PLOD2_HUMAN - dbPTM
PLOD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLOD2_HUMAN
UniProt AC O00469
Protein Name Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
Gene Name PLOD2
Organism Homo sapiens (Human).
Sequence Length 737
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 MGGCTVKPQLLLLALVLHPWNPCLGADSEKPSSIPTDKLLVITVATKESDGFHRFMQSAKYFNYTVKVLGQGEEWRGGDGINSIGGGQKVRLMKEVMEHYADQDDLVVMFTECFDVIFAGGPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGYAPYVNRIVQQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARAKNTFYETLPVAINGNGPTKILLNYFGNYVPNSWTQDNGCTLCEFDTVDLSAVDVHPNVSIGVFIEQPTPFLPRFLDILLTLDYPKEALKLFIHNKEVYHEKDIKVFFDKAKHEIKTIKIVGPEENLSQAEARNMGMDFCRQDEKCDYYFSVDADVVLTNPRTLKILIEQNRKIIAPLVTRHGKLWSNFWGALSPDGYYARSEDYVDIVQGNRVGVWNVPYMANVYLIKGKTLRSEMNERNYFVRDKLDPDMALCRNAREMGVFMYISNRHEFGRLLSTANYNTSHYNNDLWQIFENPVDWKEKYINRDYSKIFTENIVEQPCPDVFWFPIFSEKACDELVEEMEHYGKWSGGKHHDSRISGGYENVPTDDIHMKQVDLENVWLHFIREFIAPVTLKVFAGYYTKGFALLNFVVKYSPERQRSLRPHHDASTFTINIALNNVGEDFQGGGCKFLRYNCSIESPRKGWSFMHPGRLTHLHEGLPVKNGTRYIAVSFIDP
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
61PhosphorylationRFMQSAKYFNYTVKV
HHHHHHHCCCEEEEE		9.2123898821
63N-linked_GlycosylationMQSAKYFNYTVKVLG
HHHHHCCCEEEEECC		28.60UniProtKB CARBOHYD
64PhosphorylationQSAKYFNYTVKVLGQ
HHHHCCCEEEEECCC		11.7423898821
65PhosphorylationSAKYFNYTVKVLGQG
HHHCCCEEEEECCCC		18.2423898821
76MethylationLGQGEEWRGGDGINS
CCCCCCCCCCCCCCC		42.36115487901
89UbiquitinationNSIGGGQKVRLMKEV
CCCCCHHHHHHHHHH		32.3729967540
148UbiquitinationDGILWPDKRLADKYP
CCCCCCCHHHHHCCC		45.2729967540
153UbiquitinationPDKRLADKYPVVHIG
CCHHHHHCCCEEEEC		45.9429967540
163PhosphorylationVVHIGKRYLNSGGFI
EEEECCEECCCCCCC		17.45-
168 (in isoform 3)Phosphorylation-15.72-
170 (in isoform 3)Phosphorylation-4.70-
172PhosphorylationNSGGFIGYAPYVNRI
CCCCCCCHHHHHHHH		10.29-
204UbiquitinationKVYIDPLKREAINIT
EEEECCCCHHHEEEE		54.2929967540
209N-linked_GlycosylationPLKREAINITLDHKC
CCCHHHEEEECCCCC		28.3919159218
241UbiquitinationENGKARAKNTFYETL
ECCCCCEECCEEEEC		51.4729967540
249UbiquitinationNTFYETLPVAINGNG
CCEEEECCEEECCCC		22.4021890473
252UbiquitinationYETLPVAINGNGPTK
EEECCEEECCCCCCE		7.4521890473
257UbiquitinationVAINGNGPTKILLNY
EEECCCCCCEEEEEC		34.2222817900
297N-linked_GlycosylationSAVDVHPNVSIGVFI
CEEECCCCCEEEEEE		25.87UniProtKB CARBOHYD
320PhosphorylationRFLDILLTLDYPKEA
HHHHHHHHCCCCHHH		17.7119060867
323PhosphorylationDILLTLDYPKEALKL
HHHHHCCCCHHHHHH		21.2219060867
329UbiquitinationDYPKEALKLFIHNKE
CCCHHHHHHHHCCCC		48.6929967540
335UbiquitinationLKLFIHNKEVYHEKD
HHHHHCCCCCCCHHH		34.1029967540
341UbiquitinationNKEVYHEKDIKVFFD
CCCCCCHHHHEEEEE		51.9822817900
341 (in isoform 1)Ubiquitination-51.9821890473
341 (in isoform 2)Ubiquitination-51.9821890473
341UbiquitinationNKEVYHEKDIKVFFD
CCCCCCHHHHEEEEE		51.9821890473
344 (in isoform 1)Ubiquitination-43.0221890473
344 (in isoform 2)Ubiquitination-43.0221890473
344UbiquitinationVYHEKDIKVFFDKAK
CCCHHHHEEEEEHHC		43.0222817900
344UbiquitinationVYHEKDIKVFFDKAK
CCCHHHHEEEEEHHC		43.0221890473
349UbiquitinationDIKVFFDKAKHEIKT
HHEEEEEHHCCEEEE		54.9322817900
355UbiquitinationDKAKHEIKTIKIVGP
EHHCCEEEEEEEECC		41.0129967540
358UbiquitinationKHEIKTIKIVGPEEN
CCEEEEEEEECCHHC		36.2529967540
365N-linked_GlycosylationKIVGPEENLSQAEAR
EEECCHHCCCHHHHH		43.24UniProtKB CARBOHYD
387 (in isoform 2)Phosphorylation-18.8427251275
387PhosphorylationRQDEKCDYYFSVDAD
HCCCCCCEEEEEECC		18.8427251275
