AK1C3_HUMAN - dbPTM
AK1C3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AK1C3_HUMAN
UniProt AC P42330
Protein Name Aldo-keto reductase family 1 member C3
Gene Name AKR1C3
Organism Homo sapiens (Human).
Sequence Length 323
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the conversion of aldehydes and ketones to alcohols. Catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ) and the oxidation of 9-alpha,11-beta-PGF2 to PGD2. Functions as a bi-directional 3-alpha-, 17-beta- and 20-alpha HSD. Can interconvert active androgens, estrogens and progestins with their cognate inactive metabolites. Preferentially transforms androstenedione (4-dione) to testosterone..
Protein Sequence MDSKHQCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYFNSDSFASHPNYPYSDEY
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
3Phosphorylation-----MDSKHQCVKL
-----CCCCCCEEEC		30.6428857561
42-Hydroxyisobutyrylation----MDSKHQCVKLN
----CCCCCCEEECC		33.17-
9SumoylationDSKHQCVKLNDGHFM
CCCCCEEECCCCCEE		49.55-
10 (in isoform 2)Phosphorylation-3.3525849741
23PhosphorylationMPVLGFGTYAPPEVP
EEEECCCCCCCCCCC		17.7826356563
24PhosphorylationPVLGFGTYAPPEVPR
EEECCCCCCCCCCCH		19.9326356563
33UbiquitinationPPEVPRSKALEVTKL
CCCCCHHHHHHHHHH		59.27-
332-HydroxyisobutyrylationPPEVPRSKALEVTKL
CCCCCHHHHHHHHHH		59.27-
39UbiquitinationSKALEVTKLAIEAGF
HHHHHHHHHHHHHCC		40.89-
51PhosphorylationAGFRHIDSAHLYNNE
HCCCEEEEEECCCCH		19.58110744505
55PhosphorylationHIDSAHLYNNEEQVG
EEEEEECCCCHHHHH		13.1826356563
60UbiquitinationHLYNNEEQVGLAIRS
ECCCCHHHHHHHHHH		28.53-
64UbiquitinationNEEQVGLAIRSKIAD
CHHHHHHHHHHHCCC		6.82-
66UbiquitinationEQVGLAIRSKIADGS
HHHHHHHHHHCCCCC		26.70-
67PhosphorylationQVGLAIRSKIADGSV
HHHHHHHHHCCCCCC		23.46-
68UbiquitinationVGLAIRSKIADGSVK
HHHHHHHHCCCCCCC		31.87-
73PhosphorylationRSKIADGSVKREDIF
HHHCCCCCCCHHHCE		25.6428857561
75SumoylationKIADGSVKREDIFYT
HCCCCCCCHHHCEEE		52.33-
75UbiquitinationKIADGSVKREDIFYT
HCCCCCCCHHHCEEE		52.33-
75SumoylationKIADGSVKREDIFYT
HCCCCCCCHHHCEEE		52.33-
75AcetylationKIADGSVKREDIFYT
HCCCCCCCHHHCEEE		52.3322646271
81PhosphorylationVKREDIFYTSKLWST
CCHHHCEEEEHHHHH		15.5083945
82PhosphorylationKREDIFYTSKLWSTF
CHHHCEEEEHHHHHC		14.5027251275
83PhosphorylationREDIFYTSKLWSTFH
HHHCEEEEHHHHHCC		17.8622617229
102PhosphorylationVRPALENSLKKAQLD
HHHHHHHHHHHHHCC		31.9927499020
1042-HydroxyisobutyrylationPALENSLKKAQLDYV
HHHHHHHHHHHCCEE		45.97-
105AcetylationALENSLKKAQLDYVD
HHHHHHHHHHCCEEE		46.8130586847
110PhosphorylationLKKAQLDYVDLYLIH
HHHHHCCEEEEEEEC		12.40119569
114PhosphorylationQLDYVDLYLIHSPMS
HCCEEEEEEECCCCC		10.1128102081
118PhosphorylationVDLYLIHSPMSLKPG
EEEEEECCCCCCCCC		18.46110744511
121PhosphorylationYLIHSPMSLKPGEEL
EEECCCCCCCCCCCC		36.3026657352
129PhosphorylationLKPGEELSPTDENGK
CCCCCCCCCCCCCCC		29.0925159151
131PhosphorylationPGEELSPTDENGKVI
CCCCCCCCCCCCCEE		53.2022199227
147PhosphorylationDIVDLCTTWEAMEKC
EHHHHHHHHHHHHHH		21.9550564471
161UbiquitinationCKDAGLAKSIGVSNF
HHHHCCHHHHCCCCC		47.88-
