ID A0A0D9S5R7_CHLSB Unreviewed; 665 AA.
AC A0A0D9S5R7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=E3 ubiquitin-protein ligase CHFR {ECO:0000256|ARBA:ARBA00017908};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Checkpoint with forkhead and RING finger domains protein {ECO:0000256|ARBA:ARBA00031332};
DE AltName: Full=RING-type E3 ubiquitin transferase CHFR {ECO:0000256|ARBA:ARBA00029800};
GN Name=CHFR {ECO:0000313|Ensembl:ENSCSAP00000016206.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000016206.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000016206.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000016206.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus, PML body
CC {ECO:0000256|ARBA:ARBA00004322}.
CC -!- SIMILARITY: Belongs to the CHFR family.
CC {ECO:0000256|ARBA:ARBA00005797}.
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DR EMBL; AQIB01153253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008003517.1; XM_008005326.1.
DR AlphaFoldDB; A0A0D9S5R7; -.
DR STRING; 60711.ENSCSAP00000016206; -.
DR Ensembl; ENSCSAT00000016705.1; ENSCSAP00000016206.1; ENSCSAG00000001822.1.
DR GeneID; 103239459; -.
DR CTD; 55743; -.
DR eggNOG; KOG0802; Eukaryota.
DR GeneTree; ENSGT00400000022306; -.
DR OMA; SNYWFPG; -.
DR OrthoDB; 450556at2759; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 103239459; 1 hit in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 11.
DR Bgee; ENSCSAG00000001822; Expressed in blood and 7 other cell types or tissues.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044779; P:meiotic spindle checkpoint signaling; IEA:Ensembl.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR CDD; cd22672; FHA_CHFR; 1.
DR CDD; cd16503; RING-HC_CHFR; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.30.40.140; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR040909; CHFR_Znf-CRD.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR Pfam; PF17979; zf-CRD; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 38..89
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 306..345
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 145..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 665 AA; 73821 MW; BD061D985CD743B3 CRC64;
MERPEEGKQP PLPQPWGRLL RLGAEEGEPH VLLRKREWTI GRRRGCDLSF PGNKLVSGDH
CKIVVDEKSG QVTLEDTSTN GTVINKLKVV KKQTCPLQSG DIIYLVYRKN EPEYNVAYLY
ESLNEKQGMT RESFEANKEN VFHGTKDASG AGVGAGPGAD PWLPPLSPTA QVCFEEPQPS
TSTSDLFPTA LASSTEPPPA GREHSSSCES GGGGISPKGC GPSVASDKIS SFASALSDRK
PASFSSLEPR DQEDLEPVKK KMKGDGDLDL NLQLLVAQPR RNAQTVQEDV RAATGRPDKM
EETLTCIICQ DLLHDCVSLQ PCMHTFCAAC YSGWMERSSL CPTCRCPVER ICKNHILNNL
VEAYLTQHPD KSRSEEDVQS MDARNKITQD MLQPKVRRSF SDEEGSSEDL LELSDVDSES
SDISQPYVVC RQCPEYRRQV VQPPHCPAPE GEPGAPQALG DVPSTSVSLT TVQDYVCPLQ
GSHALCTCCF QPMPDRRAER EQDPRVAPQQ CAVCLQPFCH LYWGCTRTGC FGCLAPFCEL
NLGDKCLDGV LNNNSYESDI LKNYLATRGL TWKNMLTESL VALQRGVFLL SDYRVTGNTV
LCYCCGLRSF RELTYQYRRN IPASELPVAV TSRPDCYWGR NCRTQVKAHH AMKFNHICEQ
TRFKN
//
