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O14656 (TOR1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Torsin-1A
Alternative name(s):
Dystonia 1 protein
Torsin ATPase-1A
EC=3.6.4.-
Torsin family 1 member A
Gene names
Name:TOR1A
Synonyms:DQ2, DYT1, TA, TORA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non-neural tissues. Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.23

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.23

Subunit structure

Homohexamer. Interacts with TOR1B; the interaction may be specific of neural tissues. Interacts (ATP-bound) with TOR1AIP1 and TOR1AIP2; the interactions induce ATPase activity. Interacts with KLHL14; preferentially when ATP-free. Interacts with KLC1 (via TPR repeats); the interaction associates TOR1A with the kinesin oligomeric complex. Interacts with COPS4; the interaction associates TOR1A with the CSN complex. Interacts with SNAPIN; the interaction is direct and associates SNAPIN with the CSN complex. Interacts with STON2. Interacts (ATP-bound) with SYNE3 (via KASH domain); the interaction is required for SYNE3 nuclear envelope localization. Interacts with VIM; the interaction associates TOR1A with the cytoskeleton. Interacts with PLEC. Interacts (ATP-bound) with SLC6A3; regulates SLC6A3 transport to the plasma membrane. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.22 Ref.23

Subcellular location

Endoplasmic reticulum lumen. Nucleus membrane; Peripheral membrane protein. Cell projectiongrowth cone By similarity. Cytoplasmic vesicle membrane By similarity. Cytoplasmic vesiclesecretory vesicle By similarity. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle. Cytoplasmcytoskeleton. Note: Upon oxidative stress, redistributes to protusions from the cell surface By similarity. Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus membrane is mediated by the interaction with TOR1AIP2. Ref.6 Ref.8 Ref.12 Ref.13 Ref.17 Ref.18 Ref.22

Tissue specificity

Widely expressed. Highest levels in kidney and liver. In the brain, high levels found in the dopaminergic neurons of the substantia nigra pars compacta, as well as in the neocortex, hippocampus and cerebellum. Also highly expressed in the spinal cord. Ref.7 Ref.8 Ref.9

Post-translational modification

N-glycosylated. Ref.6 Ref.8 Ref.13

Involvement in disease

Dystonia 1, torsion, autosomal dominant (DYT1) [MIM:128100]: A primary torsion dystonia, and the most common and severe form. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. Dystonia type 1 is characterized by involuntary, repetitive, sustained muscle contractions or postures involving one or more sites of the body, in the absence of other neurological symptoms. Typically, symptoms develop first in an arm or leg in middle to late childhood and progress in approximately 30% of patients to other body regions (generalized dystonia) within about five years. 'Torsion' refers to the twisting nature of body movements observed in DYT1, often affecting the trunk. Distribution and severity of symptoms vary widely between affected individuals, ranging from mild focal dystonia to severe generalized dystonia, even within families.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.19 Ref.22 Ref.25 Ref.26

Sequence similarities

Belongs to the ClpA/ClpB family. Torsin subfamily.

Ontologies

Keywords
   Cellular componentCell junction
Cell projection
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Endoplasmic reticulum
Membrane
Nucleus
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Dystonia
   DomainSignal
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.23. Source: UniProtKB

ER-associated misfolded protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cell adhesion

Inferred from mutant phenotype Ref.12. Source: UniProtKB

chaperone mediated protein folding requiring cofactor

Inferred from electronic annotation. Source: InterPro

chaperone-mediated protein folding

Inferred from direct assay Ref.19. Source: UniProtKB

chaperone-mediated protein transport

Inferred from direct assay Ref.10. Source: UniProtKB

intermediate filament cytoskeleton organization

Inferred from mutant phenotype Ref.12. Source: UniProtKB

neuron projection development

Inferred from mutant phenotype Ref.12. Source: UniProtKB

nuclear envelope organization

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear membrane organization

Inferred from sequence or structural similarity. Source: UniProtKB

organelle organization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of synaptic vesicle endocytosis

