MSI2H_HUMAN
ID MSI2H_HUMAN Reviewed; 328 AA.
AC Q96DH6; Q7Z6M7; Q8N9T4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=RNA-binding protein Musashi homolog 2;
DE Short=Musashi-2;
GN Name=MSI2;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP CHROMOSOMAL TRANSLOCATIONS, AND TISSUE SPECIFICITY.
RX PubMed=12649177;
RA Barbouti A., Hoeglund M., Johansson B., Lassen C., Nilsson P.-G.,
RA Hagemeijer A., Mitelman F., Fioretos T.;
RT "A novel gene, MSI2, encoding a putative RNA-binding protein is recurrently
RT rearranged at disease progression of chronic myeloid leukemia and forms a
RT fusion gene with HOXA9 as a result of the cryptic t(7;17)(p15;q23).";
RL Cancer Res. 63:1202-1206(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORM 2), CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-228 AND ARG-261, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: RNA binding protein that regulates the expression of target
CC mRNAs at the translation level. May play a role in the proliferation
CC and maintenance of stem cells in the central nervous system (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q96DH6; P31943: HNRNPH1; NbExp=3; IntAct=EBI-2462339, EBI-351590;
CC Q96DH6; P55795: HNRNPH2; NbExp=6; IntAct=EBI-2462339, EBI-352823;
CC Q96DH6; P10636-8: MAPT; NbExp=2; IntAct=EBI-2462339, EBI-366233;
CC Q96DH6; P50222: MEOX2; NbExp=3; IntAct=EBI-2462339, EBI-748397;
CC Q96DH6; Q96DH6: MSI2; NbExp=4; IntAct=EBI-2462339, EBI-2462339;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Associated with polysomes.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=A;
CC IsoId=Q96DH6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96DH6-2; Sequence=VSP_011168, VSP_011170, VSP_011171;
CC Name=3;
CC IsoId=Q96DH6-3; Sequence=VSP_011169, VSP_011170, VSP_011171;
CC -!- TISSUE SPECIFICITY: Ubiquitous; detected at low levels.
CC {ECO:0000269|PubMed:12649177}.
CC -!- INDUCTION: Up-regulated in astrocytes after brain injury.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- DISEASE: Note=Chromosomal aberrations involving MSI2 may contribute to
CC disease progression in chronic myeloid leukemia. Translocation
CC t(7;17)(p15;q23) with HOXA9; translocation t(7;17)(q32-34;q23).
CC {ECO:0000269|PubMed:12649177}.
CC -!- SIMILARITY: Belongs to the Musashi family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MSI2ID42893ch17q23.html";
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DR EMBL; BC001526; AAH01526.1; -; mRNA.
DR EMBL; BC017560; AAH17560.1; -; mRNA.
DR EMBL; AK093888; BAC04244.1; -; mRNA.
DR CCDS; CCDS11596.1; -. [Q96DH6-1]
DR CCDS; CCDS11597.1; -. [Q96DH6-2]
DR RefSeq; NP_620412.1; NM_138962.3. [Q96DH6-1]
DR RefSeq; NP_733839.1; NM_170721.1. [Q96DH6-2]
DR PDB; 6C8U; NMR; -; 1=21-111.
DR PDB; 6DBP; X-ray; 1.60 A; A/B=22-104.
DR PDB; 6NTY; X-ray; 2.10 A; A/B=21-111.
DR PDBsum; 6C8U; -.
DR PDBsum; 6DBP; -.
DR PDBsum; 6NTY; -.
DR AlphaFoldDB; Q96DH6; -.
DR SMR; Q96DH6; -.
DR BioGRID; 125873; 150.
DR IntAct; Q96DH6; 23.
DR MINT; Q96DH6; -.
DR STRING; 9606.ENSP00000284073; -.
DR GlyGen; Q96DH6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96DH6; -.
DR PhosphoSitePlus; Q96DH6; -.
DR BioMuta; MSI2; -.
DR DMDM; 51316513; -.
DR EPD; Q96DH6; -.
DR jPOST; Q96DH6; -.
DR MassIVE; Q96DH6; -.
DR MaxQB; Q96DH6; -.
DR PaxDb; Q96DH6; -.
DR PeptideAtlas; Q96DH6; -.
DR PRIDE; Q96DH6; -.
DR ProteomicsDB; 76288; -. [Q96DH6-1]
DR ProteomicsDB; 76289; -. [Q96DH6-2]
DR ProteomicsDB; 76290; -. [Q96DH6-3]
DR Antibodypedia; 18327; 404 antibodies from 39 providers.
