ID A0A0D9R9C4_CHLSB Unreviewed; 802 AA.
AC A0A0D9R9C4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=E3 ubiquitin-protein ligase UHRF {ECO:0000256|RuleBase:RU369101};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU369101};
DE AltName: Full=RING-type E3 ubiquitin transferase UHRF {ECO:0000256|RuleBase:RU369101};
DE AltName: Full=Ubiquitin-like PHD and RING finger domain-containing protein {ECO:0000256|RuleBase:RU369101};
DE AltName: Full=Ubiquitin-like-containing PHD and RING finger domains protein {ECO:0000256|RuleBase:RU369101};
GN Name=UHRF2 {ECO:0000313|Ensembl:ENSCSAP00000005213.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000005213.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000005213.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000005213.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Multi domain E3 ubiquitin ligase that also plays a role in
CC DNA methylation and histone modifications.
CC {ECO:0000256|RuleBase:RU369101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU369101};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369101}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00358,
CC ECO:0000256|RuleBase:RU369101}.
CC -!- DOMAIN: The YDG domain mediates the interaction with histone H3.
CC {ECO:0000256|RuleBase:RU369101}.
CC -!- DOMAIN: The tudor-like regions specifically recognize and bind histone
CC H3 unmethylated at 'Arg-2' (H3R2me0), while the PHD-type zinc finger
CC specifically recognizes and binds histone H3 trimethylated at 'Lys-9'
CC (H3K9me3). {ECO:0000256|RuleBase:RU369101}.
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DR EMBL; AQIB01021617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01021618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01021619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01021620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01021621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01021622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007967496.1; XM_007969305.1.
DR AlphaFoldDB; A0A0D9R9C4; -.
DR STRING; 60711.ENSCSAP00000005213; -.
DR Ensembl; ENSCSAT00000007025.1; ENSCSAP00000005213.1; ENSCSAG00000008957.1.
DR GeneID; 103219471; -.
DR KEGG; csab:103219471; -.
DR CTD; 115426; -.
DR eggNOG; ENOG502QRDQ; Eukaryota.
DR GeneTree; ENSGT00390000008296; -.
DR OMA; CHMCSCH; -.
DR OrthoDB; 5481936at2759; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 103219471; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 12.
DR Bgee; ENSCSAG00000008957; Expressed in fibroblast and 7 other cell types or tissues.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:Ensembl.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR CDD; cd15617; PHD_UHRF2; 1.
DR CDD; cd16770; RING-HC_UHRF2; 1.
DR CDD; cd20456; Tudor_UHRF2_rpt1; 1.
DR CDD; cd20458; Tudor_UHRF2_rpt2; 1.
DR CDD; cd17123; Ubl_UHRF2; 1.
DR Gene3D; 2.30.30.1150; -; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.30.280.10; SRA-YDG; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR047467; PHD_UHRF2.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR047466; RING-HC_UHRF2.
DR InterPro; IPR036987; SRA-YDG_sf.
DR InterPro; IPR003105; SRA_YDG.
DR InterPro; IPR021991; TTD_dom.
DR InterPro; IPR047407; Tudor_UHRF2_rpt1.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR047468; Ubl_UHRF2.
DR InterPro; IPR045134; UHRF1/2-like.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14140; E3 UBIQUITIN-PROTEIN LIGASE UHRF-RELATED; 1.
DR PANTHER; PTHR14140:SF3; E3 UBIQUITIN-PROTEIN LIGASE UHRF2; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF02182; SAD_SRA; 1.
DR Pfam; PF12148; TTD; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SMART; SM00466; SRA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS51015; YDG; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU369101};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU369101};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00358}; Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369101};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU369101};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369101};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1..74
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 344..395
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 448..612
FT /note="YDG"
FT /evidence="ECO:0000259|PROSITE:PS51015"
FT DOMAIN 733..772
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 80..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 89941 MW; 55871CDD1FB14A46 CRC64;
MWIQVRTIDG SKTCTIEDVS RKATIEELRE RVWALFDVRP ECQRLFYRGK QLENGYTLFD
YDVGLNDIIQ LLVRPDPDHL PGTSTQIEAK PCSNSPPKVK KAPRVGPSSQ PSTSARARLI
DPGFGIYKVN ELVDARDVGL GAWFEAHIHS VTRASDGQSR GKTPLKNGSS CKRTNGNIKH
KSKENTNKLD SVPSTSNSDS VAADEDVIYH IQYDEYPESG TLEMNVKDLR PRARTILKWN
ELNVGDVVMV NYNVESPGQR GFWFDAEITT LKTISRTKKE LRVKIFLGGS EGTLNDCKII
SVDEIFKIEK PGAHPLSFAD GKFLRRNDPE CDLCGGDPDK KCHSCSCRVC GGKHEPNMQL
LCDECNVAYH IYCLNPPLDK VPEEEYWYCP SCKTDSSEVV KAGERLKMSK KKAKMPSAST
ESRRDWGRGM ACVGRTRECT IVPSNHYGPI PGIPVGSTWR FRVQVSEAGV HRPHVGGIHG
RSNDGAYSLV LAGGFADEVD RGDEFTYTGS GGKNLAGNKR IGAPSADQTL TNMNRALALN
CDAPLDDKIG AESRNWRAGK PVRVIRSFKG RKISKYAPEE GNRYDGIYKV VKYWPEISSS
HGFLVWRYLL RRDDVEPAPW TSEGIERSRR LCLRLQYPAG YPSDKEGKKT KGQSKKQPSG
TTKRPISDDD RPSASKVYKA SDSAEAIEAF QLTPQQQHLI REDCQNQKLW DEVLAHLVEG
PNFLKKLEQS FMCVCCQELV YQPVTTECFH NVCKDCLQRS FKAQVFSCPA CRHDLGQNYI
MIPNEILQTL LDLFFPGYSK GR
//
