| UniProt ID | MBRL_HUMAN | |
|---|---|---|
| UniProt AC | Q4ZIN3 | |
| Protein Name | Membralin | |
| Gene Name | TMEM259 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 620 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
| Protein Description | May have a role in the ERAD pathway required for clearance of misfolded proteins in the endoplasmic reticulum (ER). Promotes survival of motor neurons, probably by protecting against ER stress.. | |
| Protein Sequence | MSEHVEPAAPGPGPNGGGGGPAPARGPRTPNLNPNPLINVRDRLFHALFFKMAVTYSRLFPPAFRRLFEFFVLLKALFVLFVLAYIHIVFSRSPINCLEHVRDKWPREGILRVEVRHNSSRAPVFLQFCDSGGRGSFPGLAVEPGSNLDMEDEEEEELTMEMFGNSSIKFELDIEPKVFKPPSSTEALNDSQEFPFPETPTKVWPQDEYIVEYSLEYGFLRLSQATRQRLSIPVMVVTLDPTRDQCFGDRFSRLLLDEFLGYDDILMSSVKGLAENEENKGFLRNVVSGEHYRFVSMWMARTSYLAAFAIMVIFTLSVSMLLRYSHHQIFVFIVDLLQMLEMNMAIAFPAAPLLTVILALVGMEAIMSEFFNDTTTAFYIILIVWLADQYDAICCHTSTSKRHWLRFFYLYHFAFYAYHYRFNGQYSSLALVTSWLFIQHSMIYFFHHYELPAILQQVRIQEMLLQAPPLGPGTPTALPDDMNNNSGAPATAPDSAGQPPALGPVSPGASGSPGPVAAAPSSLVAAAASVAAAAGGDLGWMAETAAIITDASFLSGLSASLLERRPASPLGPAGGLPHAPQDSVPPSDSAASDTTPLGAAVGGPSPASMAPTEAPSEVGS | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSEHVEPAA ------CCCCCCCCC | 36.09 | 22223895 | |
| 29 | Phosphorylation | APARGPRTPNLNPNP CCCCCCCCCCCCCCC | 21.47 | 29255136 | |
| 189 | N-linked_Glycosylation | PSSTEALNDSQEFPF CCCCCCCCCCCCCCC | 54.67 | 19159218 | |
| 271 | Ubiquitination | DILMSSVKGLAENEE HHHHHHHHHHHHCCC | 50.59 | - | |
| 280 | Ubiquitination | LAENEENKGFLRNVV HHHCCCCCCHHHHHH | 55.08 | 2190698 | |
| 280 (in isoform 1) | Ubiquitination | - | 55.08 | 21906983 | |
| 280 (in isoform 2) | Ubiquitination | - | 55.08 | 21906983 | |
| 319 | Phosphorylation | VIFTLSVSMLLRYSH HHHHHHHHHHHHCCC | 10.59 | 22210691 | |
| 568 | Phosphorylation | LLERRPASPLGPAGG HHHHCCCCCCCCCCC | 24.28 | 26074081 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of MBRL_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MBRL_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 MBRL_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of MBRL_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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| N-linked Glycosylation | |
| Reference | PubMed |
| "Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-189, AND MASSSPECTROMETRY. | |