Inferred from mutant phenotype Ref.22. Source: UniProtKB

protein deneddylation

Inferred from mutant phenotype Ref.22. Source: UniProtKB

protein homooligomerization

Inferred from direct assay Ref.20. Source: MGI

protein localization to nucleus

Inferred from mutant phenotype Ref.16. Source: UniProtKB

regulation of dopamine uptake involved in synaptic transmission

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of protein localization to cell surface

Inferred from mutant phenotype Ref.10. Source: UniProtKB

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle transport

Inferred from mutant phenotype Ref.15. Source: UniProtKB

wound healing, spreading of cells

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasmic vesicle membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum lumen

Inferred from direct assay Ref.13. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 23376485. Source: UniProt

extrinsic component of endoplasmic reticulum membrane

Inferred from direct assay Ref.13. Source: UniProtKB

growth cone

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

membrane

Inferred from direct assay Ref.23. Source: UniProtKB

nuclear envelope

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear membrane

Inferred from direct assay. Source: HPA

secretory granule

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic vesicle

Inferred from direct assay Ref.22. Source: UniProtKB

transport vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from direct assay Ref.23. Source: UniProtKB

cytoskeletal protein binding

Inferred from physical interaction Ref.12Ref.16. Source: UniProtKB

kinesin binding

Inferred from physical interaction Ref.9. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.10Ref.15Ref.16Ref.22Ref.23. Source: UniProtKB

unfolded protein binding

Traceable author statement PubMed 10814722. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14656-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O14656-2)

The sequence of this isoform differs from the canonical sequence as follows:
     149-332: DQLQLWIRGN...FTKLDYYYDD → ARMEVWNPFL...SQFPLERCRS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Probable
Chain21 – 332312Torsin-1A
PRO_0000005506

Regions

Nucleotide binding102 – 1098ATP
Region91 – 251161Interaction with SNAPIN
Region251 – 33282Interaction with KLC1
Region312 – 33221Interaction with SYNE3

Amino acid modifications

Glycosylation1431N-linked (GlcNAc...) (high mannose) Ref.6
Glycosylation1581N-linked (GlcNAc...) (high mannose) Ref.6

Natural variations

Alternative sequence149 – 332184DQLQL…YYYDD → ARMEVWNPFLDVIGFGVSLL WDEIWEFYVEMSEPGKRFMS QFPLERCRS in isoform 2.
VSP_026605
Natural variant2051F → I in DYT1; produces intracellular misfolded protein aggregates. Ref.26
VAR_070932
Natural variant2161D → H.
Corresponds to variant rs1801968 [ dbSNP | Ensembl ].
VAR_020449
Natural variant2641D → H. Ref.1
VAR_010788
Natural variant2881R → Q in DYT1; produces an enlarged perinuclear space. Ref.25
VAR_070933
Natural variant3031Missing in DYT1; dominant negative; loss of interaction with TOR1AIP1 and TOR1AIP2 with loss of ATPase activity induction; enriched in the nuclear envelope; impairs secretory pathway; produces intracellular misfolded protein aggregates; produces an enlarged perinuclear space. Ref.1 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.19 Ref.22 Ref.23 Ref.25 Ref.26
Corresponds to variant rs80358233 [ dbSNP | Ensembl ].
VAR_010789
Natural variant323 – 3286Missing Found in a patient with early-onset atypical dystonia and myoclonic features].
Corresponds to variant rs80358235 [ dbSNP | Ensembl ].
VAR_070934

Experimental info

Mutagenesis181V → F: Inhibits sequence signal cleavage. Ref.13
Mutagenesis201A → F: Inhibits sequence signal cleavage. Ref.13
Mutagenesis331V → N: N-glycosylated. Ref.13
Mutagenesis1081K → A: Loss of ATP-binding. No effect on interaction with KLHL14. Increases interaction with TOR1AIP1 and TOR1AIP2. Abolishes interaction with SLC6A3. Ref.10 Ref.17 Ref.18
Mutagenesis1431N → Q: Reduces N-glycosylation. Ref.6
Mutagenesis1581N → Q: Reduces N-glycosylation. Ref.6
Mutagenesis1711E → Q: Loss of ATP hydrolysis. Loss of interaction with KLHL14. Localizes in the nuclear envelope. Ref.17 Ref.18 Ref.20 Ref.23
Sequence conflict2591D → H in AAP35577. Ref.3
Sequence conflict2591D → H in AAH00674. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: B69B28D0B4112080

FASTA33237,809
        10         20         30         40         50         60 
MKLGRAVLGL LLLAPSVVQA VEPISLGLAL AGVLTGYIYP RLYCLFAECC GQKRSLSREA 

        70         80         90        100        110        120 
LQKDLDDNLF GQHLAKKIIL NAVFGFINNP KPKKPLTLSL HGWTGTGKNF VSKIIAENIY 

       130        140        150        160        170        180 
EGGLNSDYVH LFVATLHFPH ASNITLYKDQ LQLWIRGNVS ACARSIFIFD EMDKMHAGLI 

       190        200        210        220        230        240 
DAIKPFLDYY DLVDGVSYQK AMFIFLSNAG AERITDVALD FWRSGKQRED IKLKDIEHAL 

       250        260        270        280        290        300 
SVSVFNNKNS GFWHSSLIDR NLIDYFVPFL PLEYKHLKMC IRVEMQSRGY EIDEDIVSRV 

       310        320        330 
AEEMTFFPKE ERVFSDKGCK TVFTKLDYYY DD 

« Hide

Isoform 2 [UniParc].

Checksum: BD34184941B1B11C
Show »

FASTA19722,135

References

« Hide 'large scale' references
[1]"The early-onset torsion dystonia gene (DYT1) encodes an ATP-binding protein."
Ozelius L.J., Hewett J.W., Page C.E., Bressman S.B., Kramer P.L., Shalish C., de Leon D., Brin M.F., Raymond D., Corey D.P., Fahn S., Risch N.J., Buckler A.J., Gusella J.F., Breakefield X.O.
Nat. Genet. 17:40-48(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT DYT1 GLU-303 DEL, VARIANT HIS-264.
Tissue: Brain cortex, Hippocampus and Substantia nigra.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Kidney and Skin.
[6]"Torsin A and its torsion dystonia-associated mutant forms are lumenal glycoproteins that exhibit distinct subcellular localizations."
Kustedjo K., Bracey M.H., Cravatt B.F.
J. Biol. Chem. 275:27933-27939(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-143 AND ASN-158, MUTAGENESIS OF ASN-143 AND ASN-158.
[7]"Immunohistochemical localization and distribution of torsinA in normal human and rat brain."
Shashidharan P., Kramer B.C., Walker R.H., Olanow C.W., Brin M.F.
Brain Res. 853:197-206(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"TorsinB--perinuclear location and association with torsinA."
Hewett J.W., Kamm C., Boston H., Beauchamp R., Naismith T., Ozelius L., Hanson P.I., Breakefield X.O., Ramesh V.
J. Neurochem. 89:1186-1194(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOR1B, TISSUE SPECIFICITY, GLYCOSYLATION, SUBCELLULAR LOCATION.
[9]"The early onset dystonia protein torsinA interacts with kinesin light chain 1."
Kamm C., Boston H., Hewett J., Wilbur J., Corey D.P., Hanson P.I., Ramesh V., Breakefield X.O.
J. Biol. Chem. 279:19882-19892(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KLC1, TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT DYT1 GLU-303 DEL.
[10]"Effect of torsinA on membrane proteins reveals a loss of function and a dominant-negative phenotype of the dystonia-associated DeltaE-torsinA mutant."
Torres G.E., Sweeney A.L., Beaulieu J.M., Shashidharan P., Caron M.G.
Proc. Natl. Acad. Sci. U.S.A. 101:15650-15655(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELLULAR TRAFFICKING, SUBUNIT, INTERACTION WITH SLC6A3, CHARACTERIZATION OF VARIANT DYT1 GLU-303 DEL, MUTAGENESIS OF LYS-108.
[11]"The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein."
Goodchild R.E., Dauer W.T.
J. Cell Biol. 168:855-862(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOR1AIP1 AND TOR1AIP2.
[12]"Dystonia-causing mutant torsinA inhibits cell adhesion and neurite extension through interference with cytoskeletal dynamics."
Hewett J.W., Zeng J., Niland B.P., Bragg D.C., Breakefield X.O.
Neurobiol. Dis. 22:98-111(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CYTOSKELETON ORGANIZATION, CHARACTERIZATION OF VARIANT DYT1 GLU-303 DEL, SUBCELLULAR LOCATION, INTERACTION WITH VIM.
[13]"Biosynthesis of the dystonia-associated AAA+ ATPase torsinA at the endoplasmic reticulum."
Callan A.C., Bunning S., Jones O.T., High S., Swanton E.
Biochem. J. 401:607-612(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SIGNAL SEQUENCE CLEAVAGE SITE, GLYCOSYLATION, MUTAGENESIS OF VAL-18; ALA-20 AND VAL-33.
[14]"Mutant torsinA interferes with protein processing through the secretory pathway in DYT1 dystonia cells."
Hewett J.W., Tannous B., Niland B.P., Nery F.C., Zeng J., Li Y., Breakefield X.O.
Proc. Natl. Acad. Sci. U.S.A. 104:7271-7276(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PROTEIN PROCESSING, CHARACTERIZATION OF VARIANT DYT1 GLU-303 DEL.
[15]"The dystonia-associated protein torsinA modulates synaptic vesicle recycling."
Granata A., Watson R., Collinson L.M., Schiavo G., Warner T.T.
J. Biol. Chem. 283:7568-7579(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN VESICLE RECYCLING, INTERACTION WITH SNAPIN, CHARACTERIZATION OF VARIANT DYT1 GLU-303 DEL.
[16]"TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton."
Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y., Wiche G., Sonnenberg A., Breakefield X.O.
J. Cell Sci. 121:3476-3486(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NUCLEAR POLARITY, INTERACTION WITH PLEC; SYNE3 AND VIM, CHARACTERIZATION OF VARIANT DYT1 GLU-303 DEL.
[17]"Printor, a novel torsinA-interacting protein implicated in dystonia pathogenesis."
Giles L.M., Li L., Chin L.S.
J. Biol. Chem. 284:21765-21775(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KLHL14, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-108 AND GLU-171.
[18]"LULL1 retargets TorsinA to the nuclear envelope revealing an activity that is impaired by the DYT1 dystonia mutation."
Vander Heyden A.B., Naismith T.V., Snapp E.L., Hodzic D., Hanson P.I.
Mol. Biol. Cell 20:2661-2672(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, HEXAMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-108 AND GLU-171.
[19]"The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitro."
Burdette A.J., Churchill P.F., Caldwell G.A., Caldwell K.A.
Cell Stress Chaperones 15:605-617(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CHAPERONE, CHARACTERIZATION OF VARIANT DYT1 GLU-303 DEL.
[20]"Relative tissue expression of homologous torsinB correlates with the neuronal specific importance of DYT1 dystonia-associated torsinA."
Jungwirth M., Dear M.L., Brown P., Holbrook K., Goodchild R.
Hum. Mol. Genet. 19:888-900(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, MUTAGENESIS OF GLU-171.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"CSN complex controls the stability of selected synaptic proteins via a torsinA-dependent process."
Granata A., Koo S.J., Haucke V., Schiavo G., Warner T.T.
EMBO J. 30:181-193(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSN4; SNAPIN AND STON2, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT DYT1 GLU-303 DEL.
[23]"Regulation of Torsin ATPases by LAP1 and LULL1."
Zhao C., Brown R.S., Chase A.R., Eisele M.R., Schlieker C.
Proc. Natl. Acad. Sci. U.S.A. 110:E1545-1554(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TOR1AIP1 AND TOR1AIP2, CHARACTERIZATION OF VARIANT GLU-303 DEL, MUTAGENESIS OF GLU-171.
[24]"Novel mutation in the TOR1A (DYT1) gene in atypical early onset dystonia and polymorphisms in dystonia and early onset parkinsonism."
Leung J.C., Klein C., Friedman J., Vieregge P., Jacobs H., Doheny D., Kamm C., DeLeon D., Pramstaller P.P., Penney J.B., Eisengart M., Jankovic J., Gasser T., Bressman S.B., Corey D.P., Kramer P., Brin M.F., Ozelius L.J., Breakefield X.O.
Neurogenetics 3:133-143(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT 323-PHE--TYR-328 DEL.
[25]"Novel TOR1A mutation p.Arg288Gln in early-onset dystonia (DYT1)."
Zirn B., Grundmann K., Huppke P., Puthenparampil J., Wolburg H., Riess O., Muller U.
J. Neurol. Neurosurg. Psych. 79:1327-1330(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DYT1 GLN-288, CHARACTERIZATION OF VARIANTS DYT1 GLN-288 AND GLU-303 DEL.
[26]"Functional evidence implicating a novel TOR1A mutation in idiopathic, late-onset focal dystonia."
Calakos N., Patel V.D., Gottron M., Wang G., Tran-Viet K.N., Brewington D., Beyer J.L., Steffens D.C., Krishnan R.R., Zuechner S.
J. Med. Genet. 47:646-650(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DYT1 ILE-205, CHARACTERIZATION OF VARIANTS DYT1 ILE-205 AND GLU-303 DEL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF007871 mRNA. Translation: AAC51732.1.
AK314505 mRNA. Translation: BAG37105.1.
BT006931 mRNA. Translation: AAP35577.1.
AL158207 Genomic DNA. Translation: CAC88168.1.
BC000674 mRNA. Translation: AAH00674.1.
BC014484 mRNA. Translation: AAH14484.1.
CCDSCCDS6930.1. [O14656-1]
RefSeqNP_000104.1. NM_000113.2. [O14656-1]
UniGeneHs.534312.

3D structure databases

ProteinModelPortalO14656.
SMRO14656. Positions 94-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108193. 21 interactions.
DIPDIP-34411N.
IntActO14656. 7 interactions.
MINTMINT-7002075.
STRING9606.ENSP00000345719.

PTM databases

PhosphoSiteO14656.

Proteomic databases

MaxQBO14656.
PaxDbO14656.
PRIDEO14656.

Protocols and materials databases

DNASU1861.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351698; ENSP00000345719; ENSG00000136827. [O14656-1]
GeneID1861.
KEGGhsa:1861.
UCSCuc004byl.3. human. [O14656-1]
uc004byn.3. human. [O14656-2]

Organism-specific databases

CTD1861.
GeneCardsGC09M132575.
GeneReviewsTOR1A.
HGNCHGNC:3098. TOR1A.
HPACAB012473.
HPA051195.
MIM128100. phenotype.
605204. gene.
neXtProtNX_O14656.
Orphanet256. Early-onset generalized limb-onset dystonia.
36899. Myoclonus-dystonia syndrome.
PharmGKBPA27556.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283963.
HOGENOMHOG000115770.
HOVERGENHBG054188.
InParanoidO14656.
OMACCRPEWI.
OrthoDBEOG7TF791.
PhylomeDBO14656.
TreeFamTF314941.

Gene expression databases

ArrayExpressO14656.
BgeeO14656.
CleanExHS_TOR1A.
GenevestigatorO14656.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR027417. P-loop_NTPase.
IPR010448. Torsin.
IPR017378. Torsin_subgr.
[Graphical view]
PANTHERPTHR10760. PTHR10760. 1 hit.
PfamPF06309. Torsin. 1 hit.
[Graphical view]
PIRSFPIRSF038079. Torsin_2A. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSTOR1A. human.
GeneWikiTorsin_A.
GenomeRNAi1861.
NextBio7627.
PROO14656.
SOURCESearch...

Entry information

Entry nameTOR1A_HUMAN
AccessionPrimary (citable) accession number: O14656
Secondary accession number(s): B2RB58, Q53Y64, Q96CA0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM