TACC1_HUMAN
ID TACC1_HUMAN Reviewed; 805 AA.
AC O75410; B2RBD9; B4E302; D3DSX6; Q6Y687; Q86YG7; Q8IUJ2; Q8IUJ3; Q8IUJ4;
AC Q8IZG2; Q8NEY7; Q9UPP9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Transforming acidic coiled-coil-containing protein 1;
DE AltName: Full=Gastric cancer antigen Ga55;
DE AltName: Full=Taxin-1;
GN Name=TACC1; Synonyms=KIAA1103;
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 [MRNA] (ISOFORM 1).
RX PubMed=10435627; DOI=10.1038/sj.onc.1202801;
RA Still I.H., Hamilton M., Vince P., Wolfman A., Cowell J.K.;
RT "Cloning of TACC1, an embryonically expressed, potentially transforming
RT coiled coil containing gene, from the 8p11 breast cancer amplicon.";
RL Oncogene 18:4032-4038(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RX PubMed=15207008; DOI=10.1186/1471-2148-4-16;
RA Still I.H., Vettaikkorumakankauv A.K., DiMatteo A., Liang P.;
RT "Structure-function evolution of the transforming acidic coiled coil genes
RT revealed by analysis of phylogenetically diverse organisms.";
RL BMC Evol. Biol. 4:16-16(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
RA Li F., Yao K.T.;
RT "Cloning of a novel human gene similar to TACC1.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 9).
RC TISSUE=Testis, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 364-805 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 450-805 (ISOFORM 2).
RC TISSUE=Gastric adenocarcinoma;
RX PubMed=12087473; DOI=10.1038/sj.bjc.6600321;
RA Line A., Stengrevics A., Slucka Z., Li G., Jankevics E., Rees R.C.;
RT "Serological identification and expression analysis of gastric cancer-
RT associated genes.";
RL Br. J. Cancer 86:1824-1830(2002).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-543 (ISOFORM 3), NUCLEOTIDE SEQUENCE OF
RP 1-571 (ISOFORMS 4 AND 5), AND TISSUE SPECIFICITY.
RC TISSUE=Stomach cancer;
RX PubMed=12547166; DOI=10.1016/s0165-4608(02)00607-6;
RA Line A., Slucka Z., Stengrevics A., Li G., Rees R.C.;
RT "Altered splicing pattern of TACC1 mRNA in gastric cancer.";
RL Cancer Genet. Cytogenet. 139:78-83(2002).
RN [10]
RP CHARACTERIZATION.
RC TISSUE=Brain, Fetal brain, and Skeletal muscle;
RX PubMed=11121038; DOI=10.1073/pnas.97.26.14352;
RA Gergely F., Karlsson C., Still I.H., Cowell J.K., Kilmartin J., Raff J.W.;
RT "The TACC domain identifies a family of centrosomal proteins that can
RT interact with microtubules.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14352-14357(2000).
RN [11]
RP INTERACTION WITH KIAA0097 AND YEATS4.
RX PubMed=11903063; DOI=10.1042/0264-6021:3630195;
RA Lauffart B., Howell S.J., Tasch J.E., Cowell J.K., Still I.H.;
RT "Interaction of the transforming acidic coiled-coil 1 (TACC1) protein with
RT ch-TOG and GAS41/NuBI1 suggests multiple TACC1-containing protein complexes
RT in human cells.";
RL Biochem. J. 363:195-200(2002).
RN [12]
RP INTERACTION WITH LSM7 AND SNRPG, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=12165861; DOI=10.1038/sj.onc.1205658;
RA Conte N., Charafe-Jauffret E., Delaval B., Adelaide J., Ginestier C.,
RA Geneix J., Isnardon D., Jacquemier J., Birnbaum D.;
RT "Carcinogenesis and translational controls: TACC1 is down-regulated in
RT human cancers and associates with mRNA regulators.";
RL Oncogene 21:5619-5630(2002).
RN [13]
RP INTERACTION WITH KIAA0097; LSM7; TDRD7 AND AURKA.
RX PubMed=14603251; DOI=10.1038/sj.onc.1206972;
RA Conte N., Delaval B., Ginestier C., Ferrand A., Isnardon D., Larroque C.,
RA Prigent C., Seraphin B., Jacquemier J., Birnbaum D.;
RT "TACC1-chTOG-Aurora A protein complex in breast cancer.";
RL Oncogene 22:8102-8116(2003).
RN [14]
RP INTERACTION WITH GCN5L2 AND PCAF, AND SUBCELLULAR LOCATION.
RX PubMed=14767476; DOI=10.1038/sj.onc.1207424;
RA Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H.;
RT "The transforming acidic coiled coil proteins interact with nuclear histone
RT acetyltransferases.";
RL Oncogene 23:2559-2563(2004).
RN [15]
RP INTERACTION WITH AURKB.
RX PubMed=15064709; DOI=10.1038/sj.onc.1207593;
RA Delaval B., Ferrand A., Conte N., Larroque C., Hernandez-Verdun D.,
RA Prigent C., Birnbaum D.;
RT "Aurora B -TACC1 protein complex in cytokinesis.";
RL Oncogene 23:4516-4522(2004).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-533, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [17]
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 [18]
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 [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [21]
RP FUNCTION, IDENTIFICATION OF ISOFORMS 1; 6; 9 AND 10, INTERACTION WITH ESR1;
RP NR3C1; PPARG; RARA; RXRA; THRA AND THRB, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 609-LEU-ILE-610.
RX PubMed=20078863; DOI=10.1186/1471-2199-11-3;
RA Guyot R., Vincent S., Bertin J., Samarut J., Ravel-Chapuis P.;
RT "The transforming acidic coiled coil (TACC1) protein modulates the
RT transcriptional activity of the nuclear receptors TR and RAR.";
RL BMC Mol. Biol. 11:3-3(2010).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4 AND SER-10, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [23]
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 [24]
RP SUBCELLULAR LOCATION, INTERACTION WITH AURKC, PHOSPHORYLATION AT SER-228 BY
RP AURKC, AND MUTAGENESIS OF SER-228.
RX PubMed=21531210; DOI=10.1016/j.bbrc.2011.04.078;
RA Gabillard J.C., Ulisse S., Baldini E., Sorrenti S., Cremet J.Y.,
RA Coccaro C., Prigent C., D'Armiento M., Arlot-Bonnemains Y.;
RT "Aurora-C interacts with and phosphorylates the transforming acidic coiled-
RT coil 1 protein.";
RL Biochem. Biophys. Res. Commun. 408:647-653(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-147; SER-153; SER-248
RP AND SER-276, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-591, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [27]
RP MYRISTOYLATION AT GLY-2 (ISOFORM 5), CLEAVAGE OF INITIATOR METHIONINE
RP (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25807930; DOI=10.1002/anie.201500342;
RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA Tate E.W.;
RT "Multifunctional reagents for quantitative proteome-wide analysis of
RT protein modification in human cells and dynamic profiling of protein
RT lipidation during vertebrate development.";
RL Angew. Chem. Int. Ed. 54:5948-5951(2015).
CC -!- FUNCTION: Involved in transcription regulation induced by nuclear
CC receptors, including in T3 thyroid hormone and all-trans retinoic acid
CC pathways (PubMed:20078863). Might promote the nuclear localization of
CC the receptors (PubMed:20078863). Likely involved in the processes that
CC promote cell division prior to the formation of differentiated tissues.
CC {ECO:0000269|PubMed:20078863}.
CC -!- SUBUNIT: Interacts with KIAA0097/CH-TOG and with the oncogenic
CC transcription factor YEATS4. Interacts with AURKA, AURKB and AURKC.
CC Interacts with LSM7, TDRD7 and SNRPG. Interacts with GCN5L2 and PCAF.
CC Interacts with the thyroid hormone receptors THRB and THRA,
CC predominantly with isoform alpha-2. The interaction with THRA isoform
CC alpha-1 and THRB is decreased in the presence of thyroid hormone T3
CC (PubMed:20078863). Also interacts with other nuclear receptors,
CC including ESR1, NR3C1, PPARG, RARA and RXRA, preferentially in the
CC absence of their hormonal ligands (PubMed:20078863).
CC {ECO:0000269|PubMed:11903063, ECO:0000269|PubMed:12165861,
CC ECO:0000269|PubMed:14603251, ECO:0000269|PubMed:14767476,
CC ECO:0000269|PubMed:15064709, ECO:0000269|PubMed:20078863,
CC ECO:0000269|PubMed:21531210}.
