AK1C2_HUMAN - dbPTM
AK1C2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AK1C2_HUMAN
UniProt AC P52895
Protein Name Aldo-keto reductase family 1 member C2
Gene Name AKR1C2
Organism Homo sapiens (Human).
Sequence Length 323
Subcellular Localization Cytoplasm .
Protein Description Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Has a high bile-binding ability..
Protein Sequence MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPFSDEY
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
1Acetylation-------MDSKYQCV
-------CCCCCEEE		13.65-
4Acetylation----MDSKYQCVKLN
----CCCCCEEEECC		34.7719608861
4Sumoylation----MDSKYQCVKLN
----CCCCCEEEECC		34.7719608861
4Ubiquitination----MDSKYQCVKLN
----CCCCCEEEECC		34.7719608861
4Sumoylation----MDSKYQCVKLN
----CCCCCEEEECC		34.77-
5Phosphorylation---MDSKYQCVKLND
---CCCCCEEEECCC		15.8883941
9SumoylationDSKYQCVKLNDGHFM
CCCCEEEECCCCCEE		49.55-
9UbiquitinationDSKYQCVKLNDGHFM
CCCCEEEECCCCCEE		49.55-
23PhosphorylationMPVLGFGTYAPAEVP
EEEECCCCCCCCCCC		17.7826356563
24PhosphorylationPVLGFGTYAPAEVPK
EEECCCCCCCCCCCH		15.8027259358
31AcetylationYAPAEVPKSKALEAV
CCCCCCCHHHHHHHH		70.5319608861
31UbiquitinationYAPAEVPKSKALEAV
CCCCCCCHHHHHHHH		70.5319608861
32PhosphorylationAPAEVPKSKALEAVK
CCCCCCHHHHHHHHH		19.6628857561
33UbiquitinationPAEVPKSKALEAVKL
CCCCCHHHHHHHHHH		64.22-
39UbiquitinationSKALEAVKLAIEAGF
HHHHHHHHHHHHHCC		38.97-
67PhosphorylationQVGLAIRSKIADGSV
HHEEEEHHHCCCCCC		23.46-
68UbiquitinationVGLAIRSKIADGSVK
HEEEEHHHCCCCCCC		31.87-
73PhosphorylationRSKIADGSVKREDIF
HHHCCCCCCCHHHCE		25.6428857561
75SumoylationKIADGSVKREDIFYT
HCCCCCCCHHHCEEE		52.33-
75UbiquitinationKIADGSVKREDIFYT
HCCCCCCCHHHCEEE		52.3319608861
75AcetylationKIADGSVKREDIFYT
HCCCCCCCHHHCEEE		52.3319608861
75SumoylationKIADGSVKREDIFYT
HCCCCCCCHHHCEEE		52.3319608861
81PhosphorylationVKREDIFYTSKLWSN
CCHHHCEEECCCCCC		15.5018083107
82PhosphorylationKREDIFYTSKLWSNS
CHHHCEEECCCCCCC		14.5027251275
83PhosphorylationREDIFYTSKLWSNSH
HHHCEEECCCCCCCC		17.8622617229
84UbiquitinationEDIFYTSKLWSNSHR
HHCEEECCCCCCCCC		46.29-
104UbiquitinationPALERSLKNLQLDYV
HHHHHHHHHCCCCEE		57.78-
104SumoylationPALERSLKNLQLDYV
HHHHHHHHHCCCCEE		57.78-
110PhosphorylationLKNLQLDYVDLYLIH
HHHCCCCEEEEEEEE		12.4022817900
123UbiquitinationIHFPVSVKPGEEVIP
EECCEEECCCCCCCC		39.54-
131SumoylationPGEEVIPKDENGKIL
CCCCCCCCCCCCCEE		67.56-
141PhosphorylationNGKILFDTVDLCATW
CCCEEEEHHHHHHHH		14.4824275569
161AcetylationCKDAGLAKSIGVSNF
HHHHCCHHHHCCCCC		47.8819608861
161UbiquitinationCKDAGLAKSIGVSNF
HHHHCCHHHHCCCCC		47.8819608861
162PhosphorylationKDAGLAKSIGVSNFN
HHHCCHHHHCCCCCH		20.9722617229
179UbiquitinationLLEMILNKPGLKYKP
HHHHHHCCCCCCCCC		36.7019608861
