MS3L1_HUMAN
ID MS3L1_HUMAN Reviewed; 521 AA.
AC Q8N5Y2; A6NCU2; A6NHW8; A8K165; B4DUV8; B7Z227; Q9UG70; Q9Y5Z8;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 179.
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 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] (ISOFORM 1), AND ALTERNATIVE SPLICING (ISOFORM
RP 2).
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 MRNA] (ISOFORMS 3; 4; 5 AND 6), AND
RP VARIANT THR-2.
RC TISSUE=Amygdala, Brain, and Hepatoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 283-521.
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP IDENTIFICATION OF MSL COMPLEX COMPONENTS, FUNCTION OF THE MSL COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16227571; DOI=10.1128/mcb.25.21.9175-9188.2005;
RA Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.;
RT "A human protein complex homologous to the Drosophila MSL complex is
RT responsible for the majority of histone H4 acetylation at lysine 16.";
RL Mol. Cell. Biol. 25:9175-9188(2005).
RN [8]
RP ERRATUM OF PUBMED:16227571.
RA Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.;
RL Mol. Cell. Biol. 26:387-387(2006).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN THE MSL COMPLEX.
RX PubMed=16543150; DOI=10.1016/j.molcel.2006.02.007;
RA Mendjan S., Taipale M., Kind J., Holz H., Gebhardt P., Schelder M.,
RA Vermeulen M., Buscaino A., Duncan K., Mueller J., Wilm M.,
RA Stunnenberg H.G., Saumweber H., Akhtar A.;
RT "Nuclear pore components are involved in the transcriptional regulation of
RT dosage compensation in Drosophila.";
RL Mol. Cell 21:811-823(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-407 AND SER-411, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; THR-405 AND SER-407, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP IDENTIFICATION IN THE MSL COMPLEX, AND FUNCTION OF THE MSL COMPLEX.
RX PubMed=20018852; DOI=10.1074/jbc.c109.087981;
RA Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L.,
RA Washburn M.P., Conaway J.W., Conaway R.C.;
RT "Subunit composition and substrate specificity of a MOF-containing histone
RT acetyltransferase distinct from the male-specific lethal (MSL) complex.";
RL J. Biol. Chem. 285:4268-4272(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND IDENTIFICATION BY
RP MASS 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [15]
RP FUNCTION IN MSL COMPLEX, AND INTERACTION WITH MSL1.
RX PubMed=22547026; DOI=10.1038/cr.2012.72;
RA Huang J., Wan B., Wu L., Yang Y., Dou Y., Lei M.;
RT "Structural insight into the regulation of MOF in the male-specific lethal
RT complex and the non-specific lethal complex.";
RL Cell Res. 22:1078-1081(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; SER-367 AND SER-400, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-101 IN COMPLEX WITH DNA AND
RP HISTONE H4, MUTAGENESIS OF HIS-55; TRP-59 AND ARG-65, AND FUNCTION.
RX PubMed=20657587; DOI=10.1038/nsmb.1856;
RA Kim D., Blus B.J., Chandra V., Huang P., Rastinejad F., Khorasanizadeh S.;
RT "Corecognition of DNA and a methylated histone tail by the MSL3
RT chromodomain.";
RL Nat. Struct. Mol. Biol. 17:1027-1029(2010).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-93, MUTAGENESIS OF TYR-31, AND
RP FUNCTION.
RX PubMed=20943666; DOI=10.1074/jbc.m110.134312;
RA Moore S.A., Ferhatoglu Y., Jia Y., Al-Jiab R.A., Scott M.J.;
RT "Structural and biochemical studies on the chromo-barrel domain of male
RT specific lethal 3 (MSL3) reveal a binding preference for mono- or
RT dimethyllysine 20 on histone H4.";
RL J. Biol. Chem. 285:40879-40890(2010).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 167-517 IN COMPLEX WITH MSL1,
RP FUNCTION IN MSL COMPLEX, AND 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).
