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TACC2 (transforming, acidic coiled-coil containing protein 2)

Written2013-08Ivan H Still, Brenda Lauffart
1 Department of Biological Sciences, Arkansas Tech University, 1701 N Boulder Ave Russellville, AR 72801, USA (IHS); Department of Physical Sciences Arkansas Tech University, 1701 N Boulder Ave Russellville, AR 72801, USA (BL)

(Note : for Links provided by Atlas : click)


Alias (NCBI)AZU-1
HGNC Alias symbAZU-1
HGNC Previous nametransforming, acidic coiled-coil containing protein 2
LocusID (NCBI) 10579
Atlas_Id 42457
Location 10q26.13  [Link to chromosome band 10q26]
Location_base_pair Starts at 121989163 and ends at 122254542 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping TACC2.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
FGFR2 (10q26.13)::TACC2 (10q26.13)HIST1H3F (6p22.2)::TACC2 (10q26.13)MRFAP1 (4p16.1)::TACC2 (10q26.13)
RARG (12q13.13)::TACC2 (10q26.13)RIC1 (9p24.1)::TACC2 (10q26.13)TACC2 (10q26.13)::HS1BP3 (2p24.1)
TACC2 (10q26.13)::MICU1 (10q22.1)TACC2 (10q26.13)::MRFAP1 (4p16.1)TACC2 (10q26.13)::TACC2 (10q26.13)
TCF7L2 (10q25.2)::TACC2 (10q26.13)TINAGL1 (1p35.2)::TACC2 (10q26.13)
Note Based on published GenBank sequences, this gene has seven potential transcription start sites located at 123748689 bp, 123754142 bp, 123872554 bp, 123886229 bp, 123922941 bp, 123951963 bp, 123969557 bp from pter.


Description The gene is composed of 28 exons spanning 265369 bp.
Transcription Transcripts depicted above encompass most transcripts evident in AceView and USGC genome browsers. Most other AceView "transcripts" appear to be subsets of those shown or unspliced. AF176646 represents the published "Azu-1" variant (Chen et al., 2000); although no other cDNAs support the 5' end as a transcriptional start site (123886229 bp), a H3K27 acetylation cluster is noted in this region (ENCODE Project Consortium, 2011). AF220152 represents the "ECTACC variant" (Pu et al., 2001), first 13 bases of which do not match the genomic DNA and no other cDNAs support its 5' end as a transcriptional start site. Transcription start site at 123754142 bp identified in a global search for alternative promoters (Kimura et al., 2006) and supported by three cDNAs (AL833304, DB276457 and AK094848). AL8333304 does not encode a protein as it appears to use a "non canonical" splice site at 123781503, 4 nucleotides after initiator codon for the TACC2 "long isoforms". DB276457 appears to be incomplete at the 3' end due to the nature of its isolation (Kimura et al., 2006).