CC -!- INTERACTION:
CC O75410; Q9Y297: BTRC; NbExp=4; IntAct=EBI-624237, EBI-307461;
CC O75410; Q14008: CKAP5; NbExp=4; IntAct=EBI-624237, EBI-310585;
CC O75410; P42858: HTT; NbExp=4; IntAct=EBI-624237, EBI-466029;
CC O75410; Q9Y316: MEMO1; NbExp=4; IntAct=EBI-624237, EBI-1104564;
CC O75410; Q9H788: SH2D4A; NbExp=4; IntAct=EBI-624237, EBI-747035;
CC O75410; Q13190: STX5; NbExp=3; IntAct=EBI-624237, EBI-714206;
CC O75410; Q8NHU6: TDRD7; NbExp=4; IntAct=EBI-624237, EBI-624505;
CC O75410; O43422: THAP12; NbExp=3; IntAct=EBI-624237, EBI-2828217;
CC O75410; O95619: YEATS4; NbExp=6; IntAct=EBI-624237, EBI-399269;
CC O75410-1; Q14008: CKAP5; NbExp=3; IntAct=EBI-624252, EBI-310585;
CC O75410-1; Q9UK45: LSM7; NbExp=4; IntAct=EBI-624252, EBI-348372;
CC O75410-1; P62308: SNRPG; NbExp=5; IntAct=EBI-624252, EBI-624585;
CC O75410-1; Q8NHU6: TDRD7; NbExp=3; IntAct=EBI-624252, EBI-624505;
CC O75410-6; Q96GD4: AURKB; NbExp=2; IntAct=EBI-624278, EBI-624291;
CC O75410-6; Q14008: CKAP5; NbExp=2; IntAct=EBI-624278, EBI-310585;
CC O75410-6; Q9UK45: LSM7; NbExp=2; IntAct=EBI-624278, EBI-348372;
CC O75410-7; A0A0S2Z507: BTRC; NbExp=3; IntAct=EBI-12007872, EBI-16429247;
CC O75410-7; B7Z3H4: BTRC; NbExp=3; IntAct=EBI-12007872, EBI-16429269;
CC O75410-7; Q9Y297: BTRC; NbExp=6; IntAct=EBI-12007872, EBI-307461;
CC O75410-7; Q92889: ERCC4; NbExp=3; IntAct=EBI-12007872, EBI-2370770;
CC O75410-7; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-12007872, EBI-742802;
CC O75410-7; P42858: HTT; NbExp=12; IntAct=EBI-12007872, EBI-466029;
CC O75410-7; Q9Y316: MEMO1; NbExp=3; IntAct=EBI-12007872, EBI-1104564;
CC O75410-7; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-12007872, EBI-747035;
CC O75410-7; O43422: THAP12; NbExp=3; IntAct=EBI-12007872, EBI-2828217;
CC O75410-7; P10827: THRA; NbExp=3; IntAct=EBI-12007872, EBI-286285;
CC O75410-7; Q15911-2: ZFHX3; NbExp=3; IntAct=EBI-12007872, EBI-10237226;
CC O75410-7; Q96MX3: ZNF48; NbExp=3; IntAct=EBI-12007872, EBI-12006434;
CC O75410-10; P63059-1: Thra; Xeno; NbExp=2; IntAct=EBI-21986506, EBI-21350183;
CC O75410-10; P63059-2: Thra; Xeno; NbExp=2; IntAct=EBI-21986506, EBI-21987107;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14767476}. Nucleus
CC {ECO:0000269|PubMed:14767476}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:21531210}. Midbody
CC {ECO:0000269|PubMed:21531210}. Note=Nucleus during interphase. Weakly
CC concentrated at centrosomes during mitosis and colocalizes with AURKC
CC at the midbody during cytokinesis. {ECO:0000269|PubMed:21531210}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 10]: Cytoplasm
CC {ECO:0000269|PubMed:20078863}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1; Synonyms=A, Long, TACC1-A {ECO:0000303|PubMed:20078863};
CC IsoId=O75410-1; Sequence=Displayed;
CC Name=2; Synonyms=F, TACC1-G {ECO:0000303|PubMed:20078863};
CC IsoId=O75410-2; Sequence=VSP_012647;
CC Name=3; Synonyms=E;
CC IsoId=O75410-3; Sequence=VSP_012638;
CC Name=4; Synonyms=D;
CC IsoId=O75410-4; Sequence=VSP_012641, VSP_012642;
CC Name=5; Synonyms=C;
CC IsoId=O75410-5; Sequence=VSP_012639, VSP_012646;
CC Name=6; Synonyms=Short, TACC1-S {ECO:0000303|PubMed:20078863};
CC IsoId=O75410-6; Sequence=VSP_012644, VSP_012645;
CC Name=7;
CC IsoId=O75410-7; Sequence=VSP_012637, VSP_012643, VSP_012648;
CC Name=8;
CC IsoId=O75410-8; Sequence=VSP_012640;
CC Name=9; Synonyms=TACC1-K {ECO:0000303|PubMed:20078863};
CC IsoId=O75410-9; Sequence=VSP_012648;
CC Name=10; Synonyms=TACC1-J {ECO:0000303|PubMed:20078863};
CC IsoId=O75410-10; Sequence=VSP_012644, VSP_012645, VSP_012648;
CC -!- TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 5 are ubiquitous.
