MS3L1_MOUSE
ID MS3L1_MOUSE Reviewed; 525 AA.
AC Q9WVG9; B1AUJ7; B1AUJ8;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Male-specific lethal 3 homolog;
DE AltName: Full=Male-specific lethal-3 homolog 1;
DE AltName: Full=Male-specific lethal-3 protein-like 1;
DE Short=MSL3-like 1;
GN Name=Msl3; Synonyms=Msl31, Msl3l1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10395802; DOI=10.1006/geno.1999.5844;
RA Prakash S.K., Van den Veyver I.B., Franco B., Volta M., Ballabio A.,
RA Zoghbi H.Y.;
RT "Characterization of a novel chromo domain gene in Xp22.3 with homology to
RT Drosophila msl-3.";
RL Genomics 59:77-84(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; SER-315; THR-409;
RP SER-411 AND SER-415, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH MSL1.
RX PubMed=21217699; DOI=10.1038/nsmb.1960;
RA Kadlec J., Hallacli E., Lipp M., Holz H., Sanchez-Weatherby J., Cusack S.,
RA Akhtar A.;
RT "Structural basis for MOF and MSL3 recruitment into the dosage compensation
RT complex by MSL1.";
RL Nat. Struct. Mol. Biol. 18:142-149(2011).
CC -!- FUNCTION: Has a role in chromatin remodeling and transcriptional
CC regulation. Has a role in X inactivation. Component of the MSL complex
CC which is responsible for the majority of histone H4 acetylation at
CC 'Lys-16' which is implicated in the formation of higher-order chromatin
CC structure. Specifically recognizes histone H4 monomethylated at 'Lys-
CC 20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved
CC in chromosomal targeting of the MSL complex.
CC {ECO:0000250|UniProtKB:Q8N5Y2}.
CC -!- SUBUNIT: Component of the MSL histone acetyltransferase complex at
CC least composed of the KAT8/MOF, MSL1/hampin, MSL2 and MSL3. Interacts
CC (via the MRG domain) with MSL1 and KAT8/MOF (PubMed:21217699).
CC {ECO:0000250|UniProtKB:Q8N5Y2, ECO:0000269|PubMed:21217699}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N5Y2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WVG9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WVG9-2; Sequence=VSP_007638, VSP_007639;
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DR EMBL; AF117066; AAD38500.2; -; mRNA.
DR EMBL; AL671489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010226; AAH10226.1; -; mRNA.
DR CCDS; CCDS41211.1; -. [Q9WVG9-2]
DR CCDS; CCDS90775.1; -. [Q9WVG9-1]
DR RefSeq; NP_034962.2; NM_010832.5. [Q9WVG9-2]
DR RefSeq; XP_006528804.1; XM_006528741.3.
DR AlphaFoldDB; Q9WVG9; -.
DR SMR; Q9WVG9; -.
DR BioGRID; 201532; 7.
DR ComplexPortal; CPX-859; MSL histone acetyltransferase complex.
DR IntAct; Q9WVG9; 1.
DR STRING; 10090.ENSMUSP00000107765; -.
DR iPTMnet; Q9WVG9; -.
DR PhosphoSitePlus; Q9WVG9; -.
DR EPD; Q9WVG9; -.
DR jPOST; Q9WVG9; -.
DR MaxQB; Q9WVG9; -.
DR PaxDb; Q9WVG9; -.
DR PeptideAtlas; Q9WVG9; -.
DR PRIDE; Q9WVG9; -.
DR ProteomicsDB; 290062; -. [Q9WVG9-1]
DR ProteomicsDB; 290063; -. [Q9WVG9-2]
DR Antibodypedia; 23748; 132 antibodies from 21 providers.
DR DNASU; 17692; -.
DR Ensembl; ENSMUST00000033725; ENSMUSP00000033725; ENSMUSG00000031358. [Q9WVG9-1]
DR Ensembl; ENSMUST00000112137; ENSMUSP00000107765; ENSMUSG00000031358. [Q9WVG9-2]
DR GeneID; 17692; -.
DR KEGG; mmu:17692; -.
DR UCSC; uc009uxh.2; mouse. [Q9WVG9-2]
DR UCSC; uc009uxi.1; mouse. [Q9WVG9-1]
DR CTD; 10943; -.
DR MGI; MGI:1341851; Msl3.
DR VEuPathDB; HostDB:ENSMUSG00000031358; -.
DR eggNOG; KOG3001; Eukaryota.
DR GeneTree; ENSGT00950000182965; -.
DR HOGENOM; CLU_039566_5_2_1; -.
DR InParanoid; Q9WVG9; -.
DR OMA; GMKFQFH; -.
DR OrthoDB; 1624495at2759; -.
DR PhylomeDB; Q9WVG9; -.
DR TreeFam; TF323400; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR BioGRID-ORCS; 17692; 8 hits in 61 CRISPR screens.
DR ChiTaRS; Msl3; mouse.
DR PRO; PR:Q9WVG9; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9WVG9; protein.
DR Bgee; ENSMUSG00000031358; Expressed in interventricular septum and 256 other tissues.
DR Genevisible; Q9WVG9; MM.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0072487; C:MSL complex; ISS:UniProtKB.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0046972; F:histone acetyltransferase activity (H4-K16 specific); ISS:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0043968; P:histone H2A acetylation; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR Gene3D; 1.10.274.30; -; 2.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR008676; MRG.
DR InterPro; IPR038217; MRG_C_sf.
DR InterPro; IPR026541; MRG_dom.
DR InterPro; IPR037921; MSL3.
DR InterPro; IPR025995; Tudor-knot.
DR PANTHER; PTHR10880; PTHR10880; 1.
DR PANTHER; PTHR10880:SF36; PTHR10880:SF36; 1.
DR Pfam; PF05712; MRG; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS51640; MRG; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..525
FT /note="Male-specific lethal 3 homolog"
FT /id="PRO_0000080248"
FT DOMAIN 13..72
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 172..521
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 119..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..444
FT /note="Required for the histone acetyltransferase activity
FT of the MSL complex"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y2"
FT REGION 302..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y2"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y2"
FT MOD_RES 409
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..59
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007638"
FT VAR_SEQ 60..61
FT /note="NR -> MP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007639"
SQ SEQUENCE 525 AA; 60292 MW; 0C209A8F32E1984A CRC64;
MSASEGMKFQ FHSGEKVLCF EPDPTKARVL YDAKIIDVII GKDEKGRKIP EYLIHFNGWN
RSWDRWAAEE HVLHDTDENR RLQRKLAKKA IARLRGTGKK KRRCRLPGVD SVLKSVPVKE
KSKNDENSVS STCHESCGEK NGGIKEHRQR RIKVKAKAKK KVLSLRSRKE MDERTITIDI
PDVLKKQLED DCYYINRRKR LVKLPCQTNI ITILESYVKH FAINAAFSAN ERPRHHHAMM
HTHMNVHYVP AEKNVDLCKE MVDGLRITFD YTLPLVLLYP YEQTQYKRVT SSKFFLPIKE
STTTTNRSQE ELSPSPPLLN PSTPQSTESQ PPTGEPATPK RRKAEPEALQ SLRRSTRHST
NCDRLSESSS SPQPKRRQQD TSASMPKLFL HLEKKTPVHS RSSSPIPLTP SKDGSAVFAG
FEGRRPNEIN EVLSWKLVPD NYPPGDQPPP PSYIYGAQHL LRLFVKLPEI LGKMSFSEKN
LKALLKHFDL FLRFLAEYHD DFFPESAYVA ACEAHYSTKN PRAIY
