MSL2_MOUSE
ID MSL2_MOUSE Reviewed; 577 AA.
AC Q69ZF8; Q497U7; Q8CBI7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=E3 ubiquitin-protein ligase MSL2;
DE EC=2.3.2.-;
DE AltName: Full=E3 ubiquitin-protein transferase MSL2 {ECO:0000305};
DE AltName: Full=Male-specific lethal 2-like 1;
DE Short=MSL2-like 1;
DE AltName: Full=Male-specific lethal-2 homolog;
DE Short=MSL-2;
DE AltName: Full=Male-specific lethal-2 homolog 1;
DE AltName: Full=RING finger protein 184;
GN Name=Msl2; Synonyms=Kiaa1585, Msl2l1, Rnf184;
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 [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-577.
RC TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 422-577.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Component of histone acetyltransferase complex responsible
CC for the majority of histone H4 acetylation at lysine 16 which is
CC implicated in the formation of higher-order chromatin structure (By
CC similarity). Acts as an E3 ubiquitin ligase that promotes
CC monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that
CC of H2A. This activity is greatly enhanced by heterodimerization with
CC MSL1. H2B ubiquitination in turn stimulates histone H3 methylation at
CC 'Lys-5' (H3K4me) and 'Lys-80' (H3K79me) and leads to gene activation,
CC including that of HOXA9 and MEIS1 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a multisubunit histone acetyltransferase complex
CC (MSL) at least composed of the KAT8/MOF/MYST1, MSL1/hampin, MSL2 and
CC MSL3. Forms a MSL heterotetrameric core with MSL1.
CC {ECO:0000250|UniProtKB:Q9HCI7}.
CC -!- SIMILARITY: Belongs to the MSL2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32486.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK173208; BAD32486.1; ALT_INIT; mRNA.
DR EMBL; BC100371; AAI00372.1; -; mRNA.
DR EMBL; AK035934; BAC29248.1; -; mRNA.
DR CCDS; CCDS85717.1; -.
DR RefSeq; NP_001093921.1; NM_001100451.2.
DR AlphaFoldDB; Q69ZF8; -.
DR SMR; Q69ZF8; -.
DR BioGRID; 218973; 1.
DR ComplexPortal; CPX-859; MSL histone acetyltransferase complex.
DR STRING; 10090.ENSMUSP00000082270; -.
DR iPTMnet; Q69ZF8; -.
DR PhosphoSitePlus; Q69ZF8; -.
DR EPD; Q69ZF8; -.
DR MaxQB; Q69ZF8; -.
DR PaxDb; Q69ZF8; -.
DR PeptideAtlas; Q69ZF8; -.
DR PRIDE; Q69ZF8; -.
DR ProteomicsDB; 295595; -.
DR Antibodypedia; 1091; 174 antibodies from 22 providers.
DR Ensembl; ENSMUST00000085177; ENSMUSP00000082270; ENSMUSG00000066415.
DR GeneID; 77853; -.
DR KEGG; mmu:77853; -.
DR UCSC; uc033jml.1; mouse.
DR CTD; 55167; -.
DR MGI; MGI:1925103; Msl2.
DR VEuPathDB; HostDB:ENSMUSG00000066415; -.
DR eggNOG; ENOG502QPJR; Eukaryota.
DR GeneTree; ENSGT00390000016814; -.
DR HOGENOM; CLU_038772_0_0_1; -.
DR InParanoid; Q69ZF8; -.
DR OMA; LCTTGID; -.
DR OrthoDB; 1446941at2759; -.
DR PhylomeDB; Q69ZF8; -.
DR TreeFam; TF328848; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR BioGRID-ORCS; 77853; 7 hits in 51 CRISPR screens.
DR ChiTaRS; Msl2; mouse.
DR PRO; PR:Q69ZF8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q69ZF8; protein.
DR Bgee; ENSMUSG00000066415; Expressed in rostral migratory stream and 245 other tissues.
DR ExpressionAtlas; Q69ZF8; baseline and differential.
DR Genevisible; Q69ZF8; MM.
DR GO; GO:0072487; C:MSL complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0043984; P:histone H4-K16 acetylation; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IDA:ComplexPortal.
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 PANTHER; PTHR16048; PTHR16048; 1.
DR Pfam; PF16682; MSL2-CXC; 1.
DR Pfam; PF16685; zf-RING_10; 1.
DR SMART; SM01114; CXC; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Metal-binding; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..577
FT /note="E3 ubiquitin-protein ligase MSL2"
FT /id="PRO_0000299537"
FT ZN_FING 44..85
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..116
FT /note="Sufficient for interaction with MSL1"
FT /evidence="ECO:0000250"
FT REGION 405..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..425
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCI7"
FT CROSSLNK 375
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9HCI7"
SQ SEQUENCE 577 AA; 62538 MW; 5B76E902299191C1 CRC64;
MNPVNATALY ISASRLVLNY DPGDPKAFTE INRLLPYFRQ SLSCCVCGHL LQDPIAPTNS
TCQHYVCKTC KGKKMMMKPS CSWCKDYEQF EENKQLSILV NCYKKLCEYI TQTTLARDII
EAVDCSSDIL ALLNDGSLFC EETEKPSDSS FTLCLTHSPL PSTSEPTADP QASLSPMSES
TLSIAIGSSV INGLPTYNGL SIDRFGINIP SPEHPNTIDV CNTVDIKTED LSDNLPPVCD
TVATDLCSTG IDICSFSEDI KPGDSLLLSV EEVLRSLETV SNTEVCCPNL QPNLEATVSN
GPFLQLSSQS LSHNVFMSTS PALHGLSCTA ATPKVAKLNR KRSRSESDSE KVQPLPISTI
IRGPTLGASA PVTVKRESKI SLQPIATVPN GGTTPKISKT VLLSTKSMKK SHEHGSKKSH
SKSKPGILKK DKAVKEKMPS HHFMPGSPTK TVYKKPQEKK GCKCGRATQN PSVLTCRGQR
CPCYSNRKAC LDCICRGCQN SYMANGEKKL EAFAVPEKAL EQTRLTLGIN VTSIAVRNAS
TSTSVINVTG SPVTTFLAAS THDDKSLDEA IDMRFDC
