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Transforming acidic coiled-coil-containing protein 1 (Gastric cancer antigen Ga55) (Taxin-1)

 TACC1_HUMAN             Reviewed;         805 AA.
O75410; B2RBD9; D3DSX6; Q6Y687; Q86YG7; Q8IUJ2; Q8IUJ3; Q8IUJ4;
Q8IZG2; Q8NEY7; Q9UPP9;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 2.
22-NOV-2017, entry version 166.
RecName: Full=Transforming acidic coiled-coil-containing protein 1;
AltName: Full=Gastric cancer antigen Ga55;
AltName: Full=Taxin-1;
Name=TACC1; Synonyms=KIAA1103;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10435627; DOI=10.1038/sj.onc.1202801;
Still I.H., Hamilton M., Vince P., Wolfman A., Cowell J.K.;
"Cloning of TACC1, an embryonically expressed, potentially
transforming coiled coil containing gene, from the 8p11 breast cancer
amplicon.";
Oncogene 18:4032-4038(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
PubMed=15207008; DOI=10.1186/1471-2148-4-16;
Still I.H., Vettaikkorumakankauv A.K., DiMatteo A., Liang P.;
"Structure-function evolution of the transforming acidic coiled coil
genes revealed by analysis of phylogenetically diverse organisms.";
BMC Evol. Biol. 4:16-16(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
Li F., Yao K.T.;
"Cloning of a novel human gene similar to TACC1.";
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 364-805 (ISOFORM 2).
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 450-805 (ISOFORM 2).
TISSUE=Gastric adenocarcinoma;
PubMed=12087473; DOI=10.1038/sj.bjc.6600321;
Line A., Stengrevics A., Slucka Z., Li G., Jankevics E., Rees R.C.;
"Serological identification and expression analysis of gastric cancer-
associated genes.";
Br. J. Cancer 86:1824-1830(2002).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-543 (ISOFORM 3), NUCLEOTIDE SEQUENCE
OF 1-571 (ISOFORMS 4 AND 5), AND TISSUE SPECIFICITY.
TISSUE=Stomach cancer;
PubMed=12547166; DOI=10.1016/S0165-4608(02)00607-6;
Line A., Slucka Z., Stengrevics A., Li G., Rees R.C.;
"Altered splicing pattern of TACC1 mRNA in gastric cancer.";
Cancer Genet. Cytogenet. 139:78-83(2002).
[10]
CHARACTERIZATION.
TISSUE=Brain, Fetal brain, and Skeletal muscle;
PubMed=11121038; DOI=10.1073/pnas.97.26.14352;
Gergely F., Karlsson C., Still I.H., Cowell J.K., Kilmartin J.,
Raff J.W.;
"The TACC domain identifies a family of centrosomal proteins that can
interact with microtubules.";
Proc. Natl. Acad. Sci. U.S.A. 97:14352-14357(2000).
[11]
INTERACTION WITH KIAA0097 AND YEATS4.
PubMed=11903063; DOI=10.1042/0264-6021:3630195;
Lauffart B., Howell S.J., Tasch J.E., Cowell J.K., Still I.H.;
"Interaction of the transforming acidic coiled-coil 1 (TACC1) protein
with ch-TOG and GAS41/NuBI1 suggests multiple TACC1-containing protein
complexes in human cells.";
Biochem. J. 363:195-200(2002).
[12]
INTERACTION WITH LSM7 AND SNRPG, TISSUE SPECIFICITY, AND
PHOSPHORYLATION.
PubMed=12165861; DOI=10.1038/sj.onc.1205658;
Conte N., Charafe-Jauffret E., Delaval B., Adelaide J., Ginestier C.,
Geneix J., Isnardon D., Jacquemier J., Birnbaum D.;
"Carcinogenesis and translational controls: TACC1 is down-regulated in
human cancers and associates with mRNA regulators.";
Oncogene 21:5619-5630(2002).
[13]
INTERACTION WITH KIAA0097; LSM7; TDRD7 AND AURKA.
PubMed=14603251; DOI=10.1038/sj.onc.1206972;
Conte N., Delaval B., Ginestier C., Ferrand A., Isnardon D.,
Larroque C., Prigent C., Seraphin B., Jacquemier J., Birnbaum D.;
"TACC1-chTOG-Aurora A protein complex in breast cancer.";
Oncogene 22:8102-8116(2003).
[14]
INTERACTION WITH GCN5L2 AND PCAF, AND SUBCELLULAR LOCATION.
PubMed=14767476; DOI=10.1038/sj.onc.1207424;
Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H.;
"The transforming acidic coiled coil proteins interact with nuclear
histone acetyltransferases.";
Oncogene 23:2559-2563(2004).
