| UniProt ID | CATF_HUMAN | |
|---|---|---|
| UniProt AC | Q9UBX1 | |
| Protein Name | Cathepsin F | |
| Gene Name | CTSF | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 484 | |
| Subcellular Localization | Lysosome. | |
| Protein Description | Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.. | |
| Protein Sequence | MAPWLQLLSLLGLLPGAVAAPAQPRAASFQAWGPPSPELLAPTRFALEMFNRGRAAGTRAVLGLVRGRVRRAGQGSLYSLEATLEEPPCNDPMVCRLPVSKKTLLCSFQVLDELGRHVLLRKDCGPVDTKVPGAGEPKSAFTQGSAMISSLSQNHPDNRNETFSSVISLLNEDPLSQDLPVKMASIFKNFVITYNRTYESKEEARWRLSVFVNNMVRAQKIQALDRGTAQYGVTKFSDLTEEEFRTIYLNTLLRKEPGNKMKQAKSVGDLAPPEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKMDKACMGGLPSNAYSAIKNLGGLETEDDYSYQGHMQSCNFSAEKAKVYINDSVELSQNEQKLAAWLAKRGPISVAINAFGMQFYRHGISRPLRPLCSPWLIDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYLHRGSGACGVNTMASSAVVD | |
| 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 |
|---|---|---|---|---|---|
| 107 | Phosphorylation | SKKTLLCSFQVLDEL CCCHHHHHHHHHHHH | 20.77 | 21964256 | |
| 160 | N-linked_Glycosylation | QNHPDNRNETFSSVI HCCCCCCCHHHHHHH | 59.94 | UniProtKB CARBOHYD | |
| 164 | Phosphorylation | DNRNETFSSVISLLN CCCCHHHHHHHHHHC | 30.99 | 30576142 | |
| 185 | Phosphorylation | DLPVKMASIFKNFVI CCCHHHHHHHHCEEE | 25.67 | 24719451 | |
| 193 | Phosphorylation | IFKNFVITYNRTYES HHHCEEEEECCCCCC | 14.94 | 23663014 | |
| 194 | Phosphorylation | FKNFVITYNRTYESK HHCEEEEECCCCCCH | 7.48 | 23663014 | |
| 195 | N-linked_Glycosylation | KNFVITYNRTYESKE HCEEEEECCCCCCHH | 22.59 | UniProtKB CARBOHYD | |
| 235 | Ubiquitination | TAQYGVTKFSDLTEE CCCCCCCCHHHCCHH | 40.23 | 29967540 | |
| 251 | Phosphorylation | FRTIYLNTLLRKEPG HHHHHHHHHHHCCCC | 25.28 | 24260401 | |
| 266 | Phosphorylation | NKMKQAKSVGDLAPP CHHHCCCCCCCCCCC | 34.06 | 30622161 | |
| 353 | Phosphorylation | KNLGGLETEDDYSYQ HHCCCCCCCCCCCCC | 50.16 | 22817900 | |
| 365 | Phosphorylation | SYQGHMQSCNFSAEK CCCCCCCCCCCCHHH | 11.94 | 22817900 | |
| 367 | N-linked_Glycosylation | QGHMQSCNFSAEKAK CCCCCCCCCCHHHCE | 38.87 | 19159218 | |
| 378 | N-linked_Glycosylation | EKAKVYINDSVELSQ HHCEEEECCCEECCH | 20.16 | 16399764 | |
| 378 | N-linked_Glycosylation | EKAKVYINDSVELSQ HHCEEEECCCEECCH | 20.16 | 16399764 | |
| 440 | N-linked_Glycosylation | VLLVGYGNRSDVPFW EEEECCCCCCCCCEE | 31.62 | 16399764 | |
| 440 | N-linked_Glycosylation | VLLVGYGNRSDVPFW EEEECCCCCCCCCEE | 31.62 | 16399764 | |
| 469 | Phosphorylation | YYYLHRGSGACGVNT EEEEECCCCCCCCCC | 24.15 | - | |
| 476 | Phosphorylation | SGACGVNTMASSAVV CCCCCCCCCCCCCCC | 16.23 | 19413330 |
| 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 CATF_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CATF_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 CATF_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CATF_HUMAN !! | ||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 615362 | Ceroid lipofuscinosis, neuronal, 13 (CLN13) | |||||
| 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-367; ASN-378 AND ASN-440,AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-353 AND SER-365, ANDMASS SPECTROMETRY. | |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-476, AND MASSSPECTROMETRY. | |
