TOIP1_HUMAN
ID TOIP1_HUMAN Reviewed; 583 AA.
AC Q5JTV8; A8K630; B0QZ57; Q5JTV6; Q8IZ65; Q9H8Y6; Q9HAJ1; Q9NV52; Q9Y3X5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Torsin-1A-interacting protein 1;
DE AltName: Full=Lamin-associated protein 1B;
DE Short=LAP1B;
GN Name=TOR1AIP1; Synonyms=LAP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 87-583 (ISOFORM 1), AND VARIANTS THR-146 AND ARG-276.
RC TISSUE=Embryo, Ovarian carcinoma, and Peripheral blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-583 (ISOFORM 1), AND VARIANTS
RP THR-146 AND ARG-276.
RC TISSUE=Cervix;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 404-583 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=12061773; DOI=10.1016/s0006-291x(02)00563-6;
RA Kondo Y., Kondoh J., Hayashi D., Ban T., Takagi M., Kamei Y., Tsuji L.,
RA Kim J., Yoneda Y.;
RT "Molecular cloning of one isotype of human lamina-associated polypeptide 1s
RT and a topological analysis using its deletion mutants.";
RL Biochem. Biophys. Res. Commun. 294:770-778(2002).
RN [6]
RP INTERACTION WITH TOR1A.
RX PubMed=15767459; DOI=10.1083/jcb.200411026;
RA Goodchild R.E., Dauer W.T.;
RT "The AAA+ protein torsinA interacts with a conserved domain present in LAP1
RT and a novel ER protein.";
RL J. Cell Biol. 168:855-862(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND THR-220, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP INTERACTION WITH VIM.
RX PubMed=16361107; DOI=10.1016/j.nbd.2005.10.012;
RA Hewett J.W., Zeng J., Niland B.P., Bragg D.C., Breakefield X.O.;
RT "Dystonia-causing mutant torsinA inhibits cell adhesion and neurite
RT extension through interference with cytoskeletal dynamics.";
RL Neurobiol. Dis. 22:98-111(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-143; SER-154;
RP SER-156; SER-157; SER-186; SER-215; THR-220; SER-305 AND SER-315, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-399.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-156; SER-157;
RP THR-220; SER-227 AND SER-305, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; THR-220 AND SER-315,
RP VARIANT [LARGE SCALE ANALYSIS] THR-146, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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., Buerckstuemmer T.,
RA 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, VARIANT [LARGE SCALE
RP ANALYSIS] THR-146, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-154; SER-156;
RP SER-157; SER-186; SER-215; THR-220 AND SER-315, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP FUNCTION AS ATPASE ACTIVATOR, AND INTERACTION WITH TOR1A.
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 [20]
RP SUBCELLULAR LOCATION.
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).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-154; SER-156;
RP SER-157; SER-215 AND THR-220, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-308, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [24]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-190.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [25]
RP INVOLVEMENT IN MRRSDC, AND TISSUE SPECIFICITY.
RX PubMed=24856141; DOI=10.1016/j.nmd.2014.04.007;
RA Kayman-Kurekci G., Talim B., Korkusuz P., Sayar N., Sarioglu T., Oncel I.,
RA Sharafi P., Gundesli H., Balci-Hayta B., Purali N., Serdaroglu-Oflazer P.,
RA Topaloglu H., Dincer P.;
RT "Mutation in TOR1AIP1 encoding LAP1B in a form of muscular dystrophy: a
RT novel gene related to nuclear envelopathies.";
RL Neuromuscul. Disord. 24:624-633(2014).
CC -!- FUNCTION: Required for nuclear membrane integrity. Induces TOR1A and
CC TOR1B ATPase activity and is required for their location on the nuclear
CC membrane. Binds to A- and B-type lamins. Possible role in membrane
CC attachment and assembly of the nuclear lamina.
CC {ECO:0000269|PubMed:23569223}.
CC -!- SUBUNIT: Interacts with ATP1B4. Interacts with TOR1A (ATP-bound).
