HUMAN:HD

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	HTT (synonyms: HD, IT15)
Protein Name(s)	Huntingtin Huntington disease protein HD protein
External Links
UniProt	P42858
EMBL	L12392 AB016794 Z49154 Z49155 Z49208 Z49769 Z68756 Z69649 L27350 L27351 L27352 L27353 L27354 L34020 L20431
PIR	A46068
RefSeq	NP_002102.4
UniGene	Hs.518450
PDB	2D3X 2LD0 2LD2 3IO4 3IO6 3IOR 3IOT 3IOU 3IOV 3IOW 3LRH 4FE8 4FEB 4FEC 4FED
PDBsum	2D3X 2LD0 2LD2 3IO4 3IO6 3IOR 3IOT 3IOU 3IOV 3IOW 3LRH 4FE8 4FEB 4FEC 4FED
ProteinModelPortal	P42858
BioGrid	109314
DIP	DIP-32492N
IntAct	P42858
MINT	MINT-133355
STRING	9606.ENSP00000347184
BindingDB	P42858
ChEMBL	CHEMBL5514
PhosphoSite	P42858
DMDM	296434520
MaxQB	P42858
PaxDb	P42858
PRIDE	P42858
Ensembl	ENST00000355072
GeneID	3064
KEGG	hsa:3064
UCSC	uc021xkv.1
CTD	3064
GeneCards	GC04P003076
GeneReviews	HTT
HGNC	HGNC:4851
HPA	CAB002756 HPA026114
MIM	143100 613004
neXtProt	NX_P42858
Orphanet	399 248111
PharmGKB	PA164741646
eggNOG	NOG82191
GeneTree	ENSGT00390000015863
HOGENOM	HOG000082472
HOVERGEN	HBG005953
InParanoid	P42858
KO	K04533
OMA	DSEHLTW
OrthoDB	EOG7JQBMD
PhylomeDB	P42858
TreeFam	TF323608
SignaLink	P42858
ChiTaRS	HTT
EvolutionaryTrace	P42858
GeneWiki	Huntingtin
GenomeRNAi	3064
NextBio	12121
PRO	PR:P42858
Proteomes	UP000005640
Bgee	P42858
CleanEx	HS_HTT
ExpressionAtlas	P42858
Genevestigator	P42858
GO	GO:0005776 GO:0030424 GO:0005737 GO:0030659 GO:0005829 GO:0030425 GO:0005783 GO:0005794 GO:0016234 GO:0005770 GO:0005739 GO:0005634 GO:0043234 GO:0048487 GO:0050809 GO:0034452 GO:0045505 GO:0042802 GO:0044325 GO:0002039 GO:0008134 GO:0009952 GO:0008088 GO:0007569 GO:0000052 GO:0008340 GO:0007212 GO:0007029 GO:0016197 GO:0006888 GO:0000132 GO:0007030 GO:0007625 GO:0042445 GO:0030073 GO:0055072 GO:0051938 GO:0019244 GO:0007626 GO:2001237 GO:0043524 GO:0021990 GO:0051402 GO:0048666 GO:0021988 GO:0048513 GO:0048341 GO:0031587 GO:0006606 GO:0019805 GO:0046902 GO:0051881 GO:0034047 GO:0048167 GO:0051592 GO:0006890 GO:0035176 GO:0007283 GO:0021756 GO:0000050 GO:0047496 GO:0008542
Gene3D	1.25.10.10
InterPro	IPR011989 IPR016024 IPR000091 IPR028426 IPR024613
PANTHER	PTHR10170
Pfam	PF12372
PRINTS	PR00375
SUPFAM	SSF48371

