PYRD1_HUMAN - dbPTM
PYRD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PYRD1_HUMAN
UniProt AC Q8WU10
Protein Name Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1
Gene Name PYROXD1
Organism Homo sapiens (Human).
Sequence Length 500
Subcellular Localization Nucleus . Cytoplasm, myofibril, sarcomere .
Protein Description Involved in cellular response to oxidative stress..
Protein Sequence MEAARPPPTAGKFVVVGGGIAGVTCAEQLATHFPSEDILLVTASPVIKAVTNFKQISKILEEFDVEEQSSTMLGKRFPNIKVIESGVKQLKSEEHCIVTEDGNQHVYKKLCLCAGAKPKLICEGNPYVLGIRDTDSAQEFQKQLTKAKRIMIIGNGGIALELVYEIEGCEVIWAIKDKAIGNTFFDAGAAEFLTSKLIAEKSEAKIAHKRTRYTTEGRKKEARSKSKADNVGSALGPDWHEGLNLKGTKEFSHKIHLETMCEVKKIYLQDEFRILKKKSFTFPRDHKSVTADTEMWPVYVELTNEKIYGCDFIVSATGVTPNVEPFLHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDICTTSWQLSPVWQQMRLWTQARQMGWYAAKCMAAASSGDSIDMDFSFELFAHVTKFFNYKVVLLGKYNAQGLGSDHELMLRCTKGREYIKVVMQNGRMMGAVLIGETDLEETFENLILNQMNLSSYGEDLLDPNIDIEDYFD
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
1Acetylation-------MEAARPPP
-------CCCCCCCC		7.7419413330
17UbiquitinationAGKFVVVGGGIAGVT
CCCEEEECCCHHHHH		19.59-
37UbiquitinationATHFPSEDILLVTAS
HHCCCCCCEEEEECH		40.97-
38UbiquitinationTHFPSEDILLVTASP
HCCCCCCEEEEECHH		2.55-
44PhosphorylationDILLVTASPVIKAVT
CEEEEECHHHHHHHC		15.4424260401
46UbiquitinationLLVTASPVIKAVTNF
EEEECHHHHHHHCCH		6.94-
48UbiquitinationVTASPVIKAVTNFKQ
EECHHHHHHHCCHHH		36.7223000965
54UbiquitinationIKAVTNFKQISKILE
HHHHCCHHHHHHHHH		49.1123000965
58UbiquitinationTNFKQISKILEEFDV
CCHHHHHHHHHHCCH		53.6023000965
71UbiquitinationDVEEQSSTMLGKRFP
CHHHHHHHCCCCCCC		22.9721890473
75UbiquitinationQSSTMLGKRFPNIKV
HHHHCCCCCCCCCEE		47.07-
85PhosphorylationPNIKVIESGVKQLKS
CCCEEEHHHHCCCCC		37.4529396449
88UbiquitinationKVIESGVKQLKSEEH
EEEHHHHCCCCCCCC		54.1329967540
91UbiquitinationESGVKQLKSEEHCIV
HHHHCCCCCCCCEEE		54.0129967540
107UbiquitinationEDGNQHVYKKLCLCA
CCCCHHHHHHHHHHC		10.57-
108UbiquitinationDGNQHVYKKLCLCAG
CCCHHHHHHHHHHCC		37.8729967540
109UbiquitinationGNQHVYKKLCLCAGA
CCHHHHHHHHHHCCC		27.0929967540
117UbiquitinationLCLCAGAKPKLICEG
HHHHCCCCCEEEECC		41.5929967540
119UbiquitinationLCAGAKPKLICEGNP
HHCCCCCEEEECCCC		50.1829967540
125UbiquitinationPKLICEGNPYVLGIR
CEEEECCCCEEECEE		11.48-
130UbiquitinationEGNPYVLGIRDTDSA
CCCCEEECEECCCCH		11.66-
142UbiquitinationDSAQEFQKQLTKAKR
CCHHHHHHHHHHCCE		53.2322817900
146UbiquitinationEFQKQLTKAKRIMII
HHHHHHHHCCEEEEE		61.5822817900
175UbiquitinationGCEVIWAIKDKAIGN
CCEEEEEECCCCCCC		3.40-
178UbiquitinationVIWAIKDKAIGNTFF
EEEEECCCCCCCCCC		36.5829967540
194UbiquitinationAGAAEFLTSKLIAEK
HHHHHHHHHHHHHHH		29.18-
196UbiquitinationAAEFLTSKLIAEKSE
HHHHHHHHHHHHHHH		38.3829967540
201UbiquitinationTSKLIAEKSEAKIAH
HHHHHHHHHHHHHHH		44.5729967540
207UbiquitinationEKSEAKIAHKRTRYT
HHHHHHHHHHHHCCC		11.05-
225AcetylationRKKEARSKSKADNVG
HHHHHHHHHHCCCCH		50.887683175
227UbiquitinationKEARSKSKADNVGSA
HHHHHHHHCCCCHHH		64.5929967540
227AcetylationKEARSKSKADNVGSA
HHHHHHHHCCCCHHH		64.597683185
246UbiquitinationWHEGLNLKGTKEFSH
HHCCCCCCCCCCCCC		64.5629967540
265UbiquitinationETMCEVKKIYLQDEF
HHHEEEEEEEHHHHH		41.5829967540
277UbiquitinationDEFRILKKKSFTFPR
HHHHEEEECCCCCCC		50.6429967540
278UbiquitinationEFRILKKKSFTFPRD
HHHEEEECCCCCCCC		49.57-
287UbiquitinationFTFPRDHKSVTADTE
CCCCCCCCCCCCCCC		51.4129967540
354PhosphorylationHTSLPDIYAAGDICT
CCCCCCCHHCCCCCC		9.59-
398PhosphorylationAAASSGDSIDMDFSF
HHHHCCCCCCCCHHH		24.82-
424UbiquitinationYKVVLLGKYNAQGLG
CEEEEEECCCCCCCC		34.9929967540
446PhosphorylationRCTKGREYIKVVMQN
HHCCCHHHEEEEEEC		12.51-
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 PYRD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PYRD1_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 PYRD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UPP_HUMANUPRTphysical
16189514
A4_HUMANAPPphysical
21832049
UPP_HUMANUPRTphysical
25416956
ADRO_HUMANFDXRphysical
26344197
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 PYRD1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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