MYSM1_BRAFL
ID MYSM1_BRAFL Reviewed; 809 AA.
AC B6MUN4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Histone H2A deubiquitinase MYSM1;
DE Short=2A-DUB;
DE EC=3.4.19.-;
DE AltName: Full=Myb-like, SWIRM and MPN domain-containing protein 1;
GN Name=MYSM1; ORFNames=BRAFLDRAFT_86936;
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82; TISSUE=Testis;
RX PubMed=18563158; DOI=10.1038/nature06967;
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- FUNCTION: Metalloprotease that specifically deubiquitinates
CC monoubiquitinated histone H2A, a specific tag for epigenetic
CC transcriptional repression, thereby acting as a coactivator.
CC Preferentially deubiquitinates monoubiquitinated H2A in hyperacetylated
CC nucleosomes. Deubiquitination of histone H2A leads to facilitate the
CC phosphorylation and dissociation of histone H1 from the nucleosome.
CC Acts as a coactivator by participating in the initiation and elongation
CC steps of androgen receptor (AR)-induced gene activation (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: Binds double-stranded DNA via the SANT domain. The SWIRM domain
CC does not bind double-stranded DNA (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. MYSM1 subfamily.
CC {ECO:0000305}.
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DR EMBL; ABEP02030881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABEP02030882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABEP02030884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7739.XP_002591419.1; -.
DR eggNOG; KOG1279; Eukaryota.
DR InParanoid; B6MUN4; -.
DR Proteomes; UP000001554; Partially assembled WGS sequence.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR033497; MYSM1.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12802:SF126; PTHR12802:SF126; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF04433; SWIRM; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS50249; MPN; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 3: Inferred from homology;
KW Activator; Chromatin regulator; DNA-binding; Hydrolase; Metal-binding;
KW Metalloprotease; Nucleus; Protease; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation pathway; Zinc.
FT CHAIN 1..809
FT /note="Histone H2A deubiquitinase MYSM1"
FT /id="PRO_0000373927"
FT DOMAIN 33..78
FT /note="SANT"
FT DOMAIN 410..508
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT DOMAIN 592..719
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 153..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 671..684
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT COMPBIAS 334..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 671
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 673
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 684
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 809 AA; 90132 MW; 2A061E4A36A0893E CRC64;
MADDEEIDIE GDDDAPLLFD HKDDALALPD LPGYEPNWMF DHGQEIYGRS WTSISQFVQT
RTPLQVKNYA RHFFKTKVVQ KVEEGEDEDV DIEGEESGEE AVMELRSTCG LNPAQPAVVT
SDDTSTGENV MEETEAVTED HPSLDNLVQD DREMPQQETT GDGEQYPMDE HFLPVFPWQP
DDTQNRVIVE RIEGSVGLGS VRGDKDVRPV PGVEQNTYGP HTDMFQVQNT LLAFEKQVGA
DRIFEGPSXS KNEATDTQTE VSETKTEVIE RQTESQVDAT HMHTYGDGLM GSIERLTESV
SSSELKEDLK TGIEYVEKDD ATDSSSTAKG YDNYTLDHPE DRSKPDSVVS EKWSCEEAMS
SHTDGRTFSD SDSGKETYDL PRYNTTIFQG HSEDETSDAG QAEEETFFTF KKPTEEVVLD
RSVITEEEKE VHKEFFDGRQ TKTPERYLKI RNHLLDCWER TKPEYLRKTV ARAGLRNCGD
VNCIGRIHGY LERIGAINFG CEEANRGEFP VAKVGVKRNP QGHGEQLALQ AARLESMHVT
SDELEKQDGG VSQIRPNRSR AARTNLNSFS YDPFKLVPCK RFSEESPAPF SVKIHATALV
TIDMHAHIST AEVIGLLGGV FHRDPGALEV ASAEPCNSLS TGMQCEMDPV SQTQASEALS
QAGYSVVGWY HSHPTFAPNP SVRDIETQTK FQEWFAQGGS PFIGIIVNPY SSTRISPLSR
VTCLTISSEW NPPAIQRVKL LSRYAGHTDT TYMDKMLYSL SGHLCRGNAD SDEDGNSESL
TLLTDIRDIF ANSWTSSLGT TPRSSIASL
