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O43347

- MSI1H_HUMAN

UniProt

O43347 - MSI1H_HUMAN

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Protein
RNA-binding protein Musashi homolog 1
Gene
MSI1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 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 By similarity.

GO - Molecular functioni

  1. RNA binding Source: ProtInc
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. poly(U) RNA binding Source: Ensembl

GO - Biological processi

  1. epithelial cell differentiation Source: Ensembl
  2. nervous system development Source: ProtInc
  3. response to hormone Source: Ensembl
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:7330. MSI1.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. polysome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31137.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 362362RNA-binding protein Musashi homolog 1
PRO_0000081649Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei191 – 1911Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO43347.
PaxDbiO43347.
PRIDEiO43347.

PTM databases

PhosphoSiteiO43347.

Expressioni

Tissue specificityi

Detected in fetal kidney, brain, liver and lung, and in adult brain and pancreas. Detected in hepatoma cell lines.2 Publications

Gene expression databases

ArrayExpressiO43347.
BgeeiO43347.
CleanExiHS_MSI1.
GenevestigatoriO43347.

Organism-specific databases

HPAiCAB022337.

Interactioni

Protein-protein interaction databases

BioGridi110577. 4 interactions.
IntActiO43347. 1 interaction.
MINTiMINT-1432501.
STRINGi9606.ENSP00000257552.

Structurei

3D structure databases

ProteinModelPortaliO43347.
SMRiO43347. Positions 18-187.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 11091RRM 1
Add
BLAST
Domaini109 – 18678RRM 2
Add
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 By similarity.

Sequence similaritiesi

Belongs to the Musashi family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
HOGENOMiHOG000234441.
HOVERGENiHBG002295.
InParanoidiO43347.
KOiK14411.
OMAiMETDAPQ.
OrthoDBiEOG715Q6V.
PhylomeDBiO43347.
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]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43347-1 [UniParc]FASTAAdd to Basket

« Hide

METDAPQPGL ASPDSPHDPC KMFIGGLSWQ TTQEGLREYF GQFGEVKECL    50
VMRDPLTKRS RGFGFVTFMD QAGVDKVLAQ SRHELDSKTI DPKVAFPRRA 100
QPKMVTRTKK IFVGGLSVNT TVEDVKQYFE QFGKVDDAML MFDKTTNRHR 150
GFGFVTFESE DIVEKVCEIH FHEINNKMVE CKKAQPKEVM SPTGSARGRS 200
RVMPYGMDAF MLGIGMLGYP GFQATTYASR SYTGLAPGYT YQFPEFRVER 250
TPLPSAPVLP ELTAIPLTAY GPMAAAAAAA AVVRGTGSHP WTMAPPPGST 300
PSRTGGFLGT TSPGPMAELY GAANQDSGVS SYISAASPAP STGFGHSLGG 350
PLIATAFTNG YH 362
Length:362
Mass (Da):39,125
Last modified:June 1, 1998 - v1
Checksum:i26487B0A32CF1F40
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti160 – 1601E → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_035485

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti197 – 1971R → W in BAB70469. 1 Publication
Sequence conflicti225 – 2251T → S in BAB69769. 1 Publication
Sequence conflicti232 – 2321Y → C in BAB69769. 1 Publication
Sequence conflicti236 – 2361A → P in BAB69767. 1 Publication
Sequence conflicti245 – 2451E → K in BAB70469. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS9196.1.
RefSeqiNP_002433.1. NM_002442.3.
UniGeneiHs.158311.

Genome annotation databases

EnsembliENST00000257552; ENSP00000257552; ENSG00000135097.
GeneIDi4440.
KEGGihsa:4440.
UCSCiuc001tye.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS9196.1.
RefSeqi NP_002433.1. NM_002442.3.
UniGenei Hs.158311.

3D structure databases

ProteinModelPortali O43347.
SMRi O43347. Positions 18-187.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110577. 4 interactions.
IntActi O43347. 1 interaction.
MINTi MINT-1432501.
STRINGi 9606.ENSP00000257552.

PTM databases

PhosphoSitei O43347.

Proteomic databases

MaxQBi O43347.
PaxDbi O43347.
PRIDEi O43347.

Protocols and materials databases

DNASUi 4440.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000257552 ; ENSP00000257552 ; ENSG00000135097 .
GeneIDi 4440.
KEGGi hsa:4440.
UCSCi uc001tye.2. human.

Organism-specific databases

CTDi 4440.
GeneCardsi GC12M120779.
HGNCi HGNC:7330. MSI1.
HPAi CAB022337.
MIMi 603328. gene.
neXtProti NX_O43347.
PharmGKBi PA31137.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0724.
HOGENOMi HOG000234441.
HOVERGENi HBG002295.
InParanoidi O43347.
KOi K14411.
OMAi METDAPQ.
OrthoDBi EOG715Q6V.
PhylomeDBi O43347.
TreeFami TF325419.

Miscellaneous databases

GeneWikii MSI1.
GenomeRNAii 4440.
NextBioi 17313.
PROi O43347.
SOURCEi Search...

Gene expression databases

ArrayExpressi O43347.
Bgeei O43347.
CleanExi HS_MSI1.
Genevestigatori O43347.

Family and domain databases

Gene3Di 3.30.70.330. 2 hits.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00076. RRM_1. 2 hits.
[Graphical view ]
SMARTi SM00360. RRM. 2 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-160.

Entry informationi

Entry nameiMSI1H_HUMAN
AccessioniPrimary (citable) accession number: O43347
Secondary accession number(s): Q96PU0
, Q96PU1, Q96PU2, Q96PU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 1998
Last modified: September 3, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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