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O43347 (MSI1H_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-binding protein Musashi homolog 1

Short name=Musashi-1
Gene names
Name:MSI1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existenceEvidence 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 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

Detected in fetal kidney, brain, liver and lung, and in adult brain and pancreas. Detected in hepatoma cell lines. Ref.1 Ref.3

Domain

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

Sequence similarities

Belongs to the Musashi family.

Contains 2 RRM (RNA recognition motif) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362RNA-binding protein Musashi homolog 1
PRO_0000081649

Regions

Domain20 – 11091RRM 1
Domain109 – 18678RRM 2
Compositional bias274 – 2818Poly-Ala

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5 Ref.7
Modified residue1911Phosphoserine Ref.7

Natural variations

Natural variant1601E → Q in a breast cancer sample; somatic mutation. Ref.8
VAR_035485

Experimental info

Sequence conflict1971R → W in BAB70469. Ref.3
Sequence conflict2251T → S in BAB69769. Ref.3
Sequence conflict2321Y → C in BAB69769. Ref.3
Sequence conflict2361A → P in BAB69767. Ref.3
Sequence conflict2451E → K in BAB70469. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O43347 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 26487B0A32CF1F40

FASTA36239,125
        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 
TVEDVKQYFE QFGKVDDAML MFDKTTNRHR GFGFVTFESE DIVEKVCEIH FHEINNKMVE 

       190        200        210        220        230        240 
CKKAQPKEVM SPTGSARGRS RVMPYGMDAF MLGIGMLGYP GFQATTYASR SYTGLAPGYT 

       250        260        270        280        290        300 
YQFPEFRVER TPLPSAPVLP ELTAIPLTAY GPMAAAAAAA AVVRGTGSHP WTMAPPPGST 

       310        320        330        340        350        360 
PSRTGGFLGT TSPGPMAELY GAANQDSGVS SYISAASPAP STGFGHSLGG PLIATAFTNG 


YH 

« Hide

References

« Hide 'large scale' references
[1]"The human Musashi homolog 1 (MSI1) gene encoding the homologue of Musashi/Nrp-1, a neural RNA-binding protein putatively expressed in CNS stem cells and neural progenitor cells."
Good P., Yoda A., Sakakibara S., Yamamoto A., Imai T., Sawa H., Ikeuchi T., Tsuji S., Satoh H., Okano H.
Genomics 52:382-384(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
Tissue: Fetal brain.
[2]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Expression of the Musashi1 gene encoding the RNA-binding protein in human hepatoma cell lines."
Shu H.-J., Saito T., Watanabe H., Ito J., Takeda H., Okano H., Kawata S.
Biochem. Biophys. Res. Commun. 293:150-154(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 64-245, TISSUE SPECIFICITY.
[4]"Musashi: a translational regulator of cell fate."
Okano H., Imai T., Okabe M.
J. Cell Sci. 115:1355-1359(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[5]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-160.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB012851 mRNA. Translation: BAA33962.1.
AC003982 Genomic DNA. Translation: AAB95636.1.
AB072590 mRNA. Translation: BAB69767.1.
AB072591 mRNA. Translation: BAB69768.1.
AB072592 mRNA. Translation: BAB69769.1.
AB073212 mRNA. Translation: BAB70469.1.
RefSeqNP_002433.1. NM_002442.3.
UniGeneHs.158311.

3D structure databases

ProteinModelPortalO43347.
SMRO43347. Positions 18-187.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110577. 3 interactions.
IntActO43347. 1 interaction.
MINTMINT-1432501.
STRING9606.ENSP00000257552.

PTM databases

PhosphoSiteO43347.

Proteomic databases

PaxDbO43347.
PRIDEO43347.

Protocols and materials databases

DNASU4440.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257552; ENSP00000257552; ENSG00000135097.
GeneID4440.
KEGGhsa:4440.
UCSCuc001tye.2. human.

Organism-specific databases

CTD4440.
GeneCardsGC12M120779.
HGNCHGNC:7330. MSI1.
HPACAB022337.
MIM603328. gene.
neXtProtNX_O43347.
PharmGKBPA31137.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000234441.
HOVERGENHBG002295.
InParanoidO43347.
KOK14411.
OMAMETDAPQ.
OrthoDBEOG715Q6V.
PhylomeDBO43347.
TreeFamTF325419.

Gene expression databases

ArrayExpressO43347.
BgeeO43347.
CleanExHS_MSI1.
GenevestigatorO43347.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMSI1.
GenomeRNAi4440.
NextBio17313.
PROO43347.
SOURCESearch...

Entry information

Entry nameMSI1H_HUMAN
AccessionPrimary (citable) accession number: O43347
Secondary accession number(s): Q96PU0 expand/collapse secondary AC list , Q96PU1, Q96PU2, Q96PU3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM