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O14657 (TOR1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Torsin-1B
Alternative name(s):
Torsin ATPase-1B
EC=3.6.4.-
Torsin family 1 member B
Gene names
Name:TOR1B
Synonyms:DQ1
ORF Names:FKSG18
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. Plays a role in non-neural cells nuclear envelope and endoplasmic reticulum integrity. May have a redundant function with TOR1A in non-neural tissues. Ref.8 Ref.9

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.8 Ref.9

Subunit structure

Homohexamer. Interacts with TOR1A; the interaction may be specific of neural tissues. Interacts with TOR1AIP1; TOR1AIP1 is required for TOR1B location on the nuclear membrane. Interacts (ATP-bound) with TOR1AIP2; important for endoplasmic reticulum integrity. Ref.5 Ref.6 Ref.9

Subcellular location

Endoplasmic reticulum lumen. Nucleus membrane Ref.5.

Tissue specificity

Widely expressed with low levels in brain. Ref.5

Post-translational modification

N-glycosylated. Ref.5

Sequence similarities

Belongs to the ClpA/ClpB family. Torsin subfamily.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   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.8. Source: UniProtKB

chaperone mediated protein folding requiring cofactor

Inferred from electronic annotation. Source: InterPro

endoplasmic reticulum organization

Inferred from direct assay Ref.9. Source: UniProtKB

nuclear membrane organization

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from direct assay Ref.6. Source: MGI

response to unfolded protein

Traceable author statement PubMed 10644435. Source: ProtInc

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.5. Source: UniProtKB

endoplasmic reticulum lumen

Inferred from direct assay Ref.6. Source: MGI

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

nuclear envelope

Inferred from direct assay Ref.5. Source: UniProtKB

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from direct assay Ref.6Ref.8. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5Ref.9. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 336312Torsin-1B
PRO_0000005509

Regions

Nucleotide binding109 – 1168ATP Potential

Amino acid modifications

Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation1651N-linked (GlcNAc...) By similarity

Natural variations

Natural variant541A → T.
Corresponds to variant rs10988518 [ dbSNP | Ensembl ].
VAR_059220

Experimental info

Mutagenesis1781E → Q: Loss of ATPase activity. Produces sinusoidal endoplasmic reticulum structures where it accumulates. Highly enhances interaction with TOR1AIP2. Localizes in the nuclear envelope. Ref.6 Ref.9
Mutagenesis334 – 3363DFH → GGG: Highly reduces ATPase activity induced by TOR1AIP2. Ref.9
Mutagenesis334 – 3363Missing: Decreases interaction with TOR1AIP2. Ref.9
Mutagenesis3351F → A: No effect on interaction with TOR1AIP2. Ref.9

Sequences

Sequence LengthMass (Da)Tools
O14657 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: E729360E6468A3FC

FASTA33637,979
        10         20         30         40         50         60 
MLRAGWLRGA AALALLLAAR VVAAFEPITV GLAIGAASAI TGYLSYNDIY CRFAECCREE 

        70         80         90        100        110        120 
RPLNASALKL DLEEKLFGQH LATEVIFKAL TGFRNNKNPK KPLTLSLHGW AGTGKNFVSQ 

       130        140        150        160        170        180 
IVAENLHPKG LKSNFVHLFV STLHFPHEQK IKLYQDQLQK WIRGNVSACA NSVFIFDEMD 

       190        200        210        220        230        240 
KLHPGIIDAI KPFLDYYEQV DGVSYRKAIF IFLSNAGGDL ITKTALDFWR AGRKREDIQL 

       250        260        270        280        290        300 
KDLEPVLSVG VFNNKHSGLW HSGLIDKNLI DYFIPFLPLE YRHVKMCVRA EMRARGSAID 

       310        320        330 
EDIVTRVAEE MTFFPRDEKI YSDKGCKTVQ SRLDFH 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of FKSG18, a novel gene located on human chromosome 9."
Wang Y.-G., Gong L.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
[3]"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].
Tissue: Kidney.
[4]"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] OF 71-336.
Tissue: Brain cortex, Fetal brain and Liver.
[5]"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 TOR1A, TISSUE SPECIFICITY, GLYCOSYLATION, SUBCELLULAR LOCATION.
[6]"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, INTERACTION WITH TOR1A, MUTAGENESIS OF GLU-178.
[7]"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].
[8]"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 AS ATPASE, CATALYTIC ACTIVITY.
[9]"Arresting a Torsin ATPase reshapes the endoplasmic reticulum."
Rose A.E., Zhao C., Turner E.M., Steyer A.M., Schlieker C.
J. Biol. Chem. 289:552-564(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOPLASMIC RETICULUM INTEGRITY, CATALYTIC ACTIVITY, INTERACTION WITH TOR1AIP2, MUTAGENESIS OF GLU-178; 334-ASP--HIS-336 AND PHE-335.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF317129 mRNA. Translation: AAG50271.1.
AL158207 Genomic DNA. Translation: CAC88165.1.
BC015578 mRNA. Translation: AAH15578.1.
AF007872 mRNA. Translation: AAC51733.1.
CCDSCCDS6929.1.
RefSeqNP_055321.1. NM_014506.1.
UniGeneHs.252682.

3D structure databases

ProteinModelPortalO14657.
SMRO14657. Positions 101-127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118160. 3 interactions.
DIPDIP-56930N.
IntActO14657. 1 interaction.
STRING9606.ENSP00000259339.

PTM databases

PhosphoSiteO14657.

Proteomic databases

MaxQBO14657.
PaxDbO14657.
PRIDEO14657.

Protocols and materials databases

DNASU27348.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259339; ENSP00000259339; ENSG00000136816.
GeneID27348.
KEGGhsa:27348.
UCSCuc004byk.1. human.

Organism-specific databases

CTD27348.
GeneCardsGC09P132565.
HGNCHGNC:11995. TOR1B.
HPACAB022709.
HPA013403.
HPA013697.
MIM608050. gene.
neXtProtNX_O14657.
PharmGKBPA36676.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283963.
HOGENOMHOG000115770.
HOVERGENHBG054188.
InParanoidO14657.
OMAYEQIDGV.
OrthoDBEOG7TF791.
PhylomeDBO14657.
TreeFamTF314941.

Gene expression databases

BgeeO14657.
CleanExHS_TOR1B.
GenevestigatorO14657.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR027417. 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.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi27348.
NextBio50442.
PROO14657.
SOURCESearch...

Entry information

Entry nameTOR1B_HUMAN
AccessionPrimary (citable) accession number: O14657
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: July 9, 2014
This is version 128 of the entry and version 2 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