CHFR_XENLA
ID CHFR_XENLA Reviewed; 625 AA.
AC Q5FWP4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=15467728; DOI=10.1038/nsmb837;
RA Daniels M.J., Marson A., Venkitaraman A.R.;
RT "PML bodies control the nuclear dynamics and function of the CHFR mitotic
RT checkpoint protein.";
RL Nat. Struct. Mol. Biol. 11:1114-1121(2004).
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 -!- INTERACTION:
CC Q5FWP4; Q7ZYF2: tpt1; NbExp=3; IntAct=EBI-1783502, EBI-1783711;
CC -!- SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000269|PubMed:15467728}.
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; BC089260; AAH89260.1; -; mRNA.
DR RefSeq; NP_001089240.1; NM_001095771.1.
DR AlphaFoldDB; Q5FWP4; -.
DR SMR; Q5FWP4; -.
DR BioGRID; 592068; 4.
DR IntAct; Q5FWP4; 2.
DR DNASU; 734287; -.
DR GeneID; 734287; -.
DR KEGG; xla:734287; -.
DR CTD; 734287; -.
DR Xenbase; XB-GENE-6251657; chfr.L.
DR OMA; DEDTCPN; -.
DR OrthoDB; 1506037at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 734287; Expressed in blastula and 19 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA: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 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 1: Evidence at protein level;
KW Cell cycle; Cell division; Metal-binding; Mitosis; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..625
FT /note="E3 ubiquitin-protein ligase CHFR"
FT /id="PRO_0000385303"
FT DOMAIN 34..85
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT ZN_FING 266..305
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 594..616
FT /note="PBZ-type"
FT REGION 123..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 70019 MW; 72C0A497D48F6BDC CRC64;
MEGLDEKKPW GKLSRLLGAE TDSSSELFLY KKEWTIGRKK ACDLSFPGNK LVSGEHCKIT
VNEESGEVSL EDTSTNGTVI NKLKVIRKQT YPLKNGDVIY VVYRKNEPEQ NVAYLYKSLN
QGQDSLHDPA DTSGSEEAET QTLSSQDDQL SYEEPQPSTS TSSLFSTPTT SAIPGVQLES
AEKSGESLGG HSSTSDASPA IRASIPKSNL STQEQGSLGP PKKRIRTEDH WTTNKNFVPA
SCPIGASDES KTPSMKPDKM EETLTCIICQ ELLHDCVSLQ PCMHTFCAAC YSGWMERSSL
CPTCRCPVER ICKNHILNNL VEAYLIQHPE KCRSEEDRCS MDARNKITQD MLQPKVRRSF
SDEEGSSEDL LELSDVDSES SDISQPYTVC RQCPGFVRHS MQPPPYPPPS DTETSRTQGD
APSTSTNFPT ATQEYVCPSH GSHVICTCCF QPMPDRRAER EHNSHVAPQQ CTICLEPFCH
MYWGCNRMGC FGCLAPFCEL NLGDKCLDGV LNNNNYESDI LKNYLASRGL TWKDMLNESL
AAVQRGVFML PDYRINGTTV LCYFCGLRNF RILTYQYRQN IPASELPVTV TSRPNCYWGR
NCRTQVKAHH AMKFNHICEQ TRFKN
