Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Torsin-1A-interacting protein 1 (Lamin-associated protein 1B) (LAP1B)

 TOIP1_HUMAN             Reviewed;         583 AA.
Q5JTV8; A8K630; B0QZ57; Q5JTV6; Q8IZ65; Q9H8Y6; Q9HAJ1; Q9NV52;
Q9Y3X5;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
21-MAR-2006, sequence version 2.
23-MAY-2018, entry version 121.
RecName: Full=Torsin-1A-interacting protein 1;
AltName: Full=Lamin-associated protein 1B;
Short=LAP1B;
Name=TOR1AIP1; Synonyms=LAP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 87-583 (ISOFORM 1), AND VARIANTS
THR-146 AND ARG-276.
TISSUE=Embryo, Ovarian carcinoma, and Peripheral blood;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-583 (ISOFORM 1), AND
VARIANTS THR-146 AND ARG-276.
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 404-583 (ISOFORM 1).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
TOPOLOGY, AND SUBCELLULAR LOCATION.
PubMed=12061773; DOI=10.1016/S0006-291X(02)00563-6;
Kondo Y., Kondoh J., Hayashi D., Ban T., Takagi M., Kamei Y.,
Tsuji L., Kim J., Yoneda Y.;
"Molecular cloning of one isotype of human lamina-associated
polypeptide 1s and a topological analysis using its deletion
mutants.";
Biochem. Biophys. Res. Commun. 294:770-778(2002).
[6]
INTERACTION WITH TOR1A.
PubMed=15767459; DOI=10.1083/jcb.200411026;
Goodchild R.E., Dauer W.T.;
"The AAA+ protein torsinA interacts with a conserved domain present in
LAP1 and a novel ER protein.";
J. Cell Biol. 168:855-862(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND THR-220, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
INTERACTION WITH VIM.
PubMed=16361107; DOI=10.1016/j.nbd.2005.10.012;
Hewett J.W., Zeng J., Niland B.P., Bragg D.C., Breakefield X.O.;
"Dystonia-causing mutant torsinA inhibits cell adhesion and neurite
extension through interference with cytoskeletal dynamics.";
Neurobiol. Dis. 22:98-111(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
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, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-399.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-156; SER-157;
THR-220; SER-227 AND SER-305, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; THR-220 AND
SER-315, VARIANT [LARGE SCALE ANALYSIS] THR-146, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, VARIANT [LARGE
SCALE ANALYSIS] THR-146, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-154; SER-156;
SER-157; SER-186; SER-215; THR-220 AND SER-315, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
FUNCTION AS ATPASE ACTIVATOR, AND INTERACTION WITH TOR1A.
PubMed=23569223; DOI=10.1073/pnas.1300676110;
Zhao C., Brown R.S., Chase A.R., Eisele M.R., Schlieker C.;
"Regulation of Torsin ATPases by LAP1 and LULL1.";
Proc. Natl. Acad. Sci. U.S.A. 110:E1545-1554(2013).
[20]
SUBCELLULAR LOCATION.
PubMed=24275647; DOI=10.1074/jbc.M113.515791;
Rose A.E., Zhao C., Turner E.M., Steyer A.M., Schlieker C.;
"Arresting a Torsin ATPase reshapes the endoplasmic reticulum.";
J. Biol. Chem. 289:552-564(2014).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-154; SER-156;
SER-157; SER-215 AND THR-220, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-308, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[24]
VARIANT [LARGE SCALE ANALYSIS] ILE-190.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[25]
INVOLVEMENT IN LGMD2Y, AND TISSUE SPECIFICITY.
PubMed=24856141; DOI=10.1016/j.nmd.2014.04.007;
Kayman-Kurekci G., Talim B., Korkusuz P., Sayar N., Sarioglu T.,
Oncel I., Sharafi P., Gundesli H., Balci-Hayta B., Purali N.,
Serdaroglu-Oflazer P., Topaloglu H., Dincer P.;
"Mutation in TOR1AIP1 encoding LAP1B in a form of muscular dystrophy:
a novel gene related to nuclear envelopathies.";
Neuromuscul. Disord. 24:624-633(2014).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:23569223}.
