MSI2H_MOUSE
ID MSI2H_MOUSE Reviewed; 346 AA.
AC Q920Q6; Q8BQ90; Q920Q7;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=RNA-binding protein Musashi homolog 2;
DE Short=Musashi-2;
GN Name=Msi2; Synonyms=Msi2h;
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] (ISOFORMS 1 AND 2), FUNCTION, PHOSPHORYLATION,
RP INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J, and ICR; TISSUE=Brain;
RX PubMed=11588182; DOI=10.1523/jneurosci.21-20-08091.2001;
RA Sakakibara S., Nakamura Y., Satoh H., Okano H.;
RT "RNA-binding protein Musashi2: developmentally regulated expression in
RT neural precursor cells and subpopulations of neurons in mammalian CNS.";
RL J. Neurosci. 21:8091-8107(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=129/Ola; TISSUE=Embryo;
RX PubMed=12923295; DOI=10.1073/pnas.1734197100;
RA Aubert J., Stavridis M.P., Tweedie S., O'Reilly M., Vierlinger K., Li M.,
RA Ghazal P., Pratt T., Mason J.O., Roy D., Smith A.;
RT "Screening for mammalian neural genes via fluorescence-activated cell
RT sorter purification of neural precursors from Sox1-gfp knock-in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11836-11841(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and ICR; TISSUE=Brain, and 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 [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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-228 AND ARG-261, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: RNA binding protein that regulates the expression of target
CC mRNAs at the translation level. May play a role in the proliferation
CC and maintenance of stem cells in the central nervous system.
CC {ECO:0000269|PubMed:11588182, ECO:0000269|PubMed:12407178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11588182}.
CC Note=Associated with polysomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Msi2L;
CC IsoId=Q920Q6-1; Sequence=Displayed;
CC Name=2; Synonyms=Msi2S;
CC IsoId=Q920Q6-2; Sequence=VSP_011173;
CC Name=3;
CC IsoId=Q920Q6-3; Sequence=VSP_011172, VSP_011174;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in proliferating neural
CC precursor cells. {ECO:0000269|PubMed:11588182,
CC ECO:0000269|PubMed:12923295}.
CC -!- INDUCTION: Up-regulated in astrocytes after brain injury.
CC {ECO:0000269|PubMed:11588182}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:11588182}.
CC -!- SIMILARITY: Belongs to the Musashi family. {ECO:0000305}.
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DR EMBL; AB056102; BAB69484.1; -; mRNA.
DR EMBL; AB056103; BAB69485.1; -; mRNA.
DR EMBL; BK001483; DAA01567.1; -; mRNA.
DR EMBL; AK049637; BAC33851.1; -; mRNA.
DR EMBL; AK049688; BAC33873.1; -; mRNA.
DR EMBL; AK051269; BAC34584.1; -; mRNA.
DR CCDS; CCDS56796.1; -. [Q920Q6-1]
DR CCDS; CCDS88217.1; -. [Q920Q6-2]
DR RefSeq; NP_473384.1; NM_054043.3. [Q920Q6-1]
DR RefSeq; XP_006534505.1; XM_006534442.3.
DR AlphaFoldDB; Q920Q6; -.
DR SMR; Q920Q6; -.
DR BioGRID; 218215; 10.
DR IntAct; Q920Q6; 3.
DR STRING; 10090.ENSMUSP00000103541; -.
DR iPTMnet; Q920Q6; -.
DR PhosphoSitePlus; Q920Q6; -.
DR EPD; Q920Q6; -.
DR MaxQB; Q920Q6; -.
DR PaxDb; Q920Q6; -.
DR PRIDE; Q920Q6; -.
DR ProteomicsDB; 291354; -. [Q920Q6-1]
DR ProteomicsDB; 291355; -. [Q920Q6-2]
DR ProteomicsDB; 291356; -. [Q920Q6-3]
DR Antibodypedia; 18327; 404 antibodies from 39 providers.
DR DNASU; 76626; -.
DR Ensembl; ENSMUST00000092794; ENSMUSP00000090470; ENSMUSG00000069769. [Q920Q6-1]
DR Ensembl; ENSMUST00000107909; ENSMUSP00000103542; ENSMUSG00000069769. [Q920Q6-2]
DR GeneID; 76626; -.
DR KEGG; mmu:76626; -.
DR UCSC; uc007kvl.2; mouse. [Q920Q6-1]
DR UCSC; uc007kvn.2; mouse. [Q920Q6-3]
DR CTD; 124540; -.
DR MGI; MGI:1923876; Msi2.
DR VEuPathDB; HostDB:ENSMUSG00000069769; -.
DR eggNOG; KOG4205; Eukaryota.
DR GeneTree; ENSGT00940000155420; -.
DR HOGENOM; CLU_012062_3_0_1; -.
DR InParanoid; Q920Q6; -.
DR OMA; PLAREMW; -.
DR OrthoDB; 1565323at2759; -.
DR PhylomeDB; Q920Q6; -.
DR Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR BioGRID-ORCS; 76626; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Msi2; mouse.
DR PRO; PR:Q920Q6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q920Q6; protein.
DR Bgee; ENSMUSG00000069769; Expressed in rostral migratory stream and 222 other tissues.
DR ExpressionAtlas; Q920Q6; baseline and differential.
DR Genevisible; Q920Q6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005844; C:polysome; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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:0006417; P:regulation of translation; IBA:GO_Central.
DR GO; GO:0048864; P:stem cell development; IMP:UniProtKB.
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 Acetylation; Alternative splicing; Cytoplasm; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..346
FT /note="RNA-binding protein Musashi homolog 2"
FT /id="PRO_0000081653"
FT DOMAIN 21..111
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 110..187
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96DH6"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96DH6"
FT MOD_RES 228
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 261
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 264..282
FT /note="VLNSYSAQPNFGAPASPAG -> GRKVYGAGGSQACLVCRGR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011172"
FT VAR_SEQ 264..281
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11588182"
FT /id="VSP_011173"
FT VAR_SEQ 283..346
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011174"
SQ SEQUENCE 346 AA; 36939 MW; C2C75F2D7077AF61 CRC64;
MEANGSPGTS GSANDSQHDP GKMFIGGLSW QTSPDSLRDY FSKFGEIREC MVMRDPTTKR
SRGFGFVTFA DPASVDKVLG QPHHELDSKT IDPKVAFPRR AQPKMVTRTK KIFVGGLSAN
TVVEDVKQYF EQFGKVEDAM LMFDKTTNRH RGFGFVTFEN EDVVEKVCEI HFHEINNKMV
ECKKAQPKEV MFPPGTRGRA RGLPYTMDAF MLGMGMLGYP NFVATYGRGY PGFAPSYGYQ
FPGFPAAAYG PVAAAAVAAA RGSVLNSYSA QPNFGAPASP AGSNPARPGG FPGANSPGPV
ADLYGPASQD SGVGNYISAA SPQPGSGFGH GIAGPLIATA FTNGYH
