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E3 ubiquitin-protein ligase CHFR (EC 2.3.2.27) (Checkpoint with forkhead and RING finger domains protein) (RING-type E3 ubiquitin transferase CHFR)

 CHFR_MOUSE              Reviewed;         664 AA.
Q810L3; Q3TFD8; Q3U233; Q3U4U9; Q3UGJ9; Q8BJZ9; Q8BWH4;
02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
12-SEP-2018, entry version 138.
RecName: Full=E3 ubiquitin-protein ligase CHFR;
EC=2.3.2.27 {ECO:0000269|PubMed:15793587};
AltName: Full=Checkpoint with forkhead and RING finger domains protein;
AltName: Full=RING-type E3 ubiquitin transferase CHFR {ECO:0000305};
Name=Chfr;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, Lung, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Limb;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
PubMed=15793587; DOI=10.1038/ng1538;
Yu X., Minter-Dykhouse K., Malureanu L., Zhao W.-M., Zhang D.,
Merkle C.J., Ward I.M., Saya H., Fang G., van Deursen J., Chen J.;
"Chfr is required for tumor suppression and Aurora A regulation.";
Nat. Genet. 37:401-406(2005).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
-!- FUNCTION: E3 ubiquitin-protein ligase that functions in the
antephase checkpoint by actively delaying passage into mitosis in
response to microtubule poisons. Acts in early prophase before
chromosome condensation, when the centrosome move apart from each
other along the periphery of the nucleus. Probably involved in
signaling the presence of mitotic stress caused by microtubule
poisons by mediating the 'Lys-48'-linked ubiquitination of target
proteins, leading to their degradation by the proteasome. Promotes
the ubiquitination and subsequent degradation of AURKA and PLK1.
Probably acts as a tumor suppressor, possibly by mediating the
polyubiquitination of HDAC1, leading to its degradation. May also
promote the formation of 'Lys-63'-linked polyubiquitin chains and
functions with the specific ubiquitin-conjugating UBC13-MMS2
(UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated
at 'Lys-63' are usually not targeted for degradation, but are
rather involved in signaling cellular stress (By similarity).
{ECO:0000250|UniProtKB:Q96EP1, ECO:0000269|PubMed:15793587}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:15793587}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with HDAC1 and HDAC2. Interacts with PML (with
sumoylated form of PML). {ECO:0000250|UniProtKB:Q96EP1}.
-!- SUBCELLULAR LOCATION: Nucleus, PML body
{ECO:0000250|UniProtKB:Q96EP1}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q810L3-1; Sequence=Displayed;
Name=2;
IsoId=Q810L3-2; Sequence=VSP_009351;
Name=3;
IsoId=Q810L3-3; Sequence=VSP_038129;
Name=4;
IsoId=Q810L3-4; Sequence=VSP_038128;
Note=No experimental confirmation available.;
-!- DOMAIN: The PBZ-type zinc finger (also named CYR) mediates non-
covalent poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is
dependent on the presence of zinc and is required for its function
in antephase checkpoint. {ECO:0000250|UniProtKB:Q96EP1}.
-!- DOMAIN: The FHA domain plays a key role in the anti-proliferative
properties of the protein and is involved in initiating a cell
cycle arrest at G2/M. The FHA domain may be required to interact
with phosphorylated proteins. {ECO:0000250|UniProtKB:Q96EP1}.
-!- PTM: Poly-ADP-ribosylated. In addition to binding non covalently
poly(ADP-ribose) via its PBZ-type zinc finger, the protein is also
covalently poly-ADP-ribosylated by PARP1.
{ECO:0000250|UniProtKB:Q96EP1}.
-!- PTM: Autoubiquitinated; may regulate its cellular level.
{ECO:0000250|UniProtKB:Q96EP1}.
-!- PTM: Phosphorylated by PKB. Phosphorylation may affect its E3
ligase activity. {ECO:0000250|UniProtKB:Q96EP1}.
-!- DISRUPTION PHENOTYPE: Mice are viable and have no obvious
developmental defects. They are however cancer-prone and develop
spontaneous tumors. They also display increased skin tumor
incidence after treatment with dimethylbenz(a)anthracene.
{ECO:0000269|PubMed:15793587}.
-!- SIMILARITY: Belongs to the CHFR family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK052473; BAC35008.2; -; mRNA.
EMBL; AK077629; BAC36912.1; -; mRNA.
EMBL; AK147892; BAE28209.1; -; mRNA.
EMBL; AK154038; BAE32331.1; -; mRNA.
EMBL; AK155295; BAE33172.1; -; mRNA.
EMBL; AK155525; BAE33309.1; -; mRNA.
EMBL; AK169182; BAE40960.1; -; mRNA.
EMBL; AK169193; BAE40969.1; -; mRNA.
EMBL; CH466529; EDL20040.1; -; Genomic_DNA.
EMBL; BC049792; AAH49792.1; -; mRNA.
CCDS; CCDS19522.1; -. [Q810L3-2]
CCDS; CCDS71637.1; -. [Q810L3-1]
CCDS; CCDS80358.1; -. [Q810L3-3]
RefSeq; NP_001276506.1; NM_001289577.1. [Q810L3-1]
RefSeq; NP_001276507.1; NM_001289578.1. [Q810L3-3]
RefSeq; NP_001276508.1; NM_001289579.1. [Q810L3-4]
RefSeq; NP_001276509.1; NM_001289580.1.
RefSeq; NP_766305.2; NM_172717.4. [Q810L3-2]
RefSeq; XP_011247747.1; XM_011249445.2. [Q810L3-4]
RefSeq; XP_011247748.1; XM_011249446.2. [Q810L3-4]
UniGene; Mm.30264; -.