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:1905289	regulation of CAMKK-AMPK signaling cascade	PMID:21768291^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(UBERON:0002435)	Seeded From UniProt	complete
involved_in	GO:2000479	regulation of cAMP-dependent protein kinase activity	PMID:21768291^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q13131) occurs_in:(UBERON:0002435)	Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P42859	C		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:21909508^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0DMV8	F		Seeded From UniProt	complete
involved_in	GO:0042297	vocal learning	PMID:26436900^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(UBERON:0035807)	Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:17947297^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:17947297^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	PMID:17947297^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016234	inclusion body	PMID:17947297^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:17947297^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:17947297^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:17947297^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1904504	positive regulation of lipophagy	PMID:25686248^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903599	positive regulation of autophagy of mitochondrion	PMID:25686248^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1905337	positive regulation of aggrephagy	PMID:25686248^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019900	kinase binding	PMID:25686248^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O75385	F		Seeded From UniProt	complete
involved_in	GO:0045724	positive regulation of cilium assembly	PMID:21985783^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(CL:0000540)	Seeded From UniProt	complete
part_of	GO:0005814	centriole	PMID:21985783^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0002586)	Seeded From UniProt	complete
enables	GO:0005522	profilin binding	PMID:18573880^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07737	F		Seeded From UniProt	complete
involved_in	GO:0031587	positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity	PMID:12873381^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0044325	ion channel binding	PMID:12873381^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0043666	regulation of phosphoprotein phosphatase activity	PMID:21562226^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001237	negative regulation of extrinsic apoptotic signaling pathway	PMID:19240112^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(UniProtKB:Q13177)	Seeded From UniProt	complete
enables	GO:0048487	beta-tubulin binding	PMID:11870213^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0047496	vesicle transport along microtubule	PMID:20515468^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0045505	dynein intermediate chain binding	PMID:20515468^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:18922795^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0034452	dynactin binding	PMID:18922795^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14203	F		Seeded From UniProt	complete
part_of	GO:0030659	cytoplasmic vesicle membrane	PMID:7748555^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030425	dendrite	PMID:7748555^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030424	axon	PMID:7748555^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0007030	Golgi organization	PMID:20515468^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006890	retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum	PMID:20515468^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:20515468^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	PMID:15837803^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:17704510^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005776	autophagosome	PMID:17704510^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005770	late endosome	PMID:17704510^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15654337^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:7748555^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15064418^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15654337^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:17704510^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:12783847^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0002039	p53 binding	PMID:10823891^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04637	F		Seeded From UniProt	complete
involved_in	GO:0000132	establishment of mitotic spindle orientation	PMID:20696378^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0099524	postsynaptic cytosol	PMID:7748555^[14]	ECO:0006003	electron microscopy evidence used in manual assertion		C	part_of:(UBERON:0000061) part_of:(UBERON:0000956)	Seeded From UniProt	complete
part_of	GO:0099523	presynaptic cytosol	PMID:7748555^[14]	ECO:0006042	cell fractionation evidence used in manual assertion		C	part_of:(UBERON:0000061) part_of:(UBERON:0000956)	Seeded From UniProt	complete
part_of	GO:0099523	presynaptic cytosol	PMID:7748555^[14]	ECO:0006003	electron microscopy evidence used in manual assertion		C	part_of:(UBERON:0000061) part_of:(UBERON:0000956)	Seeded From UniProt	complete
