| UniProt ID | C1RL_HUMAN | |
|---|---|---|
| UniProt AC | Q9NZP8 | |
| Protein Name | Complement C1r subcomponent-like protein | |
| Gene Name | C1RL | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 487 | |
| Subcellular Localization | Secreted . | |
| Protein Description | Mediates the proteolytic cleavage of HP/haptoglobin in the endoplasmic reticulum.. | |
| Protein Sequence | MPGPRVWGKYLWRSPHSKGCPGAMWWLLLWGVLQACPTRGSVLLAQELPQQLTSPGYPEPYGKGQESSTDIKAPEGFAVRLVFQDFDLEPSQDCAGDSVTISFVGSDPSQFCGQQGSPLGRPPGQREFVSSGRSLRLTFRTQPSSENKTAHLHKGFLALYQTVAVNYSQPISEASRGSEAINAPGDNPAKVQNHCQEPYYQAAAAGALTCATPGTWKDRQDGEEVLQCMPVCGRPVTPIAQNQTTLGSSRAKLGNFPWQAFTSIHGRGGGALLGDRWILTAAHTIYPKDSVSLRKNQSVNVFLGHTAIDEMLKLGNHPVHRVVVHPDYRQNESHNFSGDIALLELQHSIPLGPNVLPVCLPDNETLYRSGLLGYVSGFGMEMGWLTTELKYSRLPVAPREACNAWLQKRQRPEVFSDNMFCVGDETQRHSVCQGDSGSVYVVWDNHAHHWVATGIVSWGIGCGEGYDFYTKVLSYVDWIKGVMNGKN | |
| 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 |
|---|---|---|---|---|---|
| 134 | Phosphorylation | EFVSSGRSLRLTFRT EEECCCCEEEEEEEC | 22.74 | - | |
| 147 | N-linked_Glycosylation | RTQPSSENKTAHLHK ECCCCCCCCEEEECH | 49.26 | 19159218 | |
| 166 | N-linked_Glycosylation | LYQTVAVNYSQPISE HHEEEECCCCCCCCH | 22.47 | 16335952 | |
| 178 | Phosphorylation | ISEASRGSEAINAPG CCHHHCCCCCCCCCC | 23.81 | 29759185 | |
| 209 | O-linked_Glycosylation | AAAAGALTCATPGTW HHHHHCCEECCCCCC | 10.28 | OGP | |
| 237 | Phosphorylation | PVCGRPVTPIAQNQT CCCCCCCCCCCCCCC | 16.20 | - | |
| 242 | N-linked_Glycosylation | PVTPIAQNQTTLGSS CCCCCCCCCCCCCCC | 31.95 | 17623646 | |
| 242 | N-linked_Glycosylation | PVTPIAQNQTTLGSS CCCCCCCCCCCCCCC | 31.95 | 16335952 | |
| 244 | Phosphorylation | TPIAQNQTTLGSSRA CCCCCCCCCCCCCCC | 31.38 | - | |
| 248 | Phosphorylation | QNQTTLGSSRAKLGN CCCCCCCCCCCCCCC | 21.55 | - | |
| 290 | Phosphorylation | HTIYPKDSVSLRKNQ EEECCCCCCCCCCCC | 21.52 | 24719451 | |
| 292 | Phosphorylation | IYPKDSVSLRKNQSV ECCCCCCCCCCCCEE | 26.80 | 29496963 | |
| 296 | N-linked_Glycosylation | DSVSLRKNQSVNVFL CCCCCCCCCEEEEEE | 32.69 | 16335952 | |
| 298 | Phosphorylation | VSLRKNQSVNVFLGH CCCCCCCEEEEEECC | 25.67 | - | |
| 306 | Phosphorylation | VNVFLGHTAIDEMLK EEEEECCHHHHHHHH | 24.41 | - | |
| 363 | N-linked_Glycosylation | LPVCLPDNETLYRSG ECEECCCCCHHHHCC | 42.06 | UniProtKB CARBOHYD | |
| 369 | Phosphorylation | DNETLYRSGLLGYVS CCCHHHHCCHHHHHH | 21.89 | 25404012 | |
| 374 | Phosphorylation | YRSGLLGYVSGFGME HHCCHHHHHHCCCCC | 7.45 | 25404012 | |
| 376 | Phosphorylation | SGLLGYVSGFGMEMG CCHHHHHHCCCCCCC | 21.66 | 25404012 | |
| 391 | Phosphorylation | WLTTELKYSRLPVAP EEECHHCCCCCCCCC | 16.20 | - | |
| 474 | Phosphorylation | DFYTKVLSYVDWIKG HHHHHHHHHHHHHHH | 26.54 | 19835603 | |
| 475 | Phosphorylation | FYTKVLSYVDWIKGV HHHHHHHHHHHHHHH | 9.77 | 19835603 |
| 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 C1RL_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of C1RL_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 C1RL_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of C1RL_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-147; ASN-242 AND ASN-296,AND MASS SPECTROMETRY. | |
| "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-166; ASN-242 AND ASN-296,AND MASS SPECTROMETRY. | |
