Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Aldo-keto reductase family 1 member C2  

UniProtKB / Swiss-Prot ID :  AK1C2_HUMAN

Gene Name (Synonyms) : 
AKR1C2, DDH2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm (Potential). 

Protein Function :  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 MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIA...
Predicted Secondary Structure CCCCCCEEEECCCCEEEEEEEEECCCCCCCHHHHHHHHHHHHHCCCCEEECHHHHCCHHHHHHHHHHHHH...
Protein Variant
LocationDescription
46F -> Y (in dbSNP:rs2854482). VAR_048216
79I -> V (in SRXY8; partially impairedactivity).
90H -> Q (in SRXY8; partially impairedactivity).
172L -> Q (in dbSNP:rs11474). VAR_014748
222H -> Q (in SRXY8; partially impairedactivity).
300N -> T (in SRXY8; partially impairedactivity).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
1N-acetylmethionine.----MDSKY
----CCCCC
13.65UniProtKB
Link-
4N6-acetyllysine-MDSKYQCV
-CCCCCCEE
34.77HPRD
Link
4N6-acetyllysine.-MDSKYQCV
-CCCCCCEE
34.77UniProtKB
Link
5PhosphotyrosineMDSKYQCVK
CCCCCCEEE
15.88Phosphositeplus
Link
24PhosphotyrosineGFGTYAPAE
EEEECCCCC
15.80Phosphositeplus
Link
31N6-acetyllysineAEVPKSKAL
CCCCHHHHH
70.53HPRD
Link
75N6-acetyllysineDGSVKREDI
CCCCCCEEE
52.33HPRD
Link
81PhosphotyrosineEDIFYTSKL
EEEEEEEEC
15.50Phosphositeplus
Link
161N6-acetyllysineAGLAKSIGV
CCCEEEEEE
47.88HPRD
Link
161N6-acetyllysineAGLAKSIGV
CCCEEEEEE
47.88Phosphositeplus
Link
161N6-acetyllysine.AGLAKSIGV
CCCEEEEEE
47.88UniProtKB
Link
179N6-acetyllysineMILNKPGLK
HHHHHCCCC
36.70HPRD
Link
179N6-acetyllysineMILNKPGLK
HHHHHCCCC
36.70Phosphositeplus
Link
179N6-acetyllysine.MILNKPGLK
HHHHHCCCC
36.70UniProtKB
Link
196PhosphotyrosineECHPYFNQR
ECCCCCCCH
7.47Phosphositeplus
Link
207N6-acetyllysineLDFCKSKDI
HHHHHHCCC
61.61HPRD
Link
270N6-acetyllysineVVLAKSYNE
EEEECCCCH
49.68HPRD
Link
270N6-acetyllysineVVLAKSYNE
EEEECCCCH
49.68Phosphositeplus
Link
305PhosphotyrosineRNVRYLTLD
CCCCCCCCH
10.35Phosphositeplus
Link
317PhosphotyrosineGPPNYPFSD
CCCCCCCCC
16.07Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
OMIM disease
61427946,XY sex reversal 8 (SRXY8)
Drug Reference
DrugBank
DB01586Ursodeoxycholic acid
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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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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures