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Database: UniProt
Entry: W5MV89_LEPOC
LinkDB: W5MV89_LEPOC
Original site: W5MV89_LEPOC 
ID   W5MV89_LEPOC            Unreviewed;       843 AA.
AC   W5MV89;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 57.
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:ENSLOCP00000012298.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012298.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000012298.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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; AHAT01012995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01012996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01012997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01012998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01012999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01013000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006627117.1; XM_006627054.2.
DR   AlphaFoldDB; W5MV89; -.
DR   STRING; 7918.ENSLOCP00000012298; -.
DR   Ensembl; ENSLOCT00000012319.1; ENSLOCP00000012298.1; ENSLOCG00000010051.1.
DR   GeneID; 102686253; -.
DR   KEGG; loc:102686253; -.
DR   CTD; 115426; -.
DR   eggNOG; ENOG502QRDQ; Eukaryota.
DR   GeneTree; ENSGT00390000008296; -.
DR   HOGENOM; CLU_022357_0_0_1; -.
DR   InParanoid; W5MV89; -.
DR   OMA; CHMCSCH; -.
DR   OrthoDB; 5481936at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000018468; Linkage group LG2.
DR   Bgee; ENSLOCG00000010051; Expressed in brain and 13 other cell types or tissues.
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; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   CDD; cd15617; PHD_UHRF2; 1.
DR   CDD; cd16770; RING-HC_UHRF2; 1.
DR   CDD; cd20456; Tudor_UHRF2_rpt1; 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; IPR019956; Ubiquitin_dom.
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   PRINTS; PR00348; UBIQUITIN.
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:UP000018468};
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..78
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          357..410
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          463..626
FT                   /note="YDG"
FT                   /evidence="ECO:0000259|PROSITE:PS51015"
FT   DOMAIN          774..813
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          76..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..696
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   843 AA;  94762 MW;  1C6E87EB623D3BF7 CRC64;
     MWIQVRTIDG KETRTIEDLS RLTKIECLRL KIQEIFNVNP EQQRLFYRGK QMEDGQTLFD
     YNVGLNDIVQ LLIRSQTDPP DAQGKKKEKD VTGCSSGTLT SNNNGNKSLS PQLDNQPSTS
     ARTFLIDPGI GVYKINELVD CRDVSIGAWF EASIENVTRA TKGQNGKATG KSGKMSKRTN
     GKLDQNHSSH GSNGNSNGNS AFNLDTAPST SYMDCLNSEE DVTYHIKYDD YPENGVVEMC
     ANDVRPRART LLKWDHLRVG MVVMVNYNIE IPEERGFWFD AEITSLKEIS RSNKEVKVKI
     LLGGPDDVIS DCKLLIVEEI YKIEKPGAPP LTSADGQFKR KSGPECKHCK ADPEAECRFC
     SCCVCGGKQD AHMQLLCDEC NMAFHIYCLN PPLSKIPEDE DWYCPTCKND TSEVVKAGEK
     LKASKKKAKM PSAHTESQRD WGKGMACVGR TKECTIVPSN HYGPIPGIPV GTTWKFRVQV
     SEAGVHRPHV GGIHGRSNDG SYSLVLAGGF EDEVDRGDEF TYTGSGGRDL SGNKRIGEHS
     FDQTLTHMNR ALALNCDAPL NDKDGAESRN WRAGKPVRVV RSSKGRRISK YAPEEGNRYD
     GIYKVVKYWP EIGKCGFLVW RYLLRRDDSE PAPWTPEGAE RIKKLGLSVQ YPEGYLEAMA
     NKSKKDRGKR NSGKQDKPEK AEKKEKGKEE KKEPETCPQS NGSQKRPQET ETQDHETPAK
     VGKLAEKGEA FQLSAQQQWL IREDCLNRKL WDEALNCIME GPNFLRKVEQ IFMCVCCQEL
     VYQPITTECL HNVCKTCLQR SFRAEVYTCP ACRHDLGKDY IMVLNKILQS LLDQFFPGYS
     KGR
//
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