162PhosphorylationKDAGLAKSIGVSNFN
HHHCCHHHHCCCCCC		20.9720873877
166PhosphorylationLAKSIGVSNFNRRQL
CHHHHCCCCCCHHHH		30.4120873877
179UbiquitinationQLEMILNKPGLKYKP
HHHHHHCCCCCCCCC		36.70-
183UbiquitinationILNKPGLKYKPVCNQ
HHCCCCCCCCCCCCE		58.08-
184PhosphorylationLNKPGLKYKPVCNQV
HCCCCCCCCCCCCEE		26.1020561411
185UbiquitinationNKPGLKYKPVCNQVE
CCCCCCCCCCCCEEE		29.41-
196PhosphorylationNQVECHPYFNRSKLL
CEEECCCCCCHHHHH		6.996991359
2012-HydroxyisobutyrylationHPYFNRSKLLDFCKS
CCCCCHHHHHHHHCC		50.24-
201UbiquitinationHPYFNRSKLLDFCKS
CCCCCHHHHHHHHCC		50.24-
206S-palmitoylationRSKLLDFCKSKDIVL
HHHHHHHHCCCCEEE		4.9329575903
2072-HydroxyisobutyrylationSKLLDFCKSKDIVLV
HHHHHHHCCCCEEEE		61.61-
207UbiquitinationSKLLDFCKSKDIVLV
HHHHHHHCCCCEEEE		61.61-
208PhosphorylationKLLDFCKSKDIVLVA
HHHHHHCCCCEEEEE		36.42-
209AcetylationLLDFCKSKDIVLVAY
HHHHHCCCCEEEEEE		36.6519608861
209UbiquitinationLLDFCKSKDIVLVAY
HHHHHCCCCEEEEEE		36.6519608861
217PhosphorylationDIVLVAYSALGSQRD
CEEEEEEHHCCCCCC		13.7927251275
221PhosphorylationVAYSALGSQRDKRWV
EEEHHCCCCCCCCCC		23.9227251275
232PhosphorylationKRWVDPNSPVLLEDP
CCCCCCCCCCCCCCH		23.0526657352
246UbiquitinationPVLCALAKKHKRTPA
HHHHHHHHHCCCCHH		57.1519608861
246AcetylationPVLCALAKKHKRTPA
HHHHHHHHHCCCCHH		57.1523954790
2462-HydroxyisobutyrylationPVLCALAKKHKRTPA
HHHHHHHHHCCCCHH		57.15-
247AcetylationVLCALAKKHKRTPAL
HHHHHHHHCCCCHHH		49.0719809487
247UbiquitinationVLCALAKKHKRTPAL
HHHHHHHHCCCCHHH		49.07-
270UbiquitinationRGVVVLAKSYNEQRI
CCCEEEEECCCHHHH		49.68-
270AcetylationRGVVVLAKSYNEQRI
CCCEEEEECCCHHHH		49.6822646265
272PhosphorylationVVVLAKSYNEQRIRQ
CEEEEECCCHHHHHH		23.24-
305PhosphorylationGLDRNLHYFNSDSFA
CCCCCCCCCCCCCHH		13.97119573
308PhosphorylationRNLHYFNSDSFASHP
CCCCCCCCCCHHCCC		25.4126356563
310PhosphorylationLHYFNSDSFASHPNY
CCCCCCCCHHCCCCC		23.6426356563
313PhosphorylationFNSDSFASHPNYPYS
CCCCCHHCCCCCCCC		37.1526356563
317PhosphorylationSFASHPNYPYSDEY-
CHHCCCCCCCCCCC-		14.1626356563
319PhosphorylationASHPNYPYSDEY---
HCCCCCCCCCCC---		20.5626356563
320PhosphorylationSHPNYPYSDEY----
CCCCCCCCCCC----		21.3326356563
323PhosphorylationNYPYSDEY-------
CCCCCCCC-------		28.9226356563
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 AK1C3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AK1C3_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 AK1C3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBE2W_HUMANUBE2Wphysical
16169070
ZHX1_HUMANZHX1physical
16169070
LRIF1_HUMANLRIF1physical
16169070
AK1C4_HUMANAKR1C4physical
26186194
AK1C1_HUMANAKR1C1physical
26186194
AK1D1_HUMANAKR1D1physical
26186194
AK1C1_HUMANAKR1C1physical
28514442
AK1C4_HUMANAKR1C4physical
28514442
AK1D1_HUMANAKR1D1physical
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
DB00905Bimatoprost
DB00997Doxorubicin
Regulatory Network of AK1C3_HUMAN

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Related Literatures of Post-Translational Modification

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