RN [21]
RP VARIANTS MRXSBA 281-GLN--TYR-521 DEL; PRO-308; 346-GLN--TYR-521 DEL AND
RP 458-ARG--TYR-521 DEL, INVOLVEMENT IN MRXSBA, CHARACTERIZATION OF VARIANT
RP MRXSBA 346-GLN--TYR-521 DEL, INTERACTION WITH KAT8 AND MSL1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=30224647; DOI=10.1038/s41588-018-0220-y;
RG DDD Study;
RA Basilicata M.F., Bruel A.L., Semplicio G., Valsecchi C.I.K., Aktas T.,
RA Duffourd Y., Rumpf T., Morton J., Bache I., Szymanski W.G., Gilissen C.,
RA Vanakker O., Ounap K., Mittler G., van der Burgt I., El Chehadeh S.,
RA Cho M.T., Pfundt R., Tan T.Y., Kirchhoff M., Menten B., Vergult S.,
RA Lindstrom K., Reis A., Johnson D.S., Fryer A., McKay V., Fisher R.B.,
RA Thauvin-Robinet C., Francis D., Roscioli T., Pajusalu S., Radtke K.,
RA Ganesh J., Brunner H.G., Wilson M., Faivre L., Kalscheuer V.M.,
RA Thevenon J., Akhtar A.;
RT "De novo mutations in MSL3 cause an X-linked syndrome marked by impaired
RT histone H4 lysine 16 acetylation.";
RL Nat. Genet. 50:1442-1451(2018).
CC -!- FUNCTION: Has a role in chromatin remodeling and transcriptional
CC regulation (PubMed:20018852, PubMed:20657587, PubMed:20943666,
CC PubMed:21217699, PubMed:30224647). Has a role in X inactivation
CC (PubMed:21217699). Component of the MSL complex which is responsible
CC for the majority of histone H4 acetylation at 'Lys-16' which is
CC implicated in the formation of higher-order chromatin structure
CC (PubMed:16227571, PubMed:20657587, PubMed:16543150, PubMed:30224647).
CC Specifically recognizes histone H4 monomethylated at 'Lys-20'
CC (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in
CC chromosomal targeting of the MSL complex (PubMed:20657587,
CC PubMed:20943666). {ECO:0000269|PubMed:16227571,
CC ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:20018852,
CC ECO:0000269|PubMed:20657587, ECO:0000269|PubMed:20943666,
CC ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:22547026,
CC ECO:0000269|PubMed:30224647}.
CC -!- SUBUNIT: Component of the MSL histone acetyltransferase complex at
CC least composed of the KAT8/MOF, MSL1/hampin, MSL2 and MSL3
CC (PubMed:20018852, PubMed:20657587, PubMed:21217699, PubMed:22547026,
CC PubMed:16543150). Interacts (via the MRG domain) with MSL1 and KAT8/MOF
CC (PubMed:21217699, PubMed:30224647). {ECO:0000269|PubMed:16543150,
CC ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:20657587,
CC ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:22547026,
CC ECO:0000269|PubMed:30224647}.
CC -!- INTERACTION:
CC Q8N5Y2; O76024: WFS1; NbExp=3; IntAct=EBI-2560796, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30224647}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8N5Y2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N5Y2-2; Sequence=VSP_007636, VSP_007637;
CC Name=3;
CC IsoId=Q8N5Y2-3; Sequence=VSP_043342;
CC Name=4;
CC IsoId=Q8N5Y2-4; Sequence=VSP_045652;
CC Name=5;
CC IsoId=Q8N5Y2-5; Sequence=VSP_045653, VSP_045654;
CC Name=6;
CC IsoId=Q8N5Y2-6; Sequence=VSP_055376, VSP_055377;
CC -!- TISSUE SPECIFICITY: Expressed in many tissues including liver,
CC pancreas, heart, lung, kidney, skeletal muscle, brain, and placenta,
CC with highest expression in skeletal muscle and heart.
CC -!- DISEASE: Basilicata-Akhtar syndrome (MRXSBA) [MIM:301032]: An X-linked
CC syndrome characterized by intellectual disability, global developmental
CC delay, progressive gait disturbance, poor or absent speech, facial
CC dysmorphism, and mild distal skeletal anomalies.
CC {ECO:0000269|PubMed:30224647}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: MSL3L1 gene undergoes X inactivation.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF117065; AAD38499.1; -; mRNA.
DR EMBL; AK025642; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK289780; BAF82469.1; -; mRNA.
DR EMBL; AK294255; BAH11713.1; -; mRNA.
DR EMBL; AK300814; BAG62470.1; -; mRNA.
DR EMBL; AC004554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98799.1; -; Genomic_DNA.
DR EMBL; CH471074; EAW98801.1; -; Genomic_DNA.
DR EMBL; BC031210; AAH31210.1; -; mRNA.
DR EMBL; AL050178; CAB43308.1; -; mRNA.
DR EMBL; AL713667; CAD28473.1; -; mRNA.
DR CCDS; CCDS14147.1; -. [Q8N5Y2-1]
DR CCDS; CCDS14148.1; -. [Q8N5Y2-5]
DR CCDS; CCDS14149.1; -. [Q8N5Y2-4]
DR CCDS; CCDS55369.1; -. [Q8N5Y2-3]
DR CCDS; CCDS65213.1; -. [Q8N5Y2-6]
DR PIR; T08795; T08795.
DR RefSeq; NP_001180199.1; NM_001193270.2. [Q8N5Y2-3]
DR RefSeq; NP_001269103.1; NM_001282174.1. [Q8N5Y2-6]
DR RefSeq; NP_006791.2; NM_006800.3. [Q8N5Y2-4]
DR RefSeq; NP_523352.1; NM_078628.1. [Q8N5Y2-5]
DR RefSeq; NP_523353.2; NM_078629.3. [Q8N5Y2-1]
DR RefSeq; XP_005274497.1; XM_005274440.2.
DR PDB; 2Y0N; X-ray; 3.00 A; A/B/C/D=167-289, A/B/C/D=442-518.
DR PDB; 3OA6; X-ray; 2.35 A; A/B=1-101.
DR PDB; 3OB9; X-ray; 2.50 A; A/B/C/D/E=2-93.
DR PDBsum; 2Y0N; -.
DR PDBsum; 3OA6; -.
DR PDBsum; 3OB9; -.
DR AlphaFoldDB; Q8N5Y2; -.
DR SMR; Q8N5Y2; -.
DR BioGRID; 116143; 25.
DR ComplexPortal; CPX-815; MSL histone acetyltransferase complex.
DR CORUM; Q8N5Y2; -.
DR DIP; DIP-56857N; -.
DR IntAct; Q8N5Y2; 18.
DR MINT; Q8N5Y2; -.
DR STRING; 9606.ENSP00000312244; -.
DR iPTMnet; Q8N5Y2; -.
DR PhosphoSitePlus; Q8N5Y2; -.
DR BioMuta; MSL3; -.
DR DMDM; 32171482; -.
DR EPD; Q8N5Y2; -.
DR jPOST; Q8N5Y2; -.
DR MassIVE; Q8N5Y2; -.
DR MaxQB; Q8N5Y2; -.
DR PaxDb; Q8N5Y2; -.
DR PeptideAtlas; Q8N5Y2; -.
DR PRIDE; Q8N5Y2; -.
DR ProteomicsDB; 1230; -.
DR ProteomicsDB; 6399; -.
DR ProteomicsDB; 72108; -. [Q8N5Y2-1]
DR ProteomicsDB; 72109; -. [Q8N5Y2-2]
DR ProteomicsDB; 72110; -. [Q8N5Y2-3]
DR ProteomicsDB; 863; -.
DR Antibodypedia; 23748; 132 antibodies from 21 providers.
DR DNASU; 10943; -.
