| UniProt ID | CHFR_HUMAN | |
|---|---|---|
| UniProt AC | Q96EP1 | |
| Protein Name | E3 ubiquitin-protein ligase CHFR | |
| Gene Name | CHFR | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 664 | |
| Subcellular Localization | Nucleus, PML body . | |
| Protein Description | 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.. | |
| Protein Sequence | MERPEEGKQSPPPQPWGRLLRLGAEEGEPHVLLRKREWTIGRRRGCDLSFPSNKLVSGDHCRIVVDEKSGQVTLEDTSTSGTVINKLKVVKKQTCPLQTGDVIYLVYRKNEPEHNVAYLYESLSEKQGMTQESFEANKENVFHGTKDTSGAGAGRGADPRVPPSSPATQVCFEEPQPSTSTSDLFPTASASSTEPSPAGRERSSSCGSGGGGISPKGSGPSVASDEVSSFASALPDRKTASFSSLEPQDQEDLEPVKKKMRGDGDLDLNGQLLVAQPRRNAQTVHEDVRAAAGKPDKMEETLTCIICQDLLHDCVSLQPCMHTFCAACYSGWMERSSLCPTCRCPVERICKNHILNNLVEAYLIQHPDKSRSEEDVQSMDARNKITQDMLQPKVRRSFSDEEGSSEDLLELSDVDSESSDISQPYVVCRQCPEYRRQAAQPPHCPAPEGEPGAPQALGDAPSTSVSLTTAVQDYVCPLQGSHALCTCCFQPMPDRRAEREQDPRVAPQQCAVCLQPFCHLYWGCTRTGCYGCLAPFCELNLGDKCLDGVLNNNSYESDILKNYLATRGLTWKNMLTESLVALQRGVFLLSDYRVTGDTVLCYCCGLRSFRELTYQYRQNIPASELPVAVTSRPDCYWGRNCRTQVKAHHAMKFNHICEQTRFKN | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 10 | Phosphorylation | RPEEGKQSPPPQPWG CCCCCCCCCCCCCHH | 42.74 | 23401153 | |
| 86 | Ubiquitination | TSGTVINKLKVVKKQ CCCCEEEEEEEECCC | 38.26 | 32015554 | |
| 116 (in isoform 5) | Phosphorylation | - | 3.90 | 24275569 | |
| 122 (in isoform 5) | Phosphorylation | - | 24.52 | 24275569 | |
| 130 | Phosphorylation | LSEKQGMTQESFEAN HHHHCCCCHHHHHHH | 35.69 | - | |
| 130 (in isoform 2) | Phosphorylation | - | 35.69 | 24043423 | |
| 133 | Phosphorylation | KQGMTQESFEANKEN HCCCCHHHHHHHHHH | 20.69 | - | |
| 133 (in isoform 2) | Phosphorylation | - | 20.69 | 24043423 | |
| 136 (in isoform 2) | Phosphorylation | - | 30.31 | 24043423 | |
| 137 (in isoform 2) | Phosphorylation | - | 45.00 | 24043423 | |
| 164 | Phosphorylation | ADPRVPPSSPATQVC CCCCCCCCCCCCEEC | 42.77 | 28348404 | |
| 165 (in isoform 3) | Phosphorylation | - | 25.07 | 27251275 | |
| 165 | Phosphorylation | DPRVPPSSPATQVCF CCCCCCCCCCCEECC | 25.07 | 28348404 | |
| 167 (in isoform 3) | Phosphorylation | - | 16.77 | 27251275 | |
| 173 (in isoform 3) | Phosphorylation | - | 64.74 | 27251275 | |
| 193 | Phosphorylation | PTASASSTEPSPAGR CCCCCCCCCCCCCCC | 49.79 | 33259812 | |
| 203 | Phosphorylation | SPAGRERSSSCGSGG CCCCCCCCCCCCCCC | 23.11 | 24211406 | |
| 204 | Phosphorylation | PAGRERSSSCGSGGG CCCCCCCCCCCCCCC | 35.55 | 24211406 | |
| 205 | Phosphorylation | AGRERSSSCGSGGGG CCCCCCCCCCCCCCC | 24.60 | 33259812 | |
| 208 | Phosphorylation | ERSSSCGSGGGGISP CCCCCCCCCCCCCCC | 38.29 | 27135362 | |
| 214 | Phosphorylation | GSGGGGISPKGSGPS CCCCCCCCCCCCCCC | 24.67 | 25849741 | |
| 239 | Phosphorylation | SALPDRKTASFSSLE HHCCCCCCCCCCCCC | 28.55 | 27251275 | |
| 241 | Phosphorylation | LPDRKTASFSSLEPQ CCCCCCCCCCCCCCC | 30.78 | 23186163 | |
| 243 | Phosphorylation | DRKTASFSSLEPQDQ CCCCCCCCCCCCCCH | 31.36 | 24719451 | |
| 244 | Phosphorylation | RKTASFSSLEPQDQE CCCCCCCCCCCCCHH | 34.44 | 23917254 | |
| 372 | Phosphorylation | QHPDKSRSEEDVQSM HCCCCCCCHHHHHHH | 53.05 | 18785766 | |
| 378 | Phosphorylation | RSEEDVQSMDARNKI CCHHHHHHHHHHHHH | 20.62 | 25262027 | |
| 384 | Ubiquitination | QSMDARNKITQDMLQ HHHHHHHHHHHHHHC | 41.39 | 21768102 | |
| 386 | Phosphorylation | MDARNKITQDMLQPK HHHHHHHHHHHHCHH | 21.81 | 18785766 | |
| 393 | Ubiquitination | TQDMLQPKVRRSFSD HHHHHCHHHHHHCCC | 35.10 | 2176810 | |
| 576 | Phosphorylation | LTWKNMLTESLVALQ CCHHHHHHHHHHHHH | 16.86 | 24719451 | |
| 578 | Phosphorylation | WKNMLTESLVALQRG HHHHHHHHHHHHHHC | 23.94 | 28842319 | |
| 590 | Phosphorylation | QRGVFLLSDYRVTGD HHCCEECCCCEECCC | 34.44 | 24719451 | |
| 592 | Phosphorylation | GVFLLSDYRVTGDTV CCEECCCCEECCCEE | 12.01 | 24719451 | |
| 663 | Sumoylation | ICEQTRFKN------ HHHHHCCCC------ | 59.46 | - | |
| 663 | Sumoylation | ICEQTRFKN------ HHHHHCCCC------ | 59.46 | - |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CHFR_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CHFR_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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