| UniProt ID | TXD15_HUMAN | |
|---|---|---|
| UniProt AC | Q96J42 | |
| Protein Name | Thioredoxin domain-containing protein 15 | |
| Gene Name | TXNDC15 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 360 | |
| Subcellular Localization |
Membrane Single-pass type I membrane protein . |
|
| Protein Description | ||
| Protein Sequence | MVPAAGRRPPRVMRLLGWWQVLLWVLGLPVRGVEVAEESGRLWSEEQPAHPLQVGAVYLGEEELLHDPMGQDRAAEEANAVLGLDTQGDHMVMLSVIPGEAEDKVSSEPSGVTCGAGGAEDSRCNVRESLFSLDGAGAHFPDREEEYYTEPEVAESDAAPTEDSNNTESLKSPKVNCEERNITGLENFTLKILNMSQDLMDFLNPNGSDCTLVLFYTPWCRFSASLAPHFNSLPRAFPALHFLALDASQHSSLSTRFGTVAVPNILLFQGAKPMARFNHTDRTLETLKIFIFNQTGIEAKKNVVVTQADQIGPLPSTLIKSVDWLLVFSLFFLISFIMYATIRTESIRWLIPGQEQEHVE | |
| 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 |
|---|---|---|---|---|---|
| 39 | Phosphorylation | GVEVAEESGRLWSEE CCHHHHHHCCCCCCC | 22.25 | 29759185 | |
| 44 | Phosphorylation | EESGRLWSEEQPAHP HHHCCCCCCCCCCCC | 35.53 | 29759185 | |
| 95 | O-linked_Glycosylation | GDHMVMLSVIPGEAE CCEEEEEEECCCCCC | 10.41 | OGP | |
| 172 | Phosphorylation | NNTESLKSPKVNCEE CCCCCCCCCCCCHHH | 34.93 | 24719451 | |
| 183 | Phosphorylation | NCEERNITGLENFTL CHHHCCCCCHHHHHE | 38.98 | 30242111 | |
| 187 | N-linked_Glycosylation | RNITGLENFTLKILN CCCCCHHHHHEEEEE | 40.00 | UniProtKB CARBOHYD | |
| 194 | N-linked_Glycosylation | NFTLKILNMSQDLMD HHHEEEEECCHHHHH | 31.37 | UniProtKB CARBOHYD | |
| 206 | N-linked_Glycosylation | LMDFLNPNGSDCTLV HHHHHCCCCCCCEEE | 62.62 | UniProtKB CARBOHYD | |
| 223 | Phosphorylation | YTPWCRFSASLAPHF ECCCHHHHHHHHHHH | 9.52 | 26471730 | |
| 225 | Phosphorylation | PWCRFSASLAPHFNS CCHHHHHHHHHHHHC | 24.70 | 26471730 | |
| 272 | Ubiquitination | ILLFQGAKPMARFNH EEEEECCCCCCCCCC | 41.99 | - | |
| 293 | N-linked_Glycosylation | TLKIFIFNQTGIEAK HEEEEEECCCCCCCC | 33.42 | 12754519 | |
| 293 | N-linked_Glycosylation | TLKIFIFNQTGIEAK HEEEEEECCCCCCCC | 33.42 | 12754519 |
| 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 TXD15_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TXD15_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 TXD15_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-293, AND MASSSPECTROMETRY. | |