-!- SUBUNIT: Interacts with ATP1B4. Interacts with TOR1A (ATP-bound).
Interacts with TOR1B, TOR2A and TOR3A. Interacts with VIM.
{ECO:0000269|PubMed:15767459, ECO:0000269|PubMed:16361107,
ECO:0000269|PubMed:23569223}.
-!- INTERACTION:
Q9NYB0:TERF2IP; NbExp=2; IntAct=EBI-2559665, EBI-750109;
-!- SUBCELLULAR LOCATION: Nucleus inner membrane
{ECO:0000269|PubMed:12061773, ECO:0000269|PubMed:24275647};
Single-pass membrane protein {ECO:0000269|PubMed:12061773,
ECO:0000269|PubMed:24275647}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q5JTV8-1; Sequence=Displayed;
Name=2;
IsoId=Q5JTV8-2; Sequence=VSP_055704, VSP_055705;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q5JTV8-3; Sequence=VSP_055704;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in muscle, liver and kidney.
{ECO:0000269|PubMed:24856141}.
-!- DISEASE: Limb-girdle muscular dystrophy 2Y (LGMD2Y) [MIM:617072]:
An autosomal recessive form of limb-girdle muscular dystrophy, a
degenerative myopathy characterized by slowly progressive wasting
and weakness of the proximal muscles of arms and legs around the
pelvic or shoulder girdles, elevated creatine kinase levels and
dystrophic features on muscle biopsy. LGMD2Y is characterized by
muscle weakness initially involving the proximal lower limbs,
followed by distal upper and lower limb muscle weakness and
atrophy. Other features include joint contractures, rigid spine,
and restricted pulmonary function. Cardiac involvement has been
observed in some patients. Disease onset is in the first or second
decades of life. {ECO:0000269|PubMed:24856141}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the TOR1AIP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH23247.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB13855.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB14461.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAF84184.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK001780; BAA91906.1; -; mRNA.
EMBL; AK021613; BAB13855.1; ALT_INIT; mRNA.
EMBL; AK023204; BAB14461.1; ALT_INIT; mRNA.
EMBL; AK291495; BAF84184.1; ALT_INIT; mRNA.
EMBL; AL353708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC023247; AAH23247.1; ALT_INIT; mRNA.
EMBL; AL050126; CAB43282.1; -; mRNA.
CCDS; CCDS1335.1; -. [Q5JTV8-1]
CCDS; CCDS65737.1; -. [Q5JTV8-3]
PIR; T08767; T08767.
RefSeq; NP_001254507.1; NM_001267578.1. [Q5JTV8-3]
RefSeq; NP_056417.2; NM_015602.3. [Q5JTV8-1]
UniGene; Hs.496459; -.
PDB; 4TVS; X-ray; 1.60 A; A/B=356-583.
PDBsum; 4TVS; -.
ProteinModelPortal; Q5JTV8; -.
SMR; Q5JTV8; -.
BioGrid; 117543; 54.
DIP; DIP-56692N; -.
IntAct; Q5JTV8; 43.
MINT; Q5JTV8; -.
STRING; 9606.ENSP00000393292; -.
iPTMnet; Q5JTV8; -.
PhosphoSitePlus; Q5JTV8; -.
SwissPalm; Q5JTV8; -.
BioMuta; TOR1AIP1; -.
DMDM; 90101788; -.
EPD; Q5JTV8; -.
MaxQB; Q5JTV8; -.
PaxDb; Q5JTV8; -.
PeptideAtlas; Q5JTV8; -.
PRIDE; Q5JTV8; -.
DNASU; 26092; -.
Ensembl; ENST00000528443; ENSP00000435365; ENSG00000143337. [Q5JTV8-3]
Ensembl; ENST00000606911; ENSP00000476687; ENSG00000143337. [Q5JTV8-1]
GeneID; 26092; -.
KEGG; hsa:26092; -.
UCSC; uc001gnp.3; human. [Q5JTV8-1]
CTD; 26092; -.
DisGeNET; 26092; -.
EuPathDB; HostDB:ENSG00000143337.18; -.
GeneCards; TOR1AIP1; -.