ProteinModelPortal; Q810L3; -.
SMR; Q810L3; -.
BioGrid; 231141; 6.
STRING; 10090.ENSMUSP00000014812; -.
iPTMnet; Q810L3; -.
PhosphoSitePlus; Q810L3; -.
PaxDb; Q810L3; -.
PeptideAtlas; Q810L3; -.
PRIDE; Q810L3; -.
Ensembl; ENSMUST00000014812; ENSMUSP00000014812; ENSMUSG00000014668. [Q810L3-2]
Ensembl; ENSMUST00000112519; ENSMUSP00000108138; ENSMUSG00000014668. [Q810L3-1]
Ensembl; ENSMUST00000198633; ENSMUSP00000143480; ENSMUSG00000014668. [Q810L3-3]
GeneID; 231600; -.
KEGG; mmu:231600; -.
UCSC; uc008ypv.3; mouse. [Q810L3-1]
UCSC; uc008ypw.3; mouse. [Q810L3-2]
UCSC; uc008ypz.3; mouse. [Q810L3-3]
CTD; 55743; -.
MGI; MGI:2444898; Chfr.
eggNOG; KOG0802; Eukaryota.
eggNOG; COG5243; LUCA.
GeneTree; ENSGT00400000022306; -.
HOVERGEN; HBG048005; -.
InParanoid; Q810L3; -.
KO; K10644; -.
OMA; HLYWGCA; -.
OrthoDB; EOG091G03AR; -.
PhylomeDB; Q810L3; -.
TreeFam; TF330957; -.
UniPathway; UPA00143; -.
ChiTaRS; Chfr; mouse.
PRO; PR:Q810L3; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000014668; Expressed in 281 organ(s), highest expression level in skin of back.
CleanEx; MM_CHFR; -.
ExpressionAtlas; Q810L3; baseline and differential.
Genevisible; Q810L3; MM.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0016605; C:PML body; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; ISS:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0000278; P:mitotic cell cycle; IMP:MGI.
GO; GO:0007093; P:mitotic cell cycle checkpoint; ISS:UniProtKB.
GO; GO:0019941; P:modification-dependent protein catabolic process; ISO:MGI.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:MGI.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
GO; GO:0031648; P:protein destabilization; IDA:MGI.
GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
CDD; cd00060; FHA; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR000253; FHA_dom.
InterPro; IPR008984; SMAD_FHA_dom_sf.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00498; FHA; 1.
SMART; SM00240; FHA; 1.
SMART; SM00184; RING; 2.
SUPFAM; SSF49879; SSF49879; 1.
PROSITE; PS50006; FHA_DOMAIN; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
ADP-ribosylation; Alternative splicing; Cell cycle; Cell division;
Complete proteome; Metal-binding; Mitosis; Nucleus; Phosphoprotein;
Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 664 E3 ubiquitin-protein ligase CHFR.
/FTId=PRO_0000055873.
DOMAIN 38 89 FHA. {ECO:0000255|PROSITE-
ProRule:PRU00086}.
ZN_FING 303 342 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 633 655 PBZ-type.
MOD_RES 385 385 Phosphothreonine.
{ECO:0000244|PubMed:17525332}.
VAR_SEQ 1 140 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_038128.
VAR_SEQ 135 206 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_038129.
VAR_SEQ 470 470 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009351.
CONFLICT 98 98 Q -> H (in Ref. 1; BAC36912).
{ECO:0000305}.
CONFLICT 230 230 L -> F (in Ref. 1; BAE32331).
{ECO:0000305}.
CONFLICT 333 333 E -> V (in Ref. 1; BAE28209).
{ECO:0000305}.
CONFLICT 531 531 G -> C (in Ref. 1; BAC36912).
{ECO:0000305}.
SEQUENCE 664 AA; 73871 MW; D651BE3E463DEBB6 CRC64;
MELHGEEQPP PPQEPWGRLL RLGAEEDEPQ ILLWKREWTI GRRRGCDLSF PSNKLVSGDH
CKLTVDEISG EVTLEDTSTN GTVINKLQVV KKQTYPLQSG DIIYLVYRKN EPEHNVAYLY
ESLSGKQSLT QDSLEANKEN MFHVTKDCSG PGQGDDPQVP LLSPMAQTCL EEPQPSTSTS
DLLPTASTSS TEPELTSAGQ KHSSSSGPGN TSISPKGRSS LVANGELSSL SPVFQDKEAS
FSLLESKDHE ELEPAKKKMK GDGELDTNLQ LLVSGQRGNA QTSSEDVKDA SVKPDKMEET
LTCIICQDLL HDCVSLQPCM HTFCAACYSG WMERSSLCPT CRCPVERICK NHILNNLVEA
YLIQHPDKSR SEEDVRSMDA RNKITQDMLQ PKVRRSFSDE EGSSEDLLEL SDVDSESSDI
SQPYIVCRQC PEYRRQAVQS LPCPVPESEL GATLALGGEA PSTSASLPTA APDYMCPLQG
SHAICTCCFQ PMPDRRAERE QDPRVAPQQC AVCLQPFCHL YWGCTRTGCF GCLAPFCELN
LGDKCLDGVL NNNNYESDIL KNYLATRGLT WKSVLTESLL ALQRGVFMLS DYRITGNTVL
CYCCGLRSFR ELTYQYRQNI PASELPVTVT SRPDCYWGRN CRTQVKAHHA MKFNHICEQT
RFKN


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