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Protein

E3 ubiquitin-protein ligase CHFR

Gene

Chfr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri303 – 34240RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri633 – 65523PBZ-typeAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • nucleotide binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: MGI
  • ubiquitin-protein transferase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic cell cycle Source: MGI
  • mitotic cell cycle checkpoint Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • modification-dependent protein catabolic process Source: MGI
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
  • positive regulation of protein ubiquitination Source: MGI
  • protein destabilization Source: MGI
  • protein polyubiquitination Source: MGI
  • ubiquitin-dependent protein catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase CHFR (EC:6.3.2.-)
Alternative name(s):
Checkpoint with forkhead and RING finger domains protein
Gene namesi
Name:Chfr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2444898. Chfr.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 664664E3 ubiquitin-protein ligase CHFRPRO_0000055873Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei385 – 3851PhosphothreonineCombined sources

Post-translational modificationi

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 (By similarity).By similarity
Autoubiquitinated; may regulate its cellular level.By similarity
Phosphorylated by PKB. Phosphorylation may affect its E3 ligase activity (By similarity).By similarity

Keywords - PTMi

ADP-ribosylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ810L3.
MaxQBiQ810L3.
PaxDbiQ810L3.
PeptideAtlasiQ810L3.
PRIDEiQ810L3.

PTM databases

iPTMnetiQ810L3.
PhosphoSiteiQ810L3.

Expressioni

Gene expression databases

BgeeiQ810L3.
CleanExiMM_CHFR.
ExpressionAtlasiQ810L3. baseline and differential.
GenevisibleiQ810L3. MM.

Interactioni

Subunit structurei

Interacts with HDAC1 and HDAC2. Interacts with PML (with sumoylated form of PML) (By similarity).By similarity

Protein-protein interaction databases

BioGridi231141. 6 interactions.
STRINGi10090.ENSMUSP00000014812.

Structurei

3D structure databases

ProteinModelPortaliQ810L3.
SMRiQ810L3. Positions 14-124, 232-358, 423-663.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 8952FHAPROSITE-ProRule annotationAdd
BLAST

Domaini

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 (By similarity).By similarity
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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the CHFR family.Curated
Contains 1 FHA domain.PROSITE-ProRule annotation
Contains 1 PBZ-type zinc finger.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri303 – 34240RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri633 – 65523PBZ-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0802. Eukaryota.
COG5243. LUCA.
GeneTreeiENSGT00400000022306.
HOVERGENiHBG048005.
InParanoidiQ810L3.
KOiK10644.
OMAiELAYQYR.
OrthoDBiEOG78D7JS.
PhylomeDBiQ810L3.
TreeFamiTF330957.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q810L3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MELHGEEQPP PPQEPWGRLL RLGAEEDEPQ ILLWKREWTI GRRRGCDLSF
60 70 80 90 100
PSNKLVSGDH CKLTVDEISG EVTLEDTSTN GTVINKLQVV KKQTYPLQSG
110 120 130 140 150
DIIYLVYRKN EPEHNVAYLY ESLSGKQSLT QDSLEANKEN MFHVTKDCSG
160 170 180 190 200
PGQGDDPQVP LLSPMAQTCL EEPQPSTSTS DLLPTASTSS TEPELTSAGQ
210 220 230 240 250
KHSSSSGPGN TSISPKGRSS LVANGELSSL SPVFQDKEAS FSLLESKDHE
260 270 280 290 300
ELEPAKKKMK GDGELDTNLQ LLVSGQRGNA QTSSEDVKDA SVKPDKMEET
310 320 330 340 350
LTCIICQDLL HDCVSLQPCM HTFCAACYSG WMERSSLCPT CRCPVERICK
360 370 380 390 400
NHILNNLVEA YLIQHPDKSR SEEDVRSMDA RNKITQDMLQ PKVRRSFSDE
410 420 430 440 450
EGSSEDLLEL SDVDSESSDI SQPYIVCRQC PEYRRQAVQS LPCPVPESEL
460 470 480 490 500
GATLALGGEA PSTSASLPTA APDYMCPLQG SHAICTCCFQ PMPDRRAERE
510 520 530 540 550
QDPRVAPQQC AVCLQPFCHL YWGCTRTGCF GCLAPFCELN LGDKCLDGVL
560 570 580 590 600
NNNNYESDIL KNYLATRGLT WKSVLTESLL ALQRGVFMLS DYRITGNTVL
610 620 630 640 650
CYCCGLRSFR ELTYQYRQNI PASELPVTVT SRPDCYWGRN CRTQVKAHHA
660
MKFNHICEQT RFKN
Length:664
Mass (Da):73,871
Last modified:June 1, 2003 - v1
Checksum:iD651BE3E463DEBB6
GO
Isoform 2 (identifier: Q810L3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     470-470: Missing.

Show »
Length:663
Mass (Da):73,800
Checksum:iCBAF0A41DF4E088F
GO
Isoform 3 (identifier: Q810L3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     135-206: Missing.

Show »
Length:592
Mass (Da):66,385
Checksum:i0F74391E43FDC1D0
GO
Isoform 4 (identifier: Q810L3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-140: Missing.

