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Protein Page:
CHFR (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CHFR 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. Interacts with HDAC1 and HDAC2. Interacts with PML (with sumoylated form of PML). Ubiquitous. Belongs to the CHFR family. 5 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin ligase; EC 6.3.2.19; Ligase; Ubiquitin conjugating system; EC 6.3.2.-
Cellular Component: PML body; nucleus
Molecular Function: protein binding; zinc ion binding; nucleotide binding; ubiquitin-protein ligase activity; ligase activity
Biological Process: ubiquitin-dependent protein catabolic process; modification-dependent protein catabolic process; mitosis; protein polyubiquitination; mitotic cell cycle checkpoint
Reference #:  Q96EP1 (UniProtKB)
Alt. Names/Synonyms: checkpoint with forkhead and ring finger domains; Checkpoint with forkhead and RING finger domains protein; CHFR; E3 ubiquitin-protein ligase CHFR; FLJ10796; FLJ33629; RING finger protein 196; RNF116; RNF196
Gene Symbols: CHFR
Molecular weight: 73,386 Da
Basal Isoelectric point: 5.71  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CHFR

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 2 S10-p RPEEGKQsPPPQPWG
0 1 T130-p LSEKQGMtQEsFEAN
0 1 S133-p KQGMtQEsFEANKEN
0 2 S208-p ERSSSCGsGGGGIsP
0 5 S214-p GsGGGGIsPKGSGPS
0 2 A231 SDEVSSFASALPDRK
0 1 S244-p RKTASFSsLEPQDQE
1 0 K384-ub QSMDARNkITQDMLQ
1 0 K393-ub TQDMLQPkVRRSFSD
0 1 N573 TRGLTWKNMLTESLV
1 0 K663-sm ICEQTRFkN______
  CHFR iso3  
S10 RPEEGKQSPPPQPWG
T130 LSEKQGMTQESFEMV
S133 KQGMTQESFEMVPCC
S167 QSIVITGSGGGGISP
S173 GSGGGGISPKGSGPS
A190 SDEVSSFASALPDRK
S203 RKTASFSSLEPQDQE
K343 QSMDARNKITQDMLQ
K352 TQDMLQPKVRRSFSD
N532 TRGLTWKNMLTESLV
K622 ICEQTRFKN______
  CHFR iso5  
S10 RPEEGKQSPPPQPWG
- gap
- gap
- gap
S122-p RSGGGGIsPKGSGPS
A139 SDEVSSFASALPDRK
S152 RKTASFSSLEPQDQE
K292 QSMDARNKITQDMLQ
K301 TQDMLQPKVRRSFSD
N481 TRGLTWKNMLTESLV
K571 ICEQTRFKN______
  mouse

 
P10 LHGEEQPPPPQEPWG
T130 LSGKQSLTQDSLEAN
S133 KQSLTQDSLEANKEN
S206 GQKHSSSSGPGNTSI
S214-p GPGNTSIsPKGRSSL
S231-p NGELSSLsPVFQDKE
L243 DKEASFSLLESKDHE
K383 RSMDARNKITQDMLQ
K392 TQDMLQPKVRRSFSD
S573-p TRGLTWKsVLTESLL
K663 ICEQTRFKN______
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