Description Ten isoforms are predicted based on published cDNA sequences. Features will be referenced to their location in the largest AAO62630 isoform (2948 amino acids, 309403,40 Da). The nine other isoforms are: AAI44600, 2875 amino acids, 302586,86 Da; AAI44601, 2826 amino acids, 296742,08 Da; AAO62629, 1094 amino acids, 119330,60 Da; AAC64968, 1026 amino acids, 112110,91 Da; AAH39311, 996 amino acids, 108703,96 Da; BAH12132, 601 amino acids, 64367,07 Da; AAF29537, 906 amino acids, 99590,14 Da; ORF-BC015736 (longest open reading frame of GB:BC015736), 575 amino acids, 64675,57 Da; AAF63433, 571 amino acids, 64156,01 Da.
ORF-BC015736 and AAF63433, beginning at an "internal" AUG present in exon 9, are identical except for 4 amino acids missing in AAF63433 (amino acid 2429-2432). BAH12132 prematurely terminates due to a C-T mutation in the cDNA generating a nonsense codon; the partial cDNA coding this open reading frame is identical to other TACC2 isoforms downstream of the nonsense codon, suggesting the mutation is a cloning artefact.
Western blot analysis confirms the large ≈ 300 kDa isoforms and those of ≈ 100 kDa. Western blot often shows species 65-70 kDa (corresponding in size to ORF-BC015736 and AAF63433 isoforms), however the variability in intensity in different preparations from the same cell type suggests that these species could also arise as a product of degradation (PEST sequences support that TACC2 is subject to regulated degradation).
PSORT II predicts multiple nuclear localisation signals between amino acid 2128 and 2420 ( Multiple phosphorylation sites have been identified throughout the protein sequence by mass spectrometry (summarized at PhosphoSitePlus (Hornbeck et al., 2012)). The following lysine modifications are noted: lysine trimethylation at K1339 and K1346 (Cao et al., 2013); ubiquitylation at K2542 in HCT116 colon cancer cells (Kim et al., 2011); acetylation at K2884 in A549 lung cancer cells (Choudhary et al., 2009), K2736 in a resected liver cancer, K2927 and K2928 in NCI H2228 non small cell lung cancer cells (Hornbeck et al., 2012).
Expression Short isoforms (100-120 kDa) widely expressed in fetal and adult tissue, but large isoforms (≈ 300 kDa) expressed at high levels in muscle tissue (Lauffart et al., 2003). Short form(s) expression is upregulated by erythopoietin in human microvascular endothelial cells (Pu et al., 2001) and androgens in prostate cancer cells (Takayama et al., 2012). Induction of large forms occurs as development proceeds in the tissues that express them (Still et al., unpublished).
Localisation TACC2 short isoforms can be located in the nucleus and/or cytosol of interphase cells (Chen et al., 2000; Gergely et al., 2000; Lauffart et al., 2003). TACC2 interacts with the centrosome and mitotic spindle during mitosis (Gergely et al., 2000). In some cells, overexpression can result in accumulation of the protein into cytoplasmic punctate structures due to oligmerisation (Gergely et al., 2000). The oligomerisation motif is located between amino acid 2740 and 2815 (Tei et al., 2009).
Function TACC2 plays a role in microtubule dynamics during mitosis based upon interactions with Aurora C kinase (Tien et al., 2004) and CKAP5 (ch-TOG/XMAP215) via the TACC domain (see Peset and Vernos, 2008 for Review). TACC2 is implicated in G2/M progression (Takayama et al., 2012) and its ability to function in the maintenance of normal mitotic spindle dynamics is targeted by SV40 T-antigen (Tei et al., 2009). TACC2 is an effector of a mitotic checkpoint control kinase, TTK, with disruption of TTK activity preventing phosphorylation of 100-120 kD TACC2 short isoforms, subsequent recruitment of the TACC2 to the centrosome, leading to reduction of centrosome-centrosome distance in mitotic cells (Dou et al., 2004). TACC2 also interacts with mitotic regulatory proteins Haus 1, Haus 4 and PRC1 (Hutchins et al., 2010).
Alternative functions have been ascribed in transcription through direct interaction with coregulators FHL2 and FHL3 proteins (Lauffart et al., 2007b), YEATS4 (GAS41) and the SWI/SNF chromatin remodeling complex (Lauffart et al., 2002), histone acetyltransferases KAT2A (hGCN5L2)/KAT2B (pCAF)/Ep300/CREBBP (Gangisetty et al., 2004), a core component of a histone deacetylase complex, HMG20B (BRAF35) (Stelzl et al., 2005) and the retinoid-X receptor (Vettaikkorumakankauv et al., 2008). TACC2 enhances transcriptional regulation from a cAMP response element (Lauffart et al., 2007b), and retinoid-X-receptor responsive genes (Vettaikkorumakankauv et al., 2008). Interaction with nucleoporin NUP155 has been identified by mass throughput technologies (Havugimana et al., 2012).
TACC2 is found in complexes containing BRCA1, BARD1, p53 and Ku70 and may therefore also have a role in DNA damage/repair (Lauffart et al., 2007a).
TACC2 is phosphorylated during mitosis (Dephoure et al., 2008; Olsen et al., 2010) and in response to activation of EGFR and oncogenic signaling pathways (Rikova et al., 2007; Chen et al., 2009; Moritz et al., 2010). Tumour suppressive properties of TACC2 are thought to function through the PLCγ pathway (Cheng et al., 2011). PPP1CC, protein phosphatase 1 may be involved in dephosphorylation of TACC2 (Esteves et al., 2013). Acetylation, ubiquitylation and trimethylation of TACC2 may also impact TACC2's function (Choudhary et al., 2009; Kim et al., 2011; Hornbeck et al., 2012; Cao et al., 2013).
Homology Member of the TACC family, based on the presence of the conserved approximately 200 amino acid carboxy terminal coiled coil domain (TACC domain) (Still et al., 1999; Still et al., 2004). Both TACC1 and TACC2 contain a 16 amino acid SFP motif SSDSE-X2- FETPE-X2-TP, and a conserved string of nine amino acids, HATDEEKLA. These two motifs are specific to TACC1 and 2 only. Additionally, TACC2 contains two copies of the 33 amino acid SDP repeat, which is conserved between the members of the vertebrate TACC family (Lauffart et al., 2002). In TACC1, the SDP repeat serves as the binding site for the SWI/SNF component/accessory factor, YEATS4 (Lauffart et al., 2002).


