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MSI1H_HUMAN
ID   MSI1H_HUMAN             Reviewed;         362 AA.
AC   O43347; Q96PU0; Q96PU1; Q96PU2; Q96PU3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=RNA-binding protein Musashi homolog 1;
DE            Short=Musashi-1;
GN   Name=MSI1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RC   TISSUE=Fetal brain;
RX   PubMed=9790759; DOI=10.1006/geno.1998.5456;
RA   Good P., Yoda A., Sakakibara S., Yamamoto A., Imai T., Sawa H., Ikeuchi T.,
RA   Tsuji S., Satoh H., Okano H.;
RT   "The human Musashi homolog 1 (MSI1) gene encoding the homologue of
RT   Musashi/Nrp-1, a neural RNA-binding protein putatively expressed in CNS
RT   stem cells and neural progenitor cells.";
RL   Genomics 52:382-384(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 64-245, AND TISSUE SPECIFICITY.
RX   PubMed=12054577; DOI=10.1016/s0006-291x(02)00175-4;
RA   Shu H.-J., Saito T., Watanabe H., Ito J., Takeda H., Okano H., Kawata S.;
RT   "Expression of the Musashi1 gene encoding the RNA-binding protein in human
RT   hepatoma cell lines.";
RL   Biochem. Biophys. Res. Commun. 293:150-154(2002).
RN   [4]
RP   REVIEW.
RX   PubMed=11896183; DOI=10.1242/jcs.115.7.1355;
RA   Okano H., Imai T., Okabe M.;
RT   "Musashi: a translational regulator of cell fate.";
RL   J. Cell Sci. 115:1355-1359(2002).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-191, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [8]
RP   VARIANT [LARGE SCALE ANALYSIS] GLN-160.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: RNA binding protein that regulates the expression of target
CC       mRNAs at the translation level. Regulates expression of the NOTCH1
CC       antagonist NUMB. Binds RNA containing the sequence 5'-GUUAGUUAGUUAGUU-
CC       3' and other sequences containing the pattern 5'-[GA]U(1-3)AGU-3'. May
CC       play a role in the proliferation and maintenance of stem cells in the
CC       central nervous system (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       O43347; P52597: HNRNPF; NbExp=3; IntAct=EBI-726515, EBI-352986;
CC       O43347; P55795: HNRNPH2; NbExp=5; IntAct=EBI-726515, EBI-352823;
CC       O43347; P10636-8: MAPT; NbExp=2; IntAct=EBI-726515, EBI-366233;
CC       O43347; O43347: MSI1; NbExp=2; IntAct=EBI-726515, EBI-726515;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q61474}. Nucleus
CC       {ECO:0000250|UniProtKB:Q61474}.
CC   -!- TISSUE SPECIFICITY: Detected in fetal kidney, brain, liver and lung,
CC       and in adult brain and pancreas. Detected in hepatoma cell lines.
CC       {ECO:0000269|PubMed:12054577, ECO:0000269|PubMed:9790759}.
CC   -!- DOMAIN: The first RNA recognition motif binds more strongly to RNA
CC       compared to the second one. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Musashi family. {ECO:0000305}.
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DR   EMBL; AB012851; BAA33962.1; -; mRNA.
DR   EMBL; AC003982; AAB95636.1; -; Genomic_DNA.
DR   EMBL; AB072590; BAB69767.1; -; mRNA.
DR   EMBL; AB072591; BAB69768.1; -; mRNA.
DR   EMBL; AB072592; BAB69769.1; -; mRNA.
DR   EMBL; AB073212; BAB70469.1; -; mRNA.
DR   CCDS; CCDS9196.1; -.
DR   RefSeq; NP_002433.1; NM_002442.3.
DR   RefSeq; XP_011536663.1; XM_011538361.2.
DR   AlphaFoldDB; O43347; -.
DR   SMR; O43347; -.
DR   BioGRID; 110577; 123.
DR   IntAct; O43347; 14.
DR   MINT; O43347; -.
DR   STRING; 9606.ENSP00000257552; -.
DR   GlyGen; O43347; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; O43347; -.
DR   PhosphoSitePlus; O43347; -.
DR   SwissPalm; O43347; -.
DR   BioMuta; MSI1; -.