Note: No experimental confirmation available.
Show »
Length:524
Mass (Da):57,925
Checksum:iD36040F01A7453B2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981Q → H in BAC36912 (PubMed:16141072).Curated
Sequence conflicti230 – 2301L → F in BAE32331 (PubMed:16141072).Curated
Sequence conflicti333 – 3331E → V in BAE28209 (PubMed:16141072).Curated
Sequence conflicti531 – 5311G → C in BAC36912 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 140140Missing in isoform 4. 1 PublicationVSP_038128Add
BLAST
Alternative sequencei135 – 20672Missing in isoform 3. 1 PublicationVSP_038129Add
BLAST
Alternative sequencei470 – 4701Missing in isoform 2. 1 PublicationVSP_009351

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052473 mRNA. Translation: BAC35008.2.
AK077629 mRNA. Translation: BAC36912.1.
AK147892 mRNA. Translation: BAE28209.1.
AK154038 mRNA. Translation: BAE32331.1.
AK155295 mRNA. Translation: BAE33172.1.
AK155525 mRNA. Translation: BAE33309.1.
AK169182 mRNA. Translation: BAE40960.1.
AK169193 mRNA. Translation: BAE40969.1.
CH466529 Genomic DNA. Translation: EDL20040.1.
BC049792 mRNA. Translation: AAH49792.1.
CCDSiCCDS19522.1. [Q810L3-2]
CCDS71637.1. [Q810L3-1]
CCDS80358.1. [Q810L3-3]
RefSeqiNP_001276506.1. NM_001289577.1. [Q810L3-1]
NP_001276507.1. NM_001289578.1. [Q810L3-3]
NP_001276508.1. NM_001289579.1. [Q810L3-4]
NP_001276509.1. NM_001289580.1.
NP_766305.2. NM_172717.4. [Q810L3-2]
XP_011247747.1. XM_011249445.1. [Q810L3-4]
XP_011247748.1. XM_011249446.1. [Q810L3-4]
UniGeneiMm.30264.

Genome annotation databases

EnsembliENSMUST00000014812; ENSMUSP00000014812; ENSMUSG00000014668. [Q810L3-2]
ENSMUST00000112519; ENSMUSP00000108138; ENSMUSG00000014668. [Q810L3-1]
ENSMUST00000198633; ENSMUSP00000143480; ENSMUSG00000014668. [Q810L3-3]
GeneIDi231600.
KEGGimmu:231600.
UCSCiuc008ypv.3. mouse. [Q810L3-1]
uc008ypw.3. mouse. [Q810L3-2]
uc008ypz.3. mouse. [Q810L3-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052473 mRNA. Translation: BAC35008.2.
AK077629 mRNA. Translation: BAC36912.1.
AK147892 mRNA. Translation: BAE28209.1.
AK154038 mRNA. Translation: BAE32331.1.
AK155295 mRNA. Translation: BAE33172.1.
AK155525 mRNA. Translation: BAE33309.1.
AK169182 mRNA. Translation: BAE40960.1.
AK169193 mRNA. Translation: BAE40969.1.
CH466529 Genomic DNA. Translation: EDL20040.1.
BC049792 mRNA. Translation: AAH49792.1.
CCDSiCCDS19522.1. [Q810L3-2]
CCDS71637.1. [Q810L3-1]
CCDS80358.1. [Q810L3-3]
RefSeqiNP_001276506.1. NM_001289577.1. [Q810L3-1]
NP_001276507.1. NM_001289578.1. [Q810L3-3]
NP_001276508.1. NM_001289579.1. [Q810L3-4]
NP_001276509.1. NM_001289580.1.
NP_766305.2. NM_172717.4. [Q810L3-2]
XP_011247747.1. XM_011249445.1. [Q810L3-4]
XP_011247748.1. XM_011249446.1. [Q810L3-4]
UniGeneiMm.30264.

3D structure databases

ProteinModelPortaliQ810L3.
SMRiQ810L3. Positions 14-124, 232-358, 423-663.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231141. 6 interactions.
STRINGi10090.ENSMUSP00000014812.

PTM databases

iPTMnetiQ810L3.
PhosphoSiteiQ810L3.

Proteomic databases

EPDiQ810L3.
MaxQBiQ810L3.
PaxDbiQ810L3.
PeptideAtlasiQ810L3.
PRIDEiQ810L3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000014812; ENSMUSP00000014812; ENSMUSG00000014668. [Q810L3-2]
ENSMUST00000112519; ENSMUSP00000108138; ENSMUSG00000014668. [Q810L3-1]
ENSMUST00000198633; ENSMUSP00000143480; ENSMUSG00000014668. [Q810L3-3]
GeneIDi231600.
KEGGimmu:231600.
UCSCiuc008ypv.3. mouse. [Q810L3-1]
uc008ypw.3. mouse. [Q810L3-2]
uc008ypz.3. mouse. [Q810L3-3]

Organism-specific databases

CTDi55743.
MGIiMGI:2444898. Chfr.

Phylogenomic databases

eggNOGiKOG0802. Eukaryota.
COG5243. LUCA.
GeneTreeiENSGT00400000022306.
HOVERGENiHBG048005.
InParanoidiQ810L3.
KOiK10644.
OMAiELAYQYR.
OrthoDBiEOG78D7JS.
PhylomeDBiQ810L3.
TreeFamiTF330957.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiChfr. mouse.
PROiQ810L3.
SOURCEiSearch...

Gene expression databases

BgeeiQ810L3.
CleanExiMM_CHFR.
ExpressionAtlasiQ810L3. baseline and differential.
GenevisibleiQ810L3. MM.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
    Strain: C57BL/6J and NOD.
    Tissue: Kidney, Lung and Thymus.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Limb.
  4. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiCHFR_MOUSE
AccessioniPrimary (citable) accession number: Q810L3
Secondary accession number(s): Q3TFD8
, Q3U233, Q3U4U9, Q3UGJ9, Q8BJZ9, Q8BWH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: June 1, 2003
Last modified: July 6, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.