MS3L1_PONAB
ID MS3L1_PONAB Reviewed; 521 AA.
AC Q5R6Y9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=MSL3L1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in chromatin remodeling and transcriptional
CC regulation. May have a role in X inactivation. Component of the MSL
CC complex which is responsible for the majority of histone H4 acetylation
CC at 'Lys-16' which is implicated in the formation of higher-order
CC chromatin structure. Specifically recognizes histone H4 monomethylated
CC at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be
CC involved in chromosomal targeting of the MSL complex (By similarity).
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.
CC {ECO:0000250|UniProtKB:Q8N5Y2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N5Y2}.
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DR EMBL; CR860334; CAH92471.1; -; mRNA.
DR RefSeq; NP_001126456.1; NM_001132984.2.
DR AlphaFoldDB; Q5R6Y9; -.
DR SMR; Q5R6Y9; -.
DR STRING; 9601.ENSPPYP00000022509; -.
DR Ensembl; ENSPPYT00000023467; ENSPPYP00000022509; ENSPPYG00000020123.
DR GeneID; 100173442; -.
DR KEGG; pon:100173442; -.
DR CTD; 10943; -.
DR eggNOG; KOG3001; Eukaryota.
DR GeneTree; ENSGT00950000182965; -.
DR HOGENOM; CLU_039566_5_2_1; -.
DR InParanoid; Q5R6Y9; -.
DR OMA; GMKFQFH; -.
DR OrthoDB; 1624495at2759; -.
DR TreeFam; TF323400; -.
DR Proteomes; UP000001595; Chromosome X.
DR GO; GO:0072487; C:MSL complex; ISS:UniProtKB.
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:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Chromatin regulator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..521
FT /note="Male-specific lethal 3 homolog"
FT /id="PRO_0000314289"
FT DOMAIN 13..71
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 168..517
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 114..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..440
FT /note="Required for the histone acetyltransferase activity
FT of the MSL complex"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y2"
FT REGION 298..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVG9"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y2"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y2"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y2"
FT MOD_RES 405
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y2"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y2"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Y2"
SQ SEQUENCE 521 AA; 59810 MW; 5F2499E1870BECFC CRC64;
MSASEGMKFK FHSGEKVLCF EPDPTKARVL YDAKIVDVIV GKDEKGRKIP EYLIHFNGWN
RSWDRWAAED HVLRDTDENR RLQRKLARKA VARLRSTGRK KKRCRLPGVD SVLKGLPTEE
KDENDENSLS SSSDCSENKD EEISEESDIE EKTEVKEEPE LQTRREMEER TITIEIPEVL
KKQLEDDCYY INRRKRLVKL PCQTNIITIL ESYVKHFAIN AAFSANERPR HHHVMPHANM
NVHYIPAEKN VDLCKEMVDG LRITFDYTLP LVLLYPYEQA QYKKVTSSKF FLPIKESATS
TNRSQEELSP SPPLLNPSTP QSTESQPTTG EPATPKRRKA EPEALQSLRR STRHSANCDR
LSESSASPQP KRRQQDTSGS MPKLFLHLEK KTPVHSRSSS PIPLTPSKEG SAVFAGFEGR
RTNEINEVLS WKLVPDNYPP GDQPPPPSYI YGAQHLLRLF VKLPEILGKM SFSEKNLKAL
LKHFDLFLRF LAEYHDDFFP ESAYVAACEA HYSTKNPRAI Y
