CHFR_XENTR
ID CHFR_XENTR Reviewed; 626 AA.
AC Q6P256;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=E3 ubiquitin-protein ligase CHFR;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q96EP1};
DE AltName: Full=Checkpoint with forkhead and RING finger domains protein;
DE AltName: Full=RING-type E3 ubiquitin transferase CHFR {ECO:0000305};
GN Name=chfr;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that functions in the antephase
CC checkpoint by actively delaying passage into mitosis in response to
CC microtubule poisons. Acts in early prophase before chromosome
CC condensation, when the centrosome move apart from each other along the
CC periphery of the nucleus. Probably involved in signaling the presence
CC of mitotic stress caused by microtubule poisons by mediating the 'Lys-
CC 48'-linked ubiquitination of target proteins, leading to their
CC degradation by the proteasome. May also promote the formation of 'Lys-
CC 63'-linked polyubiquitin chains and functions with the specific
CC ubiquitin-conjugating ubc13-mms2 (ube2n-ube2v2) heterodimer. Substrates
CC that are polyubiquitinated at 'Lys-63' are usually not targeted for
CC degradation, but are rather involved in signaling cellular stress.
CC {ECO:0000250|UniProtKB:Q96EP1}.
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:0000250|UniProtKB:Q96EP1};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250|UniProtKB:Q5FWP4}.
CC -!- DOMAIN: The PBZ-type zinc finger (also named CYR) mediates non-covalent
CC poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is dependent on the
CC presence of zinc and is required for its function in antephase
CC checkpoint. {ECO:0000250|UniProtKB:Q96EP1}.
CC -!- DOMAIN: The FHA domain plays a key role in the anti-proliferative
CC properties of the protein and is involved in initiating a cell cycle
CC arrest at G2/M. {ECO:0000250|UniProtKB:Q96EP1}.
CC -!- SIMILARITY: Belongs to the CHFR family. {ECO:0000305}.
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DR EMBL; BC064721; AAH64721.1; -; mRNA.
DR RefSeq; NP_989378.1; NM_204047.1.
DR RefSeq; XP_012813996.1; XM_012958542.2.
DR RefSeq; XP_012814001.1; XM_012958547.2.
DR AlphaFoldDB; Q6P256; -.
DR SMR; Q6P256; -.
DR STRING; 8364.ENSXETP00000052239; -.
DR PaxDb; Q6P256; -.
DR DNASU; 395009; -.
DR Ensembl; ENSXETT00000052239; ENSXETP00000052239; ENSXETG00000024212.
DR GeneID; 395009; -.
DR KEGG; xtr:395009; -.
DR CTD; 55743; -.
DR Xenbase; XB-GENE-998659; chfr.
DR eggNOG; KOG0802; Eukaryota.
DR HOGENOM; CLU_032966_0_0_1; -.
DR InParanoid; Q6P256; -.
DR OMA; CYGDWRA; -.
DR OrthoDB; 1506037at2759; -.
DR PhylomeDB; Q6P256; -.
DR TreeFam; TF330957; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000024212; Expressed in egg cell and 13 other tissues.
DR ExpressionAtlas; Q6P256; differential.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; ISS:UniProtKB.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019406; APLF_PBZ.
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 Pfam; PF00498; FHA; 1.
DR Pfam; PF10283; zf-CCHH; 1.
DR Pfam; PF17979; zf-CRD; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Metal-binding; Mitosis; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..626
FT /note="E3 ubiquitin-protein ligase CHFR"
FT /id="PRO_0000385304"
FT DOMAIN 34..85
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT ZN_FING 267..306
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 595..617
FT /note="PBZ-type"
FT REGION 123..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 69961 MW; 94DDF60D9E3DDA60 CRC64;
MDGLGEKKPW GKLSRLLGAE TESSSELFLY KKEWTIGRKK ACDLSFPGNK LVSGEHCKIT
VNEESGSVSL EDTSTNGTVI NKLKVVKKQT YPLKNGDVIY VVYRKNEPEQ NVAYLYKSLN
QAEDSMQNPA DTSGSEEADT QTLSSQDDQL SYEEPQPSTS TSSLFSTPTT SASEPACTLL
YKSQASVPGV QLESGEKSGE SLEGHSSTSD ATAHEKGSLG PPKKRMRTED LWTGNKNLVS
ASCSKGASDE SKTPSMKPDK MEETLTCIIC QELLHDCVSL QPCMHTFCAA CYSGWMERSS
LCPTCRCPVE RICKNHILNN LVEAYLIQHP EKCRSEEDRC SMDARNKITQ DMLQPKVRRS
FSDEEGSSED LLELSDVDSE SSDISQPYTV CRQCPGYVRH NIQPPPYPPP SDTEASRTQG
DAPSTSTNFP TATQEYVCPS HGSHVICTCC FQPMPDRRAE REHNSHVAPQ QCTICLEPFC
HMYWGCNRMG CFGCLAPFCE LNLGDKCLDG VLNNNNYESD ILKNYLASRG LTWKDMLNES
LSAAQRGVFM LPDYRINGTT VLCYFCGLRN FRILTYQYRQ NIPASELPVT VTSRPNCYWG
RNCRTQVKAH HAMKFNHICE QTRFKN
