ID A0A2K6T5Z8_SAIBB Unreviewed; 729 AA.
AC A0A2K6T5Z8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
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:ENSSBOP00000015053.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000015053.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000015053.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_010337073.1; XM_010338771.1.
DR AlphaFoldDB; A0A2K6T5Z8; -.
DR Ensembl; ENSSBOT00000031851.1; ENSSBOP00000015053.1; ENSSBOG00000024260.1.
DR GeneID; 101027750; -.
DR CTD; 115426; -.
DR GeneTree; ENSGT00390000008296; -.
DR OMA; CHMCSCH; -.
DR OrthoDB; 5481936at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd15617; PHD_UHRF2; 1.
DR CDD; cd16770; RING-HC_UHRF2; 1.
DR CDD; cd17123; Ubl_UHRF2; 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); 2.
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; 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:UP000233220};
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 271..322
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 375..539
FT /note="YDG"
FT /evidence="ECO:0000259|PROSITE:PS51015"
FT DOMAIN 660..699
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 80..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 81457 MW; 657C2641CC22AB49 CRC64;
MWIQVRTIDG SKTCTIEDVS RKATIEELRE RVWALFDVRP ECQRLFYRGK QLENGYTLFD
YDVGLNDIIQ LLVRPDLDHL PGTSKQTETK PCSNSSPKVK KAPRVGSSIQ PSTSARARLI
DPGFGIYKVN ELVDARDVGL GAWFEAHIHS VTRASDGQSR GKTPLKNGSS CKRTNGNINH
KSKANTNKLD SVPSTSNSDS VAADEDVIYH IQYDEGSEGT LNDCKIVSVD EIFKIEKPGA
HPLSFADGKF LRRNDPECDL CGGDPDKKCH SCSCRVCGGK HEPNMQLLCD ECNVAYHIYC
LNPPLDKVPE EEYWYCPSCK TDSSEVVKAG ERLKMSKKKA KMPSASTESR RDWGRGMACV
GRTRECTIVP SNHYGPIPGI PVGSTWRFRV QVSEAGVHRP HVGGIHGRSN DGAYSLVLAG
GFADEVDRGD EFTYTGSGGK NLAGNKRIGA PSADQTLTNM NRALALNCDA PLDDKIGAES
RNWRAGKPVR VIRSFKGRKI SKYAPEEGNR YDGIYKVVKY WPEISSSHGF LVWRYLLRRD
DVEPAPWTSE GIERSRRLCL RLQYPAGYPS DKEGKKTKGQ SKKQPSGTKK RPISDDDCPS
ASKVFKASDS TEAIEAFQLT PQQQHLIRED CQNQKLWDEV LAHLVEGPNF LKKLEQSFMC
VCCQELVYQP VTTECFHNVC KDCLQRSFKA QVFSCPACRH DLGQNYIMIP NEILQTLLDL
FFPGYSKGR
//