DR   EPD; O43347; -.
DR   jPOST; O43347; -.
DR   MassIVE; O43347; -.
DR   MaxQB; O43347; -.
DR   PaxDb; O43347; -.
DR   PeptideAtlas; O43347; -.
DR   PRIDE; O43347; -.
DR   ProteomicsDB; 48907; -.
DR   Antibodypedia; 18945; 658 antibodies from 41 providers.
DR   DNASU; 4440; -.
DR   Ensembl; ENST00000257552.7; ENSP00000257552.2; ENSG00000135097.7.
DR   GeneID; 4440; -.
DR   KEGG; hsa:4440; -.
DR   MANE-Select; ENST00000257552.7; ENSP00000257552.2; NM_002442.4; NP_002433.1.
DR   UCSC; uc001tye.2; human.
DR   CTD; 4440; -.
DR   DisGeNET; 4440; -.
DR   GeneCards; MSI1; -.
DR   HGNC; HGNC:7330; MSI1.
DR   HPA; ENSG00000135097; Tissue enriched (retina).
DR   MIM; 603328; gene.
DR   neXtProt; NX_O43347; -.
DR   OpenTargets; ENSG00000135097; -.
DR   PharmGKB; PA31137; -.
DR   VEuPathDB; HostDB:ENSG00000135097; -.
DR   eggNOG; KOG4205; Eukaryota.
DR   GeneTree; ENSGT00940000156515; -.
DR   InParanoid; O43347; -.
DR   OMA; SWQTTQV; -.
DR   OrthoDB; 1565323at2759; -.
DR   PhylomeDB; O43347; -.
DR   TreeFam; TF325419; -.
DR   PathwayCommons; O43347; -.
DR   Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR   SignaLink; O43347; -.
DR   SIGNOR; O43347; -.
DR   BioGRID-ORCS; 4440; 16 hits in 1077 CRISPR screens.
DR   ChiTaRS; MSI1; human.
DR   GeneWiki; MSI1; -.
DR   GenomeRNAi; 4440; -.
DR   Pharos; O43347; Tbio.
DR   PRO; PR:O43347; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; O43347; protein.
DR   Bgee; ENSG00000135097; Expressed in ventricular zone and 111 other tissues.
DR   ExpressionAtlas; O43347; baseline and differential.
DR   Genevisible; O43347; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005844; C:polysome; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0008266; F:poly(U) RNA binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0006417; P:regulation of translation; IBA:GO_Central.
DR   GO; GO:0009725; P:response to hormone; IEA:Ensembl.
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; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; RNA-binding.
FT   CHAIN           1..362
FT                   /note="RNA-binding protein Musashi homolog 1"
FT                   /id="PRO_0000081649"
FT   DOMAIN          20..110
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          109..186
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   VARIANT         160
FT                   /note="E -> Q (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035485"
FT   CONFLICT        197
FT                   /note="R -> W (in Ref. 3; BAB70469)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="T -> S (in Ref. 3; BAB69769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232
FT                   /note="Y -> C (in Ref. 3; BAB69769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        236
FT                   /note="A -> P (in Ref. 3; BAB69767)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245
FT                   /note="E -> K (in Ref. 3; BAB70469)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   362 AA;  39125 MW;  26487B0A32CF1F40 CRC64;
     METDAPQPGL ASPDSPHDPC KMFIGGLSWQ TTQEGLREYF GQFGEVKECL VMRDPLTKRS
     RGFGFVTFMD QAGVDKVLAQ SRHELDSKTI DPKVAFPRRA QPKMVTRTKK IFVGGLSVNT
     TVEDVKQYFE QFGKVDDAML MFDKTTNRHR GFGFVTFESE DIVEKVCEIH FHEINNKMVE
     CKKAQPKEVM SPTGSARGRS RVMPYGMDAF MLGIGMLGYP GFQATTYASR SYTGLAPGYT
     YQFPEFRVER TPLPSAPVLP ELTAIPLTAY GPMAAAAAAA AVVRGTGSHP WTMAPPPGST
     PSRTGGFLGT TSPGPMAELY GAANQDSGVS SYISAASPAP STGFGHSLGG PLIATAFTNG
     YH
 
 
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