CBR1_HUMAN - dbPTM
CBR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CBR1_HUMAN
UniProt AC P16152
Protein Name Carbonyl reductase [NADPH] 1
Gene Name CBR1
Organism Homo sapiens (Human).
Sequence Length 277
Subcellular Localization Cytoplasm.
Protein Description NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione..
Protein Sequence MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTKKGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKATKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW
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
2Phosphorylation------MSSGIHVAL
------CCCCEEEEE		36.9520068231
2Acetylation------MSSGIHVAL
------CCCCEEEEE		36.9520068231
3Phosphorylation-----MSSGIHVALV
-----CCCCEEEEEE		40.2320068231
11PhosphorylationGIHVALVTGGNKGIG
CEEEEEEECCCCCHH		39.9823612710
30PhosphorylationRDLCRLFSGDVVLTA
HHHHHHHCCCEEEEE		38.3828857561
36PhosphorylationFSGDVVLTARDVTRG
HCCCEEEEECCCHHH		14.1924719451
41PhosphorylationVLTARDVTRGQAAVQ
EEEECCCHHHHHHHH		33.1128857561
42MethylationLTARDVTRGQAAVQQ
EEECCCHHHHHHHHH		34.77-
56PhosphorylationQLQAEGLSPRFHQLD
HHHHCCCCCCCCCCC		25.5320873877
69PhosphorylationLDIDDLQSIRALRDF
CCHHHHHHHHHHHHH		22.7224076635
96AcetylationNNAGIAFKVADPTPF
ECCCEEEEECCCCCC		27.7324889043
101PhosphorylationAFKVADPTPFHIQAE
EEEECCCCCCEEEEE		38.8528060719
110PhosphorylationFHIQAEVTMKTNFFG
CEEEEEEEECCCCCC		12.4028857561
111SulfoxidationHIQAEVTMKTNFFGT
EEEEEEEECCCCCCC		6.4330846556
123PhosphorylationFGTRDVCTELLPLIK
CCCHHHHHHHHHHCC		29.5321712546
130UbiquitinationTELLPLIKPQGRVVN
HHHHHHCCCCCCEEE		38.68-
139PhosphorylationQGRVVNVSSIMSVRA
CCCEEEHHHHHHHHH		14.6720873877
140PhosphorylationGRVVNVSSIMSVRAL
CCEEEHHHHHHHHHH		20.3020873877
142SulfoxidationVVNVSSIMSVRALKS
EEEHHHHHHHHHHHH		3.0730846556
143PhosphorylationVNVSSIMSVRALKSC
EEHHHHHHHHHHHHC		13.5420873877
148UbiquitinationIMSVRALKSCSPELQ
HHHHHHHHHCCHHHH		48.72-
1482-HydroxyisobutyrylationIMSVRALKSCSPELQ
HHHHHHHHHCCHHHH		48.72-
148MalonylationIMSVRALKSCSPELQ
HHHHHHHHHCCHHHH		48.7226320211
148AcetylationIMSVRALKSCSPELQ
HHHHHHHHHCCHHHH		48.7226051181
149PhosphorylationMSVRALKSCSPELQQ
HHHHHHHHCCHHHHH		22.2223663014
151PhosphorylationVRALKSCSPELQQKF
HHHHHHCCHHHHHHH		28.6225159151
157UbiquitinationCSPELQQKFRSETIT
CCHHHHHHHHHCCCC		29.77-
157AcetylationCSPELQQKFRSETIT
CCHHHHHHHHHCCCC		29.7721466224
1572-HydroxyisobutyrylationCSPELQQKFRSETIT
CCHHHHHHHHHCCCC		29.77-
160PhosphorylationELQQKFRSETITEEE
HHHHHHHHCCCCHHH		42.0729514088
162PhosphorylationQQKFRSETITEEELV
HHHHHHCCCCHHHHH		34.1529514088
164PhosphorylationKFRSETITEEELVGL
HHHHCCCCHHHHHHH		44.7729514088
172SulfoxidationEEELVGLMNKFVEDT
HHHHHHHHHHHHHHH		4.1630846556
174UbiquitinationELVGLMNKFVEDTKK
HHHHHHHHHHHHHHC		36.5021906983
1802-HydroxyisobutyrylationNKFVEDTKKGVHQKE
HHHHHHHHCCCCCCC		60.91-
181AcetylationKFVEDTKKGVHQKEG
HHHHHHHCCCCCCCC		69.157695795
186MalonylationTKKGVHQKEGWPSSA
HHCCCCCCCCCCHHH		43.2326320211