part_of	GO:0099523	presynaptic cytosol	PMID:7748555^[14]	ECO:0000279	western blot evidence used in manual assertion		C	part_of:(UBERON:0000061) part_of:(UBERON:0000956)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25848931^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P42858	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23275563^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P42858	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22119730^[24]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P42858	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19487684^[25]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P42858	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000091	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000091	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0053	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
	GO:0046825	regulation of protein export from nucleus	PMID:12783847^[19]	ECO:0000314			P		Figure 1 shows the analysis of a putative nuclear localization signal of huntingtin in an in vivo assay of human HeLa epithelial cells. It does not contain a classic nuclear localization signal.	complete CACAO 9328
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Ju, TC et al. (2011) Nuclear translocation of AMPK-alpha1 potentiates striatal neurodegeneration in Huntington's disease. J. Cell Biol. 194 209-27 PubMed GONUTS page
↑ Chakrabortee, S et al. (2012) Intrinsically disordered proteins as molecular shields. Mol Biosyst 8 210-9 PubMed GONUTS page
↑ Liu, WC et al. (2015) Human mutant huntingtin disrupts vocal learning in transgenic songbirds. Nat. Neurosci. 18 1617-22 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 Raychaudhuri, S et al. (2008) HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity. Hum. Mol. Genet. 17 240-55 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Rui, YN et al. (2015) Huntingtin functions as a scaffold for selective macroautophagy. Nat. Cell Biol. 17 262-75 PubMed GONUTS page
↑ ^6.0 ^6.1 Keryer, G et al. (2011) Ciliogenesis is regulated by a huntingtin-HAP1-PCM1 pathway and is altered in Huntington disease. J. Clin. Invest. 121 4372-82 PubMed GONUTS page
↑ Shao, J et al. (2008) Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation. Mol. Cell. Biol. 28 5196-208 PubMed GONUTS page
↑ ^8.0 ^8.1 Tang, TS et al. (2003) Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1. Neuron 39 227-39 PubMed GONUTS page
↑ Wang, Y et al. (2011) Dictyostelium huntingtin controls chemotaxis and cytokinesis through the regulation of myosin II phosphorylation. Mol. Biol. Cell 22 2270-81 PubMed GONUTS page
↑ Luo, S & Rubinsztein, DC (2009) Huntingtin promotes cell survival by preventing Pak2 cleavage. J. Cell. Sci. 122 875-85 PubMed GONUTS page
↑ Hoffner, G et al. (2002) Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: relevance to Huntington's disease. J. Cell. Sci. 115 941-8 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 ^12.4 Pardo, R et al. (2010) pARIS-htt: an optimised expression platform to study huntingtin reveals functional domains required for vesicular trafficking. Mol Brain 3 17 PubMed GONUTS page
↑ ^13.0 ^13.1 Shimojo, M (2008) Huntingtin regulates RE1-silencing transcription factor/neuron-restrictive silencer factor (REST/NRSF) nuclear trafficking indirectly through a complex with REST/NRSF-interacting LIM domain protein (RILP) and dynactin p150 Glued. J. Biol. Chem. 283 34880-6 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 ^14.6 ^14.7 DiFiglia, M et al. (1995) Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons. Neuron 14 1075-81 PubMed GONUTS page
↑ Sahlender, DA et al. (2005) Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis. J. Cell Biol. 169 285-95 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 Atwal, RS et al. (2007) Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity. Hum. Mol. Genet. 16 2600-15 PubMed GONUTS page
↑ ^17.0 ^17.1 Cornett, J et al. (2005) Polyglutamine expansion of huntingtin impairs its nuclear export. Nat. Genet. 37 198-204 PubMed GONUTS page
↑ Steffan, JS et al. (2004) SUMO modification of Huntingtin and Huntington's disease pathology. Science 304 100-4 PubMed GONUTS page
↑ ^19.0 ^19.1 Xia, J et al. (2003) Huntingtin contains a highly conserved nuclear export signal. Hum. Mol. Genet. 12 1393-403 PubMed GONUTS page
↑ Steffan, JS et al. (2000) The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc. Natl. Acad. Sci. U.S.A. 97 6763-8 PubMed GONUTS page
↑ Godin, JD et al. (2010) Huntingtin is required for mitotic spindle orientation and mammalian neurogenesis. Neuron 67 392-406 PubMed GONUTS page
↑ Jimenez-Sanchez, M et al. (2015) siRNA screen identifies QPCT as a druggable target for Huntington's disease. Nat. Chem. Biol. 11 347-354 PubMed GONUTS page
↑ Suter, B et al. (2013) Development and application of a DNA microarray-based yeast two-hybrid system. Nucleic Acids Res. 41 1496-507 PubMed GONUTS page
↑ Herrera, F & Outeiro, TF (2012) α-Synuclein modifies huntingtin aggregation in living cells. FEBS Lett. 586 7-12 PubMed GONUTS page
↑ Nekooki-Machida, Y et al. (2009) Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proc. Natl. Acad. Sci. U.S.A. 106 9679-84 PubMed GONUTS page

