Thr3
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Home > Phosphorylation Site Page: > Thr3  -  Huntingtin (human)

Site Information
_____MAtLEkLMkA   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 10206804

In vivo Characterization
Methods used to characterize site in vivo:
immunoprecipitation ( 8 ) , mass spectrometry ( 11 , 13 ) , mass spectrometry (in vitro) ( 4 , 5 ) , microscopy-colocalization with upstream kinase ( 13 ) , mutation of modification site ( 1 , 3 , 4 , 8 , 10 , 12 , 13 ) , phospho-antibody ( 4 , 5 , 8 , 13 ) , western blotting ( 4 , 5 , 8 , 10 , 12 , 13 )
Disease tissue studied:
Huntington's disease ( 10 )
Relevant cell line - cell type - tissue:
'brain, cerebral cortex' ( 13 ) , 'brain, striatum' ( 13 ) , 293 (epithelial) ( 4 , 11 ) , E.coli (bacterial) ( 3 , 5 ) , eye cell ( 13 ) , HEK293T (epithelial) ( 1 , 5 , 8 , 10 , 12 ) , HeLa (cervical) ( 13 ) , monocyte-blood ( 8 ) , ST14A ( 13 )

Upstream Regulation
Putative in vivo kinases:
GCK (human) ( 5 ) , HGK (human) ( 5 ) , IKKB (human) ( 10 ) , TNIK (human) ( 5 )
Kinases, in vitro:
GCK (human) ( 5 ) , HGK (human) ( 5 ) , TNIK (human) ( 5 )

Downstream Regulation
Effects of modification on Huntingtin:
molecular association, regulation ( 3 , 13 ) , phosphorylation ( 1 ) , protein conformation ( 7 , 8 , 9 ) , protein stabilization ( 9 )
Induce interaction with:
Huntingtin (human) ( 3 , 13 )

Disease / Diagnostics Relevance
Relevant diseases:
Huntington's disease ( 8 )

References 

1

Cariulo C, et al. (2023) IKBKB reduces huntingtin aggregation by phosphorylating serine 13 via a non-canonical IKK pathway. Life Sci Alliance 6
37553253   Curated Info

2

Chiki A, et al. (2021) Investigating Crosstalk Among PTMs Provides Novel Insight Into the Structural Basis Underlying the Differential Effects of Nt17 PTMs on Mutant Httex1 Aggregation. Front Mol Biosci 8, 686086
34381813   Curated Info

3

Groover SE, Beasley M, Ramamurthy V, Legleiter J (2020) Phosphomimetic Mutations Impact Huntingtin Aggregation in the Presence of a Variety of Lipid Systems. Biochemistry 59, 4681-4693
33256402   Curated Info

4

Hegde RN, et al. (2020) TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington's disease models. EMBO J 39, e104671
32757223   Curated Info

5

Chiki A, et al. (2020) Site-specific phosphorylation of Huntingtin exon 1 recombinant proteins enabled by the discovery of novel kinases. Chembiochem
32805086   Curated Info

6

Cariulo C, et al. (2019) Ultrasensitive quantitative measurement of huntingtin phosphorylation at residue S13. Biochem Biophys Res Commun
31677786   Curated Info

7

Deguire SM, et al. (2018) N-terminal Huntingtin (Htt) phosphorylation is a molecular switch regulating Htt aggregation, helical conformation, internalization, and nuclear targeting. J Biol Chem
30185623   Curated Info

8

Cariulo C, et al. (2017) Phosphorylation of huntingtin at residue T3 is decreased in Huntington's disease and modulates mutant huntingtin protein conformation. Proc Natl Acad Sci U S A 114, E10809-E10818
29162692   Curated Info

9

Chiki A, et al. (2017) Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6. Angew Chem Int Ed Engl 56, 5202-5207
28334491   Curated Info

10

Bustamante MB, et al. (2015) Detection of huntingtin exon 1 phosphorylation by Phos-Tag SDS-PAGE: Predominant phosphorylation on threonine 3 and regulation by IKKβ. Biochem Biophys Res Commun 463, 1317-22
26106822   Curated Info

11

Huang B, et al. (2015) Scalable production in human cells and biochemical characterization of full-length normal and mutant huntingtin. PLoS One 10, e0121055
25799558   Curated Info

12

Fodale V, et al. (2014) Polyglutamine- and temperature-dependent conformational rigidity in mutant huntingtin revealed by immunoassays and circular dichroism spectroscopy. PLoS One 9, e112262
25464275   Curated Info

13

Aiken CT, et al. (2009) Phosphorylation of threonine 3: implications for Huntingtin aggregation and neurotoxicity. J Biol Chem 284, 29427-36
19710014   Curated Info

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