CC Isoform 2 is strongly expressed in the brain, weakly detectable in lung
CC and colon, and overexpressed in gastric cancer. Isoform 4 is not
CC detected in normal tissues, but strong expression was found in gastric
CC cancer tissues. Down-regulated in a subset of cases of breast cancer.
CC {ECO:0000269|PubMed:12165861, ECO:0000269|PubMed:12547166}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high level during early
CC embryogenesis.
CC -!- PTM: Isoform 1 is heavily phosphorylated; isoform 6 is not.
CC {ECO:0000269|PubMed:12165861, ECO:0000269|PubMed:21531210}.
CC -!- SIMILARITY: Belongs to the TACC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG65314.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TACC1ID42456ch8p11.html";
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DR EMBL; AF049910; AAC32327.1; -; mRNA.
DR EMBL; AY177411; AAO53446.1; -; mRNA.
DR EMBL; AY139007; AAN28955.1; -; mRNA.
DR EMBL; AK304507; BAG65314.1; ALT_INIT; mRNA.
DR EMBL; AK314620; BAG37186.1; -; mRNA.
DR EMBL; CH471080; EAW63293.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63296.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63298.1; -; Genomic_DNA.
DR EMBL; BC041391; AAH41391.1; -; mRNA.
DR EMBL; AB029026; BAA83055.1; -; mRNA.
DR EMBL; AY039239; AAK68658.1; -; mRNA.
DR EMBL; AY072874; AAL62461.1; -; mRNA.
DR EMBL; AY072875; AAL62462.1; -; mRNA.
DR EMBL; AY072876; AAL62463.2; -; mRNA.
DR CCDS; CCDS47845.1; -. [O75410-6]
DR CCDS; CCDS55224.1; -. [O75410-3]
DR CCDS; CCDS6109.1; -. [O75410-1]
DR CCDS; CCDS87601.1; -. [O75410-7]
DR RefSeq; NP_001116296.1; NM_001122824.1. [O75410-6]
DR RefSeq; NP_001139688.1; NM_001146216.2. [O75410-3]
DR RefSeq; NP_006274.2; NM_006283.2. [O75410-1]
DR RefSeq; XP_005273682.1; XM_005273625.4. [O75410-2]
DR RefSeq; XP_011542933.1; XM_011544631.1.
DR RefSeq; XP_011542934.1; XM_011544632.2. [O75410-2]
DR RefSeq; XP_011542936.1; XM_011544634.1.
DR RefSeq; XP_011542938.1; XM_011544636.2. [O75410-5]
DR RefSeq; XP_011542939.1; XM_011544637.1.
DR RefSeq; XP_016869261.1; XM_017013772.1.
DR RefSeq; XP_016869262.1; XM_017013773.1.
DR RefSeq; XP_016869263.1; XM_017013774.1.
DR AlphaFoldDB; O75410; -.
DR SMR; O75410; -.
DR BioGRID; 112730; 151.
DR CORUM; O75410; -.
DR IntAct; O75410; 63.
DR MINT; O75410; -.
DR STRING; 9606.ENSP00000321703; -.
DR iPTMnet; O75410; -.
DR PhosphoSitePlus; O75410; -.
DR BioMuta; TACC1; -.
DR EPD; O75410; -.
DR jPOST; O75410; -.
DR MassIVE; O75410; -.
DR MaxQB; O75410; -.
DR PaxDb; O75410; -.
DR PeptideAtlas; O75410; -.
DR PRIDE; O75410; -.
DR ProteomicsDB; 49977; -. [O75410-1]
DR ProteomicsDB; 49978; -. [O75410-2]
DR ProteomicsDB; 49979; -. [O75410-3]
DR ProteomicsDB; 49980; -. [O75410-4]
DR ProteomicsDB; 49981; -. [O75410-5]
DR ProteomicsDB; 49982; -. [O75410-6]
DR ProteomicsDB; 49983; -. [O75410-7]
DR ProteomicsDB; 49984; -. [O75410-8]
DR Antibodypedia; 4470; 244 antibodies from 32 providers.
