| UniProt ID | CO9A1_HUMAN | |
|---|---|---|
| UniProt AC | P20849 | |
| Protein Name | Collagen alpha-1(IX) chain | |
| Gene Name | COL9A1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 921 | |
| Subcellular Localization | Secreted, extracellular space, extracellular matrix. | |
| Protein Description | Structural component of hyaline cartilage and vitreous of the eye.. | |
| Protein Sequence | MKTCWKIPVFFFVCSFLEPWASAAVKRRPRFPVNSNSNGGNELCPKIRIGQDDLPGFDLISQFQVDKAASRRAIQRVVGSATLQVAYKLGNNVDFRIPTRNLYPSGLPEEYSFLTTFRMTGSTLKKNWNIWQIQDSSGKEQVGIKINGQTQSVVFSYKGLDGSLQTAAFSNLSSLFDSQWHKIMIGVERSSATLFVDCNRIESLPIKPRGPIDIDGFAVLGKLADNPQVSVPFELQWMLIHCDPLRPRRETCHELPARITPSQTTDERGPPGEQGPPGPPGPPGVPGIDGIDGDRGPKGPPGPPGPAGEPGKPGAPGKPGTPGADGLTGPDGSPGSIGSKGQKGEPGVPGSRGFPGRGIPGPPGPPGTAGLPGELGRVGPVGDPGRRGPPGPPGPPGPRGTIGFHDGDPLCPNACPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGTKGEPGKPGPPGDAGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKLGSLGSPGLPGLPGPPGLPGMKGDRGVVGEPGPKGEQGASGEEGEAGERGELGDIGLPGPKGSAGNPGEPGLRGPEGSRGLPGVEGPRGPPGPRGVQGEQGATGLPGVQGPPGRAPTDQHIKQVCMRVIQEHFAEMAASLKRPDSGATGLPGRPGPPGPPGPPGENGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPPGRGPNGLPGAIGLPGDPGPASYGRNGRDGERGPPGVAGIPGVPGPPGPPGLPGFCEPASCTMQAGQRAFNKGPDP | |
| 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 |
|---|---|---|---|---|---|
| 80 | Phosphorylation | AIQRVVGSATLQVAY HHHHHHCCCHHHHHH | 13.38 | 30622161 | |
| 82 | Phosphorylation | QRVVGSATLQVAYKL HHHHCCCHHHHHHHC | 21.30 | 30622161 | |
| 87 | Phosphorylation | SATLQVAYKLGNNVD CCHHHHHHHCCCCCC | 14.11 | 30622161 | |
| 171 | N-linked_Glycosylation | LQTAAFSNLSSLFDS HHHHHHHCHHHHHHH | 37.17 | UniProtKB CARBOHYD | |
| 203 | Phosphorylation | VDCNRIESLPIKPRG EECCCEECCCCCCCC | 36.75 | 24719451 | |
| 260 | Phosphorylation | HELPARITPSQTTDE HCCCCCCCCCCCCCC | 16.01 | 29083192 | |
| 262 | Phosphorylation | LPARITPSQTTDERG CCCCCCCCCCCCCCC | 31.35 | 29083192 | |
| 264 | Phosphorylation | ARITPSQTTDERGPP CCCCCCCCCCCCCCC | 40.32 | 29083192 | |
| 265 | Phosphorylation | RITPSQTTDERGPPG CCCCCCCCCCCCCCC | 28.38 | 29083192 | |
| 719 | Phosphorylation | GLRGPEGSRGLPGVE CCCCCCCCCCCCCCC | 22.85 | 24275569 | |
| 780 | Phosphorylation | HFAEMAASLKRPDSG HHHHHHHHCCCCCCC | 25.53 | 24719451 |
| 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 CO9A1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CO9A1_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 CO9A1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CO2A1_HUMAN | COL2A1 | physical | 11724554 | |
| PYRG2_HUMAN | CTPS2 | physical | 26186194 | |
| CO2A1_HUMAN | COL2A1 | physical | 26186194 | |
| CO6A2_HUMAN | COL6A2 | physical | 26186194 | |
| CO6A1_HUMAN | COL6A1 | physical | 26186194 | |
| CO4A2_HUMAN | COL4A2 | physical | 26186194 | |
| PP12C_HUMAN | PPP1R12C | physical | 26186194 | |
| VHL_HUMAN | VHL | physical | 26186194 | |
| PP12C_HUMAN | PPP1R12C | physical | 28514442 | |
| VHL_HUMAN | VHL | physical | 28514442 | |
| CO2A1_HUMAN | COL2A1 | physical | 28514442 | |
| CO6A1_HUMAN | COL6A1 | physical | 28514442 | |
| CO6A2_HUMAN | COL6A2 | physical | 28514442 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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