| UniProt ID | CLC4K_HUMAN | |
|---|---|---|
| UniProt AC | Q9UJ71 | |
| Protein Name | C-type lectin domain family 4 member K | |
| Gene Name | CD207 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 328 | |
| Subcellular Localization |
Membrane Single-pass type II membrane protein . Found in Birbeck granules (BGs), which are organelles consisting of superimposed and zippered membranes. |
|
| Protein Description | Calcium-dependent lectin displaying mannose-binding specificity. Induces the formation of Birbeck granules (BGs); is a potent regulator of membrane superimposition and zippering. Binds to sulfated as well as mannosylated glycans, keratan sulfate (KS) and beta-glucans. Facilitates uptake of antigens and is involved in the routing and/or processing of antigen for presentation to T cells. Major receptor on primary Langerhans cells for Candida species, Saccharomyces species, and Malassezia furfur. Protects against human immunodeficiency virus-1 (HIV-1) infection. Binds to high-mannose structures present on the envelope glycoprotein which is followed by subsequent targeting of the virus to the Birbeck granules leading to its rapid degradation.. | |
| Protein Sequence | MTVEKEAPDAHFTVDKQNISLWPREPPPKSGPSLVPGKTPTVRAALICLTLVLVASVLLQAVLYPRFMGTISDVKTNVQLLKGRVDNISTLDSEIKKNSDGMEAAGVQIQMVNESLGYVRSQFLKLKTSVEKANAQIQILTRSWEEVSTLNAQIPELKSDLEKASALNTKIRALQGSLENMSKLLKRQNDILQVVSQGWKYFKGNFYYFSLIPKTWYSAEQFCVSRNSHLTSVTSESEQEFLYKTAGGLIYWIGLTKAGMEGDWSWVDDTPFNKVQSVRFWIPGEPNNAGNNEHCGNIKAPSLQAWNDAPCDKTFLFICKRPYVPSEP | |
| 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 |
|---|---|---|---|---|---|
| 87 | N-linked_Glycosylation | LLKGRVDNISTLDSE HHCCCCCCHHHHCHH | 27.53 | UniProtKB CARBOHYD | |
| 113 | N-linked_Glycosylation | GVQIQMVNESLGYVR HHEEEEHHHHHHHHH | 28.00 | UniProtKB CARBOHYD | |
| 180 | N-linked_Glycosylation | ALQGSLENMSKLLKR HHHHHHHHHHHHHHH | 45.37 | UniProtKB CARBOHYD | |
| 196 | Phosphorylation | NDILQVVSQGWKYFK CHHHHHHHHCHHEEC | 24.90 | - | |
| 217 | Phosphorylation | SLIPKTWYSAEQFCV EECCCCCEEHHHHHH | 11.84 | 21214269 | |
| 231 | Phosphorylation | VSRNSHLTSVTSESE HHCCCCCEECCCHHH | 18.74 | 19690332 | |
| 232 | Phosphorylation | SRNSHLTSVTSESEQ HCCCCCEECCCHHHH | 29.74 | 19690332 | |
| 237 | Phosphorylation | LTSVTSESEQEFLYK CEECCCHHHHHHHHH | 44.33 | 19690332 | |
| 243 | Phosphorylation | ESEQEFLYKTAGGLI HHHHHHHHHHHHHEE | 16.18 | 19690332 |
| 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 CLC4K_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CLC4K_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 CLC4K_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CLC4K_HUMAN !! | ||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 613393 | Birbeck granule deficiency (BIRGD) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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