PCSK9_HUMAN - dbPTM
PCSK9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCSK9_HUMAN
UniProt AC Q8NBP7
Protein Name Proprotein convertase subtilisin/kexin type 9
Gene Name PCSK9
Organism Homo sapiens (Human).
Sequence Length 692
Subcellular Localization Cytoplasm. Secreted. Endosome. Lysosome. Cell surface. Endoplasmic reticulum. Golgi apparatus. Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi apparatus and for the secretion of the mature protein. Local
Protein Description Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments. [PubMed: 18039658 Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation]
Protein Sequence MGTVSSRRSWWPLPLLLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAVARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAEASMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSEGAVTAVAICCRSRHLAQASQELQ
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
3Phosphorylation-----MGTVSSRRSW
-----CCCCCCCCCC		18.8629759185
38SulfationQEDEDGDYEELVLAL
CCCCCCCHHHHHHHH		19.48-
38SulfationQEDEDGDYEELVLAL
CCCCCCCHHHHHHHH		19.4816912035
47PhosphorylationELVLALRSEEDGLAE
HHHHHHHCCCCCCCC		46.3021082442
60O-linked_GlycosylationAEAPEHGTTATFHRC
CCCCCCCCCCEEEEC		18.37OGP
60PhosphorylationAEAPEHGTTATFHRC
CCCCCCCCCCEEEEC		18.3724702127
61PhosphorylationEAPEHGTTATFHRCA
CCCCCCCCCEEEECC		28.4324702127
63PhosphorylationPEHGTTATFHRCAKD
CCCCCCCEEEECCCC		20.2024702127
69UbiquitinationATFHRCAKDPWRLPG
CEEEECCCCCCCCCC		68.8729967540
77PhosphorylationDPWRLPGTYVVVLKE
CCCCCCCEEEEEECC		15.9422210691
78PhosphorylationPWRLPGTYVVVLKEE
CCCCCCEEEEEECCC		9.3622210691
86PhosphorylationVVVLKEETHLSQSER
EEEECCCCCCCHHHH		29.25-
89PhosphorylationLKEETHLSQSERTAR
ECCCCCCCHHHHHHH		24.85-
91PhosphorylationEETHLSQSERTARRL
CCCCCCHHHHHHHHH		26.18-
94PhosphorylationHLSQSERTARRLQAQ
CCCHHHHHHHHHHHH		22.06-
127PhosphorylationPGFLVKMSGDLLELA
HHHHHEECHHHHHHH		24.3630631047
162PhosphorylationPWNLERITPPRYRAD
CCCHHHCCCCCCCCC		33.2024719451
221PhosphorylationTRFHRQASKCDSHGT
CCCCHHHHCCCCCCC		26.0225954137
222UbiquitinationRFHRQASKCDSHGTH
CCCHHHHCCCCCCCE		45.1129967540
228PhosphorylationSKCDSHGTHLAGVVS
HCCCCCCCEEEEECC		14.3225954137
235PhosphorylationTHLAGVVSGRDAGVA
CEEEEECCCCCCCCC		26.2118669648
243UbiquitinationGRDAGVAKGASMRSL
CCCCCCCCCCCCCEE		53.2421963094
260PhosphorylationLNCQGKGTVSGTLIG
EECCCCCCEECEEEE		18.2523879269
262PhosphorylationCQGKGTVSGTLIGLE
CCCCCCEECEEEEHH		26.3723879269
264PhosphorylationGKGTVSGTLIGLEFI
CCCCEECEEEEHHHH		14.0123879269
274PhosphorylationGLEFIRKSQLVQPVG
EHHHHHHHHCCCCCC		20.9223879269
533N-linked_GlycosylationCCLLPQANCSVHTAP
HEECCCCCCEEEECC		17.2212552133
533N-linked_GlycosylationCCLLPQANCSVHTAP
HEECCCCCCEEEECC		17.2216912035
548PhosphorylationPAEASMGTRVHCHQQ
HHHCCCCCEEEEECC		22.3720068231
662PhosphorylationVVRSRDVSTTGSTSE
EEECCCCCCCCCCCC		25.2525072903
663PhosphorylationVRSRDVSTTGSTSEG
EECCCCCCCCCCCCC		34.7225072903
664PhosphorylationRSRDVSTTGSTSEGA
ECCCCCCCCCCCCCH		22.9425072903
666PhosphorylationRDVSTTGSTSEGAVT
CCCCCCCCCCCCHHH		27.0325072903
667PhosphorylationDVSTTGSTSEGAVTA
CCCCCCCCCCCHHHH		31.9425072903
668PhosphorylationVSTTGSTSEGAVTAV
CCCCCCCCCCHHHHH		35.4125072903
688PhosphorylationSRHLAQASQELQ---
HHHHHHHHHHHC---		16.4719664994
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
47SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
688SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
-KUbiquitinationE3 ubiquitin ligaseBIRC2Q13490
PMID:23085658
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCSK9_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 PCSK9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BACE1_HUMANBACE1physical
18660751
UGGG1_HUMANUGGT1physical
23085658
PDIA4_HUMANPDIA4physical
23085658
TXTP_HUMANSLC25A1physical
23085658
DNJA1_HUMANDNAJA1physical
23085658
CLGN_HUMANCLGNphysical
23085658
DNJA2_HUMANDNAJA2physical
23085658
BIRC2_HUMANBIRC2physical
23085658
TRAF2_HUMANTRAF2physical
23085658
DIC_HUMANSLC25A10physical
23085658
DJB11_HUMANDNAJB11physical
23085658
CDIPT_HUMANCDIPTphysical
23085658
DJC10_HUMANDNAJC10physical
23085658
DNJA3_HUMANDNAJA3physical
23085658
MIRO1_HUMANRHOT1physical
23085658
AGK_HUMANAGKphysical
23085658
HSPB1_HUMANHSPB1physical
23085658
RCN1_HUMANRCN1physical
23085658
CHIP_HUMANSTUB1physical
23085658
CMC1_HUMANSLC25A12physical
23085658
TBB6_HUMANTUBB6physical
23085658
PGRC1_HUMANPGRMC1physical
23085658
RL28_HUMANRPL28physical
23085658
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
603776Hypercholesterolemia, autosomal dominant, 3 (HCHOLA3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCSK9_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-688, AND MASSSPECTROMETRY.

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