CC Interacts with TOR1B, TOR2A and TOR3A. Interacts with VIM.
CC {ECO:0000269|PubMed:15767459, ECO:0000269|PubMed:16361107,
CC ECO:0000269|PubMed:23569223}.
CC -!- INTERACTION:
CC Q5JTV8; Q8N302-2: AGGF1; NbExp=3; IntAct=EBI-2559665, EBI-25838028;
CC Q5JTV8; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-2559665, EBI-10693038;
CC Q5JTV8; P62136: PPP1CA; NbExp=2; IntAct=EBI-2559665, EBI-357253;
CC Q5JTV8; Q06323: PSME1; NbExp=3; IntAct=EBI-2559665, EBI-712149;
CC Q5JTV8; Q13573: SNW1; NbExp=3; IntAct=EBI-2559665, EBI-632715;
CC Q5JTV8; Q496A3: SPATS1; NbExp=3; IntAct=EBI-2559665, EBI-3923692;
CC Q5JTV8; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-2559665, EBI-750109;
CC Q5JTV8; O14656: TOR1A; NbExp=2; IntAct=EBI-2559665, EBI-524257;
CC Q5JTV8; Q8WUU4: ZNF296; NbExp=3; IntAct=EBI-2559665, EBI-8834821;
CC Q5JTV8-3; P36873-1: PPP1CC; NbExp=4; IntAct=EBI-21448143, EBI-356289;
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:12061773, ECO:0000269|PubMed:24275647}; Single-pass
CC membrane protein {ECO:0000269|PubMed:12061773,
CC ECO:0000269|PubMed:24275647}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5JTV8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JTV8-2; Sequence=VSP_055704, VSP_055705;
CC Name=3;
CC IsoId=Q5JTV8-3; Sequence=VSP_055704;
CC -!- TISSUE SPECIFICITY: Expressed in muscle, liver and kidney.
CC {ECO:0000269|PubMed:24856141}.
CC -!- DISEASE: Myopathy, autosomal recessive, with rigid spine and distal
CC joint contractures (MRRSDC) [MIM:617072]: An autosomal recessive
CC degenerative myopathy characterized by muscle weakness initially
CC involving the proximal lower limbs, followed by distal upper and lower
CC limb muscle weakness and atrophy. Other features include joint
CC contractures, rigid spine, and restricted pulmonary function. Cardiac
CC involvement has been observed in some patients. Disease onset is in the
CC first or second decades of life. {ECO:0000269|PubMed:24856141}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the TOR1AIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23247.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB13855.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14461.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF84184.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK001780; BAA91906.1; -; mRNA.
DR EMBL; AK021613; BAB13855.1; ALT_INIT; mRNA.
DR EMBL; AK023204; BAB14461.1; ALT_INIT; mRNA.
DR EMBL; AK291495; BAF84184.1; ALT_INIT; mRNA.
DR EMBL; AL353708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023247; AAH23247.1; ALT_INIT; mRNA.
DR EMBL; AL050126; CAB43282.1; -; mRNA.
DR CCDS; CCDS1335.1; -. [Q5JTV8-1]
DR CCDS; CCDS65737.1; -. [Q5JTV8-3]
DR PIR; T08767; T08767.
DR RefSeq; NP_001254507.1; NM_001267578.1. [Q5JTV8-3]
DR RefSeq; NP_056417.2; NM_015602.3. [Q5JTV8-1]
DR PDB; 4TVS; X-ray; 1.60 A; A/B=356-583.
DR PDBsum; 4TVS; -.
DR AlphaFoldDB; Q5JTV8; -.
DR SMR; Q5JTV8; -.
DR BioGRID; 117543; 210.
DR CORUM; Q5JTV8; -.
DR DIP; DIP-56692N; -.
DR IntAct; Q5JTV8; 65.
DR MINT; Q5JTV8; -.
DR STRING; 9606.ENSP00000435365; -.
