ALDR_HUMAN - dbPTM
ALDR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALDR_HUMAN
UniProt AC P15121
Protein Name Aldose reductase
Gene Name AKR1B1
Organism Homo sapiens (Human).
Sequence Length 316
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies..
Protein Sequence MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALLSCTSHKDYPFHEEF
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------MASRLLLNN
------CCCCEECCC		11.898281941
3Phosphorylation-----MASRLLLNNG
-----CCCCEECCCC		23.3525159151
12UbiquitinationLLLNNGAKMPILGLG
EECCCCCCCCEECCC		46.7521906983
12AcetylationLLLNNGAKMPILGLG
EECCCCCCCCEECCC		46.7525953088
20PhosphorylationMPILGLGTWKSPPGQ
CCEECCCCCCCCCCC		34.4621406692
22AcetylationILGLGTWKSPPGQVT
EECCCCCCCCCCCHH		53.5825953088
22UbiquitinationILGLGTWKSPPGQVT
EECCCCCCCCCCCHH		53.58-
23PhosphorylationLGLGTWKSPPGQVTE
ECCCCCCCCCCCHHH		28.0825159151
29PhosphorylationKSPPGQVTEAVKVAI
CCCCCCHHHHHHEEE		15.4426437602
40PhosphorylationKVAIDVGYRHIDCAH
HEEEEECCCEEEEEE		10.005051185
49PhosphorylationHIDCAHVYQNENEVG
EEEEEEEEECCCCHH		8.8571673
62UbiquitinationVGVAIQEKLREQVVK
HHHHHHHHHHHHHCC		36.15-
69UbiquitinationKLREQVVKREELFIV
HHHHHHCCHHHHHHE		56.06-
77PhosphorylationREELFIVSKLWCTYH
HHHHHHEEEEHHHHH		19.7421712546
83PhosphorylationVSKLWCTYHEKGLVK
EEEEHHHHHHHCCHH		12.5825839225
86UbiquitinationLWCTYHEKGLVKGAC
EHHHHHHHCCHHHHH		44.2121906983
86AcetylationLWCTYHEKGLVKGAC
EHHHHHHHCCHHHHH		44.2119608861
90UbiquitinationYHEKGLVKGACQKTL
HHHHCCHHHHHHHHH		45.92-
95SuccinylationLVKGACQKTLSDLKL
CHHHHHHHHHHHHCC		51.8523954790
95UbiquitinationLVKGACQKTLSDLKL
CHHHHHHHHHHHHCC		51.8519608861
95AcetylationLVKGACQKTLSDLKL
CHHHHHHHHHHHHCC		51.8519608861
96PhosphorylationVKGACQKTLSDLKLD
HHHHHHHHHHHHCCC		12.9622673903
98PhosphorylationGACQKTLSDLKLDYL
HHHHHHHHHHCCCCE		46.2422673903
104PhosphorylationLSDLKLDYLDLYLIH
HHHHCCCCEEEEEEC		16.74119561
108PhosphorylationKLDYLDLYLIHWPTG
CCCCEEEEEECCCCC		11.8622673903
117AcetylationIHWPTGFKPGKEFFP
ECCCCCCCCCCCCCC		54.9625825284
173AcetylationQVEMILNKPGLKYKP
EEEEHHCCCCCCCCC		36.7026051181
178PhosphorylationLNKPGLKYKPAVNQI
HCCCCCCCCCCCCEE		27.5226437602
179SuccinylationNKPGLKYKPAVNQIE
CCCCCCCCCCCCEEE		25.5527452117
179UbiquitinationNKPGLKYKPAVNQIE
CCCCCCCCCCCCEEE		25.55-
190PhosphorylationNQIECHPYLTQEKLI
CEEECCCCCCHHHHH		9.9427259358
192PhosphorylationIECHPYLTQEKLIQY
EECCCCCCHHHHHHH		28.9227259358
195AcetylationHPYLTQEKLIQYCQS
CCCCCHHHHHHHHHH		40.8625038526
195UbiquitinationHPYLTQEKLIQYCQS
CCCCCHHHHHHHHHH		40.86-
199PhosphorylationTQEKLIQYCQSKGIV
CHHHHHHHHHHCCEE		5.8614583555
200S-palmitoylationQEKLIQYCQSKGIVV
HHHHHHHHHHCCEEE		1.7929575903
202PhosphorylationKLIQYCQSKGIVVTA
HHHHHHHHCCEEEEE		29.3228857561
208PhosphorylationQSKGIVVTAYSPLGS
HHCCEEEEEECCCCC		14.6920873877
210PhosphorylationKGIVVTAYSPLGSPD
CCEEEEEECCCCCCC		11.0620873877
211PhosphorylationGIVVTAYSPLGSPDR
CEEEEEECCCCCCCC		15.9327422710
215PhosphorylationTAYSPLGSPDRPWAK
EEECCCCCCCCCCCC		31.1720873877
