| UniProt ID | PGGHG_HUMAN | |
|---|---|---|
| UniProt AC | Q32M88 | |
| Protein Name | Protein-glucosylgalactosylhydroxylysine glucosidase {ECO:0000303|PubMed:26682924} | |
| Gene Name | PGGHG {ECO:0000303|PubMed:26682924, ECO:0000312|HGNC:HGNC:26210} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 737 | |
| Subcellular Localization | ||
| Protein Description | Catalyzes the hydrolysis of glucose from the disaccharide unit linked to hydroxylysine residues of collagen and collagen-like proteins.. | |
| Protein Sequence | MEDAGEDPTTFAAHSLPSDPRLLATVTNAYLGTRVFHDTLHVSGVYNGAGGDTHRAMLPSPLNVRLEAPAGMGEQLTETFALDTNTGSFLHTLEGPRFRASQCIYAHRTLPHVLAFRVSIARLAPGSGPITLLLRSAFSPESPDLDLHQGPDFQGARYLYGHTLTPEQPGGPQQEVHMLWTPAPPDLTLGEGEEARTWDFLTAVGGSQAEAQACLTEALQLQARGALYTAHAQAWAQLWVECGLDVVGPLQLRQALRGSLYYLLSALPQPKAPGYICHGLSPGGLSNGSREECYWGHVFWDQDLWMFPSILMFHPEAARAILEYRIRTLDGALENAQNLGYQGAKFAWESADSGLEVCPEDIYGVQEVHVNGAVVLAFELYYHTTQDLQLFREAGGWDVVRAVAEFWCSRVEWSPREEKYHLRGVMSPDEYHSGVNNSVYTNVLVQNSLRFAAALAQDLGLPIPSQWLAVADKIKVPFDVEQNFHPEFDGYEPGEVVKQADVVLLGYPVPFSLSPDVRRKNLEIYEAVTSPQGPAMTWSMFAVGWMELKDAVRARGLLDRSFANMAEPFKVWTENADGSGAVNFLTGMGGFLQAVVFGCTGFRVTRAGVTFDPVCLSGISRVSVSGIFYQGNKLNFSFSEDSVTVEVTARAGPWAPHLEAELWPSQSRLSLLPGHKVSFPRSAGRIQMSPPKLPGSSSSEFPGRTFSDVRDPLQSPLWVTLGSSSPTESLTVDPASE | |
| 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 |
|---|---|---|---|---|---|
| 25 | Phosphorylation | SDPRLLATVTNAYLG CCHHHHHHHHHHHCC | 29083192 | ||
| 27 | Phosphorylation | PRLLATVTNAYLGTR HHHHHHHHHHHCCCC | 29083192 | ||
| 30 | Phosphorylation | LATVTNAYLGTRVFH HHHHHHHHCCCCEEC | 29083192 | ||
| 33 | Phosphorylation | VTNAYLGTRVFHDTL HHHHHCCCCEECCEE | 29083192 | ||
| 414 | Phosphorylation | WCSRVEWSPREEKYH HHHCCCCCCCHHHHC | 24719451 | ||
| 448 | Phosphorylation | TNVLVQNSLRFAAAL HHHHHHHHHHHHHHH | 24719451 | ||
| 475 | Ubiquitination | LAVADKIKVPFDVEQ HHHHCCCCCCCCCCC | - | ||
| 512 | Phosphorylation | LGYPVPFSLSPDVRR ECCCCCCCCCHHHHH | 22199227 | ||
| 514 | Phosphorylation | YPVPFSLSPDVRRKN CCCCCCCCHHHHHHC | 22199227 | ||
| 689 | Phosphorylation | SAGRIQMSPPKLPGS CCCCEEECCCCCCCC | 27080861 | ||
| 696 | Phosphorylation | SPPKLPGSSSSEFPG CCCCCCCCCCCCCCC | 27080861 | ||
| 697 | Phosphorylation | PPKLPGSSSSEFPGR CCCCCCCCCCCCCCC | 23312004 | ||
| 698 | Phosphorylation | PKLPGSSSSEFPGRT CCCCCCCCCCCCCCC | 27080861 | ||
| 699 | Phosphorylation | KLPGSSSSEFPGRTF CCCCCCCCCCCCCCH | 29802988 | ||
| 723 | Phosphorylation | PLWVTLGSSSPTESL CEEEEECCCCCCCCC | 28348404 | ||
| 724 | Phosphorylation | LWVTLGSSSPTESLT EEEEECCCCCCCCCE | 27690223 | ||
| 725 | Phosphorylation | WVTLGSSSPTESLTV EEEECCCCCCCCCEE | 27690223 | ||
| 727 | Phosphorylation | TLGSSSPTESLTVDP EECCCCCCCCCEECC | 27690223 | ||
| 729 | Phosphorylation | GSSSPTESLTVDPAS CCCCCCCCCEECCCC | 24719451 | ||
| 731 | Phosphorylation | SSPTESLTVDPASE- CCCCCCCEECCCCC- | 28348404 | ||
| 736 | Phosphorylation | SLTVDPASE------ CCEECCCCC------ | 28348404 |
| 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 PGGHG_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PGGHG_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 PGGHG_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of PGGHG_HUMAN !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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