NCPR_MOUSE - dbPTM
NCPR_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCPR_MOUSE
UniProt AC P37040
Protein Name NADPH--cytochrome P450 reductase {ECO:0000255|HAMAP-Rule:MF_03212}
Gene Name Por {ECO:0000255|HAMAP-Rule:MF_03212}
Organism Mus musculus (Mouse).
Sequence Length 678
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein
Cytoplasmic side .
Protein Description This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5..
Protein Sequence MGDSHEDTSATVPEAVAEEVSLFSTTDIVLFSLIVGVLTYWFIFKKKKEEIPEFSKIQTTAPPVKESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETDVDLTGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEFFGVEATGEESSIRQYELVVHEDMDTAKVYTGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHLMHLELDISDSKIRYESGDHVAVYPANDSTLVNQIGEILGADLDVIMSLNNLDEESNKKHPFPCPTTYRTALTYYLDITNPPRTNVLYELAQYASEPSEQEHLHKMASSSGEGKELYLSWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVAVEYEAKSGRVNKGVATSWLRTKEPAGENGRRALVPMFVRKSQFRLPFKPTTPVIMVGPGTGVAPFMGFIQERAWLREQGKEVGETLLYYGCRRSDEDYLYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDKEHLWKLIHEGGAHIYVCGDARNMAKDVQNTFYDIVAEFGPMEHTQAVDYVKKLMTKGRYSLDVWS
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------MGDSHEDTS
------CCCCCCCCC		45.16-
56UbiquitinationEEIPEFSKIQTTAPP
HHCCCCCCCCCCCCC		44.1222790023
65UbiquitinationQTTAPPVKESSFVEK
CCCCCCCCHHHHHHH		58.6222790023
65MalonylationQTTAPPVKESSFVEK
CCCCCCCCHHHHHHH		58.6232601280
68PhosphorylationAPPVKESSFVEKMKK
CCCCCHHHHHHHHHH		34.1124719451
72AcetylationKESSFVEKMKKTGRN
CHHHHHHHHHHHCCC		51.2023864654
105PhosphorylationLSKDAHRYGMRGMSA
HHHHHHHHHCCCCCC		12.8522817900
111PhosphorylationRYGMRGMSADPEEYD
HHHCCCCCCCHHHCC		32.1322817900
117PhosphorylationMSADPEEYDLADLSS
CCCCHHHCCCCHHHC		18.0023984901
176UbiquitinationAVFGLGNKTYEHFNA
EEEECCCCHHHHHHH		51.1622790023
186AcetylationEHFNAMGKYVDQRLE
HHHHHHHHHHHHHHH		29.0823201123
186UbiquitinationEHFNAMGKYVDQRLE
HHHHHHHHHHHHHHH		29.0822790023
245PhosphorylationEESSIRQYELVVHED
CCCCEEEEEEEEECC		11.0326643407
255PhosphorylationVVHEDMDTAKVYTGE
EEECCCCCCEEEECC		23.0326643407
257UbiquitinationHEDMDTAKVYTGEMG
ECCCCCCEEEECCCC		37.5622790023
259PhosphorylationDMDTAKVYTGEMGRL
CCCCCEEEECCCCCC		14.3426643407
260PhosphorylationMDTAKVYTGEMGRLK
CCCCEEEECCCCCCC		29.6526643407
268PhosphorylationGEMGRLKSYENQKPP
CCCCCCCCCCCCCCC		42.1223140645
269PhosphorylationEMGRLKSYENQKPPF
CCCCCCCCCCCCCCC		19.8123140645
273MalonylationLKSYENQKPPFDAKN
CCCCCCCCCCCCCCC		67.2626320211
273UbiquitinationLKSYENQKPPFDAKN
CCCCCCCCCCCCCCC		67.2627667366
279AcetylationQKPPFDAKNPFLAAV
CCCCCCCCCCHHEEH		67.9823201123
279UbiquitinationQKPPFDAKNPFLAAV
CCCCCCCCCCHHEEH		67.9822790023
311UbiquitinationELDISDSKIRYESGD
EEECCCCEEEEECCC		35.8722790023
358MalonylationLDEESNKKHPFPCPT
CCHHHCCCCCCCCCC		61.8426320211
358UbiquitinationLDEESNKKHPFPCPT
CCHHHCCCCCCCCCC		61.84-
363S-palmitoylationNKKHPFPCPTTYRTA
CCCCCCCCCCHHCCE		4.8428526873
373PhosphorylationTYRTALTYYLDITNP
HHCCEEEEEHHCCCC		11.6822817900
374PhosphorylationYRTALTYYLDITNPP
HCCEEEEEHHCCCCC		7.8322817900
387PhosphorylationPPRTNVLYELAQYAS
CCCCCHHHHHHHHCC		12.4817242355
404UbiquitinationSEQEHLHKMASSSGE
HHHHHHHHHHHCCCC		42.3922790023
472S-nitrosylationHPNSVHICAVAVEYE
CCCCEEEEEEEEEEE		1.1822178444
487UbiquitinationAKSGRVNKGVATSWL
CCCCCCCCCCCCCCH		52.4822790023
523UbiquitinationSQFRLPFKPTTPVIM
HHCCCCCCCCCCEEE		39.2422790023
555AcetylationAWLREQGKEVGETLL
HHHHHHHHHHHHHHH		49.2523864654
555MalonylationAWLREQGKEVGETLL
HHHHHHHHHHHHHHH		49.2526320211
555UbiquitinationAWLREQGKEVGETLL
HHHHHHHHHHHHHHH		49.25-
566S-nitrosylationETLLYYGCRRSDEDY
HHHHHHCCCCCCCHH		1.5622178444
566S-palmitoylationETLLYYGCRRSDEDY
HHHHHHCCCCCCCHH		1.5628526873
575PhosphorylationRSDEDYLYREELARF
CCCCHHHCHHHHHHH		15.1117622165
584AcetylationEELARFHKDGALTQL
HHHHHHCCCCCHHHH		55.9623954790
584UbiquitinationEELARFHKDGALTQL
HHHHHHCCCCCHHHH		55.96-
584MalonylationEELARFHKDGALTQL
HHHHHHCCCCCHHHH		55.9626320211
604PhosphorylationREQAHKVYVQHLLKR
HHHHHHHHHHHHHHH		10.1325195567
610AcetylationVYVQHLLKRDKEHLW
HHHHHHHHHCHHHHH		65.982372971
610UbiquitinationVYVQHLLKRDKEHLW
HHHHHHHHHCHHHHH		65.9822790023
630S-nitrosylationGGAHIYVCGDARNMA
CCCEEEEECCHHHHH		1.9822178444
664AcetylationTQAVDYVKKLMTKGR
HHHHHHHHHHHHCCC		33.6823954790
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 NCPR_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCPR_MOUSE !!
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 NCPR_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FANCC_MOUSEFanccphysical
9787138
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NCPR_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-575, AND MASSSPECTROMETRY.

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