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Protein

Torsin-1A-interacting protein 1

Gene

TOR1AIP1

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

Functioni

Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina.1 Publication

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Torsin-1A-interacting protein 1
Alternative name(s):
Lamin-associated protein 1B
Short name:
LAP1B
Gene namesi
Name:TOR1AIP1
Synonyms:LAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:29456. TOR1AIP1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 338338NuclearSequence analysisAdd
BLAST
Transmembranei339 – 35517HelicalSequence analysisAdd
BLAST
Topological domaini356 – 583228Perinuclear spaceSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • nuclear inner membrane Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670715.

Polymorphism and mutation databases

BioMutaiTOR1AIP1.
DMDMi90101788.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 583583Torsin-1A-interacting protein 1PRO_0000228835Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601PhosphoserineBy similarity
Modified residuei135 – 1351PhosphoserineCombined sources
Modified residuei143 – 1431PhosphoserineCombined sources
Modified residuei143 – 1431Phosphoserine; in variant Thr-146Combined sources
Modified residuei154 – 1541PhosphoserineCombined sources
Modified residuei156 – 1561PhosphoserineCombined sources
Modified residuei157 – 1571PhosphoserineCombined sources
Modified residuei186 – 1861PhosphoserineCombined sources
Modified residuei215 – 2151PhosphoserineCombined sources
Modified residuei220 – 2201PhosphothreonineCombined sources
Modified residuei227 – 2271PhosphoserineCombined sources
Modified residuei230 – 2301PhosphoserineBy similarity
Modified residuei242 – 2421PhosphoserineBy similarity
Modified residuei305 – 3051PhosphoserineCombined sources
Modified residuei315 – 3151PhosphoserineCombined sources
Glycosylationi399 – 3991N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ5JTV8.
MaxQBiQ5JTV8.
PaxDbiQ5JTV8.
PeptideAtlasiQ5JTV8.
PRIDEiQ5JTV8.

PTM databases

iPTMnetiQ5JTV8.
PhosphoSiteiQ5JTV8.
SwissPalmiQ5JTV8.

Miscellaneous databases

PMAP-CutDBQ5JTV8.

Expressioni

Gene expression databases

BgeeiQ5JTV8.
CleanExiHS_TOR1AIP1.
ExpressionAtlasiQ5JTV8. baseline and differential.
GenevisibleiQ5JTV8. HS.

Organism-specific databases

HPAiHPA047151.
HPA050546.

Interactioni

Subunit structurei

Interacts with ATP1B4. Interacts with TOR1A (ATP-bound). Interacts with TOR1B, TOR2A and TOR3A. Interacts with VIM.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TERF2IPQ9NYB02EBI-2559665,EBI-750109

GO - Molecular functioni

  • ATPase binding Source: UniProtKB
  • cytoskeletal protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117543. 53 interactions.
DIPiDIP-56692N.
IntActiQ5JTV8. 31 interactions.
STRINGi9606.ENSP00000393292.

Structurei

Secondary structure

1
583
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi363 – 37816Combined sources
Helixi384 – 39815Combined sources
Beta strandi408 – 4147Combined sources
Helixi416 – 4183Combined sources
Helixi419 – 43416Combined sources
Helixi435 – 4373Combined sources
Beta strandi442 – 4454Combined sources
Helixi446 – 4483Combined sources
Turni449 – 4513Combined sources
Helixi454 – 47017Combined sources
Beta strandi475 – 4795Combined sources
Helixi481 – 4833Combined sources
Helixi486 – 4905Combined sources
Helixi491 – 4966Combined sources
Turni498 – 5003Combined sources
Beta strandi507 – 5137Combined sources
Beta strandi515 – 5173Combined sources
Helixi525 – 54218Combined sources
Beta strandi548 – 5503Combined sources
Helixi554 – 56411Combined sources
Beta strandi566 – 5705Combined sources
Helixi575 – 5773Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TVSX-ray1.60A/B356-583[»]
ProteinModelPortaliQ5JTV8.
SMRiQ5JTV8. Positions 360-583.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni356 – 583228Interaction with TOR1AAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili359 – 43577Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the TOR1AIP family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IJUB. Eukaryota.
ENOG4111IZJ. LUCA.
GeneTreeiENSGT00390000012166.
HOVERGENiHBG083152.
InParanoidiQ5JTV8.
PhylomeDBiQ5JTV8.
TreeFamiTF329438.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5JTV8-1) [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
MAGDGRRAEA VREGWGVYVT PRAPIREGRG RLAPQNGGSS DAPAYRTPPS
60 70 80 90 100
RQGRREVRFS DEPPEVYGDF EPLVAKERSP VGKRTRLEEF RSDSAKEEVR
110 120 130 140 150
ESAYYLRSRQ RRQPRPQETE EMKTRRTTRL QQQHSEQPPL QPSPVMTRRG
160 170 180 190 200
LRDSHSSEED EASSQTDLSQ TISKKTVRSI QEAPVSEDLV IRLRRPPLRY
210 220 230 240 250
PRYEATSVQQ KVNFSEEGET EEDDQDSSHS SVTTVKARSR DSDESGDKTT
260 270 280 290 300
RSSSQYIESF WQSSQSQNFT AHDKQPSVLS SGYQKTPQEW APQTARIRTR
310 320 330 340 350
MQNDSILKSE LGNQSPSTSS RQVTGQPQNA SFVKRNRWWL LPLIAALASG
360 370 380 390 400
SFWFFSTPEV ETTAVQEFQN QMNQLKNKYQ GQDEKLWKRS QTFLEKHLNS
410 420 430 440 450
SHPRSQPAIL LLTAARDAEE ALRCLSEQIA DAYSSFRSVR AIRIDGTDKA
460 470 480 490 500
TQDSDTVKLE VDQELSNGFK NGQNAAVVHR FESFPAGSTL IFYKYCDHEN
510 520 530 540 550
AAFKDVALVL TVLLEEETLG TSLGLKEVEE KVRDFLKVKF TNSNTPNSYN
560 570 580
HMDPDKLNGL WSRISHLVLP VQPENALKRG ICL
Length:583
Mass (Da):66,248
Last modified:March 21, 2006 - v2
Checksum:i3EE90CAAF49054FC
GO
Isoform 2 (identifier: Q5JTV8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     184-184: P → PA
     283-487: Missing.

