MSL2_DROME
ID MSL2_DROME Reviewed; 773 AA.
AC P50534; Q9VQR1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=E3 ubiquitin-protein ligase msl-2;
DE EC=2.3.2.-;
DE AltName: Full=E3 ubiquitin-protein transferase msl-2 {ECO:0000305};
DE AltName: Full=Protein male-specific lethal-2;
GN Name=msl-2; ORFNames=CG3241;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH MSL-1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=7781064; DOI=10.1016/0092-8674(95)90007-1;
RA Kelley R.L., Solovyeva I., Lyman L.M., Richman R., Solovyev V.,
RA Kuroda M.I.;
RT "Expression of msl-2 causes assembly of dosage compensation regulators on
RT the X chromosomes and female lethality in Drosophila.";
RL Cell 81:867-877(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH MSL-1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=7796814; DOI=10.1002/j.1460-2075.1995.tb07288.x;
RA Zhou S., Yang Y., Scott M.J., Pannuti A., Fehr K.C., Eisen A., Koonin E.V.,
RA Fouts D.L., Wrightsman R., Manning J.E., Lucchesi J.C.;
RT "Male-specific lethal 2, a dosage compensation gene of Drosophila,
RT undergoes sex-specific regulation and encodes a protein with a RING finger
RT and a metallothionein-like cysteine cluster.";
RL EMBO J. 14:2884-2895(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH MSL-1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=7588059; DOI=10.1242/dev.121.10.3245;
RA Bashaw G.J., Baker B.S.;
RT "The msl-2 dosage compensation gene of Drosophila encodes a putative DNA-
RT binding protein whose expression is sex specifically regulated by Sex-
RT lethal.";
RL Development 121:3245-3258(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP 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 [8]
RP FUNCTION AS E3 UBIQUITIN LIGASE.
RX PubMed=21726816; DOI=10.1016/j.molcel.2011.05.015;
RA Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y.;
RT "The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase
RT for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation.";
RL Mol. Cell 43:132-144(2011).
CC -!- FUNCTION: The Msl proteins are essential for elevating transcription of
CC the single X chromosome in the male (X chromosome dosage compensation).
CC Msl-2 is required for translation and/or stability of msl-1 in males.
CC In complex with msl-1, acts as an E3 ubiquitin ligase that promotes
CC ubiquitination of histone H2B. {ECO:0000269|PubMed:21726816,
CC ECO:0000269|PubMed:7588059, ECO:0000269|PubMed:7781064,
CC ECO:0000269|PubMed:7796814}.
CC -!- SUBUNIT: Component of the male-specific lethal (MSL) histone
CC acetyltransferase complex at least composed of mof, msl-1, msl-2 and
CC msl-3. {ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:7588059,
CC ECO:0000269|PubMed:7781064, ECO:0000269|PubMed:7796814}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Msl-1 and msl-2
CC colocalize to many sites on the male X chromosome.
CC -!- DEVELOPMENTAL STAGE: Only produced in males.
CC -!- SIMILARITY: Belongs to the MSL2 family. {ECO:0000305}.
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DR EMBL; L42553; AAA75573.1; -; Genomic_DNA.
DR EMBL; Z48443; CAA88358.1; -; Genomic_DNA.
DR EMBL; X89241; CAA61529.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51104.1; -; Genomic_DNA.
DR EMBL; AY128426; AAM75019.1; -; mRNA.
DR PIR; S55554; S55554.
DR RefSeq; NP_523467.1; NM_078743.5.
DR RefSeq; NP_722907.1; NM_164536.2.
DR PDB; 2LUA; NMR; -; A=520-570.
DR PDB; 4RKG; X-ray; 2.50 A; A/B=520-570.
DR PDB; 4RKH; X-ray; 2.00 A; C/D/E/F=520-570.
DR PDBsum; 2LUA; -.
DR PDBsum; 4RKG; -.
DR PDBsum; 4RKH; -.
DR AlphaFoldDB; P50534; -.
DR BMRB; P50534; -.
DR SMR; P50534; -.
DR BioGRID; 59776; 28.
DR IntAct; P50534; 2.
DR STRING; 7227.FBpp0077259; -.
DR PaxDb; P50534; -.
DR DNASU; 33565; -.
DR EnsemblMetazoa; FBtr0077570; FBpp0077259; FBgn0005616.
DR EnsemblMetazoa; FBtr0077571; FBpp0077260; FBgn0005616.
DR GeneID; 33565; -.
DR KEGG; dme:Dmel_CG3241; -.
DR CTD; 33565; -.
DR FlyBase; FBgn0005616; msl-2.
DR VEuPathDB; VectorBase:FBgn0005616; -.
DR eggNOG; ENOG502QPJR; Eukaryota.
DR GeneTree; ENSGT00390000016814; -.
DR HOGENOM; CLU_009669_0_0_1; -.
DR InParanoid; P50534; -.
DR OMA; LCTTGID; -.
DR OrthoDB; 943810at2759; -.