H-InvDB; HIX0001382; -.
H-InvDB; HIX0199815; -.
HGNC; HGNC:29456; TOR1AIP1.
HPA; HPA047151; -.
HPA; HPA050546; -.
MalaCards; TOR1AIP1; -.
MIM; 614512; gene.
MIM; 617072; phenotype.
neXtProt; NX_Q5JTV8; -.
OpenTargets; ENSG00000143337; -.
PharmGKB; PA142670715; -.
eggNOG; ENOG410IJUB; Eukaryota.
eggNOG; ENOG4111IZJ; LUCA.
GeneTree; ENSGT00390000012166; -.
HOVERGEN; HBG083152; -.
InParanoid; Q5JTV8; -.
PhylomeDB; Q5JTV8; -.
TreeFam; TF329438; -.
ChiTaRS; TOR1AIP1; human.
GeneWiki; TOR1AIP1; -.
GenomeRNAi; 26092; -.
PMAP-CutDB; Q5JTV8; -.
PRO; PR:Q5JTV8; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143337; -.
CleanEx; HS_TOR1AIP1; -.
ExpressionAtlas; Q5JTV8; baseline and differential.
Genevisible; Q5JTV8; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
GO; GO:0008092; F:cytoskeletal protein binding; IPI:UniProtKB.
GO; GO:0005521; F:lamin binding; IEA:Ensembl.
GO; GO:0071763; P:nuclear membrane organization; IEA:Ensembl.
GO; GO:0032781; P:positive regulation of ATPase activity; IDA:UniProtKB.
GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
Gene3D; 3.40.50.12190; -; 1.
InterPro; IPR008662; Lamina-ass_polypeptide_CLAP1C.
InterPro; IPR038599; LAP1C-like_C_sf.
PANTHER; PTHR18843; PTHR18843; 1.
Pfam; PF05609; LAP1C; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Coiled coil; Complete proteome;
Glycoprotein; Isopeptide bond; Limb-girdle muscular dystrophy;
Membrane; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1 583 Torsin-1A-interacting protein 1.
/FTId=PRO_0000228835.
TOPO_DOM 1 338 Nuclear. {ECO:0000255}.
TRANSMEM 339 355 Helical. {ECO:0000255}.
TOPO_DOM 356 583 Perinuclear space. {ECO:0000255}.
REGION 356 583 Interaction with TOR1A.
COILED 359 435 {ECO:0000255}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000250|UniProtKB:Q921T2}.
MOD_RES 135 135 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 154 154 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 220 220 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 227 227 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 230 230 Phosphoserine.
{ECO:0000250|UniProtKB:Q5PQX1}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000250|UniProtKB:Q5PQX1}.
MOD_RES 305 305 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CARBOHYD 399 399 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CROSSLNK 308 308 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 184 184 P -> PA (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055704.
VAR_SEQ 283 487 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055705.
VARIANT 146 146 M -> T (in dbSNP:rs1281378).
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_025717.
VARIANT 190 190 V -> I (in a breast cancer sample;
somatic mutation; dbSNP:rs775134055).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035818.
VARIANT 276 276 P -> R (in dbSNP:rs609521).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_025718.
VARIANT 293 293 Q -> H (in dbSNP:rs17279712).
/FTId=VAR_034566.
CONFLICT 160 160 D -> V (in Ref. 1; BAB13855).
{ECO:0000305}.
CONFLICT 200 200 Y -> C (in Ref. 1; BAB14461).
{ECO:0000305}.
HELIX 363 378 {ECO:0000244|PDB:4TVS}.
HELIX 384 398 {ECO:0000244|PDB:4TVS}.
STRAND 408 414 {ECO:0000244|PDB:4TVS}.
HELIX 416 418 {ECO:0000244|PDB:4TVS}.
HELIX 419 434 {ECO:0000244|PDB:4TVS}.
HELIX 435 437 {ECO:0000244|PDB:4TVS}.
STRAND 442 445 {ECO:0000244|PDB:4TVS}.
HELIX 446 448 {ECO:0000244|PDB:4TVS}.
TURN 449 451 {ECO:0000244|PDB:4TVS}.
