ST1A2_HUMAN - dbPTM
ST1A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ST1A2_HUMAN
UniProt AC P50226
Protein Name Sulfotransferase 1A2
Gene Name SULT1A2
Organism Homo sapiens (Human).
Sequence Length 295
Subcellular Localization Cytoplasm.
Protein Description 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 MELIQDISRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDMIYQGGDLEKCHRAPIFMRVPFLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALLPQTLLDQKVKVVYVARNAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDLMVEHTSFKEMKKNPMTNYTTVRREFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAKKMAGCSLSFRSEL
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
8PhosphorylationMELIQDISRPPLEYV
CCCCCCCCCCCHHHH		47.2026330541
14PhosphorylationISRPPLEYVKGVPLI
CCCCCHHHHCCCHHH		18.3626330541
23PhosphorylationKGVPLIKYFAEALGP
CCCHHHHHHHHHHCC		10.8826330541
33PhosphorylationEALGPLQSFQARPDD
HHHCCHHHCCCCCCC		27.3228857561
44PhosphorylationRPDDLLISTYPKSGT
CCCCEEEEECCCCCC		23.1226330541
45PhosphorylationPDDLLISTYPKSGTT
CCCEEEEECCCCCCC		36.5326330541
46PhosphorylationDDLLISTYPKSGTTW
CCEEEEECCCCCCCH		11.2426330541
49PhosphorylationLISTYPKSGTTWVSQ
EEEECCCCCCCHHHH		36.55-
69UbiquitinationYQGGDLEKCHRAPIF
HCCCCHHHHHCCCEE		42.51-
106UbiquitinationTPAPRLLKTHLPLAL
CCCCHHHHHCCCHHH		38.1921890473
106AcetylationTPAPRLLKTHLPLAL
CCCCHHHHHCCCHHH		38.1969739
106UbiquitinationTPAPRLLKTHLPLAL
CCCCHHHHHCCCHHH		38.1921890473
107PhosphorylationPAPRLLKTHLPLALL
CCCHHHHHCCCHHHC		28.72-
117PhosphorylationPLALLPQTLLDQKVK
CHHHCCHHHHCCCCE		27.61-
122UbiquitinationPQTLLDQKVKVVYVA
CHHHHCCCCEEEEEE		43.6321906983
124UbiquitinationTLLDQKVKVVYVARN
HHHCCCCEEEEEECC		32.7833845483
138PhosphorylationNAKDVAVSYYHFYHM
CCHHHHHHHHEHHHH		15.3828258704
140PhosphorylationKDVAVSYYHFYHMAK
HHHHHHHHEHHHHCC		4.30-
193PhosphorylationHPVLYLFYEDMKENP
CCEEHHCHHHHHHCH		14.3921253578
197UbiquitinationYLFYEDMKENPKREI
HHCHHHHHHCHHHHH		67.6622817900
201UbiquitinationEDMKENPKREIQKIL
HHHHHCHHHHHHHHH		74.3922817900
208UbiquitinationKREIQKILEFVGRSL
HHHHHHHHHHHHCCC		5.5724816145
249UbiquitinationTVRREFMDHSISPFM
HHHHHHHHCCCCHHH		37.3924816145
250UbiquitinationVRREFMDHSISPFMR
HHHHHHHCCCCHHHH		18.4232015554
251PhosphorylationRREFMDHSISPFMRK
HHHHHHCCCCHHHHC		22.0926330541
253PhosphorylationEFMDHSISPFMRKGM
HHHHCCCCHHHHCCC		18.3326330541
283UbiquitinationFDADYAKKMAGCSLS
CCHHHHHHHCCCCCE		26.3029967540
288PhosphorylationAKKMAGCSLSFRSEL
HHHHCCCCCEECCCC		26.5720873877
288UbiquitinationAKKMAGCSLSFRSEL
HHHHCCCCCEECCCC		26.5724816145
290PhosphorylationKMAGCSLSFRSEL--
HHCCCCCEECCCC--		11.4320873877
293PhosphorylationGCSLSFRSEL-----
CCCCEECCCC-----		41.0426434776
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 ST1A2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ST1A2_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 ST1A2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NIF3L_HUMANNIF3L1physical
25416956
ST1A3_HUMANSULT1A3physical
26186194
ST1A4_HUMANSULT1A3physical
26186194
TPPC3_HUMANTRAPPC3physical
26186194
TPPC9_HUMANTRAPPC9physical
26186194
CACO2_HUMANCALCOCO2physical
26186194
ST1A3_HUMANSULT1A3physical
28514442
ST1A4_HUMANSULT1A3physical
28514442
CACO2_HUMANCALCOCO2physical
28514442
TPPC9_HUMANTRAPPC9physical
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
There are no disease associations of PTM sites.
Regulatory Network of ST1A2_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-106, AND MASS SPECTROMETRY.

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