218MethylationSPLGSPDRPWAKPED
CCCCCCCCCCCCCCC		31.85-
222UbiquitinationSPDRPWAKPEDPSLL
CCCCCCCCCCCCCHH		45.1019608861
222MethylationSPDRPWAKPEDPSLL
CCCCCCCCCCCCCHH		45.1019608861
222AcetylationSPDRPWAKPEDPSLL
CCCCCCCCCCCCCHH		45.1019608861
227PhosphorylationWAKPEDPSLLEDPRI
CCCCCCCCHHCCHHH		58.8929978859
233MethylationPSLLEDPRIKAIAAK
CCHHCCHHHHHHHHH		56.19-
240UbiquitinationRIKAIAAKHNKTTAQ
HHHHHHHHCCCCCHH		38.39-
243AcetylationAIAAKHNKTTAQVLI
HHHHHCCCCCHHHHE		47.1525825284
243UbiquitinationAIAAKHNKTTAQVLI
HHHHHCCCCCHHHHE		47.15-
244PhosphorylationIAAKHNKTTAQVLIR
HHHHCCCCCHHHHEE		32.4528857561
245PhosphorylationAAKHNKTTAQVLIRF
HHHCCCCCHHHHEEC		19.3926437602
263MalonylationRNLVVIPKSVTPERI
CCEEEECCCCCHHHH		46.5726320211
263UbiquitinationRNLVVIPKSVTPERI
CCEEEECCCCCHHHH		46.5721890473
263AcetylationRNLVVIPKSVTPERI
CCEEEECCCCCHHHH		46.5719608861
264PhosphorylationNLVVIPKSVTPERIA
CEEEECCCCCHHHHH		26.35101680295
266PhosphorylationVVIPKSVTPERIAEN
EEECCCCCHHHHHHH		26.9072260439
282PhosphorylationKVFDFELSSQDMTTL
EEEEEEECCCCHHHH		20.8228857561
283PhosphorylationVFDFELSSQDMTTLL
EEEEEECCCCHHHHH		42.7128857561
288PhosphorylationLSSQDMTTLLSYNRN
ECCCCHHHHHHCCCC		21.0428857561
299S-nitrosocysteineYNRNWRVCALLSCTS
CCCCCEEEEEEECCC		1.33-
299GlutathionylationYNRNWRVCALLSCTS
CCCCCEEEEEEECCC		1.339398310
299S-nitrosylationYNRNWRVCALLSCTS
CCCCCEEEEEEECCC		1.3322178444
303PhosphorylationWRVCALLSCTSHKDY
CEEEEEEECCCCCCC		19.0528857561
304S-nitrosocysteineRVCALLSCTSHKDYP
EEEEEEECCCCCCCC		4.58-
304S-nitrosylationRVCALLSCTSHKDYP
EEEEEEECCCCCCCC		4.5819483679
305PhosphorylationVCALLSCTSHKDYPF
EEEEEECCCCCCCCC		30.4128857561
306PhosphorylationCALLSCTSHKDYPFH
EEEEECCCCCCCCCC		32.6328857561
308AcetylationLLSCTSHKDYPFHEE
EEECCCCCCCCCCCC		59.7425825284
308UbiquitinationLLSCTSHKDYPFHEE
EEECCCCCCCCCCCC		59.74-
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 ALDR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ALDR_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 ALDR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DHSO_HUMANSORDphysical
22939629
AK1BF_HUMANAKR1B15physical
26186194
MEMO1_HUMANMEMO1physical
26344197
AK1BF_HUMANAKR1B15physical
28514442
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
DB00605Sulindac
Regulatory Network of ALDR_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 ALA-2, AND MASS SPECTROMETRY.
"Sequence of pig lens aldose reductase and electrospray massspectrometry of non-covalent and covalent complexes.";
Jaquinod M., Potier N., Klarskov K., Reymann J.-M., Sorokine O.,Kieffer S., Barth P., Andriantomanga V., Biellmann J.-F.,van Dorsselaer A.;
Eur. J. Biochem. 218:893-903(1993).
Cited for: PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT ALA-2.
"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-95; LYS-222 AND LYS-263, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND TYR-40, AND MASSSPECTROMETRY.

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