UniProt: A0A383Z2K7

Database: UniProt
Entry: A0A383Z2K7_BALAS

LinkDB:  A0A383Z2K7_BALAS 
Original site:  A0A383Z2K7_BALAS

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (21)   
   InterPro (12)   
   Pfam (3)   
   PROSITE (4)   
   SMART (2)   
All databases (31)   

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ID   A0A383Z2K7_BALAS        Unreviewed;       750 AA.
AC   A0A383Z2K7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|RuleBase:RU369101};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU369101};
GN   Name=UHRF1 {ECO:0000313|RefSeq:XP_007169306.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007169306.1};
RN   [1] {ECO:0000313|RefSeq:XP_007169306.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007169306.1};
RG   RefSeq;
RL   Submitted (JAN-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|RuleBase:RU369101};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {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}.
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DR   RefSeq; XP_007169306.1; XM_007169244.1.
DR   AlphaFoldDB; A0A383Z2K7; -.
DR   STRING; 310752.A0A383Z2K7; -.
DR   KEGG; bacu:103015154; -.
DR   CTD; 29128; -.
DR   InParanoid; A0A383Z2K7; -.
DR   OrthoDB; 5481936at2759; -.
DR   Proteomes; UP000261681; 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR   CDD; cd16769; RING-HC_UHRF1; 1.
DR   CDD; cd20455; Tudor_UHRF1_rpt1; 1.
DR   CDD; cd20457; Tudor_UHRF1_rpt2; 1.
DR   CDD; cd17122; Ubl_UHRF1; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 2.30.30.30; -; 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; IPR015947; PUA-like_sf.
DR   InterPro; IPR014722; Rib_uL2_dom2.
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; IPR047406; Ubl_UHRF1.
DR   InterPro; IPR045134; UHRF1/2-like.
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:SF2; E3 UBIQUITIN-PROTEIN LIGASE UHRF1; 1.
DR   Pfam; PF02182; SAD_SRA; 1.
DR   Pfam; PF12148; TTD; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00466; SRA; 1.
DR   SMART; SM00213; UBQ; 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; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
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:UP000261681};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369101};
KW   Ubl conjugation pathway {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..75
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          379..542
FT                   /note="YDG"
FT                   /evidence="ECO:0000259|PROSITE:PS51015"
FT   DOMAIN          681..720
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          80..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   750 AA;  84048 MW;  55048A8847417F50 CRC64;
     MWIQVRTMDG KVAHTVDSLS RLTKVEELRK KIQELFQVGP GLQRLFYRGK QMEDGHTLFD
     YDVRLNDTIQ LLVRQSLVLP APSGGGTGGG SKERDSELSD TDSGCCLAQS ESDKSSNSGE
     AAAEPEGKAD EDEWDETELG LYKAGEYVDA RDTNMGAWFE AKVIRVTRKV PAQDEPCSST
     SSPKPEDDIV YHVKYDDYPE NGVVQMNSRN VRARARHIIK WQDLEVGQMV MVNYNPDNPK
     DRGFWYDAEI LRKRETRTVR ELHANVRIGD DSLNDCRIIF VDEVFKIERP GEGNPMVENP
     TRSEFRSRPS AVGGQGTRYC PECRIDSSEV VQAGEKLKES KKKAKMASAT SSSQRDWGKG
     MACVGRTKEC TIVPSNHFGP IPGIPVGTMW RFRVQVSESG VHRPHVAGIH GRSNDGAYSL
     VLAGGYEDDV DHGNSFTYTG SGGRDLSGNK RTAEQSCDQK LTNTNRALAL NCFAPINDLK
     GAEAKDWRSG KPVRVVRNVK GRKHSKYAPI EGNRYDGIYK VVRYWPEKGK SGFLVWRFLL
     RRDDIEPGPW TKEGKDRIKK LGLTMQYPEG YLEALARREK EKENSKRAAL EKEEDGEEGF
     PSPRKGKRKS KSAGGDGSSR GAPKKTKVEP YSLTTQQSNL IKEDKSNTKL WTEILKSLKD
     GPASDSPFQK FLSKVEEAFQ CICCQELVFR PITTVCQHTV CKDCLDRSFR AQVFSCPACR
     YDLGRSYAMH VNQPLQAVLN QLFPGYGSGR
//

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