UniProt ID | TMED7_HUMAN | |
---|---|---|
UniProt AC | Q9Y3B3 | |
Protein Name | Transmembrane emp24 domain-containing protein 7 | |
Gene Name | TMED7 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 224 | |
Subcellular Localization |
Endoplasmic reticulum membrane Single-pass type I membrane protein. Golgi apparatus, cis-Golgi network membrane Single-pass type I membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane Single-pass type I membrane protein. Cyto |
|
Protein Description | Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Appears to play a role in the biosynthesis of secreted cargo including processing and post-translational modifications.. | |
Protein Sequence | MPRPGSAQRWAAVAGRWGCRLLALLLLVPGPGGASEITFELPDNAKQCFYEDIAQGTKCTLEFQVITGGHYDVDCRLEDPDGKVLYKEMKKQYDSFTFTASKNGTYKFCFSNEFSTFTHKTVYFDFQVGEDPPLFPSENRVSALTQMESACVSIHEALKSVIDYQTHFRLREAQGRSRAEDLNTRVAYWSVGEALILLVVSIGQVFLLKSFFSDKRTTTTRVGS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
6 | Phosphorylation | --MPRPGSAQRWAAV --CCCCCCHHHHHHH | 24.74 | 30619164 | |
46 | Ubiquitination | FELPDNAKQCFYEDI EECCCCHHEEEHHHH | 54.58 | - | |
50 | Phosphorylation | DNAKQCFYEDIAQGT CCHHEEEHHHHHCCC | 21.96 | 28152594 | |
57 | Phosphorylation | YEDIAQGTKCTLEFQ HHHHHCCCEEEEEEE | 15.74 | 28152594 | |
83 | Ubiquitination | RLEDPDGKVLYKEMK EEECCCCCEEEHHHH | 36.13 | 21906983 | |
83 | Acetylation | RLEDPDGKVLYKEMK EEECCCCCEEEHHHH | 36.13 | 27452117 | |
87 | Ubiquitination | PDGKVLYKEMKKQYD CCCCEEEHHHHHHHC | 47.36 | 21906983 | |
91 | Ubiquitination | VLYKEMKKQYDSFTF EEEHHHHHHHCCEEE | 53.43 | 21906983 | |
93 | Phosphorylation | YKEMKKQYDSFTFTA EHHHHHHHCCEEEEE | 23.57 | 28152594 | |
95 | Phosphorylation | EMKKQYDSFTFTASK HHHHHHCCEEEEECC | 22.66 | 28152594 | |
97 | Phosphorylation | KKQYDSFTFTASKNG HHHHCCEEEEECCCC | 24.83 | 28152594 | |
103 | N-linked_Glycosylation | FTFTASKNGTYKFCF EEEEECCCCEEEEEE | 45.61 | UniProtKB CARBOHYD | |
105 | Phosphorylation | FTASKNGTYKFCFSN EEECCCCEEEEEECC | 32.69 | - | |
142 | Phosphorylation | FPSENRVSALTQMES CCCCCHHHHHHHHHH | 17.83 | 20068231 | |
145 | O-linked_Glycosylation | ENRVSALTQMESACV CCHHHHHHHHHHHHH | 26.11 | OGP | |
153 | Phosphorylation | QMESACVSIHEALKS HHHHHHHHHHHHHHH | 20.36 | 20068231 | |
164 | Phosphorylation | ALKSVIDYQTHFRLR HHHHHHHHHHHHHHH | 12.27 | 28152594 | |
166 | Phosphorylation | KSVIDYQTHFRLREA HHHHHHHHHHHHHHH | 19.42 | 28152594 | |
213 | Phosphorylation | FLLKSFFSDKRTTTT HHHHHHHCCCCCCCC | 39.96 | 28355574 | |
215 | Ubiquitination | LKSFFSDKRTTTTRV HHHHHCCCCCCCCCC | 50.90 | 21906983 | |
215 | Acetylation | LKSFFSDKRTTTTRV HHHHHCCCCCCCCCC | 50.90 | 27452117 |
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 TMED7_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TMED7_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 TMED7_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TMPS3_HUMAN | TMPRSS3 | physical | 21988832 |
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. |
loading...