PCYOX_HUMAN - dbPTM
PCYOX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCYOX_HUMAN
UniProt AC Q9UHG3
Protein Name Prenylcysteine oxidase 1
Gene Name PCYOX1
Organism Homo sapiens (Human).
Sequence Length 505
Subcellular Localization Lysosome.
Protein Description Involved in the degradation of prenylated proteins. Cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine..
Protein Sequence MGRVVAELVSSLLGLWLLLCSCGCPEGAELRAPPDKIAIIGAGIGGTSAAYYLRQKFGKDVKIDLFEREEVGGRLATMMVQGQEYEAGGSVIHPLNLHMKRFVKDLGLSAVQASGGLLGIYNGETLVFEESNWFIINVIKLVWRYGFQSLRMHMWVEDVLDKFMRIYRYQSHDYAFSSVEKLLHALGGDDFLGMLNRTLLETLQKAGFSEKFLNEMIAPVMRVNYGQSTDINAFVGAVSLSCSDSGLWAVEGGNKLVCSGLLQASKSNLISGSVMYIEEKTKTKYTGNPTKMYEVVYQIGTETRSDFYDIVLVATPLNRKMSNITFLNFDPPIEEFHQYYQHIVTTLVKGELNTSIFSSRPIDKFGLNTVLTTDNSDLFINSIGIVPSVREKEDPEPSTDGTYVWKIFSQETLTKAQILKLFLSYDYAVKKPWLAYPHYKPPEKCPSIILHDRLYYLNGIECAASAMEMSAIAAHNAALLAYHRWNGHTDMIDQDGLYEKLKTEL
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
47PhosphorylationIGAGIGGTSAAYYLR
EECCCCHHHHHHHHH		15.24-
51PhosphorylationIGGTSAAYYLRQKFG
CCHHHHHHHHHHHHC		11.62-
62UbiquitinationQKFGKDVKIDLFERE
HHHCCCCEEEEEECC		40.4129967540
149PhosphorylationVWRYGFQSLRMHMWV
HHHHCHHHHHHHHHH		18.7124719451
162UbiquitinationWVEDVLDKFMRIYRY
HHHHHHHHHHHHHHH		36.5817370265
169PhosphorylationKFMRIYRYQSHDYAF
HHHHHHHHCCCCCCH		9.4426437602
171PhosphorylationMRIYRYQSHDYAFSS
HHHHHHCCCCCCHHH		14.9126437602
174PhosphorylationYRYQSHDYAFSSVEK
HHHCCCCCCHHHHHH		12.24-
177PhosphorylationQSHDYAFSSVEKLLH
CCCCCCHHHHHHHHH		25.8828060719
178PhosphorylationSHDYAFSSVEKLLHA
CCCCCHHHHHHHHHH		28.0428060719
196N-linked_GlycosylationDDFLGMLNRTLLETL
CCHHHHHHHHHHHHH		26.4616335952
202PhosphorylationLNRTLLETLQKAGFS
HHHHHHHHHHHCCCC		34.1620068231
205UbiquitinationTLLETLQKAGFSEKF
HHHHHHHHCCCCHHH		54.3022817900
205UbiquitinationTLLETLQKAGFSEKF
HHHHHHHHCCCCHHH		54.3021890473
258S-nitrosylationEGGNKLVCSGLLQAS
ECCCEEEEEHHHHHH		3.7519483679
258S-nitrosocysteineEGGNKLVCSGLLQAS
ECCCEEEEEHHHHHH		3.75-
271PhosphorylationASKSNLISGSVMYIE
HHHCCCCCCCEEEEE		28.3425690035
276PhosphorylationLISGSVMYIEEKTKT
CCCCCEEEEEECCCC		11.7425690035
301PhosphorylationEVVYQIGTETRSDFY
EEEEECCCCCHHHCC		35.4929759185
303PhosphorylationVYQIGTETRSDFYDI
EEECCCCCHHHCCEE		35.0029759185
308PhosphorylationTETRSDFYDIVLVAT
CCCHHHCCEEEEEEE		15.11-
323N-linked_GlycosylationPLNRKMSNITFLNFD
CCCCCCCCCEEECCC		33.5416335952
339PhosphorylationPIEEFHQYYQHIVTT
CHHHHHHHHHHHHHH		9.12-
353N-linked_GlycosylationTLVKGELNTSIFSSR
HHHCCCCCCCHHCCC		27.7216335952
392UbiquitinationIVPSVREKEDPEPST
CCCCCCCCCCCCCCC		57.7829967540
399PhosphorylationKEDPEPSTDGTYVWK
CCCCCCCCCCCEEEE		49.5226437602
403PhosphorylationEPSTDGTYVWKIFSQ
CCCCCCCEEEEEECH		15.1626437602
415MalonylationFSQETLTKAQILKLF
ECHHCCCHHHHHHHH		41.2130639696
415AcetylationFSQETLTKAQILKLF
ECHHCCCHHHHHHHH		41.2125825284
415UbiquitinationFSQETLTKAQILKLF
ECHHCCCHHHHHHHH		41.2123000965
420UbiquitinationLTKAQILKLFLSYDY
CCHHHHHHHHHCCCH		38.5323000965
425PhosphorylationILKLFLSYDYAVKKP
HHHHHHCCCHHCCCC		18.34-
427PhosphorylationKLFLSYDYAVKKPWL
HHHHCCCHHCCCCCC		12.69-
430SuccinylationLSYDYAVKKPWLAYP
HCCCHHCCCCCCCCC		44.9723954790
482PhosphorylationHNAALLAYHRWNGHT
HHHHHHHHHCCCCCC		7.59-
498PhosphorylationMIDQDGLYEKLKTEL
CCCCCCHHHHHHHCC		19.2926437602
500UbiquitinationDQDGLYEKLKTEL--
CCCCHHHHHHHCC--		41.5521890473
500UbiquitinationDQDGLYEKLKTEL--
CCCCHHHHHHHCC--		41.5521890473
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 PCYOX_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCYOX_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 PCYOX_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PCYOX_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCYOX_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-196 AND ASN-353, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196; ASN-323 AND ASN-353,AND MASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-162, AND MASSSPECTROMETRY.

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