Note To date, no mutations in the TACC2 gene have been detected.

Implicated in

Entity Infant acute lymphoblastic leukemia
Prognosis In a gene array analysis of 97 patients, increased expression was correlated with an intermediate or high risk for a poorer outcome, independent of patient age (Kang et al., 2012). Results were not confirmed at the protein level.
Oncogenesis Upregulation of TACC2 may be triggered by the underlying alteration in the MLL gene in patients, resulting in recruitment of histone methylases to target genes. Proposed mechanism based on previous identification of the regulation of the TACC2 gene by the histone methylase SMYD2 (Abu-Farha et al., 2008).
Entity Neuroblastoma
Prognosis Identified as a marker of minimal residue disease based on Affymetrix U-95 gene chip expression array analysis of 48 stage 4 tumours and 9 remission bone marrows. Expression of TACC2 in tumour as compared to marrow was superior to that of tyrosine hydroxylase, however, TACC2 expression failed to be of prognostic value for progression-free survival (Cheung et al., 2008).
Entity Intracranial ependymoma
Prognosis Single allele deletion detected by high-resolution matrix-based CGH in 11/68 intracranial ependymoma (Mendrzyk et al., 2006), not linked to clinicopathologic subgroups.
Oncogenesis Apparent overexpression from remaining allele in the tumours observed by qRT-PCR (Mendrzyk et al., 2006).
Entity Breast cancer
Prognosis Decreased expression of TACC2 was noted in a survey of breast cancer samples by immunohistochemistry of tumour microarrays derived from 552 breast cancer patients (Jacquemier et al., 2005). In another study, "increased" levels of TACC2 were reported, based on quantitative rt-PCR and analysis of protein levels in "macro-dissected" tumours, to be associated with poorer prognosis, grade and short disease-free survival (Cheng et al., 2010). However, the intensity of immunohistochemical staining of the tumour cells appeared to be the same as in normal breast epithelium used in the study. Thus, in this study, TACC2 staining may only reflect the percentage of the resected tumour tissue occupied by tumour cells and may reflect retention of expression of TACC2 at normal levels seen in the precursor mammary epithelial cells (Cheng et al., 2010).
Oncogenesis The TACC2 transcript AF176646 (AZU1) is downregulated in the more malignant derivatives of the HMT-3522 tumour progression cell model (Chen et al., 2000). Expression of exogenous TACC2 short isoforms (AF176646, AF095791 or AF528098) reduces malignant potential of breast tumour cells (Chen et al., 2000; Lauffart et al., 2003). Tumor suppressor properties may operate through PLCγ (Cheng et al., 2011).
Entity Prostate cancer
Prognosis Positive correlation between Gleason score and immunohistochemical staining for TACC2 noted in a survey of 103 prostate cancer samples (Takayama et al., 2012).
Oncogenesis The TACC2 gene is androgen responsive, with two confirmed androgen receptor binding sites in intron 4*; at 123870283-123870871 (Takayama et al., 2012). TACC2 promotes cell proliferation in androgen sensitive and androgen-independent prostate cancer cells. A single-nucleotide polymorphism, rs3763763, inside an estrogen response element is associated with prostate cancer-specific mortality and "all-cause mortality" after androgen-deprivation therapy (Huang et al., 2012) suggesting that hormonally regulated expression of TACC2 is important in the oncogenic process. It has been noted that TACC2 interacts with androgen receptor regulator FHL2 (Lauffart et al., 2007b), a protein of known importance in attainment of androgen independence in prostate cancer (McGrath et al., 2013), suggesting potential positive feedback on TACC2 expression.
*designated based on genomic structure of the AF528099 long form (see genomic model).


