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Protein

RNA-binding protein Musashi homolog 1

Gene

Msi1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RNA binding protein that regulates the expression of target mRNAs at the translation level. Regulates expression of the NOTCH1 antagonist NUMB. Binds RNA containing the sequence 5'-GUUAGUUAGUUAGUU-3' and other sequences containing the pattern 5'-[GA]U1-3AGU-3'. May play a role in the proliferation and maintenance of stem cells in the central nervous system.2 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: MGI
  • poly(U) RNA binding Source: MGI
  • single-stranded RNA binding Source: MGI
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding protein Musashi homolog 1
Short name:
Musashi-1
Gene namesi
Name:Msi1
Synonyms:Msi1h
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:107376. Msi1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nucleus Source: MGI
  • polysome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631F → L: Abolishes RNA binding; when associated with L-65 and L-68. 1 Publication
Mutagenesisi65 – 651F → L: Abolishes RNA binding; when associated with L-63 and L-68. 1 Publication
Mutagenesisi68 – 681F → L: Abolishes RNA binding; when associated with L-63 and L-65. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 362362RNA-binding protein Musashi homolog 1PRO_0000081650Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei191 – 1911PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ61474.
MaxQBiQ61474.
PaxDbiQ61474.
PRIDEiQ61474.

PTM databases

iPTMnetiQ61474.
PhosphoSiteiQ61474.

Expressioni

Tissue specificityi

Detected in olfactory bulb, brain stem, small intestine, and at low levels in brain cortex, hippocampus and ovary. Detected in neural progenitor cells, including neural stem cells.1 Publication

Developmental stagei

Highly expressed in embryonic brain at day 12. Expressed at intermediate levels during the rest of embryonic development and in newborns up to day 3. After this expression decreases and stabilizes at low levels of expression around day 13.

Gene expression databases

BgeeiQ61474.
CleanExiMM_MSI1.
ExpressionAtlasiQ61474. baseline and differential.
GenevisibleiQ61474. MM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-8327453,EBI-8327453

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

IntActiQ61474. 5 interactions.
MINTiMINT-4102437.
STRINGi10090.ENSMUSP00000120516.

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 265Combined sources
Helixi34 – 407Combined sources
Turni41 – 433Combined sources
Beta strandi49 – 524Combined sources
Beta strandi57 – 593Combined sources
Beta strandi61 – 666Combined sources
Helixi73 – 797Combined sources
Turni80 – 823Combined sources
Beta strandi83 – 853Combined sources
Beta strandi91 – 944Combined sources
Beta strandi111 – 1144Combined sources
Helixi122 – 1309Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi151 – 1566Combined sources
Helixi160 – 1678Combined sources
Beta strandi168 – 1703Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi180 – 1823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UAWNMR-A20-96[»]
2MSSNMR-A110-184[»]
2MSTNMR-A110-184[»]
2RS2NMR-A20-103[»]
ProteinModelPortaliQ61474.
SMRiQ61474. Positions 18-187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ61474.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 11091RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini109 – 18678RRM 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi274 – 2818Poly-Ala

Domaini

The first RNA recognition motif binds more strongly to RNA compared to the second one.

Sequence similaritiesi

Belongs to the Musashi family.Curated
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4205. Eukaryota.
ENOG410YA8Z. LUCA.
GeneTreeiENSGT00730000110584.
HOVERGENiHBG002295.
InParanoidiQ61474.
KOiK14411.
OMAiHYFEQFG.
OrthoDBiEOG715Q6V.
PhylomeDBiQ61474.
TreeFamiTF325419.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q61474-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
METDAPQPGL ASPDSPHDPC KMFIGGLSWQ TTQEGLREYF GQFGEVKECL
60 70 80 90 100
VMRDPLTKRS RGFGFVTFMD QAGVDKVLAQ SRHELDSKTI DPKVAFPRRA
110 120 130 140 150
QPKMVTRTKK IFVGGLSVNT TVEDVKHYFE QFGKVDDAML MFDKTTNRHR
160 170 180 190 200
GFGFVTFESE DIVEKVCEIH FHEINNKMVE CKKAQPKEVM SPTGSARGRS
210 220 230 240 250
RVMPYGMDAF MLGIGMLGYP GFQATTYASR SYTGLAPGYT YQFPEFRVER
260 270 280 290 300
SPLPSAPVLP ELTAIPLTAY GPMAAAAAAA AVVRGTGSHP WTMAPPPGST
310 320 330 340 350
PSRTGGFLGT TSPGPMAELY GAANQDSGVS SYISAASPAP STGFGHSLGG
360
PLIATAFTNG YH
Length:362
Mass (Da):39,119
Last modified:November 1, 1996 - v1
Checksum:i75C316BB384AE211
GO
Isoform 2 (identifier: Q61474-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     264-362: AIPLTAYGPM...IATAFTNGYH → GQWLRFRASH...GREAKPGRRR

Note: No experimental confirmation available.
Show »
Length:301
Mass (Da):34,029
Checksum:i9DE83A292A51E4B1
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121Missing in isoform 2. 1 PublicationVSP_011166Add
BLAST
Alternative sequencei264 – 36299AIPLT…TNGYH → GQWLRFRASHRPRGEKGGER DCPLPRGEAGRTTVPGHWPV SSATWPSRVGREAKPGRRR in isoform 2. 1 PublicationVSP_011167Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49654 mRNA. Translation: BAA08530.1.
AK084019 mRNA. Translation: BAC39099.1.
CCDSiCCDS19591.1. [Q61474-1]
RefSeqiNP_032655.1. NM_008629.1. [Q61474-1]
UniGeneiMm.391995.
Mm.5077.

