UniProt ID | PLOD1_MOUSE | |
---|---|---|
UniProt AC | Q9R0E2 | |
Protein Name | Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 | |
Gene Name | Plod1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 728 | |
Subcellular Localization |
Rough endoplasmic reticulum membrane Peripheral membrane protein Lumenal side. |
|
Protein Description | Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils. [PubMed: 27119146 Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (By similarity These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links] | |
Protein Sequence | MRSLLLLAPLAWLLLVQAKDDAKLEDNLLVLTVATKETEGFRRFKRSAQFFNYKIQSLGLGEDWSVDGGPAAAGGGQKVRLLKKALEKHADKEDLVILFVDSYDVVFASGPRELLKKFQQAKSQVVFSAEEHIYPDRRLEAKYPTVPDGKRFLGSGGFIGYAPSLSKLVAEWEGQDSDSDQLFYTKIFLNPEKREQINISLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVVVHGNGPTKLQLNYLGNYIPRFWTFETGCTVCDEGLRSLKGIGDEALPTVLVGVFIEQPTPFLSLFFLRLLRLRYPQKQMRLFIHNQERHHKLQVEQFLAEHGSEYQSVKLVGPEVRMANADARNMGADLCRQDQTCTYYFSVDADVALTEPNSLRLLIEQNKNVIAPLMTRHGRLWSNFWGGLSADGYYARSEDYVDIVQGRRVGVWNVPYISNIYLIKGSALRAELQNVDLFHYSKLDSDMSFCANVRQQEVFMFLTNRHTFGHLLSLDNYQTTHLHNDLWEVFSNPEDWKEKYIHENYTKALAGKLVETPCPDVYWFPIFTEAACDELVEEMEHYGQWSLGDNKDNRIQGGYENVPTIDIHMNQITFEREWHKFLVEYIAPMTEKLYPGYYTRAQFDLAFVVRYKPDEQPSLMPHHDASTFTVNIALNRVGEDYEGGGCRFLRYNCSVRAPRKGWALLHPGRLTHYHEGLPTTKGTRYIAVSFVDP | |
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 |
---|---|---|---|---|---|
177 | Phosphorylation | AEWEGQDSDSDQLFY HHHCCCCCCHHCEEE | 31.00 | 26525534 | |
179 | Phosphorylation | WEGQDSDSDQLFYTK HCCCCCCHHCEEEEE | 31.07 | 26525534 | |
198 | N-linked_Glycosylation | PEKREQINISLDHRC HHHHHHCEECHHHHH | 19.93 | 19349973 | |
402 | Acetylation | RLLIEQNKNVIAPLM HHHHHCCCCCHHHHH | 52.89 | 22826441 | |
539 | N-linked_Glycosylation | KEKYIHENYTKALAG HHHHHCHHHHHHHCC | 35.29 | - | |
687 | N-linked_Glycosylation | GCRFLRYNCSVRAPR CEEEEEEEEEECCCC | 12.73 | - |
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 PLOD1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PLOD1_MOUSE !! |
* 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 PLOD1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of PLOD1_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198, AND MASSSPECTROMETRY. |