Ser13
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Home > Phosphorylation Site Page: > Ser13  -  Huntingtin (human)

Site Information
kLMkAFEsLksFQQQ   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 10206805

In vivo Characterization
Methods used to characterize site in vivo:
electrophoretic mobility shift ( 2 ) , immunoassay ( 6 , 7 , 8 , 15 ) , immunoprecipitation ( 4 , 14 , 16 ) , mass spectrometry ( 4 , 17 ) , mass spectrometry (in vitro) ( 4 , 5 ) , mutation of modification site ( 1 , 3 , 4 , 6 , 8 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 ) , phospho-antibody ( 1 , 2 , 4 , 5 , 6 , 7 , 14 , 16 ) , western blotting ( 1 , 2 , 4 , 5 , 6 , 9 , 10 , 13 , 14 , 15 , 16 )
Disease tissue studied:
Huntington's disease ( 6 , 9 , 10 , 11 )
Relevant cell line - cell type - tissue:
'brain, cerebral cortex' ( 16 ) , 'neuron, cortical' ( 6 ) , 'neuron, striatal' ( 6 ) , 'neuron, striatal'-brain ( 4 , 8 ) , 293 (epithelial) ( 4 , 14 ) , brain ( 6 ) , E.coli (bacterial) ( 3 , 5 ) , HEK293T (epithelial) ( 1 , 4 , 5 , 6 , 9 , 10 , 13 ) , HeLa (cervical) ( 2 , 17 ) , hTERT ( 7 ) , mononuclear-blood ( 9 ) , ST14A ( 17 ) , STHdh ('neuron, striatal') ( 6 , 11 , 15 )

Upstream Regulation
Regulatory protein:
PPP2CA (human) ( 1 )
Putative in vivo kinases:
CK2A1 (human) ( 15 ) , HGK (human) ( 5 ) , IKKB (human) ( 1 , 4 , 10 ) , IKKE (human) ( 4 ) , TBK1 (human) ( 4 , 5 ) , TNIK (human) ( 5 )
Kinases, in vitro:
HGK (human) ( 5 ) , IKKB (human) ( 4 ) , TBK1 (human) ( 4 , 5 ) , TNIK (human) ( 5 )
Treatments:
Bay_11-7082 ( 15 ) , heat_shock ( 15 ) , IC261 ( 15 ) , LY294002 ( 15 ) , okadaic_acid ( 1 , 2 ) , piceatannol ( 15 ) , Ro31-8220 ( 15 ) , siRNA ( 4 ) , staurosporine ( 2 , 15 ) , wortmannin ( 15 ) , Y27632 ( 15 )

Downstream Regulation
Effects of modification on Huntingtin:
intracellular localization ( 4 , 8 , 14 ) , molecular association, regulation ( 2 , 3 , 7 , 8 , 14 ) , protein conformation ( 8 , 9 , 15 ) , receptor internalization, induced ( 8 )
Effects of modification on biological processes:
apoptosis, inhibited ( 12 ) , cytoskeletal reorganization ( 11 ) , exocytosis, inhibited ( 2 )
Induce interaction with:
HMGB1 (human) ( 7 ) , Huntingtin (human) ( 3 )
Inhibit interaction with:
Exportin-1 (human) ( 14 ) , Huntingtin (human) ( 2 , 8 )

Disease / Diagnostics Relevance
Relevant diseases:
Huntington's disease ( 4 , 16 )

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

Ahat E, et al. (2022) GRASP55 regulates the unconventional secretion and aggregation of mutant huntingtin. J Biol Chem 298, 102219
35780830   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

Son S, et al. (2018) High-mobility group box 1 links sensing of reactive oxygen species by huntingtin to its nuclear entry. J Biol Chem
30538129   Curated Info

8

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

9

Daldin M, et al. (2017) Polyglutamine expansion affects huntingtin conformation in multiple Huntington's disease models. Sci Rep 7, 5070
28698602   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

Caron NS, Hung CL, Atwal RS, Truant R (2014) Live cell imaging and biophotonic methods reveal two types of mutant huntingtin inclusions. Hum Mol Genet 23, 2324-38
24334607   Curated Info

12

Watkin EE, et al. (2014) Phosphorylation of mutant huntingtin at serine 116 modulates neuronal toxicity. PLoS One 9, e88284
24505464   Curated Info

13

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

14

Maiuri T, Woloshansky T, Xia J, Truant R (2013) The huntingtin N17 domain is a multifunctional CRM1 and Ran-dependent nuclear and cilial export signal. Hum Mol Genet 22, 1383-94
23297360   Curated Info

15

Atwal RS, et al. (2011) Kinase inhibitors modulate huntingtin cell localization and toxicity. Nat Chem Biol 7, 453-60
21623356   Curated Info

16

Gu X, et al. (2009) Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice. Neuron 64, 828-40
20064390   Curated Info

17

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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