Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Torsin-1A-interacting protein 2

Gene

TOR1AIP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity.3 Publications

GO - Molecular functioni

  • ATPase activator activity Source: UniProtKB
  • ATPase binding Source: UniProtKB

GO - Biological processi

  • endoplasmic reticulum organization Source: UniProtKB
  • positive regulation of ATPase activity Source: UniProtKB
  • protein localization to nuclear envelope Source: CACAO
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Torsin-1A-interacting protein 2
Alternative name(s):
Lumenal domain-like LAP1
Gene namesi
Name:TOR1AIP2
Synonyms:IFRG15, LULL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:24055. TOR1AIP2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 214213CytoplasmicSequence analysisAdd
BLAST
Transmembranei215 – 23521HelicalSequence analysisAdd
BLAST
Topological domaini236 – 470235LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670716.

Polymorphism and mutation databases

BioMutaiTOR1AIP2.
DMDMi74751288.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 470469Torsin-1A-interacting protein 2PRO_0000228838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei13 – 131PhosphoserineCombined sources
Modified residuei120 – 1201PhosphoserineCombined sources
Modified residuei163 – 1631PhosphoserineCombined sources
Modified residuei176 – 1761PhosphothreonineCombined sources
Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ8NFQ8.
PaxDbiQ8NFQ8.
PeptideAtlasiQ8NFQ8.
PRIDEiQ8NFQ8.

PTM databases

iPTMnetiQ8NFQ8.
PhosphoSiteiQ8NFQ8.
SwissPalmiQ8NFQ8.

Expressioni

Gene expression databases

BgeeiQ8NFQ8.
CleanExiHS_TOR1AIP2.
ExpressionAtlasiQ8NFQ8. baseline and differential.
GenevisibleiQ8NFQ8. HS.

Organism-specific databases

HPAiHPA051849.
HPA054763.

Interactioni

Subunit structurei

Interacts with TOR1A and TOR1B (ATP-bound).3 Publications

GO - Molecular functioni

  • ATPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi127870. 66 interactions.
IntActiQ8NFQ8. 4 interactions.
STRINGi9606.ENSP00000356584.

Structurei

3D structure databases

ProteinModelPortaliQ8NFQ8.
SMRiQ8NFQ8. Positions 251-469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni236 – 470235Interaction with TOR1AAdd
BLAST

Sequence similaritiesi

Belongs to the TOR1AIP family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IJUB. Eukaryota.
ENOG4111IZJ. LUCA.
GeneTreeiENSGT00390000012166.
HOGENOMiHOG000154661.
HOVERGENiHBG094081.
InParanoidiQ8NFQ8.
OMAiHHVADAY.
OrthoDBiEOG7G7KQH.
PhylomeDBiQ8NFQ8.
TreeFamiTF329438.

Family and domain databases

InterProiIPR008662. Lamina-ass_polypeptide_CLAP1C.
[Graphical view]
PfamiPF05609. LAP1C. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform TOR1AIP2 (identifier: Q8NFQ8-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MADSGLREPQ EDSQKDLEND PSVNSQAQET TIIASNAEEA EILHSACGLS
60 70 80 90 100
KDHQEVETEG PESADTGDKS ESPDEANVGK HPKDKTEDEN KQSFLDGGKG
110 120 130 140 150
HHLPSENLGK EPLDPDPSHS PSDKVGRADA HLGSSSVALP KEASDGTGAS
160 170 180 190 200
QEPPTTDSQE AQSPGHSSAG QEGEDTLRRR LLAPEAGSHP QQTQKLEEIK
210 220 230 240 250
ENAQDTMRQI NKKGFWSYGP VILVVLVVAV VASSVNSYYS SPAQQVPKNP
260 270 280 290 300
ALEAFLAQFS QLEDKFPGQS SFLWQRGRKF LQKHLNASNP TEPATIIFTA
310 320 330 340 350
AREGRETLKC LSHHVADAYT SSQKVSPIQI DGAGRTWQDS DTVKLLVDLE
360 370 380 390 400
LSYGFENGQK AAVVHHFESF PAGSTLIFYK YCDHENAAFK DVALVLTVLL
410 420 430 440 450
EEETLEASVG PRETEEKVRD LLWAKFTNSD TPTSFNHMDS DKLSGLWSRI
460 470
SHLVLPVQPV SSIEEQGCLF
Length:470
Mass (Da):51,263
Last modified:October 1, 2002 - v1
Checksum:i275CB5E28B7D4338
GO
Isoform IFRG15 (identifier: Q9H496-1) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry Q9H496.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: No experimental confirmation available. Dubious isoform.
Length:131
Mass (Da):15,348
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF464140 mRNA. Translation: AAM50514.1.
AL359853 Genomic DNA. Translation: CAH70382.1.
BC101532 mRNA. Translation: AAI01533.1.
BC112225 mRNA. Translation: AAI12226.1.
CCDSiCCDS1334.1. [Q8NFQ8-1]
RefSeqiNP_001186189.1. NM_001199260.1. [Q8NFQ8-1]
NP_659471.1. NM_145034.4. [Q8NFQ8-1]
XP_005244996.1. XM_005244939.3. [Q8NFQ8-1]
UniGeneiHs.571797.
Hs.723247.