Note No translocation or deletions within the TACC2 gene have been identified.


The tale of two domains: proteomics and genomics analysis of SMYD2, a new histone methyltransferase.
Abu-Farha M, Lambert JP, Al-Madhoun AS, Elisma F, Skerjanc IS, Figeys D.
Mol Cell Proteomics. 2008 Mar;7(3):560-72. Epub 2007 Dec 7.
PMID 18065756
Large-scale global identification of protein lysine methylation in vivo.
Cao XJ, Arnaudo AM, Garcia BA.
Epigenetics. 2013 May;8(5):477-85. doi: 10.4161/epi.24547. Epub 2013 Apr 17.
PMID 23644510
AZU-1: a candidate breast tumor suppressor and biomarker for tumor progression.
Chen HM, Schmeichel KL, Mian IS, Lelievre S, Petersen OW, Bissell MJ.
Mol Biol Cell. 2000 Apr;11(4):1357-67.
PMID 10749935
CDC25B mediates rapamycin-induced oncogenic responses in cancer cells.
Chen RQ, Yang QK, Lu BW, Yi W, Cantin G, Chen YL, Fearns C, Yates JR 3rd, Lee JD.
Cancer Res. 2009 Mar 15;69(6):2663-8. doi: 10.1158/0008-5472.CAN-08-3222. Epub 2009 Mar 10.
PMID 19276368
Transforming acidic coiled-coil-containing protein 2 (TACC2) in human breast cancer, expression pattern and clinical/prognostic relevance.
Cheng S, Douglas-Jones A, Yang X, Mansel RE, Jiang WG.
Cancer Genomics Proteomics. 2010 Mar-Apr;7(2):67-73.
PMID 20335520
Putative Breast Tumor Suppressor TACC2 Suppresses the Aggressiveness of Breast Cancer Cells through a PLCgamma Pathway.
Cheng S, Martin TA, Teng X, Jiang WG.
Current Signal Transduction Therapy, Volume 6, Number 1, January 2011 , pp. 55-64(10).
Exploiting gene expression profiling to identify novel minimal residual disease markers of neuroblastoma.
Cheung IY, Feng Y, Gerald W, Cheung NK.
Clin Cancer Res. 2008 Nov 1;14(21):7020-7. doi: 10.1158/1078-0432.CCR-08-0541.
PMID 18980998
Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16.
PMID 19608861
A quantitative atlas of mitotic phosphorylation.
Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP.
Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31.
PMID 18669648
TTK kinase is essential for the centrosomal localization of TACC2.
Dou Z, Ding X, Zereshki A, Zhang Y, Zhang J, Wang F, Sun J, Huang H, Yao X.
FEBS Lett. 2004 Aug 13;572(1-3):51-6.
PMID 15304323
A user's guide to the encyclopedia of DNA elements (ENCODE).
ENCODE Project Consortium.
PLoS Biol. 2011 Apr;9(4):e1001046. doi: 10.1371/journal.pbio.1001046. Epub 2011 Apr 19.
PMID 21526222
Protein phosphatase 1gamma isoforms linked interactions in the brain.
Esteves SL, Korrodi-Gregorio L, Cotrim CZ, van Kleeff PJ, Domingues SC, da Cruz e Silva OA, Fardilha M, da Cruz e Silva EF.
J Mol Neurosci. 2013 May;50(1):179-97. doi: 10.1007/s12031-012-9902-6. Epub 2012 Oct 19.
PMID 23080069
The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases.
Gangisetty O, Lauffart B, Sondarva GV, Chelsea DM, Still IH.
Oncogene. 2004 Apr 1;23(14):2559-63.
PMID 14767476
The TACC domain identifies a family of centrosomal proteins that can interact with microtubules.
Gergely F, Karlsson C, Still I, Cowell J, Kilmartin J, Raff JW.
Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14352-7.
PMID 11121038
A census of human soluble protein complexes.
Havugimana PC, Hart GT, Nepusz T, Yang H, Turinsky AL, Li Z, Wang PI, Boutz DR, Fong V, Phanse S, Babu M, Craig SA, Hu P, Wan C, Vlasblom J, Dar VU, Bezginov A, Clark GW, Wu GC, Wodak SJ, Tillier ER, Paccanaro A, Marcotte EM, Emili A.
Cell. 2012 Aug 31;150(5):1068-81. doi: 10.1016/j.cell.2012.08.011.
PMID 22939629
PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse.
Hornbeck PV, Kornhauser JM, Tkachev S, Zhang B, Skrzypek E, Murray B, Latham V, Sullivan M.
Nucleic Acids Res. 2012 Jan;40(Database issue):D261-70. doi: 10.1093/nar/gkr1122. Epub 2011 Dec 1.
PMID 22135298
Genetic polymorphisms in oestrogen receptor-binding sites affect clinical outcomes in patients with prostate cancer receiving androgen-deprivation therapy.
Huang CN, Huang SP, Pao JB, Hour TC, Chang TY, Lan YH, Lu TL, Lee HZ, Juang SH, Wu PP, Huang CY, Hsieh CJ, Bao BY.
J Intern Med. 2012 May;271(5):499-509. doi: 10.1111/j.1365-2796.2011.02449.x. Epub 2011 Sep 29.
PMID 21880074
Systematic analysis of human protein complexes identifies chromosome segregation proteins.
Hutchins JR, Toyoda Y, Hegemann B, Poser I, Heriche JK, Sykora MM, Augsburg M, Hudecz O, Buschhorn BA, Bulkescher J, Conrad C, Comartin D, Schleiffer A, Sarov M, Pozniakovsky A, Slabicki MM, Schloissnig S, Steinmacher I, Leuschner M, Ssykor A, Lawo S, Pelletier L, Stark H, Nasmyth K, Ellenberg J, Durbin R, Buchholz F, Mechtler K, Hyman AA, Peters JM.
Science. 2010 Apr 30;328(5978):593-9. doi: 10.1126/science.1181348. Epub 2010 Apr 1.
PMID 20360068
Protein expression profiling identifies subclasses of breast cancer and predicts prognosis.
Jacquemier J, Ginestier C, Rougemont J, Bardou VJ, Charafe-Jauffret E, Geneix J, Adelaide J, Koki A, Houvenaeghel G, Hassoun J, Maraninchi D, Viens P, Birnbaum D, Bertucci F.
Cancer Res. 2005 Feb 1;65(3):767-79.
PMID 15705873
Gene expression profiles predictive of outcome and age in infant acute lymphoblastic leukemia: a Children's Oncology Group study.
Kang H, Wilson CS, Harvey RC, Chen IM, Murphy MH, Atlas SR, Bedrick EJ, Devidas M, Carroll AJ, Robinson BW, Stam RW, Valsecchi MG, Pieters R, Heerema NA, Hilden JM, Felix CA, Reaman GH, Camitta B, Winick N, Carroll WL, Dreyer ZE, Hunger SP, Willman CL.
Blood. 2012 Feb 23;119(8):1872-81. doi: 10.1182/blood-2011-10-382861. Epub 2011 Dec 30.
PMID 22210879
Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. doi: 10.1016/j.molcel.2011.08.025. Epub 2011 Sep 8.
PMID 21906983
Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.
Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S.
Genome Res. 2006 Jan;16(1):55-65. Epub 2005 Dec 12.
PMID 16344560
Interaction of TACC proteins with the FHL family: implications for ERK signaling.
Lauffart B, Sondarva GV, Gangisetty O, Cincotta M, Still IH.
J Cell Commun Signal. 2007b Jun;1(1):5-15. doi: 10.1007/s12079-007-0001-3. Epub 2007 Mar 28.
PMID 18481206
Regulation of the Transcriptional Coactivator FHL2 Licenses Activation of the Androgen Receptor in Castrate-Resistant Prostate Cancer.
McGrath MJ, Binge LC, Sriratana A, Wang H, Robinson PA, Pook D, Fedele CG, Brown S, Dyson JM, Cottle DL, Cowling BS, Niranjan B, Risbridger GP, Mitchell CA.
Cancer Res. 2013 Aug 15;73(16):5066-5079. Epub 2013 Jun 25.
PMID 23801747
Identification of gains on 1q and epidermal growth factor receptor overexpression as independent prognostic markers in intracranial ependymoma.
Mendrzyk F, Korshunov A, Benner A, Toedt G, Pfister S, Radlwimmer B, Lichter P.
Clin Cancer Res. 2006 Apr 1;12(7 Pt 1):2070-9.
PMID 16609018
Akt-RSK-S6 kinase signaling networks activated by oncogenic receptor tyrosine kinases.
Moritz A, Li Y, Guo A, Villen J, Wang Y, MacNeill J, Kornhauser J, Sprott K, Zhou J, Possemato A, Ren JM, Hornbeck P, Cantley LC, Gygi SP, Rush J, Comb MJ.
Sci Signal. 2010 Aug 24;3(136):ra64. doi: 10.1126/scisignal.2000998.
PMID 20736484
Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M.
Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475.
PMID 20068231
The TACC proteins: TACC-ling microtubule dynamics and centrosome function.
Peset I, Vernos I.
Trends Cell Biol. 2008 Aug;18(8):379-88. doi: 10.1016/j.tcb.2008.06.005. Epub 2008 Jul 23. (REVIEW)
PMID 18656360
Cloning and structural characterization of ECTACC, a new member of the transforming acidic coiled coil (TACC) gene family: cDNA sequence and expression analysis in human microvascular endothelial cells.
Pu JJ, Li C, Rodriguez M, Banerjee D.
Cytokine. 2001 Feb 7;13(3):129-37.
PMID 11161455
Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.
Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ.
Cell. 2007 Dec 14;131(6):1190-203.
PMID 18083107
A human protein-protein interaction network: a resource for annotating the proteome.
Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksoz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE.
Cell. 2005 Sep 23;122(6):957-68.
PMID 16169070
Cloning of TACC1, an embryonically expressed, potentially transforming coiled coil containing gene, from the 8p11 breast cancer amplicon.
Still IH, Hamilton M, Vince P, Wolfman A, Cowell JK.
Oncogene. 1999 Jul 8;18(27):4032-8.
PMID 10435627
Structure-function evolution of the transforming acidic coiled coil genes revealed by analysis of phylogenetically diverse organisms.
Still IH, Vettaikkorumakankauv AK, DiMatteo A, Liang P.
BMC Evol Biol. 2004 Jun 18;4:16.
PMID 15207008
TACC2 is an androgen-responsive cell cycle regulator promoting androgen-mediated and castration-resistant growth of prostate cancer.
Takayama K, Horie-Inoue K, Suzuki T, Urano T, Ikeda K, Fujimura T, Takahashi S, Homma Y, Ouchi Y, Inoue S.
Mol Endocrinol. 2012 May;26(5):748-61. doi: 10.1210/me.2011-1242. Epub 2012 Mar 28.
PMID 22456197
Simian virus 40 large T antigen targets the microtubule-stabilizing protein TACC2.
Tei S, Saitoh N, Funahara T, Iida S, Nakatsu Y, Kinoshita K, Kinoshita Y, Saya H, Nakao M.
J Cell Sci. 2009 Sep 1;122(Pt 17):3190-8. doi: 10.1242/jcs.049627. Epub 2009 Aug 11.
PMID 19671663
Identification of the substrates and interaction proteins of aurora kinases from a protein-protein interaction model.
Tien AC, Lin MH, Su LJ, Hong YR, Cheng TS, Lee YC, Lin WJ, Still IH, Huang CY.
Mol Cell Proteomics. 2004 Jan;3(1):93-104. Epub 2003 Nov 5.
PMID 14602875
The TACC proteins are coregulators of the Retinoid X Receptor beta.
Vettaikkorumakankauv AK, Lauffart B, Gangisetty O, Cincotta MA, Hawthorne LA, Cowell JK, Still IH.
Cancer Therapy. 2008 Dec; 6 (2): 805-816.


This paper should be referenced as such :
Still, IH ; Lauffart, B
TACC2 (transforming, acidic coiled-coil containing protein 2)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(3):183-188.
Free journal version : [ pdf ]   [ DOI ]

External links

HGNC (Hugo)TACC2   11523
Entrez_Gene (NCBI)TACC2    transforming acidic coiled-coil containing protein 2
AliasesAZU-1; ECTACC
GeneCards (Weizmann)TACC2
Ensembl hg19 (Hinxton)ENSG00000138162 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000138162 [Gene_View]  ENSG00000138162 [Sequence]  chr10:121989163-122254542 [Contig_View]  TACC2 [Vega]
ICGC DataPortalENSG00000138162
TCGA cBioPortalTACC2
Genatlas (Paris)TACC2
SOURCE (Princeton)TACC2
Genetics Home Reference (NIH)TACC2
Genomic and cartography
GoldenPath hg38 (UCSC)TACC2  -     chr10:121989163-122254542 +  10q26.13   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)TACC2  -     10q26.13   [Description]    (hg19-Feb_2009)
GoldenPathTACC2 - 10q26.13 [CytoView hg19]  TACC2 - 10q26.13 [CytoView hg38]
Genome Data Viewer NCBITACC2 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AF095791 AF176646 AF220152 AF528098 AF528099
RefSeq transcript (Entrez)NM_001291876 NM_001291877 NM_001291878 NM_001291879 NM_006997 NM_206860 NM_206861 NM_206862
Consensus coding sequences : CCDS (NCBI)TACC2
Gene ExpressionTACC2 [ NCBI-GEO ]   TACC2 [ EBI - ARRAY_EXPRESS ]   TACC2 [ SEEK ]   TACC2 [ MEM ]
Gene Expression Viewer (FireBrowse)TACC2 [ Firebrowse - Broad ]
GenevisibleExpression of TACC2 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)10579
GTEX Portal (Tissue expression)TACC2
Human Protein AtlasENSG00000138162-TACC2 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
Domain families : Pfam (Sanger)
Domain families : Pfam (NCBI)
Conserved Domain (NCBI)TACC2
Human Protein Atlas [tissue]ENSG00000138162-TACC2 [tissue]
Protein Interaction databases
Ontologies - Pathways
PubMed50 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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