8660864). Detected in neural progenitor cells,
CC including neural stem cells (PubMed:8660864).
CC {ECO:0000269|PubMed:16554442, ECO:0000269|PubMed:8660864}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in embryonic brain at day 12.
CC 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 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}.
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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 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 PDB; 5X3Y; NMR; -; A=109-200.
DR PDB; 5X3Z; NMR; -; A=109-200.
DR PDBsum; 1UAW; -.
DR PDBsum; 2MSS; -.
DR PDBsum; 2MST; -.
DR PDBsum; 2RS2; -.
DR PDBsum; 5X3Y; -.
DR PDBsum; 5X3Z; -.
DR AlphaFoldDB; Q61474; -.
DR SMR; Q61474; -.
DR BioGRID; 201530; 1.
DR IntAct; Q61474; 4.
DR STRING; 10090.ENSMUSP00000120516; -.
DR iPTMnet; Q61474; -.
DR PhosphoSitePlus; Q61474; -.
DR MaxQB; Q61474; -.
DR PaxDb; Q61474; -.
DR PeptideAtlas; Q61474; -.
DR PRIDE; Q61474; -.
DR ProteomicsDB; 291419; -. [Q61474-1]
DR ProteomicsDB; 291420; -. [Q61474-2]
DR Antibodypedia; 18945; 658 antibodies from 41 providers.
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 VEuPathDB; HostDB:ENSMUSG00000054256; -.
DR eggNOG; KOG4205; Eukaryota.
DR GeneTree; ENSGT00940000156515; -.
DR InParanoid; Q61474; -.
DR OMA; SWQTTQV; -.
DR OrthoDB; 1565323at2759; -.
DR PhylomeDB; Q61474; -.
DR TreeFam; TF325419; -.
DR BioGRID-ORCS; 17690; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Msi1; mouse.
DR EvolutionaryTrace; Q61474; -.
DR PRO; PR:Q61474; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q61474; protein.
DR Bgee; ENSMUSG00000054256; Expressed in retinal neural layer and 177 other tissues.
DR ExpressionAtlas; Q61474; baseline and differential.
DR Genevisible; Q61474; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005844; C:polysome; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:MGI.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:MGI.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0006417; P:regulation of translation; IBA:GO_Central.
DR GO; GO:0009725; P:response to hormone; ISO:MGI.
DR CDD; cd12576; RRM1_MSI; 1.
DR CDD; cd12323; RRM2_MSI; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034130; MSI_RRM1.
DR InterPro; IPR034126; MSI_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..362
FT /note="RNA-binding protein Musashi homolog 1"
FT /id="PRO_0000081650"
FT DOMAIN 20..110
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 109..186
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43347"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43347"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011166"
FT VAR_SEQ 264..362
FT /note="AIPLTAYGPMAAAAAAAAVVRGTGSHPWTMAPPPGSTPSRTGGFLGTTSPGP
FT MAELYGAANQDSGVSSYISAASPAPSTGFGHSLGGPLIATAFTNGYH -> GQWLRFRA
FT SHRPRGEKGGERDCPLPRGEAGRTTVPGHWPVSSATWPSRVGREAKPGRRR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011167"
FT MUTAGEN 63
FT /note="F->L: Abolishes RNA binding; when associated with L-
FT 65 and L-68."
FT /evidence="ECO:0000269|PubMed:11359897"
FT MUTAGEN 65
FT /note="F->L: Abolishes RNA binding; when associated with L-
FT 63 and L-68."
FT /evidence="ECO:0000269|PubMed:11359897"
FT MUTAGEN 68
FT /note="F->L: Abolishes RNA binding; when associated with L-
FT 63 and L-65."
FT /evidence="ECO:0000269|PubMed:11359897"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:1UAW"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:1UAW"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1UAW"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1UAW"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1UAW"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1UAW"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:1UAW"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1UAW"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2RS2"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:1UAW"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:2MSS"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:2MSS"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2MSS"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2MSS"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:2MSS"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:2MSS"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2MSS"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2MSS"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2MSS"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:5X3Z"
FT TURN 192..197
FT /evidence="ECO:0007829|PDB:5X3Z"
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