Genome annotation databases

EnsembliENSMUST00000150779; ENSMUSP00000120516; ENSMUSG00000054256. [Q61474-1]
GeneIDi17690.
KEGGimmu:17690.
UCSCiuc008zdu.1. mouse. [Q61474-2]
uc008zdv.1. mouse. [Q61474-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49654 mRNA. Translation: BAA08530.1.
AK084019 mRNA. Translation: BAC39099.1.
CCDSiCCDS19591.1. [Q61474-1]
RefSeqiNP_032655.1. NM_008629.1. [Q61474-1]
UniGeneiMm.391995.
Mm.5077.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UAWNMR-A20-96[»]
2MSSNMR-A110-184[»]
2MSTNMR-A110-184[»]
2RS2NMR-A20-103[»]
ProteinModelPortaliQ61474.
SMRiQ61474. Positions 18-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ61474. 5 interactions.
MINTiMINT-4102437.
STRINGi10090.ENSMUSP00000120516.

PTM databases

iPTMnetiQ61474.
PhosphoSiteiQ61474.

Proteomic databases

EPDiQ61474.
MaxQBiQ61474.
PaxDbiQ61474.
PRIDEiQ61474.

Protocols and materials databases

DNASUi17690.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000150779; ENSMUSP00000120516; ENSMUSG00000054256. [Q61474-1]
GeneIDi17690.
KEGGimmu:17690.
UCSCiuc008zdu.1. mouse. [Q61474-2]
uc008zdv.1. mouse. [Q61474-1]

Organism-specific databases

CTDi4440.
MGIiMGI:107376. Msi1.

Phylogenomic databases

eggNOGiKOG4205. Eukaryota.
ENOG410YA8Z. LUCA.
GeneTreeiENSGT00730000110584.
HOVERGENiHBG002295.
InParanoidiQ61474.
KOiK14411.
OMAiHYFEQFG.
OrthoDBiEOG715Q6V.
PhylomeDBiQ61474.
TreeFamiTF325419.

Miscellaneous databases

EvolutionaryTraceiQ61474.
NextBioi292270.
PROiQ61474.
SOURCEiSearch...

Gene expression databases

BgeeiQ61474.
CleanExiMM_MSI1.
ExpressionAtlasiQ61474. baseline and differential.
GenevisibleiQ61474. MM.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse-Musashi-1, a neural RNA-binding protein highly enriched in the mammalian CNS stem cell."
    Sakakibara S., Imai T., Hamaguchi K., Okabe M., Aruga J., Nakajima K., Yasutomi D., Nagata T., Kurihara Y., Uesugi S., Miyata T., Ogawa M., Mikoshiba K., Okano H.
    Dev. Biol. 176:230-242(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, TISSUE SPECIFICITY.
    Strain: ICR.
    Tissue: Cerebellum.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Spinal ganglion.
  3. "The neural RNA-binding protein Musashi1 translationally regulates mammalian numb gene expression by interacting with its mRNA."
    Imai T., Tokunaga A., Yoshida T., Hashimoto M., Mikoshiba K., Weinmaster G., Nakafuku M., Okano H.
    Mol. Cell. Biol. 21:3888-3900(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF PHE-63; PHE-65 AND PHE-68.
  4. "RNA-binding protein Musashi family: roles for CNS stem cells and a subpopulation of ependymal cells revealed by targeted disruption and antisense ablation."
    Sakakibara S., Nakamura Y., Yoshida T., Shibata S., Koike M., Takano H., Ueda S., Uchiyama Y., Noda T., Okano H.
    Proc. Natl. Acad. Sci. U.S.A. 99:15194-15199(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.
  6. "Structure, backbone dynamics and interactions with RNA of the C-terminal RNA-binding domain of a mouse neural RNA-binding protein, Musashi1."
    Nagata T., Kanno R., Kurihara Y., Uesugi S., Imai T., Sakakibara S., Okano H., Katahira M.
    J. Mol. Biol. 287:315-330(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 110-184, INTERACTION WITH RNA.
  7. "Origin of higher affinity to RNA of the N-terminal RNA-binding domain than that of the C-terminal one of a mouse neural protein, musashi1, as revealed by comparison of their structures, modes of interaction, surface electrostatic potentials, and backbone dynamics."
    Miyanoiri Y., Kobayashi H., Imai T., Watanabe M., Nagata T., Uesugi S., Okano H., Katahira M.
    J. Biol. Chem. 278:41309-41315(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 20-96, INTERACTION WITH RNA.

Entry informationi

Entry nameiMSI1H_MOUSE
AccessioniPrimary (citable) accession number: Q61474
Secondary accession number(s): Q8BNC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1996
Last modified: April 13, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.