| UniProt ID | HGD_HUMAN | |
|---|---|---|
| UniProt AC | Q93099 | |
| Protein Name | Homogentisate 1,2-dioxygenase | |
| Gene Name | HGD | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 445 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MAELKYISGFGNECSSEDPRCPGSLPEGQNNPQVCPYNLYAEQLSGSAFTCPRSTNKRSWLYRILPSVSHKPFESIDEGQVTHNWDEVDPDPNQLRWKPFEIPKASQKKVDFVSGLHTLCGAGDIKSNNGLAIHIFLCNTSMENRCFYNSDGDFLIVPQKGNLLIYTEFGKMLVQPNEICVIQRGMRFSIDVFEETRGYILEVYGVHFELPDLGPIGANGLANPRDFLIPIAWYEDRQVPGGYTVINKYQGKLFAAKQDVSPFNVVAWHGNYTPYKYNLKNFMVINSVAFDHADPSIFTVLTAKSVRPGVAIADFVIFPPRWGVADKTFRPPYYHRNCMSEFMGLIRGHYEAKQGGFLPGGGSLHSTMTPHGPDADCFEKASKVKLAPERIADGTMAFMFESSLSLAVTKWGLKASRCLDENYHKCWEPLKSHFTPNSRNPAEPN | |
| 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 |
|---|---|---|---|---|---|
| 40 | Phosphorylation | QVCPYNLYAEQLSGS CCCCCHHEEHHHCCC | 12.40 | - | |
| 67 | Phosphorylation | WLYRILPSVSHKPFE HHHHHCCCCCCCCCC | 32.57 | 24275569 | |
| 98 | Acetylation | DPNQLRWKPFEIPKA CCCCCCCCCCCCCCH | 33.14 | 19608861 | |
| 166 | Phosphorylation | QKGNLLIYTEFGKML CCCCEEEEECCCCEE | 10.53 | - | |
| 167 | Phosphorylation | KGNLLIYTEFGKMLV CCCEEEEECCCCEEC | 20.18 | - | |
| 244 | Phosphorylation | RQVPGGYTVINKYQG CCCCCCEEEEEEECC | 20.41 | - | |
| 249 | Phosphorylation | GYTVINKYQGKLFAA CEEEEEEECCEEEEE | 20.29 | 24719451 | |
| 296 | Phosphorylation | AFDHADPSIFTVLTA ECCCCCCCCEEEEEE | 30.77 | 19664995 | |
| 302 | Phosphorylation | PSIFTVLTAKSVRPG CCCEEEEEECCCCCC | 27.92 | 19664995 | |
| 333 | Phosphorylation | DKTFRPPYYHRNCMS CCCCCCCCHHHHHHH | 18.00 | - | |
| 334 | Phosphorylation | KTFRPPYYHRNCMSE CCCCCCCHHHHHHHH | 10.48 | - | |
| 414 | Succinylation | AVTKWGLKASRCLDE HHHHHCHHHHHHHCC | 40.14 | - | |
| 414 | Succinylation | AVTKWGLKASRCLDE HHHHHCHHHHHHHCC | 40.14 | - | |
| 416 | O-linked_Glycosylation | TKWGLKASRCLDENY HHHCHHHHHHHCCCH | 23.18 | 30379171 | |
| 423 | Phosphorylation | SRCLDENYHKCWEPL HHHHCCCHHHHCHHH | 10.70 | - |
| 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 HGD_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HGD_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 HGD_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| PCDGK_HUMAN | PCDHGC3 | physical | 21988832 | |
| HGD_HUMAN | HGD | physical | 25416956 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 203500 | Alkaptonuria (AKU) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-98, AND MASS SPECTROMETRY. | |