PLOD3_HUMAN - dbPTM
PLOD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLOD3_HUMAN
UniProt AC O60568
Protein Name Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
Gene Name PLOD3
Organism Homo sapiens (Human).
Sequence Length 738
Subcellular Localization Rough endoplasmic reticulum membrane
Peripheral membrane protein
Lumenal side.
Protein Description Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links..
Protein Sequence MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFLAVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLVGPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSRHGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRDVFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDWKEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRLAGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDEQPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHEGLPTTWGTRYIMVSFVDP
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
23PhosphorylationLLLPPAASASDRPRG
HHCCCCCCCCCCCCC		30.34-
25PhosphorylationLPPAASASDRPRGRD
CCCCCCCCCCCCCCC		31.49-
52PhosphorylationATAETEGYLRFLRSA
EECCCHHHHHHHHHH		6.62-
63N-linked_GlycosylationLRSAEFFNYTVRTLG
HHHHHHCCEEEEECC		36.5730089812
63N-linked_GlycosylationLRSAEFFNYTVRTLG
HHHHHHCCEEEEECC		36.5730089812
76MethylationLGLGEEWRGGDVART
CCCCCCCCCCCCCHH		42.36115487915
113PhosphorylationMIIMFVDSYDVILAG
CEEEEECCCCEEECC		20.2422210691
127AcetylationGSPTELLKKFVQSGS
CCHHHHHHHHHHCCC		57.7111792697
128AcetylationSPTELLKKFVQSGSR
CHHHHHHHHHHCCCC		51.2211792707
128UbiquitinationSPTELLKKFVQSGSR
CHHHHHHHHHHCCCC		51.22-
132PhosphorylationLLKKFVQSGSRLLFS
HHHHHHHCCCCEEEE		33.1728509920
134PhosphorylationKKFVQSGSRLLFSAE
HHHHHCCCCEEEEHH		25.6328509920
174PhosphorylationGGFIGFATTIHQIVR
CCCCEEEHHHHHHHH		24.83-
175PhosphorylationGFIGFATTIHQIVRQ
CCCEEEHHHHHHHHH		17.03-
186UbiquitinationIVRQWKYKDDDDDQL
HHHHHCCCCCCCCCE		51.45-
207UbiquitinationLDPGLREKLSLNLDH
CCCCHHHHHCCCCCH		36.62-
209PhosphorylationPGLREKLSLNLDHKS
CCHHHHHCCCCCHHH		26.6928122231
215UbiquitinationLSLNLDHKSRIFQNL
HCCCCCHHHHHHHHH		40.89-
232UbiquitinationALDEVVLKFDRNRVR
CCCHHHHHCCCCCEE		33.34-
288PhosphorylationFCNQDRRTLPGGQPP
CCCCCCCCCCCCCCC		37.8923312004
367PhosphorylationVGPEEALSPGEARDM
CCHHHHCCHHHHHHH		37.60-
411MethylationRILIEENRKVIAPML
HHHHHHCCCCHHHHH		37.59115487909
419PhosphorylationKVIAPMLSRHGKLWS
CCHHHHHHHCCCHHH		18.9127251275
441PhosphorylationPDEYYARSEDYVELV
HHHHHCCCHHHHHHH		27.0120068231
444PhosphorylationYYARSEDYVELVQRK
HHCCCHHHHHHHHHH		7.5620068231
460PhosphorylationVGVWNVPYISQAYVI
CCCCCCCEEEEEEEE		14.66-
487PhosphorylationDVFSGSDTDPDMAFC
CCCCCCCCCCCCHHH		51.6422210691
495UbiquitinationDPDMAFCKSFRDKGI
CCCCHHHHHHHHCEE		46.29-
500UbiquitinationFCKSFRDKGIFLHLS
HHHHHHHCEEEEEEC		50.04-
548N-linked_GlycosylationKEQYIHENYSRALEG
HHHHHHHHHHHHHCC		26.3930089812
548N-linked_GlycosylationKEQYIHENYSRALEG
HHHHHHHHHHHHHCC		26.3930089812
615UbiquitinationPTVDIHMKQVGYEDQ
CEEEEEEHHCCCHHH		27.89-
619PhosphorylationIHMKQVGYEDQWLQL
EEEHHCCCHHHHHHH		19.9225690035
629PhosphorylationQWLQLLRTYVGPMTE
HHHHHHHHHHCCCCC		23.6425599653
630PhosphorylationWLQLLRTYVGPMTES
HHHHHHHHHCCCCCC		9.2926503514
645MalonylationLFPGYHTKARAVMNF
CCCCHHHHHHHHEEE		23.6732601280
645AcetylationLFPGYHTKARAVMNF
CCCCHHHHHHHHEEE		23.6726051181
645UbiquitinationLFPGYHTKARAVMNF
CCCCHHHHHHHHEEE		23.672190698
701PhosphorylationLRYDCVISSPRKGWA
EEEEEEEECCCCEEE		17.5624719451
702PhosphorylationRYDCVISSPRKGWAL
EEEEEEECCCCEEEE		20.0121815630
730PhosphorylationPTTWGTRYIMVSFVD
CCCCCCEEEEEEEEC		8.00-
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 PLOD3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLOD3_HUMAN !!
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 PLOD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CC85B_HUMANCCDC85Bphysical
16189514
RHXF2_HUMANRHOXF2physical
16189514
F153A_HUMANFAM153Aphysical
16189514
EHMT2_HUMANEHMT2physical
16189514
DPPA2_HUMANDPPA2physical
16189514
PLOD3_HUMANPLOD3physical
11956192
EHMT2_HUMANEHMT2physical
25416956
EFHC2_HUMANEFHC2physical
25416956
RAB3I_HUMANRAB3IPphysical
25416956
NCPR_HUMANPORphysical
26344197
Drug and Disease Associations
Kegg Disease
H01192 Lysyl hydroxylase 3 (LH3) deficiency; Bone fragility with contractures arterial rupture and deafness
OMIM Disease
612394Lysyl hydroxylase 3 deficiency (LH3 deficiency)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00139Succinic acid
DB00126Vitamin C
Regulatory Network of PLOD3_HUMAN

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Related Literatures of Post-Translational Modification

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