390 (in isoform 2)Phosphorylation-11.7227251275
390PhosphorylationEKCDYYFSVDADVVL
CCCCEEEEEECCEEE		11.7227251275
412UbiquitinationILIEQNRKIIAPLVT
HHHHHCCCCHHHHHC		46.1129967540
426PhosphorylationTRHGKLWSNFWGALS
CCCCCHHHCCCCCCC		32.3620068231
433PhosphorylationSNFWGALSPDGYYAR
HCCCCCCCCCCCEEC		22.0220068231
437PhosphorylationGALSPDGYYARSEDY
CCCCCCCCEECCHHC		11.0020068231
438PhosphorylationALSPDGYYARSEDYV
CCCCCCCEECCHHCE		10.8920068231
444PhosphorylationYYARSEDYVDIVQGN
CEECCHHCEEEECCC		8.93-
486UbiquitinationRNYFVRDKLDPDMAL
CCCHHHHCCCHHHHH		44.2029967540
505PhosphorylationREMGVFMYISNRHEF
HHHCEEEEEECHHHH		6.9629978859
506UbiquitinationEMGVFMYISNRHEFG
HHCEEEEEECHHHHH		1.6529967540
507PhosphorylationMGVFMYISNRHEFGR
HCEEEEEECHHHHHH		15.4329978859
508 (in isoform 2)Phosphorylation-39.51-
510 (in isoform 2)Phosphorylation-38.70-
522N-linked_GlycosylationLLSTANYNTSHYNND
HHHHCCCCCCCCCCC		34.6119159218
543UbiquitinationNPVDWKEKYINRDYS
CCCCHHHHHCCCCHH		47.9429967540
564UbiquitinationIVEQPCPDVFWFPIF
CCCCCCCCCCEEECC		55.7729967540
588UbiquitinationEEMEHYGKWSGGKHH
HHHHHHCCCCCCCCC		30.9029967540
590PhosphorylationMEHYGKWSGGKHHDS
HHHHCCCCCCCCCCC		40.95-
593UbiquitinationYGKWSGGKHHDSRIS
HCCCCCCCCCCCCCC		41.0929967540
600PhosphorylationKHHDSRISGGYENVP
CCCCCCCCCCCCCCC		25.6725159151
603PhosphorylationDSRISGGYENVPTDD
CCCCCCCCCCCCCCC		14.0929449344
608PhosphorylationGGYENVPTDDIHMKQ
CCCCCCCCCCCEECE		41.86-
609UbiquitinationGYENVPTDDIHMKQV
CCCCCCCCCCEECEE		46.9629967540
614UbiquitinationPTDDIHMKQVDLENV
CCCCCEECEECHHHH		32.7629967540
634PhosphorylationREFIAPVTLKVFAGY
HHHHHHHHHHHCCEE		21.58-
655PhosphorylationLLNFVVKYSPERQRS
HHEEEEEECHHHHHC		20.1824719451
656PhosphorylationLNFVVKYSPERQRSL
HEEEEEECHHHHHCC		17.9924719451
676 (in isoform 2)Phosphorylation-4.0024719451
677 (in isoform 2)Phosphorylation-10.3524719451
696N-linked_GlycosylationGCKFLRYNCSIESPR
CCEEEEEECEECCCC		13.46UniProtKB CARBOHYD
704AcetylationCSIESPRKGWSFMHP
CEECCCCCCCCCCCC		69.0230591401
704SuccinylationCSIESPRKGWSFMHP
CEECCCCCCCCCCCC		69.02-
704SuccinylationCSIESPRKGWSFMHP
CEECCCCCCCCCCCC		69.02-
725N-linked_GlycosylationHEGLPVKNGTRYIAV
ECCCCCCCCCEEEEE		58.25UniProtKB CARBOHYD
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 PLOD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLOD2_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 PLOD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLOD2_HUMANPLOD2physical
11956192
AP2B1_HUMANAP2B1physical
22863883
SYFB_HUMANFARSBphysical
22863883
PUR2_HUMANGARTphysical
22863883
HS105_HUMANHSPH1physical
22863883
PLAK_HUMANJUPphysical
22863883
NUCL_HUMANNCLphysical
22863883
NUSAP_HUMANNUSAP1physical
22863883
PACN2_HUMANPACSIN2physical
22863883
ANM3_HUMANPRMT3physical
22863883
RANB3_HUMANRANBP3physical
22863883
RL24_HUMANRPL24physical
22863883
SET_HUMANSETphysical
22863883
SF01_HUMANSF1physical
22863883
SPT5H_HUMANSUPT5Hphysical
22863883
SWP70_HUMANSWAP70physical
22863883
VASN_HUMANVASNphysical
22863883
XPO7_HUMANXPO7physical
22863883
Drug and Disease Associations
Kegg Disease
H00514 Bruck syndrome
OMIM Disease
609220Bruck syndrome 2 (BRKS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00126Vitamin C
Regulatory Network of PLOD2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-209 AND ASN-522, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320 AND TYR-323, ANDMASS SPECTROMETRY.

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