UniProt: A9JS25

Database: UniProt
Entry: A9JS25_XENLA

LinkDB:  A9JS25_XENLA 
Original site:  A9JS25_XENLA

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   XENBASE (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (21)   

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ID   A9JS25_XENLA            Unreviewed;       965 AA.
AC   A9JS25;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   Name=rnf20.L {ECO:0000313|RefSeq:NP_001106332.1,
GN   ECO:0000313|Xenbase:XB-GENE-5746958};
GN   Synonyms=LOC100127292 {ECO:0000313|EMBL:AAI55891.1}, rnf20
GN   {ECO:0000313|RefSeq:NP_001106332.1,
GN   ECO:0000313|Xenbase:XB-GENE-5746958};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAI55891.1};
RN   [1] {ECO:0000313|RefSeq:NP_001106332.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAI55891.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus/thymocytes {ECO:0000313|EMBL:AAI55891.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001106332.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (APR-2022) to UniProtKB.
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:RU365038};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU365038}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU365038}.
CC   -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000256|ARBA:ARBA00005555,
CC       ECO:0000256|RuleBase:RU365038}.
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DR   EMBL; BC155890; AAI55891.1; -; mRNA.
DR   RefSeq; NP_001106332.1; NM_001112861.2.
DR   IntAct; A9JS25; 2.
DR   STRING; 8355.A9JS25; -.
DR   PaxDb; 8355-A9JS25; -.
DR   GeneID; 100127292; -.
DR   KEGG; xla:100127292; -.
DR   AGR; Xenbase:XB-GENE-5746958; -.
DR   CTD; 100127292; -.
DR   Xenbase; XB-GENE-5746958; rnf20.L.
DR   OMA; YSNIDTR; -.
DR   OrthoDB; 53681at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 100127292; Expressed in zone of skin and 19 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase 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; cd16814; RING-HC_RNF20; 1.
DR   Gene3D; 1.20.1170.10; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23163:SF2; E3 UBIQUITIN-PROTEIN LIGASE BRE1A; 1.
DR   PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|RuleBase:RU365038};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU365038};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365038};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU365038};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365038};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          912..951
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          51..82
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          225..298
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          336..373
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          431..507
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        510..529
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..617
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   965 AA;  112241 MW;  1A79BE98C53FA463 CRC64;
     MSGPGSKRVA GDVGSLGPPE KKAAVEDSGT TVETIKLGSV SSTEEQDLRT LQLKNKKLAG
     MLDQRQAIED ELRDRIETLE RRQATDDASL LIVNRYWSQF DENIGILLGR YDLDQDLGEF
     LTERKALVLP EPEPDSDSNP ERKENERGEG LWEAPLSFLA TLASSSSEEI ESQLQERVES
     SRRAVSRIVL VYDRLHDQLD HLSKKLNSTD PSQMEEAIRD LNSMLSNENV RLQEISNLLQ
     EKQQNMSQEF LQMQSRLESA ESRVLVLDGH IEDLQWDIDK IRKREQRLNR HLSEVLERVN
     SKGYKVYGAG SSLYGGTITI NSRKFEEMTS EVDLNKELAV NRLQELEKLR QDLQEVTSEN
     QELQAELASA VEENVRLSPE YRCMQSQFSV LYNESLQLKT QLDEARSLLH GTRSNHQRQL
     ELIERDEISL QKKVRTEVIQ LEDTLAQVRK EYEMLRIEFE QTLAANEQAG PINREMRHLI
     SSLQNHNHQL KGEVLRYKRR LREIQGDISK MRSRSSSSLF LLPSQSSTEE TREETAEIKT
     EPEDTFANAP APPQPEIVPK REEEEVQPPL QQPQRDRRER ERERERDRGR EKERGDSSKE
     KPKHEADTKR KDADTVKQMK ADLKRVQESL RDMKLLLDMY RSAPKEQRDK VQLMAAERKS
     KAELEELRLR LRELEERERR DSKKMADEDA LRRMRAAEEQ TEVLQKRLSV AKQEEEALLS
     EMDVTGQAFE DMQEQNIRLM QQLREKDDAN FKLMSERIKS NQIHKLLKEE KEELADQLLT
     LRTQVDAQLQ VLRKLEEKEH LLQTSINTGE KELTLRTQAL DLCKRKATES SQQAEELRSQ
     LELSQKKLQD LRGEIIENTA SREKDAFNYK RAQEDISRLR KKLESTKKPD LVPTCDKILM
     EEIKEYKARL TCPCCNSRKM DAVLTKCFHV FCFECVKTRY DTRQRKCPKC NAAFGANDFH
     RIYIG
//

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