1862-HydroxyisobutyrylationTKKGVHQKEGWPSSA
HHCCCCCCCCCCHHH		43.23-
186UbiquitinationTKKGVHQKEGWPSSA
HHCCCCCCCCCCHHH		43.2321890473
186AcetylationTKKGVHQKEGWPSSA
HHCCCCCCCCCCHHH		43.2323954790
191PhosphorylationHQKEGWPSSAYGVTK
CCCCCCCHHHCCCHH		22.5325307156
192PhosphorylationQKEGWPSSAYGVTKI
CCCCCCHHHCCCHHH		22.7928857561
194PhosphorylationEGWPSSAYGVTKIGV
CCCCHHHCCCHHHHH		17.6821253578
198AcetylationSSAYGVTKIGVTVLS
HHHCCCHHHHHHHHH		34.7526051181
202PhosphorylationGVTKIGVTVLSRIHA
CCHHHHHHHHHHHHH		15.5420068231
205PhosphorylationKIGVTVLSRIHARKL
HHHHHHHHHHHHHHH		25.5020068231
213PhosphorylationRIHARKLSEQRKGDK
HHHHHHHHHHCCCCE		34.4220068231
220UbiquitinationSEQRKGDKILLNACC
HHHCCCCEEEEECCC		43.87-
227GlutathionylationKILLNACCPGWVRTD
EEEEECCCCCCCCCC		3.0322833525
239UbiquitinationRTDMAGPKATKSPEE
CCCCCCCCCCCCHHC		68.70-
239CarboxyethylationRTDMAGPKATKSPEE
CCCCCCCCCCCCHHC		68.708421682
239N6-1-carboxyethyl lysineRTDMAGPKATKSPEE
CCCCCCCCCCCCHHC		68.70-
242UbiquitinationMAGPKATKSPEEGAE
CCCCCCCCCHHCCCC		69.72-
243PhosphorylationAGPKATKSPEEGAET
CCCCCCCCHHCCCCC		32.9420873877
250PhosphorylationSPEEGAETPVYLALL
CHHCCCCCCEEEEEC		19.9528857561
253PhosphorylationEGAETPVYLALLPPD
CCCCCCEEEEECCCC		6.3520873877
270PhosphorylationGPHGQFVSEKRVEQW
CCCCCCCCHHHCCCC		38.3928857561
2722-HydroxyisobutyrylationHGQFVSEKRVEQW--
CCCCCCHHHCCCC--		54.99-
272UbiquitinationHGQFVSEKRVEQW--
CCCCCCHHHCCCC--		54.99-
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 CBR1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CBR1_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 CBR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBM12_HUMANRBM12physical
26344197
MYH1_HUMANMYH1physical
26496610
ICAM5_HUMANICAM5physical
26496610
APBA3_HUMANAPBA3physical
26496610
Z518A_HUMANZNF518Aphysical
26496610
TXN4A_HUMANTXNL4Aphysical
26496610
SC61B_HUMANSEC61Bphysical
26496610
DEND3_HUMANDENND3physical
26496610
NCBP2_HUMANNCBP2physical
26496610
ZC3HD_HUMANZC3H13physical
26496610
FAF2_HUMANFAF2physical
26496610
PKHM2_HUMANPLEKHM2physical
26496610
TM208_HUMANTMEM208physical
26496610
WAC_HUMANWACphysical
26496610
PPHLN_HUMANPPHLN1physical
26496610
CBR1_HUMANCBR1physical
26381805
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
DB00997Doxorubicin
DB00502Haloperidol
DB01046Lubiprostone
DB04844Tetrabenazine
Regulatory Network of CBR1_HUMAN

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Related Literatures of Post-Translational Modification
N6-1-carboxyethyl lysine
ReferencePubMed
"Carboxyethyllysine in a protein: native carbonyl reductase/NADP(+)-dependent prostaglandin dehydrogenase.";
Krook M., Ghosh D., Stroemberg R., Carlquist M., Joernvall H.;
Proc. Natl. Acad. Sci. U.S.A. 90:502-506(1993).
Cited for: PARTIAL PROTEIN SEQUENCE, AND N6-1-CARBOXYETHYLATION AT LYS-239.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-194, AND MASSSPECTROMETRY.

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