[PMID:21768291-1] 1.0 ^1.1 Ju, TC et al. (2011) Nuclear translocation of AMPK-alpha1 potentiates striatal neurodegeneration in Huntington's disease. J. Cell Biol. 194 209-27 PubMed GONUTS page

[PMID:21909508-2] Chakrabortee, S et al. (2012) Intrinsically disordered proteins as molecular shields. Mol Biosyst 8 210-9 PubMed GONUTS page

[PMID:26436900-3] Liu, WC et al. (2015) Human mutant huntingtin disrupts vocal learning in transgenic songbirds. Nat. Neurosci. 18 1617-22 PubMed GONUTS page

[PMID:17947297-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 Raychaudhuri, S et al. (2008) HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity. Hum. Mol. Genet. 17 240-55 PubMed GONUTS page

[PMID:25686248-5] 5.0 ^5.1 ^5.2 ^5.3 Rui, YN et al. (2015) Huntingtin functions as a scaffold for selective macroautophagy. Nat. Cell Biol. 17 262-75 PubMed GONUTS page

[PMID:21985783-6] 6.0 ^6.1 Keryer, G et al. (2011) Ciliogenesis is regulated by a huntingtin-HAP1-PCM1 pathway and is altered in Huntington disease. J. Clin. Invest. 121 4372-82 PubMed GONUTS page

[PMID:18573880-7] Shao, J et al. (2008) Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation. Mol. Cell. Biol. 28 5196-208 PubMed GONUTS page

[PMID:12873381-8] 8.0 ^8.1 Tang, TS et al. (2003) Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1. Neuron 39 227-39 PubMed GONUTS page

[PMID:21562226-9] Wang, Y et al. (2011) Dictyostelium huntingtin controls chemotaxis and cytokinesis through the regulation of myosin II phosphorylation. Mol. Biol. Cell 22 2270-81 PubMed GONUTS page

[PMID:19240112-10] Luo, S & Rubinsztein, DC (2009) Huntingtin promotes cell survival by preventing Pak2 cleavage. J. Cell. Sci. 122 875-85 PubMed GONUTS page

[PMID:11870213-11] Hoffner, G et al. (2002) Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: relevance to Huntington's disease. J. Cell. Sci. 115 941-8 PubMed GONUTS page

[PMID:20515468-12] 12.0 ^12.1 ^12.2 ^12.3 ^12.4 Pardo, R et al. (2010) pARIS-htt: an optimised expression platform to study huntingtin reveals functional domains required for vesicular trafficking. Mol Brain 3 17 PubMed GONUTS page

[PMID:18922795-13] 13.0 ^13.1 Shimojo, M (2008) Huntingtin regulates RE1-silencing transcription factor/neuron-restrictive silencer factor (REST/NRSF) nuclear trafficking indirectly through a complex with REST/NRSF-interacting LIM domain protein (RILP) and dynactin p150 Glued. J. Biol. Chem. 283 34880-6 PubMed GONUTS page

[PMID:7748555-14] 14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 ^14.6 ^14.7 DiFiglia, M et al. (1995) Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons. Neuron 14 1075-81 PubMed GONUTS page

[PMID:15837803-15] Sahlender, DA et al. (2005) Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis. J. Cell Biol. 169 285-95 PubMed GONUTS page

[PMID:17704510-16] 16.0 ^16.1 ^16.2 ^16.3 Atwal, RS et al. (2007) Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity. Hum. Mol. Genet. 16 2600-15 PubMed GONUTS page

[PMID:15654337-17] 17.0 ^17.1 Cornett, J et al. (2005) Polyglutamine expansion of huntingtin impairs its nuclear export. Nat. Genet. 37 198-204 PubMed GONUTS page

[PMID:15064418-18] Steffan, JS et al. (2004) SUMO modification of Huntingtin and Huntington's disease pathology. Science 304 100-4 PubMed GONUTS page

[PMID:12783847-19] 19.0 ^19.1 Xia, J et al. (2003) Huntingtin contains a highly conserved nuclear export signal. Hum. Mol. Genet. 12 1393-403 PubMed GONUTS page

[PMID:10823891-20] Steffan, JS et al. (2000) The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc. Natl. Acad. Sci. U.S.A. 97 6763-8 PubMed GONUTS page

[PMID:20696378-21] Godin, JD et al. (2010) Huntingtin is required for mitotic spindle orientation and mammalian neurogenesis. Neuron 67 392-406 PubMed GONUTS page

[PMID:25848931-22] Jimenez-Sanchez, M et al. (2015) siRNA screen identifies QPCT as a druggable target for Huntington's disease. Nat. Chem. Biol. 11 347-354 PubMed GONUTS page

[PMID:23275563-23] Suter, B et al. (2013) Development and application of a DNA microarray-based yeast two-hybrid system. Nucleic Acids Res. 41 1496-507 PubMed GONUTS page

[PMID:22119730-24] Herrera, F & Outeiro, TF (2012) α-Synuclein modifies huntingtin aggregation in living cells. FEBS Lett. 586 7-12 PubMed GONUTS page

[PMID:19487684-25] Nekooki-Machida, Y et al. (2009) Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proc. Natl. Acad. Sci. U.S.A. 106 9679-84 PubMed GONUTS page

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HUMAN:HD

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