CHFR report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0032436Biological processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
GO_0016567Biological processprotein ubiquitination
GO_0006511Biological processubiquitin-dependent protein catabolic process
GO_0044818Biological processmitotic G2/M transition checkpoint
GO_0031398Biological processpositive regulation of protein ubiquitination
GO_0051301Biological processcell division
GO_0044779Biological processmeiotic spindle checkpoint signaling
GO_0000209Biological processprotein polyubiquitination
GO_0007093Biological processmitotic cell cycle checkpoint signaling
GO_0031648Biological processprotein destabilization
GO_0016605Cellular componentPML body
GO_0005634Cellular componentnucleus
GO_0061630Molecular functionubiquitin protein ligase activity
GO_0004842Molecular functionubiquitin-protein transferase activity
GO_0005515Molecular functionprotein binding
GO_0046872Molecular functionmetal ion binding
GO_0000166Molecular functionnucleotide binding

IV. Literature review

[source]
Gene nameCHFR
Protein nameE3 ubiquitin-protein ligase CHFR (EC 2.3.2.27) (Checkpoint with forkhead and RING finger domains protein) (RING finger protein 196) (RING-type E3 ubiquitin transferase CHFR)
Checkpoint with forkhead and ring finger domains
SynonymsRNF196
DescriptionFUNCTION: 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. .

AccessionsENST00000542714.5
ENST00000540963.1
ENST00000315585.11
F5H375
ENST00000443047.6 [Q96EP1-5]
A0A087X0W6
ENST00000536932.5
A0A087WUN4
Q96EP1
ENST00000541817.5
F5GWH4
ENST00000266880.11 [Q96EP1-3]
F5H829
U3KPU9
A0A096P6K8
ENST00000535527.5
ENST00000432561.6 [Q96EP1-1]
ENST00000540537.5
ENST00000544093.5
F5H5P5
ENST00000450056.7 [Q96EP1-2]