179AcetylationLLEMILNKPGLKYKP
HHHHHHCCCCCCCCC		36.7019608861
183UbiquitinationILNKPGLKYKPVCNQ
HHCCCCCCCCCCCCE		58.08-
184PhosphorylationLNKPGLKYKPVCNQV
HCCCCCCCCCCCCEE		26.1020561411
185UbiquitinationNKPGLKYKPVCNQVE
CCCCCCCCCCCCEEE		29.41-
196PhosphorylationNQVECHPYFNQRKLL
CEEECCCCCCHHHHH		7.4721253578
201UbiquitinationHPYFNQRKLLDFCKS
CCCCCHHHHHHHHCC		43.57-
206S-palmitoylationQRKLLDFCKSKDIVL
HHHHHHHHCCCCEEE		4.9329575903
207AcetylationRKLLDFCKSKDIVLV
HHHHHHHCCCCEEEE		61.6119608861
207UbiquitinationRKLLDFCKSKDIVLV
HHHHHHHCCCCEEEE		61.6119608861
208PhosphorylationKLLDFCKSKDIVLVA
HHHHHHCCCCEEEEE		36.4250564463
209UbiquitinationLLDFCKSKDIVLVAY
HHHHHCCCCEEEEEE		36.65-
216PhosphorylationKDIVLVAYSALGSHR
CCEEEEEECCCCCCC		6.2325867546
217PhosphorylationDIVLVAYSALGSHRE
CEEEEEECCCCCCCC		13.7925867546
221PhosphorylationVAYSALGSHREEPWV
EEECCCCCCCCCCCC		21.8825867546
232PhosphorylationEPWVDPNSPVLLEDP
CCCCCCCCCCCCCCH		23.0526657352
246AcetylationPVLCALAKKHKRTPA
HHHHHHHHHCCCCHH		57.1569741
246UbiquitinationPVLCALAKKHKRTPA
HHHHHHHHHCCCCHH		57.15-
247AcetylationVLCALAKKHKRTPAL
HHHHHHHHCCCCHHH		49.0719809595
247UbiquitinationVLCALAKKHKRTPAL
HHHHHHHHCCCCHHH		49.07-
270AcetylationRGVVVLAKSYNEQRI
CCCEEEEECCCHHHH		49.6819608861
270UbiquitinationRGVVVLAKSYNEQRI
CCCEEEEECCCHHHH		49.6819608861
272PhosphorylationVVVLAKSYNEQRIRQ
CEEEEECCCHHHHHH		23.24-
289PhosphorylationQVFEFQLTSEEMKAI
EEEEEECCHHHHHHH		24.2525072903
290PhosphorylationVFEFQLTSEEMKAID
EEEEECCHHHHHHHC		39.9028258704
294UbiquitinationQLTSEEMKAIDGLNR
ECCHHHHHHHCCCCC		45.53-
305PhosphorylationGLNRNVRYLTLDIFA
CCCCCCEEEEEEECC		10.351965335
317PhosphorylationIFAGPPNYPFSDEY-
ECCCCCCCCCCCCC-		16.071965383
323AcetylationNYPFSDEY-------
CCCCCCCC-------		28.9219608861
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 AK1C2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AK1C2_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 AK1C2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AK1C2_HUMANAKR1C2physical
11514561
IPO8_HUMANIPO8physical
26186194
AK1C4_HUMANAKR1C4physical
26186194
AK1C3_HUMANAKR1C3physical
26186194
AK1C1_HUMANAKR1C1physical
26186194
ZFP1_HUMANZFP1physical
26186194
CK054_HUMANC11orf54physical
26344197
MIF_HUMANMIFphysical
26344197
AK1C1_HUMANAKR1C1physical
28514442
AK1C4_HUMANAKR1C4physical
28514442
ZFP1_HUMANZFP1physical
28514442
AK1C3_HUMANAKR1C3physical
28514442
IPO8_HUMANIPO8physical
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
DB01586Ursodeoxycholic acid
Regulatory Network of AK1C2_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 MET-1; LYS-4; LYS-161 ANDLYS-179, AND MASS SPECTROMETRY.

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