QOR_HUMAN - dbPTM
QOR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID QOR_HUMAN
UniProt AC Q08257
Protein Name Quinone oxidoreductase
Gene Name CRYZ
Organism Homo sapiens (Human).
Sequence Length 329
Subcellular Localization Cytoplasm .
Protein Description Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. Enhances the stability of mRNA coding for BCL2. NADPH binding interferes with mRNA binding..
Protein Sequence MATGQKLMRAVRVFEFGGPEVLKLRSDIAVPIPKDHQVLIKVHACGVNPVETYIRSGTYSRKPLLPYTPGSDVAGVIEAVGDNASAFKKGDRVFTSSTISGGYAEYALAADHTVYKLPEKLDFKQGAAIGIPYFTAYRALIHSACVKAGESVLVHGASGGVGLAACQIARAYGLKILGTAGTEEGQKIVLQNGAHEVFNHREVNYIDKIKKYVGEKGIDIIIEMLANVNLSKDLSLLSHGGRVIVVGSRGTIEINPRDTMAKESSIIGVTLFSSTKEEFQQYAAALQAGMEIGWLKPVIGSQYPLEKVAEAHENIIHGSGATGKMILLL
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
2Acetylation------MATGQKLMR
------CCHHHHHHH		22.0422814378
6Acetylation--MATGQKLMRAVRV
--CCHHHHHHHHHHH		45.6623749302
6Ubiquitination--MATGQKLMRAVRV
--CCHHHHHHHHHHH		45.6624816145
23AcetylationFGGPEVLKLRSDIAV
CCCHHHEEEECCEEE		47.2119608861
23UbiquitinationFGGPEVLKLRSDIAV
CCCHHHEEEECCEEE		47.2121963094
23UbiquitinationFGGPEVLKLRSDIAV
CCCHHHEEEECCEEE		47.2121890473
26PhosphorylationPEVLKLRSDIAVPIP
HHHEEEECCEEEECC		43.7528857561
342-HydroxyisobutyrylationDIAVPIPKDHQVLIK
CEEEECCCCCEEEEE		69.44-
34UbiquitinationDIAVPIPKDHQVLIK
CEEEECCCCCEEEEE		69.4429967540
34MalonylationDIAVPIPKDHQVLIK
CEEEECCCCCEEEEE		69.4426320211
34AcetylationDIAVPIPKDHQVLIK
CEEEECCCCCEEEEE		69.4426051181
34SuccinylationDIAVPIPKDHQVLIK
CEEEECCCCCEEEEE		69.4427452117
38UbiquitinationPIPKDHQVLIKVHAC
ECCCCCEEEEEEEEC		5.5329967540
45S-nitrosylationVLIKVHACGVNPVET
EEEEEEECCCCCCHH		3.6424105792
50UbiquitinationHACGVNPVETYIRSG
EECCCCCCHHHHCCC		7.8729967540
52PhosphorylationCGVNPVETYIRSGTY
CCCCCCHHHHCCCCC		25.20-
53PhosphorylationGVNPVETYIRSGTYS
CCCCCHHHHCCCCCC		4.8421253578
62UbiquitinationRSGTYSRKPLLPYTP
CCCCCCCCCCCCCCC		33.7921906983
71UbiquitinationLLPYTPGSDVAGVIE
CCCCCCCCCHHHHHH		30.0729967540
71AcetylationLLPYTPGSDVAGVIE
CCCCCCCCCHHHHHH		30.0719608861
88UbiquitinationGDNASAFKKGDRVFT
CCCHHHHHCCCEEEE		56.4121906983
88AcetylationGDNASAFKKGDRVFT
CCCHHHHHCCCEEEE		56.4125038526
882-HydroxyisobutyrylationGDNASAFKKGDRVFT
CCCHHHHHCCCEEEE		56.41-
89UbiquitinationDNASAFKKGDRVFTS
CCHHHHHCCCEEEEE		60.6422817900
89AcetylationDNASAFKKGDRVFTS
CCHHHHHCCCEEEEE		60.647826005
95PhosphorylationKKGDRVFTSSTISGG
HCCCEEEEECEECCC		20.93-
96PhosphorylationKGDRVFTSSTISGGY
CCCEEEEECEECCCH		17.64-
97PhosphorylationGDRVFTSSTISGGYA
CCEEEEECEECCCHH		27.05-
98PhosphorylationDRVFTSSTISGGYAE
CEEEEECEECCCHHH		20.94-
103PhosphorylationSSTISGGYAEYALAA
ECEECCCHHHHHHCC		10.37-
106PhosphorylationISGGYAEYALAADHT
ECCCHHHHHHCCCCE		9.95-
1202-HydroxyisobutyrylationTVYKLPEKLDFKQGA
EEEECCCCCCCCCCC		51.95-
120MalonylationTVYKLPEKLDFKQGA
EEEECCCCCCCCCCC		51.9526320211
120AcetylationTVYKLPEKLDFKQGA
EEEECCCCCCCCCCC		51.9523236377
120UbiquitinationTVYKLPEKLDFKQGA
EEEECCCCCCCCCCC		51.9529967540
133PhosphorylationGAAIGIPYFTAYRAL
CCCCCCCHHHHHHHH		16.1921406692
135PhosphorylationAIGIPYFTAYRALIH
CCCCCHHHHHHHHHH		19.5521406692
137PhosphorylationGIPYFTAYRALIHSA
CCCHHHHHHHHHHHH		8.0521406692
158PhosphorylationSVLVHGASGGVGLAA
EEEEECCCCCHHHHH		40.4426437602
175UbiquitinationIARAYGLKILGTAGT
HHHHHCCEEEEECCC		31.3629967540
187UbiquitinationAGTEEGQKIVLQNGA
CCCHHHCEEEEECCC		45.7129967540
208UbiquitinationREVNYIDKIKKYVGE
CCCCHHHHHHHHHHH		47.0319608861
208AcetylationREVNYIDKIKKYVGE
CCCCHHHHHHHHHHH		47.0323236377
235PhosphorylationVNLSKDLSLLSHGGR
CCCCCCHHHHCCCCE		37.0821406692
238PhosphorylationSKDLSLLSHGGRVIV
CCCHHHHCCCCEEEE		25.9421406692
248PhosphorylationGRVIVVGSRGTIEIN
CEEEEECCCCEEEEC		18.8720068231
251PhosphorylationIVVGSRGTIEINPRD
EEECCCCEEEECCCC		17.8326437602
264PhosphorylationRDTMAKESSIIGVTL
CCCCCCCCCEEEEEE		26.57-
296SuccinylationGMEIGWLKPVIGSQY
CCCCCCCCCCCCCCC		30.63-
296SuccinylationGMEIGWLKPVIGSQY
CCCCCCCCCCCCCCC		30.63-
319PhosphorylationHENIIHGSGATGKMI
HHHCCCCCCCCCCEE		15.8728857561
322PhosphorylationIIHGSGATGKMILLL
CCCCCCCCCCEEEEC		40.6420068231
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 QOR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of QOR_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 QOR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
G3P_HUMANGAPDHphysical
22863883
TBA4A_HUMANTUBA4Aphysical
22863883
TBB5_HUMANTUBBphysical
22863883
TRXR1_HUMANTXNRD1physical
22863883
CAB39_HUMANCAB39physical
26344197
DCXR_HUMANDCXRphysical
26344197
LEG3_HUMANLGALS3physical
26344197
NNMT_HUMANNNMTphysical
26344197
SMAP2_HUMANSMAP2physical
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
DB00266Dicoumarol
Regulatory Network of QOR_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23 AND LYS-208, AND MASSSPECTROMETRY.

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