| UniProt ID | AMFR_HUMAN | |
|---|---|---|
| UniProt AC | Q9UKV5 | |
| Protein Name | E3 ubiquitin-protein ligase AMFR | |
| Gene Name | AMFR | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 643 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . Palmitoylation promotes localization to the peripheral endoplasmic reticulum. |
|
| Protein Description | E3 ubiquitin-protein ligase that mediates the polyubiquitination of a number of proteins such as CD3D, CYP3A4, CFTR and APOB for proteasomal degradation. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD). The VCP/p97-AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG complex at the ER membrane and initiating ubiquitination of HMGCR. The ubiquitinated HMGCR is then released from the ER by the complex into the cytosol for subsequent destruction. Also regulates ERAD through the ubiquitination of UBL4A a component of the BAG6/BAT3 complex. Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation. Mediates tumor invasion and metastasis as a receptor for the GPI/autocrine motility factor.. | |
| Protein Sequence | MPLLFLERFPWPSLRTYTGLSGLALLGTIISAYRALSQPEAGPGEPDQLTASLQPEPPAPARPSAGGPRARDVAQYLLSDSLFVWVLVNTACCVLMLVAKLIQCIVFGPLRVSERQHLKDKFWNFIFYKFIFIFGVLNVQTVEEVVMWCLWFAGLVFLHLMVQLCKDRFEYLSFSPTTPMSSHGRVLSLLVAMLLSCCGLAAVCSITGYTHGMHTLAFMAAESLLVTVRTAHVILRYVIHLWDLNHEGTWEGKGTYVYYTDFVMELTLLSLDLMHHIHMLLFGNIWLSMASLVIFMQLRYLFHEVQRRIRRHKNYLRVVGNMEARFAVATPEELAVNNDDCAICWDSMQAARKLPCGHLFHNSCLRSWLEQDTSCPTCRMSLNIADNNRVREEHQGENLDENLVPVAAAEGRPRLNQHNHFFHFDGSRIASWLPSFSVEVMHTTNILGITQASNSQLNAMAHQIQEMFPQVPYHLVLQDLQLTRSVEITTDNILEGRIQVPFPTQRSDSIRPALNSPVERPSSDQEEGETSAQTERVPLDLSPRLEETLDFGEVEVEPSEVEDFEARGSRFSKSADERQRMLVQRKDELLQQARKRFLNKSSEDDAASESFLPSEGASSDPVTLRRRMLAAAAERRLQKQQTS | |
| 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 |
|---|---|---|---|---|---|
| 21 | Phosphorylation | LRTYTGLSGLALLGT HHHCCCHHHHHHHHH | 24719451 | ||
| 25 | Ubiquitination | TGLSGLALLGTIISA CCHHHHHHHHHHHHH | 21906983 | ||
| 28 | Phosphorylation | SGLALLGTIISAYRA HHHHHHHHHHHHHHH | 28348404 | ||
| 52 | O-linked_Glycosylation | EPDQLTASLQPEPPA CCCCCCCCCCCCCCC | OGP | ||
| 181 | Phosphorylation | FSPTTPMSSHGRVLS CCCCCCCCCHHHHHH | 30387612 | ||
| 182 | Phosphorylation | SPTTPMSSHGRVLSL CCCCCCCCHHHHHHH | 30387612 | ||
| 353 | Ubiquitination | DSMQAARKLPCGHLF HHHHHHHHCCCCCCC | - | ||
| 507 | Phosphorylation | VPFPTQRSDSIRPAL CCCCCCCCCCCCHHC | 30266825 | ||
| 509 | Phosphorylation | FPTQRSDSIRPALNS CCCCCCCCCCHHCCC | 30266825 | ||
| 516 | Phosphorylation | SIRPALNSPVERPSS CCCHHCCCCCCCCCC | 30266825 | ||
| 522 | Phosphorylation | NSPVERPSSDQEEGE CCCCCCCCCCCCCCC | 23401153 | ||
| 523 | Phosphorylation | SPVERPSSDQEEGET CCCCCCCCCCCCCCC | 30266825 | ||
| 530 | Phosphorylation | SDQEEGETSAQTERV CCCCCCCCCCCCEEC | 30266825 | ||
| 531 | Phosphorylation | DQEEGETSAQTERVP CCCCCCCCCCCEECC | 30266825 | ||
| 534 | Phosphorylation | EGETSAQTERVPLDL CCCCCCCCEECCCCC | 30266825 | ||
| 542 | Phosphorylation | ERVPLDLSPRLEETL EECCCCCCHHHHHCC | 30266825 | ||
| 548 | Phosphorylation | LSPRLEETLDFGEVE CCHHHHHCCCCCEEE | 46162861 | ||
| 559 | Phosphorylation | GEVEVEPSEVEDFEA CEEEECHHHHHCCHH | 110760307 | ||
| 573 | Ubiquitination | ARGSRFSKSADERQR HCCCCCCCCHHHHHH | - | ||
| 586 | Ubiquitination | QRMLVQRKDELLQQA HHHHHHCHHHHHHHH | - | ||
| 600 | Ubiquitination | ARKRFLNKSSEDDAA HHHHHHCCCCCCHHH | 21906983 | ||
| 601 | Phosphorylation | RKRFLNKSSEDDAAS HHHHHCCCCCCHHHH | 18669648 | ||
| 602 | Phosphorylation | KRFLNKSSEDDAASE HHHHCCCCCCHHHHH | 28555341 | ||
| 608 | Phosphorylation | SSEDDAASESFLPSE CCCCHHHHHCCCCCC | 28555341 | ||
| 623 | Phosphorylation | GASSDPVTLRRRMLA CCCCCHHHHHHHHHH | 45562887 | ||
| 639 | Ubiquitination | AAERRLQKQQTS--- HHHHHHHHHHCC--- | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 516 | S | Phosphorylation | Kinase | CDK5 | Q00535 | PSP |
| - | K | Ubiquitination | E3 ubiquitin ligase | TRIM25 | Q14258 | PMID:24810856 |
| - | K | Ubiquitination | E3 ubiquitin ligase | SYVN1 | Q86TM6 | PMID:18216283 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AMFR_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 AMFR_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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