Note: No experimental confirmation available.
Show »
Length:379
Mass (Da):43,090
Checksum:i2EB6838DDCE5D504
GO
Isoform 3 (identifier: Q5JTV8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     184-184: P → PA

Note: No experimental confirmation available.
Show »
Length:584
Mass (Da):66,319
Checksum:iD5BEACC6B305B89B
GO

Sequence cautioni

The sequence AAH23247.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB13855.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14461.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAF84184.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601D → V in BAB13855 (PubMed:14702039).Curated
Sequence conflicti200 – 2001Y → C in BAB14461 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti146 – 1461M → T.Combined sources2 Publications
Corresponds to variant rs1281378 [ dbSNP | Ensembl ].
VAR_025717
Natural varianti190 – 1901V → I in a breast cancer sample; somatic mutation. 1 Publication
Corresponds to variant rs775134055 [ dbSNP | Ensembl ].
VAR_035818
Natural varianti276 – 2761P → R.2 Publications
Corresponds to variant rs609521 [ dbSNP | Ensembl ].
VAR_025718
Natural varianti293 – 2931Q → H.
Corresponds to variant rs17279712 [ dbSNP | Ensembl ].
VAR_034566

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei184 – 1841P → PA in isoform 2 and isoform 3. 1 PublicationVSP_055704
Alternative sequencei283 – 487205Missing in isoform 2. 1 PublicationVSP_055705Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001780 mRNA. Translation: BAA91906.1.
AK021613 mRNA. Translation: BAB13855.1. Different initiation.
AK023204 mRNA. Translation: BAB14461.1. Different initiation.
AK291495 mRNA. Translation: BAF84184.1. Different initiation.
AL353708 Genomic DNA. Translation: CAI41051.1.
AL353708 Genomic DNA. Translation: CAQ09353.1.
BC023247 mRNA. Translation: AAH23247.1. Different initiation.
AL050126 mRNA. Translation: CAB43282.1.
CCDSiCCDS1335.1. [Q5JTV8-1]
CCDS65737.1. [Q5JTV8-3]
PIRiT08767.
RefSeqiNP_001254507.1. NM_001267578.1. [Q5JTV8-3]
NP_056417.2. NM_015602.3. [Q5JTV8-1]
UniGeneiHs.496459.