DR GlyConnect; 1822; 3 N-Linked glycans (1 site).
DR GlyGen; Q5JTV8; 4 sites, 5 N-linked glycans (1 site), 1 O-linked glycan (2 sites).
DR iPTMnet; Q5JTV8; -.
DR MetOSite; Q5JTV8; -.
DR PhosphoSitePlus; Q5JTV8; -.
DR SwissPalm; Q5JTV8; -.
DR BioMuta; TOR1AIP1; -.
DR DMDM; 90101788; -.
DR EPD; Q5JTV8; -.
DR jPOST; Q5JTV8; -.
DR MassIVE; Q5JTV8; -.
DR MaxQB; Q5JTV8; -.
DR PaxDb; Q5JTV8; -.
DR PeptideAtlas; Q5JTV8; -.
DR PRIDE; Q5JTV8; -.
DR ProteomicsDB; 63233; -. [Q5JTV8-1]
DR ProteomicsDB; 63234; -. [Q5JTV8-2]
DR ABCD; Q5JTV8; 1 sequenced antibody.
DR Antibodypedia; 34423; 118 antibodies from 27 providers.
DR DNASU; 26092; -.
DR Ensembl; ENST00000528443.6; ENSP00000435365.2; ENSG00000143337.19. [Q5JTV8-3]
DR Ensembl; ENST00000606911.7; ENSP00000476687.1; ENSG00000143337.19. [Q5JTV8-1]
DR GeneID; 26092; -.
DR KEGG; hsa:26092; -.
DR MANE-Select; ENST00000606911.7; ENSP00000476687.1; NM_015602.4; NP_056417.2.
DR UCSC; uc001gnp.3; human. [Q5JTV8-1]
DR CTD; 26092; -.
DR DisGeNET; 26092; -.
DR GeneCards; TOR1AIP1; -.
DR HGNC; HGNC:29456; TOR1AIP1.
DR HPA; ENSG00000143337; Low tissue specificity.
DR MalaCards; TOR1AIP1; -.
DR MIM; 614512; gene.
DR MIM; 617072; phenotype.
DR neXtProt; NX_Q5JTV8; -.
DR OpenTargets; ENSG00000143337; -.
DR Orphanet; 424261; TOR1AIP1-related limb-girdle muscular dystrophy.
DR PharmGKB; PA142670715; -.
DR VEuPathDB; HostDB:ENSG00000143337; -.
DR eggNOG; ENOG502QUV7; Eukaryota.
DR GeneTree; ENSGT00390000012166; -.
DR HOGENOM; CLU_034263_0_1_1; -.
DR InParanoid; Q5JTV8; -.
DR OMA; FSEEGDT; -.
DR PhylomeDB; Q5JTV8; -.
DR TreeFam; TF329438; -.
DR PathwayCommons; Q5JTV8; -.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; Q5JTV8; -.
DR SIGNOR; Q5JTV8; -.
DR BioGRID-ORCS; 26092; 20 hits in 1100 CRISPR screens.
DR ChiTaRS; TOR1AIP1; human.
DR GeneWiki; TOR1AIP1; -.
DR GenomeRNAi; 26092; -.
DR Pharos; Q5JTV8; Tbio.
DR PRO; PR:Q5JTV8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5JTV8; protein.
DR Bgee; ENSG00000143337; Expressed in choroid plexus epithelium and 215 other tissues.
DR ExpressionAtlas; Q5JTV8; baseline and differential.
DR Genevisible; Q5JTV8; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:UniProtKB.
DR GO; GO:0005521; F:lamin binding; IEA:Ensembl.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0071763; P:nuclear membrane organization; IBA:GO_Central.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:UniProtKB.
DR GO; GO:0090435; P:protein localization to nuclear envelope; IEA:Ensembl.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR Gene3D; 3.40.50.12190; -; 1.
DR InterPro; IPR038599; LAP1C-like_C_sf.
DR InterPro; IPR008662; TOIP1/2.
DR PANTHER; PTHR18843; PTHR18843; 1.