DR Ensembl; ENST00000312196.10; ENSP00000312244.4; ENSG00000005302.19. [Q8N5Y2-1]
DR Ensembl; ENST00000337339.7; ENSP00000338078.2; ENSG00000005302.19. [Q8N5Y2-5]
DR Ensembl; ENST00000361672.6; ENSP00000354562.2; ENSG00000005302.19. [Q8N5Y2-6]
DR Ensembl; ENST00000398527.7; ENSP00000381538.2; ENSG00000005302.19. [Q8N5Y2-3]
DR Ensembl; ENST00000482871.6; ENSP00000498064.1; ENSG00000005302.19. [Q8N5Y2-4]
DR Ensembl; ENST00000648013.1; ENSP00000497518.1; ENSG00000005302.19. [Q8N5Y2-4]
DR Ensembl; ENST00000649078.1; ENSP00000498017.1; ENSG00000005302.19. [Q8N5Y2-4]
DR Ensembl; ENST00000649271.1; ENSP00000496967.1; ENSG00000005302.19. [Q8N5Y2-4]
DR Ensembl; ENST00000649602.1; ENSP00000498168.1; ENSG00000005302.19. [Q8N5Y2-4]
DR Ensembl; ENST00000649649.1; ENSP00000497137.1; ENSG00000005302.19. [Q8N5Y2-6]
DR Ensembl; ENST00000649685.1; ENSP00000497496.1; ENSG00000005302.19. [Q8N5Y2-6]
DR Ensembl; ENST00000650215.1; ENSP00000496944.1; ENSG00000005302.19. [Q8N5Y2-6]
DR Ensembl; ENST00000650628.1; ENSP00000496838.1; ENSG00000005302.19. [Q8N5Y2-4]
DR GeneID; 10943; -.
DR KEGG; hsa:10943; -.
DR MANE-Select; ENST00000312196.10; ENSP00000312244.4; NM_078629.4; NP_523353.2.
DR UCSC; uc004cuv.2; human. [Q8N5Y2-1]
DR CTD; 10943; -.
DR DisGeNET; 10943; -.
DR GeneCards; MSL3; -.
DR HGNC; HGNC:7370; MSL3.
DR HPA; ENSG00000005302; Low tissue specificity.
DR MalaCards; MSL3; -.
DR MIM; 300609; gene.
DR MIM; 301032; phenotype.
DR neXtProt; NX_Q8N5Y2; -.
DR OpenTargets; ENSG00000005302; -.
DR PharmGKB; PA164723161; -.
DR VEuPathDB; HostDB:ENSG00000005302; -.
DR eggNOG; KOG3001; Eukaryota.
DR GeneTree; ENSGT00950000182965; -.
DR HOGENOM; CLU_039566_5_2_1; -.
DR InParanoid; Q8N5Y2; -.
DR OMA; GMKFQFH; -.
DR OrthoDB; 1624495at2759; -.
DR PhylomeDB; Q8N5Y2; -.
DR TreeFam; TF323400; -.
DR PathwayCommons; Q8N5Y2; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q8N5Y2; -.
DR SIGNOR; Q8N5Y2; -.
DR BioGRID-ORCS; 10943; 24 hits in 709 CRISPR screens.
DR ChiTaRS; MSL3; human.
DR EvolutionaryTrace; Q8N5Y2; -.
DR GenomeRNAi; 10943; -.
DR Pharos; Q8N5Y2; Tbio.
DR PRO; PR:Q8N5Y2; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8N5Y2; protein.
DR Bgee; ENSG00000005302; Expressed in monocyte and 192 other tissues.
DR ExpressionAtlas; Q8N5Y2; baseline and differential.
DR Genevisible; Q8N5Y2; HS.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0072487; C:MSL complex; IDA:UniProtKB.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0046972; F:histone acetyltransferase activity (H4-K16 specific); IMP:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IDA: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; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR DisProt; DP01279; -.