Genome annotation databases

EnsembliENST00000367612; ENSP00000356584; ENSG00000169905. [Q8NFQ8-1]
ENST00000609928; ENSP00000477486; ENSG00000169905. [Q8NFQ8-1]
GeneIDi163590.
KEGGihsa:163590.
UCSCiuc001gnk.4. human. [Q8NFQ8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF464140 mRNA. Translation: AAM50514.1.
AL359853 Genomic DNA. Translation: CAH70382.1.
BC101532 mRNA. Translation: AAI01533.1.
BC112225 mRNA. Translation: AAI12226.1.
CCDSiCCDS1334.1. [Q8NFQ8-1]
RefSeqiNP_001186189.1. NM_001199260.1. [Q8NFQ8-1]
NP_659471.1. NM_145034.4. [Q8NFQ8-1]
XP_005244996.1. XM_005244939.3. [Q8NFQ8-1]
UniGeneiHs.571797.
Hs.723247.

3D structure databases

ProteinModelPortaliQ8NFQ8.
SMRiQ8NFQ8. Positions 251-469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127870. 66 interactions.
IntActiQ8NFQ8. 4 interactions.
STRINGi9606.ENSP00000356584.

PTM databases

iPTMnetiQ8NFQ8.
PhosphoSiteiQ8NFQ8.
SwissPalmiQ8NFQ8.

Polymorphism and mutation databases

BioMutaiTOR1AIP2.
DMDMi74751288.

Proteomic databases

EPDiQ8NFQ8.
PaxDbiQ8NFQ8.
PeptideAtlasiQ8NFQ8.
PRIDEiQ8NFQ8.

Protocols and materials databases

DNASUi163590.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367612; ENSP00000356584; ENSG00000169905. [Q8NFQ8-1]
ENST00000609928; ENSP00000477486; ENSG00000169905. [Q8NFQ8-1]
GeneIDi163590.
KEGGihsa:163590.
UCSCiuc001gnk.4. human. [Q8NFQ8-1]

Organism-specific databases

CTDi163590.
GeneCardsiTOR1AIP2.
HGNCiHGNC:24055. TOR1AIP2.
HPAiHPA051849.
HPA054763.
MIMi614513. gene.
neXtProtiNX_Q8NFQ8.
PharmGKBiPA142670716.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJUB. Eukaryota.
ENOG4111IZJ. LUCA.
GeneTreeiENSGT00390000012166.
HOGENOMiHOG000154661.
HOVERGENiHBG094081.
InParanoidiQ8NFQ8.
OMAiHHVADAY.
OrthoDBiEOG7G7KQH.
PhylomeDBiQ8NFQ8.
TreeFamiTF329438.

Miscellaneous databases

ChiTaRSiTOR1AIP2. human.
GenomeRNAii163590.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NFQ8.
CleanExiHS_TOR1AIP2.
ExpressionAtlasiQ8NFQ8. baseline and differential.
GenevisibleiQ8NFQ8. HS.

Family and domain databases

InterProiIPR008662. Lamina-ass_polypeptide_CLAP1C.
[Graphical view]
PfamiPF05609. LAP1C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Guo J.H., Yu L.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [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: Brain.
  4. "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 TORSIN-A, SUBCELLULAR LOCATION.
  5. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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, SUBCELLULAR LOCATION.
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: FUNCTION AS ATPASE ACTIVATOR, INTERACTION WITH TOR1A.
  12. "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, INTERACTION WITH TOR1B, SUBCELLULAR LOCATION.
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTOIP2_HUMAN
AccessioniPrimary (citable) accession number: Q8NFQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.