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 | ||
* 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. |