AK1A1_HUMAN - dbPTM
AK1A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AK1A1_HUMAN
UniProt AC P14550
Protein Name Alcohol dehydrogenase [NADP(+)]
Gene Name AKR1A1
Organism Homo sapiens (Human).
Sequence Length 325
Subcellular Localization
Protein Description Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN)..
Protein Sequence MAASCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKAVPREELFVTSKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPDEPVLLEEPVVLALAEKYGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVPMLTVDGKRVPRDAGHPLYPFNDPY
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------MAASCVLLH
------CCCEEEEEE		14.2125944712
4Phosphorylation----MAASCVLLHTG
----CCCEEEEEECC		8.6728857561
13AcetylationVLLHTGQKMPLIGLG
EEEECCCCCCEEEEE		43.7825953088
13UbiquitinationVLLHTGQKMPLIGLG
EEEECCCCCCEEEEE		43.78-
21PhosphorylationMPLIGLGTWKSEPGQ
CCEEEEECCCCCCCH		34.4628857561
23AcetylationLIGLGTWKSEPGQVK
EEEEECCCCCCCHHH		44.7925953088
23SumoylationLIGLGTWKSEPGQVK
EEEEECCCCCCCHHH		44.79-
23UbiquitinationLIGLGTWKSEPGQVK
EEEEECCCCCCCHHH		44.7921906983
24PhosphorylationIGLGTWKSEPGQVKA
EEEECCCCCCCHHHH		40.3528857561
30UbiquitinationKSEPGQVKAAVKYAL
CCCCCHHHHHHHHHH		23.81-
35PhosphorylationQVKAAVKYALSVGYR
HHHHHHHHHHHCCCC		13.2328152594
38PhosphorylationAAVKYALSVGYRHID
HHHHHHHHCCCCEEE		12.8124275569
50PhosphorylationHIDCAAIYGNEPEIG
EEEEEEHHCCCCHHH		14.7975275
61UbiquitinationPEIGEALKEDVGPGK
CHHHHHHHHCCCCCC		59.94-
68UbiquitinationKEDVGPGKAVPREEL
HHCCCCCCCCCHHHH		49.7121906983
79PhosphorylationREELFVTSKLWNTKH
HHHHEEEECCCCCCC		22.0528857561
80UbiquitinationEELFVTSKLWNTKHH
HHHEEEECCCCCCCC		48.4321890473
85UbiquitinationTSKLWNTKHHPEDVE
EECCCCCCCCHHHCH		36.38-
112SulfoxidationEYLDLYLMHWPYAFE
HHHHHHHHHHCCCHH		1.6430846556
127SuccinylationRGDNPFPKNADGTIC
CCCCCCCCCCCCCEE		66.21-
127SuccinylationRGDNPFPKNADGTIC
CCCCCCCCCCCCCEE		66.21-
127AcetylationRGDNPFPKNADGTIC
CCCCCCCCCCCCCEE		66.2123749302
127MalonylationRGDNPFPKNADGTIC
CCCCCCCCCCCCCEE		66.2126320211
127UbiquitinationRGDNPFPKNADGTIC
CCCCCCCCCCCCCEE		66.21-
132PhosphorylationFPKNADGTICYDSTH
CCCCCCCCEECCCCC		14.3928857561
134S-nitrosylationKNADGTICYDSTHYK
CCCCCCEECCCCCHH		2.8719483679
134S-nitrosocysteineKNADGTICYDSTHYK
CCCCCCEECCCCCHH		2.87-
137PhosphorylationDGTICYDSTHYKETW
CCCEECCCCCHHHHH		7.21187103
138PhosphorylationGTICYDSTHYKETWK
CCEECCCCCHHHHHH		26.7428857561
140PhosphorylationICYDSTHYKETWKAL
EECCCCCHHHHHHHH		15.5928857561
141UbiquitinationCYDSTHYKETWKALE
ECCCCCHHHHHHHHH		40.85-
143PhosphorylationDSTHYKETWKALEAL
CCCCHHHHHHHHHHH		28.2828857561
145UbiquitinationTHYKETWKALEALVA
CCHHHHHHHHHHHHH		50.98-
145SuccinylationTHYKETWKALEALVA
CCHHHHHHHHHHHHH		50.98-
145SuccinylationTHYKETWKALEALVA
CCHHHHHHHHHHHHH		50.98-
153UbiquitinationALEALVAKGLVQALG
HHHHHHHHHHHHHHC		45.3521906983
162PhosphorylationLVQALGLSNFNSRQI
HHHHHCCCCCCCCCH		37.2663726743
177PhosphorylationDDILSVASVRPAVLQ
HHHHHHHHCCCEEEE		19.2624719451
208PhosphorylationQARGLEVTAYSPLGS
HHCCCEEEEECCCCC		15.5328152594
210PhosphorylationRGLEVTAYSPLGSSD
CCCEEEEECCCCCCC		11.0628152594
211PhosphorylationGLEVTAYSPLGSSDR
CCEEEEECCCCCCCC		15.9325159151
215PhosphorylationTAYSPLGSSDRAWRD
EEECCCCCCCCCCCC		36.4328152594
216PhosphorylationAYSPLGSSDRAWRDP
EECCCCCCCCCCCCC		29.3528152594
263UbiquitinationRKVICIPKSITPSRI
CEEEEEECCCCHHHH		34.28-
263AcetylationRKVICIPKSITPSRI
CEEEEEECCCCHHHH		34.2826051181
263MalonylationRKVICIPKSITPSRI
CEEEEEECCCCHHHH		34.2826320211
266PhosphorylationICIPKSITPSRILQN
EEEECCCCHHHHHCC		23.4627251275
268PhosphorylationIPKSITPSRILQNIK
EECCCCHHHHHCCCE		24.2524719451
275UbiquitinationSRILQNIKVFDFTFS
HHHHCCCEEEECCCC		44.38-
280PhosphorylationNIKVFDFTFSPEEMK
CCEEEECCCCHHHHH		25.6628857561
282PhosphorylationKVFDFTFSPEEMKQL
EEEECCCCHHHHHHH		28.4869004315
286SulfoxidationFTFSPEEMKQLNALN
CCCCHHHHHHHHHCC		2.9821406390
287UbiquitinationTFSPEEMKQLNALNK
CCCHHHHHHHHHCCC		55.7121906983
287AcetylationTFSPEEMKQLNALNK
CCCHHHHHHHHHCCC		55.7125953088
294UbiquitinationKQLNALNKNWRYIVP
HHHHHCCCCCEEEEE		59.75-
298PhosphorylationALNKNWRYIVPMLTV
HCCCCCEEEEEEEEE		9.6329496907
304PhosphorylationRYIVPMLTVDGKRVP
EEEEEEEEECCEECC		15.4227050516
308UbiquitinationPMLTVDGKRVPRDAG
EEEEECCEECCCCCC		45.84-
319PhosphorylationRDAGHPLYPFNDPY-
CCCCCCCCCCCCCC-		15.3827642862
325PhosphorylationLYPFNDPY-------
CCCCCCCC-------		33.777425323
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 AK1A1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AK1A1_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 AK1A1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CK054_HUMANC11orf54physical
26344197
GNPI2_HUMANGNPDA2physical
26344197
G6PI_HUMANGPIphysical
26344197
GRHPR_HUMANGRHPRphysical
26344197
MEMO1_HUMANMEMO1physical
26344197
PCBP1_HUMANPCBP1physical
26344197
PDCD6_HUMANPDCD6physical
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
DB00997Doxorubicin
DB00898Ethanol
Regulatory Network of AK1A1_HUMAN

loading...

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.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory