Full text data of TOR1AIP1
TOR1AIP1
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Torsin-1A-interacting protein 1 (Lamin-associated protein 1B; LAP1B)
Torsin-1A-interacting protein 1 (Lamin-associated protein 1B; LAP1B)
UniProt
Q5JTV8
ID TOIP1_HUMAN Reviewed; 583 AA.
AC Q5JTV8; A8K630; B0QZ57; Q5JTV6; Q8IZ65; Q9H8Y6; Q9HAJ1; Q9NV52;
read moreAC Q9Y3X5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 22-JAN-2014, entry version 81.
DE RecName: Full=Torsin-1A-interacting protein 1;
DE AltName: Full=Lamin-associated protein 1B;
DE Short=LAP1B;
GN Name=TOR1AIP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 87-583 (ISOFORM 1), AND VARIANTS
RP 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RP VARIANTS 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
RT project: 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.
RX PubMed=12061773; DOI=10.1016/S0006-291X(02)00563-6;
RA Kondo Y., Kondoh J., Hayashi D., Ban T., Takagi M., Kamei Y.,
RA Tsuji L., Kim J., Yoneda Y.;
RT "Molecular cloning of one isotype of human lamina-associated
RT polypeptide 1s and a topological analysis using its deletion
RT mutants.";
RL Biochem. Biophys. Res. Commun. 294:770-778(2002).
RN [6]
RP INTERACTION WITH TORSIN-A.
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
RT LAP1 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
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,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 [9]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
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 MASS SPECTROMETRY.
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 [11]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-399, AND MASS
RP SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-156; SER-157;
RP THR-220; SER-227 AND SER-305, AND MASS SPECTROMETRY.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; THR-220 AND
RP SER-315, VARIANT [LARGE SCALE ANALYSIS] THR-146, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, VARIANT [LARGE
RP SCALE ANALYSIS] THR-146, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Binds to A- and B-type lamins. Possible role in membrane
CC attachment and assembly of the nuclear lamina (By similarity).
CC -!- SUBUNIT: Interacts with ATP1B4 (By similarity). Interacts with
CC TOR1A.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass membrane
CC protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5JTV8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JTV8-2; Sequence=VSP_017710;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the TOR1AIP family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23247.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB13855.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14461.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAF84184.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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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; CAI41051.1; -; Genomic_DNA.
DR EMBL; AL353708; CAQ09353.1; -; Genomic_DNA.
DR EMBL; BC023247; AAH23247.1; ALT_INIT; mRNA.
DR EMBL; AL050126; CAB43282.1; -; mRNA.
DR PIR; T08767; T08767.
DR RefSeq; NP_056417.2; NM_015602.3.
DR UniGene; Hs.496459; -.
DR ProteinModelPortal; Q5JTV8; -.
DR DIP; DIP-56692N; -.
DR IntAct; Q5JTV8; 4.
DR PhosphoSite; Q5JTV8; -.
DR DMDM; 90101788; -.
DR PaxDb; Q5JTV8; -.
DR PRIDE; Q5JTV8; -.
DR DNASU; 26092; -.
DR Ensembl; ENST00000435319; ENSP00000393292; ENSG00000143337.
DR GeneID; 26092; -.
DR KEGG; hsa:26092; -.
DR UCSC; uc001gnp.2; human.
DR CTD; 26092; -.
DR GeneCards; GC01P179851; -.
DR H-InvDB; HIX0001382; -.
DR H-InvDB; HIX0199815; -.
DR HGNC; HGNC:29456; TOR1AIP1.
DR HPA; HPA047151; -.
DR HPA; HPA050546; -.
DR MIM; 614512; gene.
DR neXtProt; NX_Q5JTV8; -.
DR PharmGKB; PA142670715; -.
DR eggNOG; NOG40503; -.
DR HOVERGEN; HBG083152; -.
DR PhylomeDB; Q5JTV8; -.
DR GeneWiki; TOR1AIP1; -.
DR GenomeRNAi; 26092; -.
DR NextBio; 48033; -.
DR PMAP-CutDB; Q5JTV8; -.
DR PRO; PR:Q5JTV8; -.
DR ArrayExpress; Q5JTV8; -.
DR Bgee; Q5JTV8; -.
DR CleanEx; HS_TOR1AIP1; -.
DR Genevestigator; Q5JTV8; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071763; P:nuclear membrane organization; IEA:Ensembl.
DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR InterPro; IPR008662; Lamina-ass_polypeptide_CLAP1C.
DR Pfam; PF05609; LAP1C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Glycoprotein;
KW Membrane; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 583 Torsin-1A-interacting protein 1.
FT /FTId=PRO_0000228835.
FT TOPO_DOM 1 338 Nuclear (Potential).
FT TRANSMEM 339 355 Helical; (Potential).
FT TOPO_DOM 356 583 Perinuclear space (Potential).
FT COILED 359 435 Potential.
FT MOD_RES 135 135 Phosphoserine.
FT MOD_RES 143 143 Phosphoserine.
FT MOD_RES 154 154 Phosphoserine.
FT MOD_RES 156 156 Phosphoserine.
FT MOD_RES 157 157 Phosphoserine.
FT MOD_RES 186 186 Phosphoserine.
FT MOD_RES 215 215 Phosphoserine.
FT MOD_RES 220 220 Phosphothreonine.
FT MOD_RES 227 227 Phosphoserine.
FT MOD_RES 305 305 Phosphoserine.
FT MOD_RES 315 315 Phosphoserine.
FT CARBOHYD 399 399 N-linked (GlcNAc...).
FT VAR_SEQ 283 487 Missing (in isoform 2).
FT /FTId=VSP_017710.
FT VARIANT 146 146 M -> T (in dbSNP:rs1281378).
FT /FTId=VAR_025717.
FT VARIANT 190 190 V -> I (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035818.
FT VARIANT 276 276 P -> R (in dbSNP:rs609521).
FT /FTId=VAR_025718.
FT VARIANT 293 293 Q -> H (in dbSNP:rs17279712).
FT /FTId=VAR_034566.
FT CONFLICT 160 160 D -> V (in Ref. 1; BAB13855).
FT CONFLICT 184 184 P -> PA (in Ref. 1; BAA91906 and 2;
FT CAQ09353).
FT CONFLICT 200 200 Y -> C (in Ref. 1; BAB14461).
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
//
ID TOIP1_HUMAN Reviewed; 583 AA.
AC Q5JTV8; A8K630; B0QZ57; Q5JTV6; Q8IZ65; Q9H8Y6; Q9HAJ1; Q9NV52;
read moreAC Q9Y3X5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 22-JAN-2014, entry version 81.
DE RecName: Full=Torsin-1A-interacting protein 1;
DE AltName: Full=Lamin-associated protein 1B;
DE Short=LAP1B;
GN Name=TOR1AIP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 87-583 (ISOFORM 1), AND VARIANTS
RP 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RP VARIANTS 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
RT project: 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.
RX PubMed=12061773; DOI=10.1016/S0006-291X(02)00563-6;
RA Kondo Y., Kondoh J., Hayashi D., Ban T., Takagi M., Kamei Y.,
RA Tsuji L., Kim J., Yoneda Y.;
RT "Molecular cloning of one isotype of human lamina-associated
RT polypeptide 1s and a topological analysis using its deletion
RT mutants.";
RL Biochem. Biophys. Res. Commun. 294:770-778(2002).
RN [6]
RP INTERACTION WITH TORSIN-A.
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
RT LAP1 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
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,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 [9]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
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 MASS SPECTROMETRY.
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 [11]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-399, AND MASS
RP SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-156; SER-157;
RP THR-220; SER-227 AND SER-305, AND MASS SPECTROMETRY.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; THR-220 AND
RP SER-315, VARIANT [LARGE SCALE ANALYSIS] THR-146, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, VARIANT [LARGE
RP SCALE ANALYSIS] THR-146, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Binds to A- and B-type lamins. Possible role in membrane
CC attachment and assembly of the nuclear lamina (By similarity).
CC -!- SUBUNIT: Interacts with ATP1B4 (By similarity). Interacts with
CC TOR1A.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass membrane
CC protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5JTV8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JTV8-2; Sequence=VSP_017710;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the TOR1AIP family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23247.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB13855.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14461.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAF84184.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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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; CAI41051.1; -; Genomic_DNA.
DR EMBL; AL353708; CAQ09353.1; -; Genomic_DNA.
DR EMBL; BC023247; AAH23247.1; ALT_INIT; mRNA.
DR EMBL; AL050126; CAB43282.1; -; mRNA.
DR PIR; T08767; T08767.
DR RefSeq; NP_056417.2; NM_015602.3.
DR UniGene; Hs.496459; -.
DR ProteinModelPortal; Q5JTV8; -.
