HUMAN:TOR1A

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	TOR1A (synonyms: DQ2, DYT1, TA, TORA)
Protein Name(s)	Torsin-1A Dystonia 1 protein Torsin ATPase-1A Torsin family 1 member A
External Links
UniProt	O14656
EMBL	AF007871 AK314505 BT006931 AL158207 BC000674 BC014484
CCDS	CCDS6930.1
RefSeq	NP_000104.1
UniGene	Hs.534312
ProteinModelPortal	O14656
BioGrid	108193
DIP	DIP-34411N
IntAct	O14656
MINT	MINT-7002075
STRING	9606.ENSP00000345719
PhosphoSite	O14656
MaxQB	O14656
PaxDb	O14656
PRIDE	O14656
DNASU	1861
Ensembl	ENST00000351698
GeneID	1861
KEGG	hsa:1861
UCSC	uc004byl.3 uc004byn.3
CTD	1861
GeneCards	GC09M132575
GeneReviews	TOR1A
HGNC	HGNC:3098
HPA	CAB012473 HPA051195
MIM	128100 605204
neXtProt	NX_O14656
Orphanet	256 36899
PharmGKB	PA27556
eggNOG	NOG283963
GeneTree	ENSGT00390000001920
HOGENOM	HOG000115770
HOVERGEN	HBG054188
InParanoid	O14656
OMA	YFPREER
OrthoDB	EOG7TF791
PhylomeDB	O14656
TreeFam	TF314941
ChiTaRS	TOR1A
GeneWiki	Torsin_A
GenomeRNAi	1861
NextBio	7627
PRO	PR:O14656
Proteomes	UP000005640
Bgee	O14656
CleanEx	HS_TOR1A
ExpressionAtlas	O14656
Genevestigator	O14656
GO	GO:0030054 GO:0030659 GO:0005856 GO:0005788 GO:0070062 GO:0042406 GO:0030426 GO:0043231 GO:0016020 GO:0005635 GO:0031965 GO:0030141 GO:0008021 GO:0030133 GO:0005524 GO:0016887 GO:0008092 GO:0019894 GO:0051082 GO:0006200 GO:0007155 GO:0051085 GO:0061077 GO:0072321 GO:0071712 GO:0045104 GO:0031175 GO:0006998 GO:0071763 GO:0006996 GO:1900244 GO:0000338 GO:0051260 GO:0034504 GO:0051584 GO:2000008 GO:0006979 GO:0048489 GO:0044319
Gene3D	3.40.50.300
InterPro	IPR027417 IPR010448 IPR017378
PANTHER	PTHR10760
Pfam	PF06309
PIRSF	PIRSF038079
SUPFAM	SSF52540

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0005783	endoplasmic reticulum	PMID:12671990^[1]	ECO:0000314			C		Fig 6a-c. Co-localization of torsin A with ER marker PDI. showing localization of torsin A to the endoplasmic reticulum.	complete CACAO 3779
part_of	GO:0005783	endoplasmic reticulum	PMID:12671990^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
involved_in	GO:2000008	regulation of protein localization to cell surface	PMID:15505207^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1900244	positive regulation of synaptic vesicle endocytosis	PMID:21102408^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0072321	chaperone-mediated protein transport	PMID:15505207^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071763	nuclear membrane organization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9ER39	P		Seeded From UniProt	complete
involved_in	GO:0071712	ER-associated misfolded protein catabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9ER39	P		Seeded From UniProt	complete
involved_in	GO:0061077	chaperone-mediated protein folding	PMID:20169475^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051584	regulation of dopamine uptake involved in synaptic transmission	PMID:15505207^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048489	synaptic vesicle transport	PMID:18167355^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045104	intermediate filament cytoskeleton organization	PMID:16361107^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0044319	wound healing, spreading of cells	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9ER39	P		Seeded From UniProt	complete
part_of	GO:0042406	extrinsic component of endoplasmic reticulum membrane	PMID:17037984^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0034504	protein localization to nucleus	PMID:18827015^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion	UniProtKB:Q6ZMZ3	P		Seeded From UniProt	complete
involved_in	GO:0034504	protein localization to nucleus	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9ER39	P		Seeded From UniProt	complete
involved_in	GO:0031175	neuron projection development	PMID:16361107^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030659	cytoplasmic vesicle membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q68G38	C		Seeded From UniProt	complete
part_of	GO:0030426	growth cone	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q68G38	C		Seeded From UniProt	complete
part_of	GO:0030141	secretory granule	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q68G38	C		Seeded From UniProt	complete
enables	GO:0019894	kinesin binding	PMID:14970196^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07866	F		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:23569223^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:23569223^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008092	cytoskeletal protein binding	PMID:16361107^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P08670	F		Seeded From UniProt	complete
enables	GO:0008092	cytoskeletal protein binding	PMID:18827015^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q15149	F		Seeded From UniProt	complete
enables	GO:0008092	cytoskeletal protein binding	PMID:18827015^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P08670	F		Seeded From UniProt	complete
part_of	GO:0008021	synaptic vesicle	PMID:21102408^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0007155	cell adhesion	PMID:16361107^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006998	nuclear envelope organization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9ER39	P		Seeded From UniProt	complete
involved_in	GO:0006996	organelle organization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9ER39	P		Seeded From UniProt	complete
part_of	GO:0005788	endoplasmic reticulum lumen	PMID:17037984^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005635	nuclear envelope	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9ER39	C		Seeded From UniProt	complete
involved_in	GO:0000338	protein deneddylation	PMID:21102408^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:20015956^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005788	endoplasmic reticulum lumen	PMID:20015956^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031965	nuclear membrane	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68G38 ensembl:ENSRNOP00000063691	C		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68G38 ensembl:ENSRNOP00000063691	C		Seeded From UniProt	complete
part_of	GO:0030659	cytoplasmic vesicle membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68G38 ensembl:ENSRNOP00000063691	C		Seeded From UniProt	complete
part_of	GO:0030426	growth cone	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68G38 ensembl:ENSRNOP00000063691	C		Seeded From UniProt	complete
part_of	GO:0030141	secretory granule	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68G38 ensembl:ENSRNOP00000063691	C		Seeded From UniProt	complete
enables	GO:0019894	kinesin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68G38 ensembl:ENSRNOP00000063691	F		Seeded From UniProt	complete
part_of	GO:0008021	synaptic vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68G38 ensembl:ENSRNOP00000063691	C		Seeded From UniProt	complete
involved_in	GO:0006979	response to oxidative stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68G38 ensembl:ENSRNOP00000063691	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q68G38 ensembl:ENSRNOP00000063691	C		Seeded From UniProt	complete
involved_in	GO:0071763	nuclear membrane organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ER39 ensembl:ENSMUSP00000028200	P		Seeded From UniProt	complete
involved_in	GO:0071712	ER-associated misfolded protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ER39 ensembl:ENSMUSP00000028200	P		Seeded From UniProt	complete
enables	GO:0051787	misfolded protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ER39 ensembl:ENSMUSP00000028200	F		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ER39 ensembl:ENSMUSP00000028200	P		Seeded From UniProt	complete
involved_in	GO:0044319	wound healing, spreading of cells	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ER39 ensembl:ENSMUSP00000028200	P		Seeded From UniProt	complete
involved_in	GO:0034504	protein localization to nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ER39 ensembl:ENSMUSP00000028200	P		Seeded From UniProt	complete
enables	GO:0008092	cytoskeletal protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ER39 ensembl:ENSMUSP00000028200	F		Seeded From UniProt	complete
involved_in	GO:0006998	nuclear envelope organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ER39 ensembl:ENSMUSP00000028200	P		Seeded From UniProt	complete
involved_in	GO:0006996	organelle organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ER39 ensembl:ENSMUSP00000028200	P		Seeded From UniProt	complete
part_of	GO:0005788	endoplasmic reticulum lumen	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ER39 ensembl:ENSMUSP00000028200	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ER39 ensembl:ENSMUSP00000028200	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ER39 ensembl:ENSMUSP00000028200	C		Seeded From UniProt	complete
part_of	GO:0005635	nuclear envelope	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ER39 ensembl:ENSMUSP00000028200	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ER39 ensembl:ENSMUSP00000028200	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010448 InterPro:IPR017378 InterPro:IPR030549	F		Seeded From UniProt	complete
part_of	GO:0005635	nuclear envelope	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030549	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR017378	C		Seeded From UniProt	complete
part_of	GO:0005788	endoplasmic reticulum lumen	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030549	C		Seeded From UniProt	complete
involved_in	GO:0006998	nuclear envelope organization	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030549	P		Seeded From UniProt	complete
involved_in	GO:0007155	cell adhesion	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030549	P		Seeded From UniProt	complete
enables	GO:0008092	cytoskeletal protein binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030549	F		Seeded From UniProt	complete
involved_in	GO:0031175	neuron projection development	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030549	P		Seeded From UniProt	complete
involved_in	GO:0045104	intermediate filament cytoskeleton organization	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030549	P		Seeded From UniProt	complete
involved_in	GO:0048489	synaptic vesicle transport	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030549	P		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030549	F		Seeded From UniProt	complete
involved_in	GO:0051085	chaperone cofactor-dependent protein refolding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR017378	P		Seeded From UniProt	complete
involved_in	GO:0061077	chaperone-mediated protein folding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030549	P		Seeded From UniProt	complete
involved_in	GO:0072321	chaperone-mediated protein transport	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030549	P		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:10814722^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-8863723 Reactome:R-HSA-8863721	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0045202	synapse	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0770	C		Seeded From UniProt	complete
part_of	GO:0030054	cell junction	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0965	C		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0031410	cytoplasmic vesicle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0968	C		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0966	C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206 UniProtKB-SubCell:SL-0090	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256	C		Seeded From UniProt	complete
part_of	GO:0030133	transport vesicle	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0244	C		Seeded From UniProt	complete
part_of	GO:0031965	nuclear membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0182	C		Seeded From UniProt	complete
part_of	GO:0030426	growth cone	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0288	C		Seeded From UniProt	complete
part_of	GO:0005788	endoplasmic reticulum lumen	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0096	C		Seeded From UniProt	complete
part_of	GO:0008021	synaptic vesicle	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0259	C		Seeded From UniProt	complete
part_of	GO:0030659	cytoplasmic vesicle membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0089	C		Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 Hewett, J et al. (2003) TorsinA in PC12 cells: localization in the endoplasmic reticulum and response to stress. J. Neurosci. Res. 72 158-68 PubMed GONUTS page
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Torres, GE et al. (2004) Effect of torsinA on membrane proteins reveals a loss of function and a dominant-negative phenotype of the dystonia-associated DeltaE-torsinA mutant. Proc. Natl. Acad. Sci. U.S.A. 101 15650-5 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Granata, A et al. (2011) CSN complex controls the stability of selected synaptic proteins via a torsinA-dependent process. EMBO J. 30 181-93 PubMed GONUTS page
↑ Burdette, AJ et al. (2010) The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitro. Cell Stress Chaperones 15 605-17 PubMed GONUTS page
↑ Granata, A et al. (2008) The dystonia-associated protein torsinA modulates synaptic vesicle recycling. J. Biol. Chem. 283 7568-79 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Hewett, JW et al. (2006) Dystonia-causing mutant torsinA inhibits cell adhesion and neurite extension through interference with cytoskeletal dynamics. Neurobiol. Dis. 22 98-111 PubMed GONUTS page
↑ ^8.0 ^8.1 Callan, AC et al. (2007) Biosynthesis of the dystonia-associated AAA+ ATPase torsinA at the endoplasmic reticulum. Biochem. J. 401 607-12 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Nery, FC et al. (2008) TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton. J. Cell. Sci. 121 3476-86 PubMed GONUTS page
↑ Kamm, C et al. (2004) The early onset dystonia protein torsinA interacts with kinesin light chain 1. J. Biol. Chem. 279 19882-92 PubMed GONUTS page
↑ ^11.0 ^11.1 Zhao, C et al. (2013) Regulation of Torsin ATPases by LAP1 and LULL1. Proc. Natl. Acad. Sci. U.S.A. 110 E1545-54 PubMed GONUTS page
↑ ^12.0 ^12.1 Jungwirth, M et al. (2010) Relative tissue expression of homologous torsinB correlates with the neuronal specific importance of DYT1 dystonia-associated torsinA. Hum. Mol. Genet. 19 888-900 PubMed GONUTS page
↑ Hewett, J et al. (2000) Mutant torsinA, responsible for early-onset torsion dystonia, forms membrane inclusions in cultured neural cells. Hum. Mol. Genet. 9 1403-13 PubMed GONUTS page

[PMID:12671990-1] 1.0 ^1.1 Hewett, J et al. (2003) TorsinA in PC12 cells: localization in the endoplasmic reticulum and response to stress. J. Neurosci. Res. 72 158-68 PubMed GONUTS page

[PMID:19199708-2] Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page

[PMID:15505207-3] 3.0 ^3.1 ^3.2 Torres, GE et al. (2004) Effect of torsinA on membrane proteins reveals a loss of function and a dominant-negative phenotype of the dystonia-associated DeltaE-torsinA mutant. Proc. Natl. Acad. Sci. U.S.A. 101 15650-5 PubMed GONUTS page

[PMID:21102408-4] 4.0 ^4.1 ^4.2 Granata, A et al. (2011) CSN complex controls the stability of selected synaptic proteins via a torsinA-dependent process. EMBO J. 30 181-93 PubMed GONUTS page

[PMID:20169475-5] Burdette, AJ et al. (2010) The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitro. Cell Stress Chaperones 15 605-17 PubMed GONUTS page

[PMID:18167355-6] Granata, A et al. (2008) The dystonia-associated protein torsinA modulates synaptic vesicle recycling. J. Biol. Chem. 283 7568-79 PubMed GONUTS page

[PMID:16361107-7] 7.0 ^7.1 ^7.2 ^7.3 Hewett, JW et al. (2006) Dystonia-causing mutant torsinA inhibits cell adhesion and neurite extension through interference with cytoskeletal dynamics. Neurobiol. Dis. 22 98-111 PubMed GONUTS page

[PMID:17037984-8] 8.0 ^8.1 Callan, AC et al. (2007) Biosynthesis of the dystonia-associated AAA+ ATPase torsinA at the endoplasmic reticulum. Biochem. J. 401 607-12 PubMed GONUTS page

[PMID:18827015-9] 9.0 ^9.1 ^9.2 Nery, FC et al. (2008) TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton. J. Cell. Sci. 121 3476-86 PubMed GONUTS page

[PMID:14970196-10] Kamm, C et al. (2004) The early onset dystonia protein torsinA interacts with kinesin light chain 1. J. Biol. Chem. 279 19882-92 PubMed GONUTS page

[PMID:23569223-11] 11.0 ^11.1 Zhao, C et al. (2013) Regulation of Torsin ATPases by LAP1 and LULL1. Proc. Natl. Acad. Sci. U.S.A. 110 E1545-54 PubMed GONUTS page

[PMID:20015956-12] 12.0 ^12.1 Jungwirth, M et al. (2010) Relative tissue expression of homologous torsinB correlates with the neuronal specific importance of DYT1 dystonia-associated torsinA. Hum. Mol. Genet. 19 888-900 PubMed GONUTS page

[PMID:10814722-13] Hewett, J et al. (2000) Mutant torsinA, responsible for early-onset torsion dystonia, forms membrane inclusions in cultured neural cells. Hum. Mol. Genet. 9 1403-13 PubMed GONUTS page

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HUMAN:TOR1A

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