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Database: UniProt
Entry: G5AY63_HETGA
LinkDB: G5AY63_HETGA
Original site: G5AY63_HETGA 
ID   G5AY63_HETGA            Unreviewed;       803 AA.
AC   G5AY63;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 72.
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|EMBL:JAN97751.1};
GN   ORFNames=GW7_14032 {ECO:0000313|EMBL:EHB01974.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB01974.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB01974.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
RN   [2] {ECO:0000313|EMBL:JAN97751.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Skin {ECO:0000313|EMBL:JAN97751.1};
RA   Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA   Platzer M., Szafranski K.;
RT   "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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; JH167493; EHB01974.1; -; Genomic_DNA.
DR   EMBL; GEBF01005881; JAN97751.1; -; Transcribed_RNA.
DR   RefSeq; XP_004838319.1; XM_004838262.1.
DR   AlphaFoldDB; G5AY63; -.
DR   STRING; 10181.G5AY63; -.
DR   GeneID; 101725090; -.
DR   KEGG; hgl:101725090; -.
DR   CTD; 115426; -.
DR   eggNOG; ENOG502QRDQ; Eukaryota.
DR   InParanoid; G5AY63; -.
DR   OMA; CHMCSCH; -.
DR   OrthoDB; 5481936at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
DR   Bgee; ENSHGLG00000015661; Expressed in zone of skin and 10 other cell types or tissues.
DR   GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
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:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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; 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:UP000006813};
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          345..396
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          449..613
FT                   /note="YDG"
FT                   /evidence="ECO:0000259|PROSITE:PS51015"
FT   DOMAIN          734..773
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          80..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          643..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..664
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   803 AA;  90185 MW;  3594310F7F7C575B CRC64;
     MWIQVRTIDG SQTRTIEDVS RKATIEELRE RVWALFDVRP ECQRLFYRGK QLENGYTLFD
     YDVGLNDIIQ LLVRPDPDLP STSKQTDVQM KPCSNSPPKV KKTSRVGSAS QPSTSARACL
     IDPGFGHYKV NELVDARDVG LGAWFEAHIH SVTRASDGHS RGKTPLKNGS SYKRTNGNVN
     HNSKENTHKL DSAPSTSNSD CVAADEDVIY HIEYDEYPES GTLEMNVKDL RPRARTILKW
     NELNVGDVVM VNYNVENPAK RGFWYDAEIT TLKAISRTKK ELRVKIFLGG SEGTLNDCRV
     IFAEEIFKIE KPGAHPLSFA DGKFLRKNDP ECDLCGGDPD KKCHMCSCHK CGEKREPNMQ
     LLCDECNMAY HIYCLNPPLD KIPEEEYWYC PCCKTDSSEV VKAGERLKMS KKKAKMPSAS
     TESRRDWGRG MACVGRTKEC TIVPSNHYGP IPGIPVGSTW RFRVQVSEAG VHRPHVGGIH
     GRSNDGAYSL VLAGGFADEV DRGDEFTYTG SGGKNLAGNK RIGAPSADQT LTNMNRALAL
     NCDAPLDDKI GAESRNWRAG KPVRVIRSFK GRKISKYAPE EGNRYDGIYK VVKYWPEISS
     SHGFLVWRYL LRRDDVEPAP WTSEGIERSR RLCLRLQYPA GYPSDKEGKK TKGQSKKQAT
     EAIKRPTSDG ECPSASKVIK ASDSAEAVEA FQLTPQQQNL IREDCQNQKL WDEVLASVVE
     GPNFLKKLEQ SFMCVCCQEL VYQPVTTECF HNVCKDCLQR SFKAQVFSCP ACRHDLGQNY
     VMIPNEILQT LLDLFFPGYS KGR
//
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