DR DNASU; 6867; -.
DR Ensembl; ENST00000276520.12; ENSP00000276520.8; ENSG00000147526.20. [O75410-6]
DR Ensembl; ENST00000317827.9; ENSP00000321703.4; ENSG00000147526.20. [O75410-1]
DR Ensembl; ENST00000518415.5; ENSP00000428706.1; ENSG00000147526.20. [O75410-7]
DR Ensembl; ENST00000520615.5; ENSP00000428450.1; ENSG00000147526.20. [O75410-3]
DR GeneID; 6867; -.
DR KEGG; hsa:6867; -.
DR MANE-Select; ENST00000317827.9; ENSP00000321703.4; NM_006283.3; NP_006274.2.
DR UCSC; uc003xlz.4; human. [O75410-1]
DR CTD; 6867; -.
DR DisGeNET; 6867; -.
DR GeneCards; TACC1; -.
DR HGNC; HGNC:11522; TACC1.
DR HPA; ENSG00000147526; Low tissue specificity.
DR MalaCards; TACC1; -.
DR MIM; 605301; gene.
DR neXtProt; NX_O75410; -.
DR OpenTargets; ENSG00000147526; -.
DR Orphanet; 251579; Giant cell glioblastoma.
DR Orphanet; 251576; Gliosarcoma.
DR PharmGKB; PA36299; -.
DR VEuPathDB; HostDB:ENSG00000147526; -.
DR eggNOG; ENOG502QUCC; Eukaryota.
DR GeneTree; ENSGT00940000156991; -.
DR HOGENOM; CLU_005375_2_1_1; -.
DR InParanoid; O75410; -.
DR OMA; DEMDGNT; -.
DR OrthoDB; 669540at2759; -.
DR PhylomeDB; O75410; -.
DR TreeFam; TF333149; -.
DR PathwayCommons; O75410; -.
DR SignaLink; O75410; -.
DR SIGNOR; O75410; -.
DR BioGRID-ORCS; 6867; 6 hits in 1082 CRISPR screens.
DR ChiTaRS; TACC1; human.
DR GeneWiki; TACC1; -.
DR GenomeRNAi; 6867; -.
DR Pharos; O75410; Tbio.
DR PRO; PR:O75410; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O75410; protein.
DR Bgee; ENSG00000147526; Expressed in middle temporal gyrus and 212 other tissues.
DR ExpressionAtlas; O75410; baseline and differential.
DR Genevisible; O75410; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IDA:UniProtKB.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IDA:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IMP:GO_Central.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IDA:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IDA:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA:UniProtKB.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IEA:InterPro.
DR InterPro; IPR039915; TACC.
DR InterPro; IPR007707; TACC_C.
DR PANTHER; PTHR13924; PTHR13924; 1.
DR Pfam; PF05010; TACC_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; Lipoprotein; Membrane; Myristate;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CHAIN 2..805
FT /note="Transforming acidic coiled-coil-containing protein
FT 1"
FT /id="PRO_0000179986"
FT DOMAIN 215..297
FT /note="SPAZ 1"
FT DOMAIN 359..507
FT /note="SPAZ 2"
FT REGION 2..55
FT /note="Interaction with LSM7 and SNRPG"
FT /evidence="ECO:0000269|PubMed:12165861"
FT REGION 23..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..259
FT /note="Interaction with TDRD7"
FT /evidence="ECO:0000269|PubMed:14603251"
FT REGION 206..427
FT /note="Interaction with YEATS4"
FT /evidence="ECO:0000269|PubMed:11903063"
FT REGION 215..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..805
FT /note="Interaction with CH-TOG"
FT COILED 610..805
FT MOTIF 226..241
FT /note="Bipartite nuclear localization signal 1"
FT /evidence="ECO:0000255"
FT MOTIF 455..471
FT /note="Bipartite nuclear localization signal 2"
FT /evidence="ECO:0000255"
FT COMPBIAS 48..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 228
FT /note="Phosphoserine; by AURKC"
FT /evidence="ECO:0000269|PubMed:21531210"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y685"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y685"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y685"
FT MOD_RES 533
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..651
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_012640"
FT VAR_SEQ 1..438
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_012639"
FT VAR_SEQ 1..426
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_012641"
FT VAR_SEQ 1..195
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12547166"
FT /id="VSP_012638"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012637"
FT VAR_SEQ 42..53
FT /note="EDSQAETKSLSF -> MNNILKLK (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012643"
FT VAR_SEQ 54
FT /note="S -> R (in isoform 6 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:15207008"
FT /id="VSP_012644"
FT VAR_SEQ 55..464
FT /note="Missing (in isoform 6 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:15207008"
FT /id="VSP_012645"
FT VAR_SEQ 427..464
FT /note="DPFKPTTTLTSSDFCSPTGNHVNEILESPKKAKSRLIT -> MGGSHSQTPR
FT GREPAGERHPRPTETATTEQVKFLCFLL (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_012642"
FT VAR_SEQ 439..464
FT /note="DFCSPTGNHVNEILESPKKAKSRLIT -> MGGSHSQTPRGREPAGERHPRP
FT TETA (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_012646"
FT VAR_SEQ 464
FT /note="T -> TTTEQVKFLCFLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10470851,
FT ECO:0000303|PubMed:12087473"
FT /id="VSP_012647"
FT VAR_SEQ 526..554
FT /note="Missing (in isoform 7, isoform 9 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012648"
FT VARIANT 187
FT /note="P -> L (in dbSNP:rs34235313)"
FT /id="VAR_053703"
FT VARIANT 243
FT /note="I -> T (in dbSNP:rs6980553)"
FT /id="VAR_053704"
FT VARIANT 255
FT /note="E -> G (in dbSNP:rs10107016)"
FT /id="VAR_053705"
FT MUTAGEN 228
FT /note="S->A: Impairs phosphorylation by AURKC."
FT /evidence="ECO:0000269|PubMed:21531210"
FT MUTAGEN 609..610
FT /note="LI->AA: Decreases interaction with THRA."
FT /evidence="ECO:0000269|PubMed:20078863"
FT CONFLICT 291
FT /note="L -> I (in Ref. 1; AAC32327)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="P -> H (in Ref. 6; AAH41391)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="G -> V (in Ref. 7; BAA83055)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="Missing (in Ref. 7; BAA83055)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="Q -> R (in Ref. 4; BAG65314)"
FT /evidence="ECO:0000305"
FT INIT_MET O75410-5:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25807930"
FT LIPID O75410-5:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25807930"
SQ SEQUENCE 805 AA; 87794 MW; 3A261EF58C165107 CRC64;
MAFSPWQILS PVQWAKWTWS AVRGGAAGED EAGGPEGDPE EEDSQAETKS LSFSSDSEGN
FETPEAETPI RSPFKESCDP SLGLAGPGAK SQESQEADEQ LVAEVVEKCS SKTCSKPSEN
EVPQQAIDSH SVKNFREEPE HDFSKISIVR PFSIETKDST DISAVLGTKA AHGCVTAVSG
KALPSSPPDA LQDEAMTEGS MGVTLEASAE ADLKAGNSCP ELVPSRRSKL RKPKPVPLRK
KAIGGEFSDT NAAVEGTPLP KASYHFSPEE LDENTSPLLG DARFQKSPPD LKETPGTLSS
DTNDSGVELG EESRSSPLKL EFDFTEDTGN IEARKALPRK LGRKLGSTLT PKIQKDGISK
SAGLEQPTDP VARDGPLSQT SSKPDPSQWE SPSFNPFGSH SVLQNSPPLS SEGSYHFDPD
NFDESMDPFK PTTTLTSSDF CSPTGNHVNE ILESPKKAKS RLITSGCKVK KHETQSLALD
ACSRDEGAVI SQISDISNRD GHATDEEKLA STSCGQKSAG AEVKGEPEED LEYFECSNVP
VSTINHAFSS SEAGIEKETC QKMEEDGSTV LGLLESSAEK APVSVSCGGE SPLDGICLSE
SDKTAVLTLI REEIITKEIE ANEWKKKYEE TRQEVLEMRK IVAEYEKTIA QMIEDEQRTS
MTSQKSFQQL TMEKEQALAD LNSVERSLSD LFRRYENLKG VLEGFKKNEE ALKKCAQDYL
ARVKQEEQRY QALKIHAEEK LDKANEEIAQ VRTKAKAESA ALHAGLRKEQ MKVESLERAL
QQKNQEIEEL TKICDELIAK LGKTD
