PLOD1_MOUSE - dbPTM
PLOD1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
177PhosphorylationAEWEGQDSDSDQLFY
HHHCCCCCCHHCEEE
31.0026525534
179PhosphorylationWEGQDSDSDQLFYTK
HCCCCCCHHCEEEEE
31.0726525534
198N-linked_GlycosylationPEKREQINISLDHRC
HHHHHHCEECHHHHH
19.9319349973
402AcetylationRLLIEQNKNVIAPLM
HHHHHCCCCCHHHHH
52.8922826441
539N-linked_GlycosylationKEKYIHENYTKALAG
HHHHHCHHHHHHHCC
35.29-
687N-linked_GlycosylationGCRFLRYNCSVRAPR
CEEEEEEEEEECCCC
12.73-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLOD1_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PLOD1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLOD1_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.

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