Genome annotation databases

EnsembliENST00000528443; ENSP00000435365; ENSG00000143337. [Q5JTV8-3]
ENST00000606911; ENSP00000476687; ENSG00000143337. [Q5JTV8-1]
GeneIDi26092.
KEGGihsa:26092.
UCSCiuc001gnp.3. human. [Q5JTV8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001780 mRNA. Translation: BAA91906.1.
AK021613 mRNA. Translation: BAB13855.1. Different initiation.
AK023204 mRNA. Translation: BAB14461.1. Different initiation.
AK291495 mRNA. Translation: BAF84184.1. Different initiation.
AL353708 Genomic DNA. Translation: CAI41051.1.
AL353708 Genomic DNA. Translation: CAQ09353.1.
BC023247 mRNA. Translation: AAH23247.1. Different initiation.
AL050126 mRNA. Translation: CAB43282.1.
CCDSiCCDS1335.1. [Q5JTV8-1]
CCDS65737.1. [Q5JTV8-3]
PIRiT08767.
RefSeqiNP_001254507.1. NM_001267578.1. [Q5JTV8-3]
NP_056417.2. NM_015602.3. [Q5JTV8-1]
UniGeneiHs.496459.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TVSX-ray1.60A/B356-583[»]
ProteinModelPortaliQ5JTV8.
SMRiQ5JTV8. Positions 360-583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117543. 53 interactions.
DIPiDIP-56692N.
IntActiQ5JTV8. 31 interactions.
STRINGi9606.ENSP00000393292.

PTM databases

iPTMnetiQ5JTV8.
PhosphoSiteiQ5JTV8.
SwissPalmiQ5JTV8.

Polymorphism and mutation databases

BioMutaiTOR1AIP1.
DMDMi90101788.

Proteomic databases

EPDiQ5JTV8.
MaxQBiQ5JTV8.
PaxDbiQ5JTV8.
PeptideAtlasiQ5JTV8.
PRIDEiQ5JTV8.

Protocols and materials databases

DNASUi26092.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000528443; ENSP00000435365; ENSG00000143337. [Q5JTV8-3]
ENST00000606911; ENSP00000476687; ENSG00000143337. [Q5JTV8-1]
GeneIDi26092.
KEGGihsa:26092.
UCSCiuc001gnp.3. human. [Q5JTV8-1]

Organism-specific databases

CTDi26092.
GeneCardsiTOR1AIP1.
H-InvDBHIX0001382.
HIX0199815.
HGNCiHGNC:29456. TOR1AIP1.
HPAiHPA047151.
HPA050546.
MIMi614512. gene.
neXtProtiNX_Q5JTV8.
PharmGKBiPA142670715.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJUB. Eukaryota.
ENOG4111IZJ. LUCA.
GeneTreeiENSGT00390000012166.
HOVERGENiHBG083152.
InParanoidiQ5JTV8.
PhylomeDBiQ5JTV8.
TreeFamiTF329438.

Miscellaneous databases

ChiTaRSiTOR1AIP1. human.
GeneWikiiTOR1AIP1.
GenomeRNAii26092.
PMAP-CutDBQ5JTV8.
PROiQ5JTV8.
SOURCEiSearch...

Gene expression databases

BgeeiQ5JTV8.
CleanExiHS_TOR1AIP1.
ExpressionAtlasiQ5JTV8. baseline and differential.
GenevisibleiQ5JTV8. 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. "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.
    , 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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-583 (ISOFORM 1), VARIANTS THR-146 AND ARG-276.
    Tissue: Embryo, Ovarian carcinoma and Peripheral blood.
  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] OF 100-583 (ISOFORM 1), VARIANTS THR-146 AND ARG-276.
    Tissue: Cervix.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 404-583 (ISOFORM 1).
    Tissue: Uterus.
  5. "Molecular cloning of one isotype of human lamina-associated polypeptide 1s and a topological analysis using its deletion mutants."
    Kondo Y., Kondoh J., Hayashi D., Ban T., Takagi M., Kamei Y., Tsuji L., Kim J., Yoneda Y.
    Biochem. Biophys. Res. Commun. 294:770-778(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY, SUBCELLULAR LOCATION.
  6. "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 TOR1A.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND THR-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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: INTERACTION WITH VIM.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. "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.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-143; SER-154; SER-156; SER-157; SER-186; SER-215; THR-220; SER-305 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-399.
    Tissue: Liver.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-156; SER-157; THR-220; SER-227 AND SER-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; THR-220 AND SER-315, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 (VARIANT THR-146), VARIANT [LARGE SCALE ANALYSIS] THR-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-154; SER-156; SER-157; SER-186; SER-215; THR-220 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  18. Cited for: FUNCTION AS ATPASE ACTIVATOR, INTERACTION WITH TOR1A.
  19. "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: SUBCELLULAR LOCATION.
  20. "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 SER-143; SER-154; SER-156; SER-157; SER-215 AND THR-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-190.
  23. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 (VARIANT THR-146), VARIANT [LARGE SCALE ANALYSIS] THR-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTOIP1_HUMAN
AccessioniPrimary (citable) accession number: Q5JTV8
Secondary accession number(s): A8K630
, B0QZ57, Q5JTV6, Q8IZ65, Q9H8Y6, Q9HAJ1, Q9NV52, Q9Y3X5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: July 6, 2016
This is version 105 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.