[15]
INTERACTION WITH AURKB.
PubMed=15064709; DOI=10.1038/sj.onc.1207593;
Delaval B., Ferrand A., Conte N., Larroque C., Hernandez-Verdun D.,
Prigent C., Birnbaum D.;
"Aurora B -TACC1 protein complex in cytokinesis.";
Oncogene 23:4516-4522(2004).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-533, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-4 AND SER-10, CLEAVAGE OF INITIATOR METHIONINE
[LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
SUBCELLULAR LOCATION, INTERACTION WITH AURKC, PHOSPHORYLATION AT
SER-228 BY AURKC, AND MUTAGENESIS OF SER-228.
PubMed=21531210; DOI=10.1016/j.bbrc.2011.04.078;
Gabillard J.C., Ulisse S., Baldini E., Sorrenti S., Cremet J.Y.,
Coccaro C., Prigent C., D'Armiento M., Arlot-Bonnemains Y.;
"Aurora-C interacts with and phosphorylates the transforming acidic
coiled-coil 1 protein.";
Biochem. Biophys. Res. Commun. 408:647-653(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-147; SER-153;
SER-248 AND SER-276, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-591, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
MYRISTOYLATION AT GLY-2 (ISOFORM 5), CLEAVAGE OF INITIATOR METHIONINE
(ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25807930; DOI=10.1002/anie.201500342;
Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J.,
Magee A.I., Tate E.W.;
"Multifunctional reagents for quantitative proteome-wide analysis of
protein modification in human cells and dynamic profiling of protein
lipidation during vertebrate development.";
Angew. Chem. Int. Ed. 54:5948-5951(2015).
-!- FUNCTION: Likely involved in the processes that promote cell
division prior to the formation of differentiated tissues.
-!- SUBUNIT: Interacts with KIAA0097/CH-TOG and with the oncogenic
transcription factor YEATS4. Interacts with AURKA, AURKB and
AURKC. Interacts with LSM7, TDRD7 and SNRPG. Interacts with GCN5L2
and PCAF. {ECO:0000269|PubMed:11903063,
ECO:0000269|PubMed:12165861, ECO:0000269|PubMed:14603251,
ECO:0000269|PubMed:14767476, ECO:0000269|PubMed:15064709,
ECO:0000269|PubMed:21531210}.
-!- INTERACTION:
Q96GD4:AURKB; NbExp=2; IntAct=EBI-624278, EBI-624291;
Q9Y297:BTRC; NbExp=3; IntAct=EBI-624237, EBI-307461;
Q14008:CKAP5; NbExp=4; IntAct=EBI-624237, EBI-310585;
P42858:HTT; NbExp=4; IntAct=EBI-624237, EBI-466029;
Q9UK45:LSM7; NbExp=4; IntAct=EBI-624252, EBI-348372;
Q9Y316:MEMO1; NbExp=4; IntAct=EBI-624237, EBI-1104564;
Q9H788:SH2D4A; NbExp=3; IntAct=EBI-624237, EBI-747035;
P62308:SNRPG; NbExp=5; IntAct=EBI-624252, EBI-624585;
Q13190:STX5; NbExp=3; IntAct=EBI-624237, EBI-714206;
Q8NHU6:TDRD7; NbExp=4; IntAct=EBI-624237, EBI-624505;
O43422:THAP12; NbExp=3; IntAct=EBI-624237, EBI-2828217;
O95619:YEATS4; NbExp=6; IntAct=EBI-624237, EBI-399269;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14767476}.
Nucleus {ECO:0000269|PubMed:14767476}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000269|PubMed:21531210}. Midbody
{ECO:0000269|PubMed:21531210}. Note=Nucleus during interphase.
Weakly concentrated at centrosomes during mitosis and colocalizes
with AURKC at the midbody during cytokinesis.
{ECO:0000269|PubMed:21531210}.
-!- SUBCELLULAR LOCATION: Isoform 5: Membrane {ECO:0000305}; Lipid-
anchor {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=A, Long;
IsoId=O75410-1; Sequence=Displayed;
Name=2; Synonyms=F;
IsoId=O75410-2; Sequence=VSP_012647;
Name=3; Synonyms=E;
IsoId=O75410-3; Sequence=VSP_012638;
Name=4; Synonyms=D;
IsoId=O75410-4; Sequence=VSP_012641, VSP_012642;
Name=5; Synonyms=C;
IsoId=O75410-5; Sequence=VSP_012639, VSP_012646;
Note=Initiator Met-1 is removed. Contains a N-myristoyl glycine
at position 2. {ECO:0000269|PubMed:25807930};
Name=6; Synonyms=Short;
IsoId=O75410-6; Sequence=VSP_012644, VSP_012645;
Name=7;
IsoId=O75410-7; Sequence=VSP_012637, VSP_012643, VSP_012648;
Name=8;
IsoId=O75410-8; Sequence=VSP_012640;
-!- TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 5 are
ubiquitous. Isoform 2 is strongly expressed in the brain, weakly
detectable in lung and colon, and overexpressed in gastric cancer.
Isoform 4 is not detected in normal tissues, but strong expression
was found in gastric cancer tissues. Down-regulated in a subset of
cases of breast cancer. {ECO:0000269|PubMed:12165861,
ECO:0000269|PubMed:12547166}.
-!- DEVELOPMENTAL STAGE: Expressed at high level during early
embryogenesis.
-!- PTM: Isoform 1 is heavily phosphorylated; isoform 6 is not.
{ECO:0000269|PubMed:12165861, ECO:0000269|PubMed:21531210}.
-!- SIMILARITY: Belongs to the TACC family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TACC1ID42456ch8p11.html";
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EMBL; AF049910; AAC32327.1; -; mRNA.
EMBL; AY177411; AAO53446.1; -; mRNA.
EMBL; AY139007; AAN28955.1; -; mRNA.
EMBL; AK314620; BAG37186.1; -; mRNA.
EMBL; CH471080; EAW63293.1; -; Genomic_DNA.
EMBL; CH471080; EAW63296.1; -; Genomic_DNA.
EMBL; CH471080; EAW63298.1; -; Genomic_DNA.
EMBL; BC041391; AAH41391.1; -; mRNA.
EMBL; AB029026; BAA83055.1; -; mRNA.
EMBL; AY039239; AAK68658.1; -; mRNA.
EMBL; AY072874; AAL62461.1; -; mRNA.
EMBL; AY072875; AAL62462.1; -; mRNA.
EMBL; AY072876; AAL62463.2; -; mRNA.
CCDS; CCDS47845.1; -. [O75410-6]
CCDS; CCDS55224.1; -. [O75410-3]
CCDS; CCDS6109.1; -. [O75410-1]
RefSeq; NP_001116296.1; NM_001122824.1. [O75410-6]
RefSeq; NP_001139688.1; NM_001146216.2. [O75410-3]
RefSeq; NP_006274.2; NM_006283.2. [O75410-1]
RefSeq; XP_005273682.1; XM_005273625.4. [O75410-2]
RefSeq; XP_011542933.1; XM_011544631.1.
RefSeq; XP_011542934.1; XM_011544632.2. [O75410-2]
RefSeq; XP_011542938.1; XM_011544636.2. [O75410-5]
RefSeq; XP_016869261.1; XM_017013772.1.
RefSeq; XP_016869262.1; XM_017013773.1.
RefSeq; XP_016869263.1; XM_017013774.1.
UniGene; Hs.279245; -.
ProteinModelPortal; O75410; -.
SMR; O75410; -.
BioGrid; 112730; 39.
CORUM; O75410; -.
IntAct; O75410; 32.
MINT; MINT-8417725; -.
STRING; 9606.ENSP00000321703; -.
iPTMnet; O75410; -.
PhosphoSitePlus; O75410; -.
BioMuta; TACC1; -.
EPD; O75410; -.
MaxQB; O75410; -.
PaxDb; O75410; -.
PeptideAtlas; O75410; -.
PRIDE; O75410; -.
DNASU; 6867; -.
Ensembl; ENST00000276520; ENSP00000276520; ENSG00000147526. [O75410-6]
Ensembl; ENST00000317827; ENSP00000321703; ENSG00000147526. [O75410-1]
Ensembl; ENST00000518415; ENSP00000428706; ENSG00000147526. [O75410-7]
Ensembl; ENST00000520615; ENSP00000428450; ENSG00000147526. [O75410-3]
GeneID; 6867; -.
KEGG; hsa:6867; -.
UCSC; uc003xlz.4; human. [O75410-1]
CTD; 6867; -.
DisGeNET; 6867; -.
EuPathDB; HostDB:ENSG00000147526.19; -.
GeneCards; TACC1; -.
H-InvDB; HIX0007462; -.
HGNC; HGNC:11522; TACC1.
HPA; CAB017041; -.
HPA; HPA024702; -.
MalaCards; TACC1; -.
MIM; 605301; gene.
neXtProt; NX_O75410; -.
OpenTargets; ENSG00000147526; -.
Orphanet; 251579; Giant cell glioblastoma.
Orphanet; 251576; Gliosarcoma.
PharmGKB; PA36299; -.
eggNOG; ENOG410IIVK; Eukaryota.
eggNOG; ENOG410YMFS; LUCA.