DR DNASU; 124540; -.
DR Ensembl; ENST00000284073.7; ENSP00000284073.2; ENSG00000153944.12. [Q96DH6-1]
DR Ensembl; ENST00000322684.7; ENSP00000313616.3; ENSG00000153944.12. [Q96DH6-2]
DR Ensembl; ENST00000579180.2; ENSP00000462264.1; ENSG00000153944.12. [Q96DH6-3]
DR Ensembl; ENST00000674964.1; ENSP00000502137.1; ENSG00000153944.12. [Q96DH6-1]
DR GeneID; 124540; -.
DR KEGG; hsa:124540; -.
DR MANE-Select; ENST00000284073.7; ENSP00000284073.2; NM_138962.4; NP_620412.1.
DR UCSC; uc002iuz.2; human. [Q96DH6-1]
DR CTD; 124540; -.
DR DisGeNET; 124540; -.
DR GeneCards; MSI2; -.
DR HGNC; HGNC:18585; MSI2.
DR HPA; ENSG00000153944; Low tissue specificity.
DR MIM; 607897; gene.
DR neXtProt; NX_Q96DH6; -.
DR OpenTargets; ENSG00000153944; -.
DR PharmGKB; PA38590; -.
DR VEuPathDB; HostDB:ENSG00000153944; -.
DR eggNOG; KOG4205; Eukaryota.
DR GeneTree; ENSGT00940000155420; -.
DR HOGENOM; CLU_012062_3_1_1; -.
DR InParanoid; Q96DH6; -.
DR OMA; PLAREMW; -.
DR OrthoDB; 1565323at2759; -.
DR PhylomeDB; Q96DH6; -.
DR TreeFam; TF325419; -.
DR PathwayCommons; Q96DH6; -.
DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
DR SignaLink; Q96DH6; -.
DR SIGNOR; Q96DH6; -.
DR BioGRID-ORCS; 124540; 35 hits in 1075 CRISPR screens.
DR ChiTaRS; MSI2; human.
DR GenomeRNAi; 124540; -.
DR Pharos; Q96DH6; Tbio.
DR PRO; PR:Q96DH6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96DH6; protein.
DR Bgee; ENSG00000153944; Expressed in corpus epididymis and 186 other tissues.
DR ExpressionAtlas; Q96DH6; baseline and differential.
DR Genevisible; Q96DH6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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:0006417; P:regulation of translation; IBA:GO_Central.
DR GO; GO:0048864; P:stem cell development; 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 3D-structure; Acetylation; Alternative splicing; Chromosomal rearrangement;
KW Cytoplasm; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..328
FT /note="RNA-binding protein Musashi homolog 2"
FT /id="PRO_0000081652"
FT DOMAIN 21..111
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 110..187
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 217..218
FT /note="Breakpoint for translocation to form MSI2/HOXA9
FT fusion protein"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 228
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 261
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011169"
FT VAR_SEQ 1..21
FT /note="MEANGSQGTSGSANDSQHDPG -> MADLTSVLTSVMFSPSS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011168"
FT VAR_SEQ 243..255
FT /note="GFPAAAYGPVAAA -> DYLPVSQDIIFIN (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011170"
FT VAR_SEQ 256..328
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011171"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:6DBP"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:6DBP"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6DBP"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:6DBP"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:6C8U"
FT STRAND 62..71
FT /evidence="ECO:0007829|PDB:6DBP"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:6DBP"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6DBP"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6DBP"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6DBP"
FT INIT_MET Q96DH6-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q96DH6-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q96DH6-2:14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
SQ SEQUENCE 328 AA; 35197 MW; 6E2FC929491748A2 CRC64;
MEANGSQGTS GSANDSQHDP GKMFIGGLSW QTSPDSLRDY FSKFGEIREC MVMRDPTTKR
SRGFGFVTFA DPASVDKVLG QPHHELDSKT IDPKVAFPRR AQPKMVTRTK KIFVGGLSAN
TVVEDVKQYF EQFGKVEDAM LMFDKTTNRH RGFGFVTFEN EDVVEKVCEI HFHEINNKMV
ECKKAQPKEV MFPPGTRGRA RGLPYTMDAF MLGMGMLGYP NFVATYGRGY PGFAPSYGYQ
FPGFPAAAYG PVAAAAVAAA RGSGSNPARP GGFPGANSPG PVADLYGPAS QDSGVGNYIS
AASPQPGSGF GHGIAGPLIA TAFTNGYH