DR PhylomeDB; P50534; -.
DR BioGRID-ORCS; 33565; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33565; -.
DR PRO; PR:P50534; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0005616; Expressed in central nervous system and 12 other tissues.
DR ExpressionAtlas; P50534; baseline and differential.
DR Genevisible; P50534; DM.
DR GO; GO:0005694; C:chromosome; IMP:FlyBase.
DR GO; GO:0046536; C:dosage compensation complex; IDA:FlyBase.
DR GO; GO:0072487; C:MSL complex; IDA:FlyBase.
DR GO; GO:0000228; C:nuclear chromosome; IDA:FlyBase.
DR GO; GO:0000805; C:X chromosome; IDA:FlyBase.
DR GO; GO:0016456; C:X chromosome located dosage compensation complex, transcription activating; NAS:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase.
DR GO; GO:0007549; P:dosage compensation; IMP:FlyBase.
DR GO; GO:0009047; P:dosage compensation by hyperactivation of X chromosome; NAS:FlyBase.
DR GO; GO:0043984; P:histone H4-K16 acetylation; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:FlyBase.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:FlyBase.
DR GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
DR CDD; cd13122; MSL2_CXC; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR037922; MSL2.
DR InterPro; IPR032049; Msl2-CXC.
DR InterPro; IPR032043; Msl2_Znf-RING.
DR InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR16048; PTHR16048; 1.
DR Pfam; PF16682; MSL2-CXC; 1.
DR Pfam; PF16685; zf-RING_10; 1.
DR SMART; SM01114; CXC; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Coiled coil; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..773
FT /note="E3 ubiquitin-protein ligase msl-2"
FT /id="PRO_0000055962"
FT ZN_FING 41..85
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 460..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 424..468
FT /evidence="ECO:0000255"
FT COMPBIAS 460..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..708
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 280
FT /note="T -> N (in Ref. 2; CAA88358)"
FT /evidence="ECO:0000305"
FT CONFLICT 367..370
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..373
FT /note="VEE -> LKT (in Ref. 1; AAA75573)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="P -> Q (in Ref. 2; CAA88358)"
FT /evidence="ECO:0000305"
FT CONFLICT 403..405
FT /note="TQT -> IQA (in Ref. 2; CAA88358)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="H -> Q (in Ref. 3; CAA61529)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="Q -> H (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 431..433
FT /note="AES -> EEP (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="E -> V (in Ref. 2; CAA88358)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="A -> P (in Ref. 2; CAA88358)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="T -> A (in Ref. 3; CAA61529)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="M -> L (in Ref. 3; CAA61529)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="E -> D (in Ref. 2; CAA88358)"
FT /evidence="ECO:0000305"
FT STRAND 530..533
FT /evidence="ECO:0007829|PDB:4RKG"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:4RKH"
FT TURN 538..540
FT /evidence="ECO:0007829|PDB:2LUA"
FT HELIX 545..548
FT /evidence="ECO:0007829|PDB:4RKH"
SQ SEQUENCE 773 AA; 84856 MW; 31830142AD64F4D7 CRC64;
MAQTAYLKVT RIAMRSASNL SKRRVEELNS GLGELRQLLS CVVCCQLLVD PYSPKGKRCQ
HNVCRLCLRG KKHLFPSCTQ CEGCSDFKTY EENRMMAAQL LCYKTLCVHL LHSALFGELA
GMRPQVAREL VPRIKLPPKT TQEFIREGSN ISDTFDIFLP QPDLPFLKDM PTSLPAETPP
TSAVTTPELP YDHHLNISDI EAEAAATAEQ GHFSPLPLLP TGSRMGMLSH AGQIVIATES
SESGFMDQAW TDQVDLSGTV SVSKYTNSGN NFAVSYVMPT SATTKFDPQE LQIGQVVQMA
DSTQLAVLAA VEETVETSTQ LTVLSTTVEE TVETSTQLEV LTSAEEPNEI SDQLANLQVE
ESDEALVEET VEEAEGTSIP SEVVAEHMEE DQHLDVHTSQ SPTQTEMEEA VEEHVATKTQ
LGHVQTELQD AESLQKDFED AKAAAEEAKE KEKDLHAISA ELQKEDSDEP TLKRKRTRTL
KASQAAKIEP VPSEVKTKVQ SGKGALRRIR GKDKEEKVKP PKPKCRCGIS GSSNTLTTCR
NSRCPCYKSY NSCAGCHCVC CKNPHKEDYV ESDEDDDLED FEMPKDVPEP MTQSEEPVVA
EPRQEENSMA PPDSSAPISL VPLNNLQQSQ HPLVLVQNEK GEYQGFNIFQ GSKPLDPVTV
GFTIRVQLQH TDGFGSLPQY AYIMPTIDPP NPPAPSLSPP PPPAPDREVI EPPAKKFRTS
RTRRGRANFS ALDTVDELVS GGSRSNSAAG DRSSATDNAH SLFEEIMSGS DDL