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 3D-structure; Alternative splicing; Chromatin regulator; DNA-binding;
KW Intellectual disability; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..521
FT /note="Male-specific lethal 3 homolog"
FT /id="PRO_0000080247"
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 REGION 298..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..381
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:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 405
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..166
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045652"
FT VAR_SEQ 1..59
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10395802"
FT /id="VSP_007636"
FT VAR_SEQ 1..34
FT /note="MSASEGMKFKFHSGEKVLCFEPDPTKARVLYDAK -> MSPSVRPGAGWAPV
FT GRPGRPIQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043342"
FT VAR_SEQ 1..6
FT /note="MSASEG -> MKMMKT (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055376"
FT VAR_SEQ 7..155
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055377"
FT VAR_SEQ 60..61
FT /note="NR -> MP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10395802"
FT /id="VSP_007637"
FT VAR_SEQ 391..416
FT /note="KTPVHSRSSSPIPLTPSKEGSAVFAG -> SRFILGCPRPGRASVYFVFSQC
FT QAWC (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045653"
FT VAR_SEQ 417..521
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045654"
FT VARIANT 2
FT /note="S -> T (in dbSNP:rs150938844)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_069061"
FT VARIANT 199
FT /note="K -> Q (in dbSNP:rs1051595)"
FT /id="VAR_048732"
FT VARIANT 281..521
FT /note="Missing (in MRXSBA)"
FT /evidence="ECO:0000269|PubMed:30224647"
FT /id="VAR_082955"
FT VARIANT 308
FT /note="L -> P (in MRXSBA; unknown pathological
FT significance; dbSNP:rs1555906707)"
FT /evidence="ECO:0000269|PubMed:30224647"
FT /id="VAR_082956"
FT VARIANT 346..521
FT /note="Missing (in MRXSBA; loss of interaction with MOF and
FT MSL1)"
FT /evidence="ECO:0000269|PubMed:30224647"
FT /id="VAR_082957"
FT VARIANT 458..521
FT /note="Missing (in MRXSBA)"
FT /evidence="ECO:0000269|PubMed:30224647"
FT /id="VAR_082958"
FT MUTAGEN 31
FT /note="Y->A: Diminishes interaction with histone H4
FT monomethylated at 'Lys-20'(H4K20Me1)."
FT /evidence="ECO:0000269|PubMed:20943666"
FT MUTAGEN 55
FT /note="H->A: Diminishes DNA-binding; when associated with
FT A-65."
FT /evidence="ECO:0000269|PubMed:20657587"
FT MUTAGEN 56
FT /note="F->A: Abolishes interaction with histone H4
FT monomethylated at 'Lys-20'(H4K20Me1)."
FT MUTAGEN 59
FT /note="W->G: Diminishes DNA-binding."
FT /evidence="ECO:0000269|PubMed:20657587"
FT MUTAGEN 65
FT /note="R->A: Diminishes DNA-binding; when associated with
FT A-55."
FT /evidence="ECO:0000269|PubMed:20657587"
FT CONFLICT 37
FT /note="D -> V (in Ref. 1; AAD38499)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="Q -> R (in Ref. 2; AK025642)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="K -> E (in Ref. 2; AK025642)"
FT /evidence="ECO:0000305"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:3OA6"
FT STRAND 30..42
FT /evidence="ECO:0007829|PDB:3OA6"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:3OA6"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3OA6"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3OA6"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:3OA6"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3OA6"
FT HELIX 77..91
FT /evidence="ECO:0007829|PDB:3OA6"
FT HELIX 178..192
FT /evidence="ECO:0007829|PDB:2Y0N"
FT HELIX 206..222
FT /evidence="ECO:0007829|PDB:2Y0N"
FT HELIX 251..272
FT /evidence="ECO:0007829|PDB:2Y0N"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2Y0N"
FT HELIX 279..287
FT /evidence="ECO:0007829|PDB:2Y0N"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:2Y0N"
FT HELIX 453..469
FT /evidence="ECO:0007829|PDB:2Y0N"
FT HELIX 474..493
FT /evidence="ECO:0007829|PDB:2Y0N"
FT HELIX 495..498
FT /evidence="ECO:0007829|PDB:2Y0N"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:2Y0N"
SQ SEQUENCE 521 AA; 59824 MW; 6DFFB9E183D0CFB9 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 KRRQQDTSAS MPKLFLHLEK KTPVHSRSSS PIPLTPSKEG SAVFAGFEGR
RTNEINEVLS WKLVPDNYPP GDQPPPPSYI YGAQHLLRLF VKLPEILGKM SFSEKNLKAL
LKHFDLFLRF LAEYHDDFFP ESAYVAACEA HYSTKNPRAI Y
