| UniProt ID | CYTF_HUMAN | |
|---|---|---|
| UniProt AC | O76096 | |
| Protein Name | Cystatin-F | |
| Gene Name | CST7 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 145 | |
| Subcellular Localization | Secreted . Cytoplasm . | |
| Protein Description | Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system.. | |
| Protein Sequence | MRAAGTLLAFCCLVLSTTGGPSPDTCSQDLNSRVKPGFPKTIKTNDPGVLQAARYSVEKFNNCTNDMFLFKESRITRALVQIVKGLKYMLEVEIGRTTCKKNQHLRLDDCDFQTNHTLKQTLSCYSEVWVVPWLQHFEVPVLRCH | |
| 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 |
|---|---|---|---|---|---|
| 44 | Phosphorylation | GFPKTIKTNDPGVLQ CCCCCCCCCCHHHHH | 40.79 | - | |
| 62 | N-linked_Glycosylation | YSVEKFNNCTNDMFL HCHHHHCCCCCCCCC | 36.80 | UniProtKB CARBOHYD | |
| 62 | N-linked_Glycosylation | YSVEKFNNCTNDMFL HCHHHHCCCCCCCCC | 36.80 | 16601115 | |
| 76 | Phosphorylation | LFKESRITRALVQIV CCCHHHHHHHHHHHH | 14.58 | - | |
| 88 | Phosphorylation | QIVKGLKYMLEVEIG HHHHHHHHHEEEEEC | 16.39 | - | |
| 97 | Phosphorylation | LEVEIGRTTCKKNQH EEEEECCCCCCCCCC | 31.19 | - | |
| 98 | Phosphorylation | EVEIGRTTCKKNQHL EEEECCCCCCCCCCC | 22.44 | - | |
| 115 | N-linked_Glycosylation | DDCDFQTNHTLKQTL CCCCCCCCCHHHHHH | 18.50 | UniProtKB CARBOHYD | |
| 115 | N-linked_Glycosylation | DDCDFQTNHTLKQTL CCCCCCCCCHHHHHH | 18.50 | 16601115 | |
| 117 | O-linked_Glycosylation | CDFQTNHTLKQTLSC CCCCCCCHHHHHHHC | 37.41 | 29351928 |
| 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 CYTF_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CYTF_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 CYTF_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| POTEE_HUMAN | POTEE | physical | 28514442 | |
| TBA3C_HUMAN | TUBA3C | physical | 28514442 | |
| ITIH3_HUMAN | ITIH3 | physical | 28514442 | |
| GALC_HUMAN | GALC | physical | 28514442 | |
| CATL1_HUMAN | CTSL | physical | 28514442 | |
| AT2A3_HUMAN | ATP2A3 | physical | 28514442 |
| 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 |
| "Structural basis of reduction-dependent activation of human cystatinF."; Schuettelkopf A.W., Hamilton G., Watts C., van Aalten D.M.F.; J. Biol. Chem. 281:16570-16575(2006). Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 20-145, SUBUNIT,GLYCOSYLATION AT ASN-62 AND ASN-115, AND DISULFIDE BONDS. | |
