MYSM1_XENLA
ID MYSM1_XENLA Reviewed; 818 AA.
AC A0JMR6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|PROSITE-ProRule:PRU00624}.
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; BC125979; AAI25980.1; -; mRNA.
DR RefSeq; NP_001090503.1; NM_001097034.1.
DR AlphaFoldDB; A0JMR6; -.
DR SMR; A0JMR6; -.
DR MEROPS; M67.005; -.
DR DNASU; 779416; -.
DR GeneID; 779416; -.
DR KEGG; xla:779416; -.
DR CTD; 779416; -.
DR Xenbase; XB-GENE-1032962; mysm1.L.
DR OMA; SWRTDNS; -.
DR OrthoDB; 590811at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 779416; Expressed in pancreas and 19 other tissues.
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:SF67; PTHR12802:SF67; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS50249; MPN; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 2: Evidence at transcript level;
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..818
FT /note="Histone H2A deubiquitinase MYSM1"
FT /id="PRO_0000373926"
FT DOMAIN 107..158
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 344..442
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT DOMAIN 548..680
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 627..640
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 745..749
FT /note="LXXLL motif"
FT BINDING 627
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 629
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 640
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 818 AA; 94084 MW; E60F8B915E1CEBE0 CRC64;
MAEEAADVDI DIEGDINESS KSIYDSLNTG FAPEHYIESA WQNEEGLAPW ALDSSISEEN
REAIKKMLLE EEYYLSNKPL AVKFWSDSQE GEKQCIKRVR SPAKASSSPV KWTKEEKNLF
EQGLATFGRR WTSIARLIGS RSVLQVKNYA RHYFKNKCKL EGFVKEEAKI GSLQIPNLQD
YENEPDITDE PTTFRGRADP NLNAIKIEKL SDDEEIDITD EVDELLSNKT NLDTIIIAKT
DKVKETKVET EVQQKSHSTT EHSQTDIPKL VLQQTETECL DSVNPLTCIT SPKWTLSPQQ
CEEDDYDQPD VQDCLQEKCL SPHAEDLTVL CENENDSQDE DDEIKPPDQE LEIDRNFILD
EEKQAIPEFF EGRQAKTPDR YLRIRNYILD QWENCKPKYL NKTSVRPGLK NCGDVNCIGR
IHTYLELIGA INFGCEQAIY NRPRPVDKTK CKEGKDTLEA YKLAHRLQSM RTRKRRVRDP
WGNWCDAKDL EGQTYEHLSA EELARRHEDK IKSYKYSKGT RQVRSSFDPF QLIPCSAFSE
EKKAPFQVKV SCEAMLVLDL HAHVSMAEVI GLLGGRYTES ESVVEICAVE PCNSLSTGLQ
CEMDPVSQTQ ASEALASRGY SVIGWYHSHP AFDPNPSIRD IDTQAKYQNY FSRGGAKFLG
MIISPYNRRN PHPQSQVACL IISDELSNDG SYRIPYKFEI EYMQGEPQWE LVFAKTRWII
EKYRSSHSSV SMDKRFRHDS ELTCLQKLLM CMKKTLGNTA CPLITEEFLH RIEEYFRTSY
KKESNYQIED NDPCKQHSDT TFTMDSFQDY EPNGRPSL
