Reviewed, UniProtKB/Swiss-Prot Q61474 (MSI1H_MOUSE)

Names and origin

Protein names

Recommended name:
    RNA-binding protein Musashi homolog 1
      Short name=Musashi-1

Gene names

Name:	Msi1
Synonyms:	Msi1h

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	362 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.3 Ref.4
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Tissue specificity	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. Ref.1
Developmental stage	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.
Domain	The first RNA recognition motif binds more strongly to RNA compared to the second one.
Sequence similarities	Belongs to the Musashi family. Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from direct assay. Source: MGI nucleus Inferred from direct assay. Source: MGI polysome Inferred from direct assay. Source: MGI
Molecular function	nucleotide binding Inferred from electronic annotation. Source: InterPro poly(U) RNA binding Inferred from direct assay. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q61474-1)

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.

Isoform 2 (identifier: Q61474-2)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 362

362

RNA-binding protein Musashi homolog 1

PRO_0000081650

Regions

Domain

20 – 110

91

RRM 1

Domain

109 – 186

78

RRM 2

Compositional bias

274 – 281

8

Poly-Ala

Amino acid modifications

Modified residue

1

1

N-acetylmethionine By similarity

Modified residue

12

1

Phosphoserine By similarity

Modified residue

191

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 21

21

Missing in isoform 2.

VSP_011166

Alternative sequence

264 – 362

99

AIPLT…TNGYH → GQWLRFRASHRPRGEKGGER DCPLPRGEAGRTTVPGHWPV SSATWPSRVGREAKPGRRR in isoform 2.

VSP_011167

Experimental info

Mutagenesis

63

1

F → L: Abolishes RNA binding; when associated with L-65 and L-68. Ref.3

Mutagenesis

65

1

F → L: Abolishes RNA binding; when associated with L-63 and L-68. Ref.3

Mutagenesis

68

1

F → L: Abolishes RNA binding; when associated with L-63 and L-65. Ref.3

Secondary structure

1

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362

Helix Strand Turn

Details...

Beta strand

22 – 26

5

Helix

34 – 40

7

Turn

41 – 43

3

Beta strand

49 – 52

4

Beta strand

57 – 59

3

Beta strand

61 – 66

6

Helix

73 – 79

7

Turn

80 – 82

3

Beta strand

91 – 94

4

Beta strand

111 – 114

4

Helix

122 – 130

9

Beta strand

136 – 138

3

Beta strand

144 – 146

3

Beta strand

151 – 156

6

Helix

160 – 167

8

Beta strand

168 – 170

3

Beta strand

174 – 176

3

Beta strand

180 – 182

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 75C316BB384AE211	FASTA	362	39,119
	10 20 30 40 50 60 METDAPQPGL ASPDSPHDPC KMFIGGLSWQ TTQEGLREYF GQFGEVKECL VMRDPLTKRS 70 80 90 100 110 120 RGFGFVTFMD QAGVDKVLAQ SRHELDSKTI DPKVAFPRRA QPKMVTRTKK IFVGGLSVNT 130 140 150 160 170 180 TVEDVKHYFE QFGKVDDAML MFDKTTNRHR GFGFVTFESE DIVEKVCEIH FHEINNKMVE 190 200 210 220 230 240 CKKAQPKEVM SPTGSARGRS RVMPYGMDAF MLGIGMLGYP GFQATTYASR SYTGLAPGYT 250 260 270 280 290 300 YQFPEFRVER SPLPSAPVLP ELTAIPLTAY GPMAAAAAAA AVVRGTGSHP WTMAPPPGST 310 320 330 340 350 360 PSRTGGFLGT TSPGPMAELY GAANQDSGVS SYISAASPAP STGFGHSLGG PLIATAFTNG YH
	Isoform 2. Checksum: 9DE83A292A51E4B1	FASTA	301	34,029
	10 20 30 40 50 60 MFIGGLSWQT TQEGLREYFG QFGEVKECLV MRDPLTKRSR GFGFVTFMDQ AGVDKVLAQS 70 80 90 100 110 120 RHELDSKTID PKVAFPRRAQ PKMVTRTKKI FVGGLSVNTT VEDVKHYFEQ FGKVDDAMLM 130 140 150 160 170 180 FDKTTNRHRG FGFVTFESED IVEKVCEIHF HEINNKMVEC KKAQPKEVMS PTGSARGRSR 190 200 210 220 230 240 VMPYGMDAFM LGIGMLGYPG FQATTYASRS YTGLAPGYTY QFPEFRVERS PLPSAPVLPE 250 260 270 280 290 300 LTGQWLRFRA SHRPRGEKGG ERDCPLPRGE AGRTTVPGHW PVSSATWPSR VGREAKPGRR R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8660864] [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: 16141072] [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: 11359897] [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: 12407178] [Abstract] Cited for: FUNCTION.
[5]	"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: 10080895] [Abstract] Cited for: STRUCTURE BY NMR OF 110-184, INTERACTION WITH RNA.
[6]	"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: 12907678] [Abstract] Cited for: STRUCTURE BY NMR OF 20-96, INTERACTION WITH RNA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D49654 mRNA. Translation: BAA08530.1.
AK084019 mRNA. Translation: BAC39099.1.

IPI

IPI00121300.
IPI00462260.

RefSeq

NP_032655.1.

UniGene

Mm.5077

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UAW	NMR	-	A	20-96	[»]
2MSS	NMR	-	A	110-184	[»]
2MST	NMR	-	A	110-184	[»]

SMR

Q61474. Positions 18-188.

ModBase

Search...

Protein-protein interaction databases

STRING

Q61474.

Proteomic databases

PRIDE

Q61474.

Genome annotation databases

Ensembl

ENSMUST00000067168; ENSMUSP00000070415; ENSMUSG00000054256; Mus musculus. [Genome view]

GeneID

17690.

KEGG

mmu:17690.

UCSC

uc008zdu.1. mouse.
uc008zdv.1. mouse.

Organism-specific databases

CTD

17690.

MGI

MGI:107376. Msi1.

Phylogenomic databases

eggNOG

roNOG08785.

HOGENOM

HBG756718.

HOVERGEN

Q61474.

InParanoid

Q61474.

OMA

FMDQAGV.

OrthoDB

EOG9QRKPM.

Gene expression databases

ArrayExpress

Q61474.

Bgee

Q61474.

CleanEx

MM_MSI1.

Genevestigator

Q61474.

GermOnline

ENSMUSG00000054256. Mus musculus.

Family and domain databases

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.

Pfam

PF00076. RRM_1. 2 hits.
[Graphical view]

SMART

SM00360. RRM. 2 hits.
[Graphical view]

PROSITE

PS50102. RRM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

292270.

SOURCE

Search...

Entry information

Entry name

MSI1H_MOUSE

Accession

Primary (citable) accession number: Q61474
Secondary accession number(s): Q8BNC7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)