AK1C4_HUMAN - dbPTM
AK1C4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AK1C4_HUMAN
UniProt AC P17516
Protein Name Aldo-keto reductase family 1 member C4
Gene Name AKR1C4
Organism Homo sapiens (Human).
Sequence Length 323
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5-alpha-androstan-3-alpha,17-beta-diol (3-alpha-diol). Also has some 20-alpha-hydroxysteroid dehydrogenase activity. The biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leads to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route..
Protein Sequence MDPKYQRVELNDGHFMPVLGFGTYAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPNSPVLLEDPVLCALAKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRYVVMDFLMDHPDYPFSDEY
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
4Acetylation----MDPKYQRVELN
----CCCCCCEEECC		50.157668211
23PhosphorylationMPVLGFGTYAPPEVP
EEEECCCCCCCCCCC		17.7826356563
24PhosphorylationPVLGFGTYAPPEVPR
EEECCCCCCCCCCCC		19.9383949
39UbiquitinationNRAVEVTKLAIEAGF
CCHHHHHHHHHHHCC		40.8933845483
53PhosphorylationFRHIDSAYLYNNEEQ
CCEEEEEEEECCHHH		17.4220561399
67PhosphorylationQVGLAIRSKIADGSV
HHHEEEHHHCCCCCC		23.46-
68UbiquitinationVGLAIRSKIADGSVK
HHEEEHHHCCCCCCC		31.87-
73PhosphorylationRSKIADGSVKREDIF
HHHCCCCCCCHHHCE		25.6428857561
75AcetylationKIADGSVKREDIFYT
HCCCCCCCHHHCEEE		52.3319608861
75SumoylationKIADGSVKREDIFYT
HCCCCCCCHHHCEEE		52.33-
75UbiquitinationKIADGSVKREDIFYT
HCCCCCCCHHHCEEE		52.3324816145
75SumoylationKIADGSVKREDIFYT
HCCCCCCCHHHCEEE		52.33-
81PhosphorylationVKREDIFYTSKLWCT
CCHHHCEEEEEEEHH		15.5022817900
82PhosphorylationKREDIFYTSKLWCTF
CHHHCEEEEEEEHHC		14.5027251275
83PhosphorylationREDIFYTSKLWCTFF
HHHCEEEEEEEHHCC		17.8622617229
161AcetylationCKDAGLAKSIGVSNF
HHHCCCHHHHCCCCC		47.8819608861
161UbiquitinationCKDAGLAKSIGVSNF
HHHCCCHHHHCCCCC		47.88-
162PhosphorylationKDAGLAKSIGVSNFN
HHCCCHHHHCCCCCC		20.9720873877
166PhosphorylationLAKSIGVSNFNCRQL
CHHHHCCCCCCHHHH		30.41-
179UbiquitinationQLEMILNKPGLKYKP
HHHHHHCCCCCCCCC		36.7022817900
183UbiquitinationILNKPGLKYKPVCNQ
HHCCCCCCCCCCCCE		58.0822817900
184PhosphorylationLNKPGLKYKPVCNQV
HCCCCCCCCCCCCEE		26.1020561411
185UbiquitinationNKPGLKYKPVCNQVE
CCCCCCCCCCCCEEE		29.4122817900
196PhosphorylationNQVECHPYLNQSKLL
CEEECCCCCCHHHHH		8.4617924679
200PhosphorylationCHPYLNQSKLLDFCK
CCCCCCHHHHHHHHC		24.9746161739
201AcetylationHPYLNQSKLLDFCKS
CCCCCHHHHHHHHCC		43.2224886175
201UbiquitinationHPYLNQSKLLDFCKS
CCCCCHHHHHHHHCC		43.22-
201MalonylationHPYLNQSKLLDFCKS
CCCCCHHHHHHHHCC		43.2226320211
206S-palmitoylationQSKLLDFCKSKDIVL
HHHHHHHHCCCCEEE		4.9329575903
207AcetylationSKLLDFCKSKDIVLV
HHHHHHHCCCCEEEE		61.6119608861
207UbiquitinationSKLLDFCKSKDIVLV
HHHHHHHCCCCEEEE		61.6129901268
208PhosphorylationKLLDFCKSKDIVLVA
HHHHHHCCCCEEEEE		36.4217929957
209UbiquitinationLLDFCKSKDIVLVAH
HHHHHCCCCEEEEEE		36.65-
221PhosphorylationVAHSALGTQRHKLWV
EEECCCCCCCCCEEC		24.2317929957
232PhosphorylationKLWVDPNSPVLLEDP
CEECCCCCCCCCCCH		23.0526657352
246UbiquitinationPVLCALAKKHKQTPA
HHHHHHHHHCCCCHH		57.1529967540
246AcetylationPVLCALAKKHKQTPA
HHHHHHHHHCCCCHH		57.1519608861
247AcetylationVLCALAKKHKQTPAL
HHHHHHHHCCCCHHH		50.8819809417
247UbiquitinationVLCALAKKHKQTPAL
HHHHHHHHCCCCHHH		50.88-
270UbiquitinationRGVVVLAKSYNEQRI
CCCEEEEECCCHHHH		49.6829901268
270SuccinylationRGVVVLAKSYNEQRI
CCCEEEEECCCHHHH		49.6823954790
270AcetylationRGVVVLAKSYNEQRI
CCCEEEEECCCHHHH		49.6825825284
272PhosphorylationVVVLAKSYNEQRIRE
CEEEEECCCHHHHHH		23.24-
290PhosphorylationVFEFQLTSEDMKVLD
EEEEECCHHHHHHHH		39.9469005589
305PhosphorylationGLNRNYRYVVMDFLM
CCCCCCCEEEEEHHH		6.2450564483
317PhosphorylationFLMDHPDYPFSDEY-
HHHCCCCCCCCCCC-		15.6150564493
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 AK1C4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AK1C4_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 AK1C4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PXDC2_HUMANPLXDC2physical
26186194
PXDC2_HUMANPLXDC2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
61427946,XY sex reversal 8 (SRXY8)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AK1C4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-75 AND LYS-270, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-196, AND MASSSPECTROMETRY.

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