DR DIP; DIP-56692N; -.
DR IntAct; Q5JTV8; 4.
DR PhosphoSite; Q5JTV8; -.
DR DMDM; 90101788; -.
DR PaxDb; Q5JTV8; -.
DR PRIDE; Q5JTV8; -.
DR DNASU; 26092; -.
DR Ensembl; ENST00000435319; ENSP00000393292; ENSG00000143337.
DR GeneID; 26092; -.
DR KEGG; hsa:26092; -.
DR UCSC; uc001gnp.2; human.
DR CTD; 26092; -.
DR GeneCards; GC01P179851; -.
DR H-InvDB; HIX0001382; -.
DR H-InvDB; HIX0199815; -.
DR HGNC; HGNC:29456; TOR1AIP1.
DR HPA; HPA047151; -.
DR HPA; HPA050546; -.
DR MIM; 614512; gene.
DR neXtProt; NX_Q5JTV8; -.
DR PharmGKB; PA142670715; -.
DR eggNOG; NOG40503; -.
DR HOVERGEN; HBG083152; -.
DR PhylomeDB; Q5JTV8; -.
DR GeneWiki; TOR1AIP1; -.
DR GenomeRNAi; 26092; -.
DR NextBio; 48033; -.
DR PMAP-CutDB; Q5JTV8; -.
DR PRO; PR:Q5JTV8; -.
DR ArrayExpress; Q5JTV8; -.
DR Bgee; Q5JTV8; -.
DR CleanEx; HS_TOR1AIP1; -.
DR Genevestigator; Q5JTV8; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071763; P:nuclear membrane organization; IEA:Ensembl.
DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR InterPro; IPR008662; Lamina-ass_polypeptide_CLAP1C.
DR Pfam; PF05609; LAP1C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Glycoprotein;
KW Membrane; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 583 Torsin-1A-interacting protein 1.
FT /FTId=PRO_0000228835.
FT TOPO_DOM 1 338 Nuclear (Potential).
FT TRANSMEM 339 355 Helical; (Potential).
FT TOPO_DOM 356 583 Perinuclear space (Potential).
FT COILED 359 435 Potential.
FT MOD_RES 135 135 Phosphoserine.
FT MOD_RES 143 143 Phosphoserine.
FT MOD_RES 154 154 Phosphoserine.
FT MOD_RES 156 156 Phosphoserine.
FT MOD_RES 157 157 Phosphoserine.
FT MOD_RES 186 186 Phosphoserine.
FT MOD_RES 215 215 Phosphoserine.
FT MOD_RES 220 220 Phosphothreonine.
FT MOD_RES 227 227 Phosphoserine.
FT MOD_RES 305 305 Phosphoserine.
FT MOD_RES 315 315 Phosphoserine.
FT CARBOHYD 399 399 N-linked (GlcNAc...).
FT VAR_SEQ 283 487 Missing (in isoform 2).
FT /FTId=VSP_017710.
FT VARIANT 146 146 M -> T (in dbSNP:rs1281378).
FT /FTId=VAR_025717.
FT VARIANT 190 190 V -> I (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035818.
FT VARIANT 276 276 P -> R (in dbSNP:rs609521).
FT /FTId=VAR_025718.
FT VARIANT 293 293 Q -> H (in dbSNP:rs17279712).
FT /FTId=VAR_034566.
FT CONFLICT 160 160 D -> V (in Ref. 1; BAB13855).
FT CONFLICT 184 184 P -> PA (in Ref. 1; BAA91906 and 2;
FT CAQ09353).
FT CONFLICT 200 200 Y -> C (in Ref. 1; BAB14461).
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
//
MIM
614512
*RECORD*
*FIELD* NO
614512
*FIELD* TI
*614512 TORSIN A-INTERACTING PROTEIN 1; TOR1AIP1
;;LAMIN-ASSOCIATED PROTEIN 1; LAP1;;
read moreLAP1B
*FIELD* TX
CLONING
By searching a database for sequences similar to rat Lap1, followed by
PCR of a HeLa cell cDNA library, Kondo et al. (2002) cloned human
TOR1AIP1, which they designated LAP1B due to its similarity with rat
Lap1 isoform B. The deduced 584-amino acid protein has a calculated
molecular mass of 66.3 kD. LAP1B is predicted to have an N-terminal
nucleoplasmic domain, a transmembrane domain, and a C-terminal luminal
domain positioned between the inner and outer nuclear membranes.
