Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Sulfotransferase 1A2  

UniProtKB / Swiss-Prot ID :  ST1A2_HUMAN

Gene Name (Synonyms) : 
SULT1A2, STP2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Is also responsible for the sulfonation and activation of minoxidil. Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk. 

Protein Sequence MELIQDISRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDMIYQGGDLEKC...
Predicted Secondary Structure CCCCCHHCCCCCCEEECCCCHHHHHHHHHHHHHCCCCCCCEEEEECCCCCHHHHHHHHHHHHHCCCHHHH...
Protein Variant
LocationDescription
7I -> T. VAR_007426
19P -> L (in dbSNP:rs10797300). VAR_057340
62Y -> F (in dbSNP:rs4987024). VAR_057341
235N -> T (in dbSNP:rs1059491). VAR_007427
239N -> S (in dbSNP:rs45472392). VAR_057342
282K -> E (in dbSNP:rs27742). VAR_061887
- top -

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
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
106N6-acetyllysinePRLLKTHLP
CCEEECCCC
38.19Phosphositeplus
Link
106N6-acetyllysine.PRLLKTHLP
CCEEECCCC
38.19UniProtKB
Link
122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LLDQKVKVV
HHHCCCEEE
43.63Phosphositeplus
Link
193PhosphotyrosineLYLFYEDMK
EEEEHHHHH
14.39Phosphositeplus
Link
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SIA8D_HUMANENSP00000338742STRING
PAPS2_HUMANENSP00000338742STRING
- top -

Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
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-106, AND MASS SPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures