ID TOR1B_HUMAN Reviewed; 336 AA. AC O14657; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 13-FEB-2019, entry version 165. DE RecName: Full=Torsin-1B; DE AltName: Full=Torsin ATPase-1B; DE EC=3.6.4.-; DE AltName: Full=Torsin family 1 member B; DE Flags: Precursor; GN Name=TOR1B; Synonyms=DQ1; ORFNames=FKSG18; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Wang Y.-G., Gong L.; RT "Cloning of FKSG18, a novel gene located on human chromosome 9."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 71-336. RC TISSUE=Brain cortex, Fetal brain, and Liver; RX PubMed=9288096; DOI=10.1038/ng0997-40; RA Ozelius L.J., Hewett J.W., Page C.E., Bressman S.B., Kramer P.L., RA Shalish C., de Leon D., Brin M.F., Raymond D., Corey D.P., Fahn S., RA Risch N.J., Buckler A.J., Gusella J.F., Breakefield X.O.; RT "The early-onset torsion dystonia gene (DYT1) encodes an ATP-binding RT protein."; RL Nat. Genet. 17:40-48(1997). RN [5] RP INTERACTION WITH TOR1A, TISSUE SPECIFICITY, GLYCOSYLATION, AND RP SUBCELLULAR LOCATION. RX PubMed=15147511; DOI=10.1111/j.1471-4159.2004.02404.x; RA Hewett J.W., Kamm C., Boston H., Beauchamp R., Naismith T., RA Ozelius L., Hanson P.I., Breakefield X.O., Ramesh V.; RT "TorsinB--perinuclear location and association with torsinA."; RL J. Neurochem. 89:1186-1194(2004). RN [6] RP SUBUNIT, INTERACTION WITH TOR1A, AND MUTAGENESIS OF GLU-178. RX PubMed=20015956; DOI=10.1093/hmg/ddp557; RA Jungwirth M., Dear M.L., Brown P., Holbrook K., Goodchild R.; RT "Relative tissue expression of homologous torsinB correlates with the RT neuronal specific importance of DYT1 dystonia-associated torsinA."; RL Hum. Mol. Genet. 19:888-900(2010). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP FUNCTION AS ATPASE, AND CATALYTIC ACTIVITY. RX PubMed=23569223; DOI=10.1073/pnas.1300676110; RA Zhao C., Brown R.S., Chase A.R., Eisele M.R., Schlieker C.; RT "Regulation of Torsin ATPases by LAP1 and LULL1."; RL Proc. Natl. Acad. Sci. U.S.A. 110:E1545-1554(2013). RN [9] RP FUNCTION IN ENDOPLASMIC RETICULUM INTEGRITY, CATALYTIC ACTIVITY, RP INTERACTION WITH TOR1AIP2, AND MUTAGENESIS OF GLU-178; RP 334-ASP--HIS-336 AND PHE-335. RX PubMed=24275647; DOI=10.1074/jbc.M113.515791; RA Rose A.E., Zhao C., Turner E.M., Steyer A.M., Schlieker C.; RT "Arresting a Torsin ATPase reshapes the endoplasmic reticulum."; RL J. Biol. Chem. 289:552-564(2014). CC -!- FUNCTION: May serve as a molecular chaperone assisting in the CC proper folding of secreted and/or membrane proteins. Plays a role CC in non-neural cells nuclear envelope and endoplasmic reticulum CC integrity. May have a redundant function with TOR1A in non-neural CC tissues. {ECO:0000269|PubMed:23569223, CC ECO:0000269|PubMed:24275647}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:23569223, CC ECO:0000269|PubMed:24275647}; CC -!- SUBUNIT: Homohexamer. Interacts with TOR1A; the interaction may be CC specific of neural tissues. Interacts with TOR1AIP1; TOR1AIP1 is CC required for TOR1B location on the nuclear membrane. Interacts CC (ATP-bound) with TOR1AIP2; important for endoplasmic reticulum CC integrity. {ECO:0000269|PubMed:15147511, CC ECO:0000269|PubMed:20015956, ECO:0000269|PubMed:24275647}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen CC {ECO:0000269|PubMed:15147511}. Nucleus membrane CC {ECO:0000269|PubMed:15147511}. CC -!- TISSUE SPECIFICITY: Widely expressed with low levels in brain. CC {ECO:0000269|PubMed:15147511}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15147511}. CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AF317129; AAG50271.1; -; mRNA. DR EMBL; AL158207; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015578; AAH15578.1; -; mRNA. DR EMBL; AF007872; AAC51733.1; -; mRNA. DR CCDS; CCDS6929.1; -. DR RefSeq; NP_001304822.1; NM_001317893.1. DR RefSeq; NP_001304823.1; NM_001317894.1. DR RefSeq; NP_055321.1; NM_014506.2. DR UniGene; Hs.252682; -. DR ProteinModelPortal; O14657; -. DR SMR; O14657; -. DR BioGrid; 118160; 14. DR CORUM; O14657; -. DR DIP; DIP-56930N; -. DR IntAct; O14657; 4. DR STRING; 9606.ENSP00000259339; -. DR GlyConnect; 1824; -. DR iPTMnet; O14657; -. DR PhosphoSitePlus; O14657; -. DR BioMuta; TOR1B; -. DR EPD; O14657; -. DR jPOST; O14657; -. DR MaxQB; O14657; -. DR PaxDb; O14657; -. DR PeptideAtlas; O14657; -. DR PRIDE; O14657; -. DR ProteomicsDB; 48154; -. DR DNASU; 27348; -. DR Ensembl; ENST00000259339; ENSP00000259339; ENSG00000136816. DR GeneID; 27348; -. DR KEGG; hsa:27348; -. DR UCSC; uc004byk.1; human. DR CTD; 27348; -. DR DisGeNET; 27348; -. DR EuPathDB; HostDB:ENSG00000136816.15; -. DR GeneCards; TOR1B; -. DR HGNC; HGNC:11995; TOR1B. DR HPA; CAB022709; -. DR HPA; HPA013403; -. DR HPA; HPA013697; -. DR MIM; 608050; gene. DR neXtProt; NX_O14657; -. DR OpenTargets; ENSG00000136816; -. DR PharmGKB; PA36676; -. DR eggNOG; KOG2170; Eukaryota. DR eggNOG; ENOG410XR06; LUCA. DR GeneTree; ENSGT00940000153192; -. DR HOGENOM; HOG000115770; -. DR HOVERGEN; HBG054188; -. DR InParanoid; O14657; -. DR KO; K22990; -. DR OMA; GCKTVQA; -. DR OrthoDB; 1453168at2759; -. DR PhylomeDB; O14657; -. DR TreeFam; TF314941; -. DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis. DR ChiTaRS; TOR1B; human. DR GenomeRNAi; 27348; -. DR PRO; PR:O14657; -. DR Proteomes; UP000005640; Chromosome 9. DR Bgee; ENSG00000136816; Expressed in 217 organ(s), highest expression level in liver. DR ExpressionAtlas; O14657; baseline and differential. DR Genevisible; O14657; HS. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:MGI. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IDA:UniProtKB. DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:InterPro. DR GO; GO:0007029; P:endoplasmic reticulum organization; IDA:UniProtKB. DR GO; GO:0071763; P:nuclear membrane organization; IEA:Ensembl. DR GO; GO:0051260; P:protein homooligomerization; IDA:MGI. DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010448; Torsin. DR InterPro; IPR030550; Torsin-1B. DR InterPro; IPR017378; Torsin_1/2. DR PANTHER; PTHR10760; PTHR10760; 1. DR PANTHER; PTHR10760:SF14; PTHR10760:SF14; 1. DR Pfam; PF06309; Torsin; 1. DR PIRSF; PIRSF038079; Torsin_2A; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 1: Evidence at protein level; KW ATP-binding; Chaperone; Complete proteome; Endoplasmic reticulum; KW Glycoprotein; Hydrolase; Membrane; Nucleotide-binding; Nucleus; KW Polymorphism; Reference proteome; Signal. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 336 Torsin-1B. FT /FTId=PRO_0000005509. FT NP_BIND 109 116 ATP. {ECO:0000255}. FT CARBOHYD 64 64 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 165 165 N-linked (GlcNAc...) asparagine. FT {ECO:0000250}. FT VARIANT 54 54 A -> T (in dbSNP:rs10988518). FT /FTId=VAR_059220. FT MUTAGEN 178 178 E->Q: Loss of ATPase activity. Produces FT sinusoidal endoplasmic reticulum FT structures where it accumulates. Highly FT enhances interaction with TOR1AIP2. FT Localizes in the nuclear envelope. FT {ECO:0000269|PubMed:20015956, FT ECO:0000269|PubMed:24275647}. FT MUTAGEN 334 336 DFH->GGG: Highly reduces ATPase activity FT induced by TOR1AIP2. FT {ECO:0000269|PubMed:24275647}. FT MUTAGEN 334 336 Missing: Decreases interaction with FT TOR1AIP2. {ECO:0000269|PubMed:24275647}. FT MUTAGEN 335 335 F->A: No effect on interaction with FT TOR1AIP2. {ECO:0000269|PubMed:24275647}. SQ SEQUENCE 336 AA; 37979 MW; E729360E6468A3FC CRC64; MLRAGWLRGA AALALLLAAR VVAAFEPITV GLAIGAASAI TGYLSYNDIY CRFAECCREE RPLNASALKL DLEEKLFGQH LATEVIFKAL TGFRNNKNPK KPLTLSLHGW AGTGKNFVSQ IVAENLHPKG LKSNFVHLFV STLHFPHEQK IKLYQDQLQK WIRGNVSACA NSVFIFDEMD KLHPGIIDAI KPFLDYYEQV DGVSYRKAIF IFLSNAGGDL ITKTALDFWR AGRKREDIQL KDLEPVLSVG VFNNKHSGLW HSGLIDKNLI DYFIPFLPLE YRHVKMCVRA EMRARGSAID EDIVTRVAEE MTFFPRDEKI YSDKGCKTVQ SRLDFH //