DR Pfam; PF05609; LAP1C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Glycoprotein;
KW Isopeptide bond; Limb-girdle muscular dystrophy; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..583
FT /note="Torsin-1A-interacting protein 1"
FT /id="PRO_0000228835"
FT TOPO_DOM 1..338
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..583
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT REGION 1..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..583
FT /note="Interaction with TOR1A"
FT COILED 359..435
FT /evidence="ECO:0000255"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q921T2"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQX1"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQX1"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CROSSLNK 308
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 184
FT /note="P -> PA (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055704"
FT VAR_SEQ 283..487
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055705"
FT VARIANT 146
FT /note="M -> T (in dbSNP:rs1281378)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT /id="VAR_025717"
FT VARIANT 190
FT /note="V -> I (in a breast cancer sample; somatic mutation;
FT dbSNP:rs775134055)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035818"
FT VARIANT 276
FT /note="P -> R (in dbSNP:rs609521)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_025718"
FT VARIANT 293
FT /note="Q -> H (in dbSNP:rs17279712)"
FT /id="VAR_034566"
FT CONFLICT 160
FT /note="D -> V (in Ref. 1; BAB13855)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="Y -> C (in Ref. 1; BAB14461)"
FT /evidence="ECO:0000305"
FT HELIX 363..378
FT /evidence="ECO:0007829|PDB:4TVS"
FT HELIX 384..398
FT /evidence="ECO:0007829|PDB:4TVS"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:4TVS"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:4TVS"
FT HELIX 419..434
FT /evidence="ECO:0007829|PDB:4TVS"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:4TVS"
FT STRAND 442..445
FT /evidence="ECO:0007829|PDB:4TVS"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:4TVS"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:4TVS"
FT HELIX 454..470
FT /evidence="ECO:0007829|PDB:4TVS"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:4TVS"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:4TVS"
FT HELIX 486..490
FT /evidence="ECO:0007829|PDB:4TVS"
FT HELIX 491..496
FT /evidence="ECO:0007829|PDB:4TVS"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:4TVS"
FT STRAND 507..513
FT /evidence="ECO:0007829|PDB:4TVS"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:4TVS"
FT HELIX 525..542
FT /evidence="ECO:0007829|PDB:4TVS"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:4TVS"
FT HELIX 554..564
FT /evidence="ECO:0007829|PDB:4TVS"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:4TVS"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:4TVS"
SQ SEQUENCE 583 AA; 66248 MW; 3EE90CAAF49054FC CRC64;
MAGDGRRAEA VREGWGVYVT PRAPIREGRG RLAPQNGGSS DAPAYRTPPS RQGRREVRFS
DEPPEVYGDF EPLVAKERSP VGKRTRLEEF RSDSAKEEVR ESAYYLRSRQ RRQPRPQETE
EMKTRRTTRL QQQHSEQPPL QPSPVMTRRG LRDSHSSEED EASSQTDLSQ TISKKTVRSI
QEAPVSEDLV IRLRRPPLRY PRYEATSVQQ KVNFSEEGET EEDDQDSSHS SVTTVKARSR
DSDESGDKTT RSSSQYIESF WQSSQSQNFT AHDKQPSVLS SGYQKTPQEW APQTARIRTR
MQNDSILKSE LGNQSPSTSS RQVTGQPQNA SFVKRNRWWL LPLIAALASG SFWFFSTPEV
ETTAVQEFQN QMNQLKNKYQ GQDEKLWKRS QTFLEKHLNS SHPRSQPAIL LLTAARDAEE
ALRCLSEQIA DAYSSFRSVR AIRIDGTDKA TQDSDTVKLE VDQELSNGFK NGQNAAVVHR
FESFPAGSTL IFYKYCDHEN AAFKDVALVL TVLLEEETLG TSLGLKEVEE KVRDFLKVKF
TNSNTPNSYN HMDPDKLNGL WSRISHLVLP VQPENALKRG ICL