Fluorescence-tagged LAP1B localized to the nuclear rim of transfected
HEK293 cells.
Using RT-PCR, Goodchild and Dauer (2005) found variable expression of
Lap1 in all mouse tissues examined.
GENE FUNCTION
Using mutation analysis and fluorescence microscopy, Kondo et al. (2002)
found that the C-terminal half of the nucleoplasmic domain and the
transmembrane region of LAP1B were required for localization of LAP1B at
the nuclear rim of transfected cells.
Goodchild and Dauer (2005) found that mouse torsin-1A (TOR1A; 605204)
interacted with both Lap1 and Lull1 (TOR1AIP2; 614513) in transfected
baby hamster kidney (BHK) cells. An ATPase-dead torsin-1A mutant and
torsin-1A with a glutamate deletion (605204.0001) associated with
early-onset torsion dystonia (DYT1; 128100) showed enhanced interaction
with Lap1 and Lull1. Mutation analysis revealed that the C-terminal
luminal domain of Lap1 or Lull1 was required for interaction with
torsin-1A. Torsin-1A normally localizes predominantly to the endoplasmic
reticulum, but interaction of torsin-1A with Lap1 recruited torsin-1A to
the nuclear envelope in BHK cells. Recruitment by Lap1 was enhanced with
ATPase-dead torsin-1A and with torsin-1A with the glutamate deletion.
MAPPING
By genomic sequence analysis, Goodchild and Dauer (2005) mapped the
TOR1AIP1 gene to chromosome 1q24, adjacent to the TOR1AIP2 gene. These
genes appeared to have arisen from a gene duplication event.
*FIELD* RF
1. 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.
2. 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.
*FIELD* CD
Patricia A. Hartz: 2/29/2012
*FIELD* ED
mgross: 02/29/2012
mgross: 2/29/2012
*RECORD*
*FIELD* NO
614512
*FIELD* TI
*614512 TORSIN A-INTERACTING PROTEIN 1; TOR1AIP1
;;LAMIN-ASSOCIATED PROTEIN 1; LAP1;;
read moreLAP1B
*FIELD* TX
CLONING
By searching a database for sequences similar to rat Lap1, followed by
PCR of a HeLa cell cDNA library, Kondo et al. (2002) cloned human
TOR1AIP1, which they designated LAP1B due to its similarity with rat
Lap1 isoform B. The deduced 584-amino acid protein has a calculated
molecular mass of 66.3 kD. LAP1B is predicted to have an N-terminal
nucleoplasmic domain, a transmembrane domain, and a C-terminal luminal
domain positioned between the inner and outer nuclear membranes.
Fluorescence-tagged LAP1B localized to the nuclear rim of transfected
HEK293 cells.
Using RT-PCR, Goodchild and Dauer (2005) found variable expression of
Lap1 in all mouse tissues examined.
GENE FUNCTION
Using mutation analysis and fluorescence microscopy, Kondo et al. (2002)
found that the C-terminal half of the nucleoplasmic domain and the
transmembrane region of LAP1B were required for localization of LAP1B at
the nuclear rim of transfected cells.
Goodchild and Dauer (2005) found that mouse torsin-1A (TOR1A; 605204)
interacted with both Lap1 and Lull1 (TOR1AIP2; 614513) in transfected
baby hamster kidney (BHK) cells. An ATPase-dead torsin-1A mutant and
torsin-1A with a glutamate deletion (605204.0001) associated with
early-onset torsion dystonia (DYT1; 128100) showed enhanced interaction
with Lap1 and Lull1. Mutation analysis revealed that the C-terminal
luminal domain of Lap1 or Lull1 was required for interaction with
torsin-1A. Torsin-1A normally localizes predominantly to the endoplasmic
reticulum, but interaction of torsin-1A with Lap1 recruited torsin-1A to
the nuclear envelope in BHK cells. Recruitment by Lap1 was enhanced with
ATPase-dead torsin-1A and with torsin-1A with the glutamate deletion.
MAPPING
By genomic sequence analysis, Goodchild and Dauer (2005) mapped the
TOR1AIP1 gene to chromosome 1q24, adjacent to the TOR1AIP2 gene. These
genes appeared to have arisen from a gene duplication event.
*FIELD* RF
1. 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.
2. 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.
*FIELD* CD
Patricia A. Hartz: 2/29/2012
*FIELD* ED
mgross: 02/29/2012
mgross: 2/29/2012