GeneTree; ENSGT00530000063855; -.
HOVERGEN; HBG105967; -.
InParanoid; O75410; -.
KO; K14281; -.
OMA; PLDGICL; -.
OrthoDB; EOG091G072Z; -.
PhylomeDB; O75410; -.
TreeFam; TF333149; -.
ChiTaRS; TACC1; human.
GeneWiki; TACC1; -.
GenomeRNAi; 6867; -.
PMAP-CutDB; O75410; -.
PRO; PR:O75410; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000147526; -.
ExpressionAtlas; O75410; baseline and differential.
Genevisible; O75410; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; IBA:GO_Central.
GO; GO:0021987; P:cerebral cortex development; IBA:GO_Central.
GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
InterPro; IPR007707; TACC_C.
Pfam; PF05010; TACC; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell cycle; Cell division;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Lipoprotein;
Membrane; Myristate; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:20068231}.
CHAIN 2 805 Transforming acidic coiled-coil-
containing protein 1.
/FTId=PRO_0000179986.
DOMAIN 215 297 SPAZ 1.
DOMAIN 359 507 SPAZ 2.
REGION 2 55 Interaction with LSM7 and SNRPG.
{ECO:0000269|PubMed:12165861}.
REGION 152 259 Interaction with TDRD7.
{ECO:0000269|PubMed:14603251}.
REGION 206 427 Interaction with YEATS4.
{ECO:0000269|PubMed:11903063}.
REGION 701 805 Interaction with CH-TOG.
COILED 610 805
MOTIF 226 241 Bipartite nuclear localization signal 1.
{ECO:0000255}.
MOTIF 455 471 Bipartite nuclear localization signal 2.
{ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 147 147 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 228 228 Phosphoserine; by AURKC.
{ECO:0000269|PubMed:21531210}.
MOD_RES 248 248 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 276 276 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 381 381 Phosphoserine.
{ECO:0000250|UniProtKB:Q6Y685}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000250|UniProtKB:Q6Y685}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000250|UniProtKB:Q6Y685}.
MOD_RES 533 533 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 591 591 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 651 Missing (in isoform 8).
{ECO:0000303|Ref.3}.
/FTId=VSP_012640.
VAR_SEQ 1 438 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_012639.
VAR_SEQ 1 426 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_012641.
VAR_SEQ 1 195 Missing (in isoform 3).
{ECO:0000303|PubMed:12547166}.
/FTId=VSP_012638.
VAR_SEQ 1 41 Missing (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012637.
VAR_SEQ 42 53 EDSQAETKSLSF -> MNNILKLK (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012643.
VAR_SEQ 54 54 S -> R (in isoform 6).
{ECO:0000303|PubMed:15207008}.
/FTId=VSP_012644.
VAR_SEQ 55 464 Missing (in isoform 6).
{ECO:0000303|PubMed:15207008}.
/FTId=VSP_012645.
VAR_SEQ 427 464 DPFKPTTTLTSSDFCSPTGNHVNEILESPKKAKSRLIT ->
MGGSHSQTPRGREPAGERHPRPTETATTEQVKFLCFLL
(in isoform 4). {ECO:0000305}.
/FTId=VSP_012642.
VAR_SEQ 439 464 DFCSPTGNHVNEILESPKKAKSRLIT -> MGGSHSQTPRG
REPAGERHPRPTETA (in isoform 5).
{ECO:0000305}.
/FTId=VSP_012646.
VAR_SEQ 464 464 T -> TTTEQVKFLCFLL (in isoform 2).
{ECO:0000303|PubMed:10470851,
ECO:0000303|PubMed:12087473}.
/FTId=VSP_012647.
VAR_SEQ 525 553 Missing (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012648.
VARIANT 187 187 P -> L (in dbSNP:rs34235313).
/FTId=VAR_053703.
VARIANT 243 243 I -> T (in dbSNP:rs6980553).
/FTId=VAR_053704.
VARIANT 255 255 E -> G (in dbSNP:rs10107016).
/FTId=VAR_053705.
MUTAGEN 228 228 S->A: Impairs phosphorylation by AURKC.
{ECO:0000269|PubMed:21531210}.
CONFLICT 291 291 L -> I (in Ref. 1; AAC32327).
{ECO:0000305}.
CONFLICT 428 428 P -> H (in Ref. 6; AAH41391).
{ECO:0000305}.
CONFLICT 588 588 G -> V (in Ref. 7; BAA83055).
{ECO:0000305}.
CONFLICT 654 654 Missing (in Ref. 7; BAA83055).
{ECO:0000305}.
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


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