HELIX 454 470 {ECO:0000244|PDB:4TVS}.
STRAND 475 479 {ECO:0000244|PDB:4TVS}.
HELIX 481 483 {ECO:0000244|PDB:4TVS}.
HELIX 486 490 {ECO:0000244|PDB:4TVS}.
HELIX 491 496 {ECO:0000244|PDB:4TVS}.
TURN 498 500 {ECO:0000244|PDB:4TVS}.
STRAND 507 513 {ECO:0000244|PDB:4TVS}.
STRAND 515 517 {ECO:0000244|PDB:4TVS}.
HELIX 525 542 {ECO:0000244|PDB:4TVS}.
STRAND 548 550 {ECO:0000244|PDB:4TVS}.
HELIX 554 564 {ECO:0000244|PDB:4TVS}.
STRAND 566 570 {ECO:0000244|PDB:4TVS}.
HELIX 575 577 {ECO:0000244|PDB:4TVS}.
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


Related products :

Catalog number Product name Quantity
EIAAB43378 Lamina-associated polypeptide 1B,Lamina-associated polypeptide 1C,Lap1b,Lap1c,Rat,Rattus norvegicus,Tor1aip1,Torsin-1A-interacting protein 1
EIAAB43454 Homo sapiens,Human,TOR2A,TORP1,Torsin family 2 member A,Torsin-2A,Torsin-related protein 1,UNQ6408_PRO21181
E1843h Rat ELISA Kit FOR Torsin-1A-interacting protein 1 96T
CSB-EL024068RA Rat Torsin-1A-interacting protein 1(TOR1AIP1) ELISA kit 96T
H6750 Torsin-1A-interacting protein 1 (TOR1AIP1), Rat, ELISA Kit 96T
E7642h Human Torsin A Interacting Protein 1 ELISA Kit 96T
E6864h Human Torsin A Interacting Protein 2 ELISA Kit 96T
H6753 Torsin-1A-interacting protein 2 (TOR1AIP2), Rat, ELISA Kit 96T
CSB-EL024069RA Rat Torsin-1A-interacting protein 2(TOR1AIP2) ELISA kit 96T
H6748 Torsin-1A-interacting protein 1 (TOR1AIP1), Human, ELISA Kit 96T
CSB-EL024069HU Human Torsin-1A-interacting protein 2(TOR1AIP2) ELISA kit 96T
H6749 Torsin-1A-interacting protein 1 (TOR1AIP1), Mouse, ELISA Kit 96T
H6751 Torsin-1A-interacting protein 2 (TOR1AIP2), Human, ELISA Kit 96T
CSB-EL024069MO Mouse Torsin-1A-interacting protein 2(TOR1AIP2) ELISA kit 96T
CSB-EL024068MO Mouse Torsin-1A-interacting protein 1(TOR1AIP1) ELISA kit 96T
EIAAB43382 Mouse,Mus musculus,Tor1aip2,Torsin-1A-interacting protein 2
H6752 Torsin-1A-interacting protein 2 (TOR1AIP2), Mouse, ELISA Kit 96T
CSB-EL024069RA Rat Torsin-1A-interacting protein 2(TOR1AIP2) ELISA kit SpeciesRat 96T
CSB-EL024068RA Rat Torsin-1A-interacting protein 1(TOR1AIP1) ELISA kit SpeciesRat 96T
CSB-EL024068HU Human Torsin-1A-interacting protein 1(TOR1AIP1) ELISA kit 96T
EIAAB43381 Rat,Rattus norvegicus,Tor1aip2,Torsin-1A-interacting protein 2
CSB-EL024069HU Human Torsin-1A-interacting protein 2(TOR1AIP2) ELISA kit SpeciesHuman 96T
CSB-EL024068HU Human Torsin-1A-interacting protein 1(TOR1AIP1) ELISA kit SpeciesHuman 96T
CSB-EL024069MO Mouse Torsin-1A-interacting protein 2(TOR1AIP2) ELISA kit SpeciesMouse 96T
TOIP2_RAT ELISA Kit FOR Torsin-1A-interacting protein 2; organism: Rat; gene name: Tor1aip2 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur