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Transforming acidic coiled-coil-containing protein 2 (Anti-Zuai-1) (AZU-1)

 TACC2_HUMAN             Reviewed;        2948 AA.
O95359; Q4VXL0; Q4VXL3; Q4VXL6; Q4VXL7; Q5U5T7; Q86WG6; Q86WG7;
Q8TCK9; Q9BVQ1; Q9NZ41; Q9NZR5;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 3.
27-SEP-2017, entry version 152.
RecName: Full=Transforming acidic coiled-coil-containing protein 2;
AltName: Full=Anti-Zuai-1;
Short=AZU-1;
Name=TACC2;
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 2), SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=10749935; DOI=10.1091/mbc.11.4.1357;
Chen H.-M., Schmeichel K.L., Mian I.S., Lelievre S., Petersen O.W.,
Bissell M.J.;
"AZU-1: a candidate breast tumor suppressor and biomarker for tumor
progression.";
Mol. Biol. Cell 11:1357-1367(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, INTERACTION WITH YEATS4, AND VARIANTS PHE-830;
ARG-1103 AND LYS-2900.
PubMed=12620397; DOI=10.1016/S0888-7543(02)00039-3;
Lauffart B., Gangisetty O., Still I.H.;
"Molecular cloning, genomic structure and interactions of the putative
breast tumor suppressor TACC2.";
Genomics 81:192-201(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
TISSUE=Placenta, and Testis;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1990-2948 (ISOFORM 3), AND TISSUE
SPECIFICITY.
TISSUE=Endothelial cell;
PubMed=11161455; DOI=10.1006/cyto.2000.0812;
Pu J.J., Li C., Rodriguez M., Banerjee D.;
"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.";
Cytokine 13:129-137(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2065-2948 (ISOFORM 3), AND
VARIANT THR-2732.
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=15304323; DOI=10.1016/j.febslet.2004.06.092;
Dou Z., Ding X., Zereshki A., Zhang Y., Zhang J., Wang F., Sun J.,
Huang H., Yao X.;
"TTK kinase is essential for the centrosomal localization of TACC2.";
FEBS Lett. 572:51-56(2004).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2317 AND SER-2321, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2256 AND SER-2512, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-201; SER-571;
SER-575; SER-758; SER-962; SER-1025; SER-1267; SER-1313; SER-1562;
SER-2072; THR-2246; SER-2256; SER-2317; SER-2321; SER-2359; SER-2389;
SER-2394; SER-2403 AND SER-2512, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT THR-325 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT THR-2625 (ISOFORM 3), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-201; SER-269;
SER-493; SER-561; SER-2226; THR-2246; SER-2256; SER-2317; SER-2321;
THR-2451; THR-2455; THR-2458; SER-2512 AND SER-2557, 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).
[14]
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2072; SER-2256; SER-2317
AND SER-2321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2256; SER-2317;
THR-2430; SER-2512; SER-2534 AND SER-2569, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2072; SER-2226 AND
SER-2317, 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).
[18]
VARIANTS [LARGE SCALE ANALYSIS] VAL-798 AND SER-1347.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Plays a role in the microtubule-dependent coupling of
the nucleus and the centrosome. Involved in the processes that
regulate centrosome-mediated interkinetic nuclear migration (INM)
of neural progenitors (By similarity). May play a role in
organizing centrosomal microtubules. May act as a tumor suppressor
protein. May represent a tumor progression marker. {ECO:0000250,
ECO:0000269|PubMed:10749935}.
-!- SUBUNIT: Interacts with CCDC100/CEP120 (By similarity). Interacts
with microtubules. Interacts with YEATS4, GCN5L2 and PCAF.
{ECO:0000250, ECO:0000269|PubMed:12620397,
ECO:0000269|PubMed:14767476}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10749935}.
Nucleus {ECO:0000269|PubMed:10749935,
ECO:0000269|PubMed:14767476}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:15304323}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=4; Synonyms=Long, TACC2s;
IsoId=O95359-4; Sequence=Displayed;
Name=1; Synonyms=Short;
IsoId=O95359-1; Sequence=VSP_022153, VSP_022156;
Name=2;
IsoId=O95359-2; Sequence=VSP_022151, VSP_006368, VSP_006369;
Note=Contains a phosphothreonine at position 325.
{ECO:0000244|PubMed:18669648};
Name=3; Synonyms=ECTACC;
IsoId=O95359-3; Sequence=VSP_006369;
Note=Contains a phosphothreonine at position 2625.
{ECO:0000244|PubMed:18669648};
Name=5; Synonyms=TACC21;
IsoId=O95359-5; Sequence=VSP_022154, VSP_022155;
Name=6;
IsoId=O95359-6; Sequence=VSP_022153, VSP_022156, VSP_022158;
-!- TISSUE SPECIFICITY: Strongly expressed in heart, skeletal muscle,
brain, prostate, thyroid and trachea.
{ECO:0000269|PubMed:11161455, ECO:0000269|PubMed:12620397}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal brain, lung, liver and
kidney. {ECO:0000269|PubMed:12620397}.
-!- PTM: Phosphorylated by TTK; which is required for localization in
centrosome. {ECO:0000269|PubMed:15304323}.
-!- SIMILARITY: Belongs to the TACC family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF29537.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=AAF63433.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF176646; AAF63433.1; ALT_INIT; mRNA.
EMBL; AF095791; AAC64968.2; -; mRNA.
EMBL; AF528098; AAO62629.1; -; mRNA.
EMBL; AF528099; AAO62630.1; -; mRNA.
EMBL; AL135793; CAI95127.1; -; Genomic_DNA.
EMBL; AC063960; CAI95127.1; JOINED; Genomic_DNA.
EMBL; AL135793; CAI95128.1; -; Genomic_DNA.
EMBL; AL135793; CAI95131.1; -; Genomic_DNA.
EMBL; AL135793; CAI95134.1; -; Genomic_DNA.
EMBL; AC063960; CAI95134.1; JOINED; Genomic_DNA.
EMBL; BC000999; AAH00999.1; -; mRNA.
EMBL; BC039311; AAH39311.1; -; mRNA.
EMBL; AF220152; AAF29537.2; ALT_SEQ; mRNA.
EMBL; AL713712; CAD28509.1; -; mRNA.
CCDS; CCDS7625.1; -. [O95359-5]
CCDS; CCDS7626.1; -. [O95359-4]
CCDS; CCDS7627.1; -. [O95359-1]
CCDS; CCDS7628.1; -. [O95359-6]
RefSeq; NP_001278807.1; NM_001291878.1.
RefSeq; NP_008928.1; NM_006997.3. [O95359-1]
RefSeq; NP_996742.1; NM_206860.2. [O95359-6]
RefSeq; NP_996743.1; NM_206861.2. [O95359-5]
RefSeq; NP_996744.3; NM_206862.3.
UniGene; Hs.501252; -.
UniGene; Hs.713875; -.
ProteinModelPortal; O95359; -.
SMR; O95359; -.
BioGrid; 115830; 21.
CORUM; O95359; -.
IntAct; O95359; 5.
MINT; MINT-1203853; -.
STRING; 9606.ENSP00000334280; -.
iPTMnet; O95359; -.
PhosphoSitePlus; O95359; -.
BioMuta; TACC2; -.
EPD; O95359; -.
PaxDb; O95359; -.
PeptideAtlas; O95359; -.
PRIDE; O95359; -.
Ensembl; ENST00000260733; ENSP00000260733; ENSG00000138162. [O95359-1]
Ensembl; ENST00000334433; ENSP00000334280; ENSG00000138162. [O95359-4]
Ensembl; ENST00000358010; ENSP00000350701; ENSG00000138162. [O95359-5]
Ensembl; ENST00000360561; ENSP00000353763; ENSG00000138162. [O95359-6]
Ensembl; ENST00000369000; ENSP00000357996; ENSG00000138162. [O95359-2]
Ensembl; ENST00000369005; ENSP00000358001; ENSG00000138162. [O95359-4]
Ensembl; ENST00000513429; ENSP00000425062; ENSG00000138162. [O95359-5]
GeneID; 10579; -.
KEGG; hsa:10579; -.
UCSC; uc001lfv.4; human. [O95359-4]
CTD; 10579; -.
DisGeNET; 10579; -.
EuPathDB; HostDB:ENSG00000138162.18; -.
GeneCards; TACC2; -.
HGNC; HGNC:11523; TACC2.
HPA; HPA031020; -.
HPA; HPA031021; -.
HPA; HPA061394; -.
MIM; 605302; gene.
neXtProt; NX_O95359; -.
OpenTargets; ENSG00000138162; -.
PharmGKB; PA36300; -.
eggNOG; ENOG410IIVK; Eukaryota.
eggNOG; ENOG410YMFS; LUCA.
GeneTree; ENSGT00530000063855; -.
HOVERGEN; HBG093142; -.
InParanoid; O95359; -.
KO; K14282; -.
OMA; SQHEEAC; -.
OrthoDB; EOG091G072Z; -.
PhylomeDB; O95359; -.
TreeFam; TF333149; -.
ChiTaRS; TACC2; human.
GeneWiki; TACC2; -.
GenomeRNAi; 10579; -.
PRO; PR:O95359; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000138162; -.
ExpressionAtlas; O95359; baseline and differential.
Genevisible; O95359; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0035257; F:nuclear hormone receptor binding; IDA:MGI.
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;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 2948 Transforming acidic coiled-coil-
containing protein 2.
/FTId=PRO_0000179988.
DOMAIN 2315 2403 SPAZ.
COILED 2675 2703 {ECO:0000255}.
COILED 2746 2947 {ECO:0000255}.
COMPBIAS 482 549 Pro-rich.
COMPBIAS 1956 2016 Pro-rich.
COMPBIAS 2420 2423 Poly-Lys.
MOD_RES 197 197 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 201 201 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 269 269 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 493 493 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 561 561 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 571 571 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 575 575 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 758 758 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 962 962 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1025 1025 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1267 1267 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1313 1313 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1562 1562 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2072 2072 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 2161 2161 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JJG0}.
MOD_RES 2226 2226 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 2246 2246 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 2256 2256 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2317 2317 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 2321 2321 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 2359 2359 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2389 2389 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2392 2392 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JJG0}.
MOD_RES 2394 2394 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2403 2403 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2430 2430 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2451 2451 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2455 2455 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2458 2458 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2512 2512 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2534 2534 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2553 2553 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9JJG0}.
MOD_RES 2557 2557 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2569 2569 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 2296 Missing (in isoform 2).
{ECO:0000303|PubMed:10749935}.
/FTId=VSP_022151.
VAR_SEQ 1 1922 Missing (in isoform 1 and isoform 6).
{ECO:0000303|PubMed:11121038,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_022153.
VAR_SEQ 49 1857 Missing (in isoform 5).
{ECO:0000303|PubMed:12620397}.
/FTId=VSP_022154.
VAR_SEQ 1900 1944 Missing (in isoform 5).
{ECO:0000303|PubMed:12620397}.
/FTId=VSP_022155.
VAR_SEQ 1923 1945 APAGDRVEASTPSCPDPAKDLSR -> MGGSQSLQPAPASD
LNLEASEAM (in isoform 1 and isoform 6).
{ECO:0000303|PubMed:11121038,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_022156.
VAR_SEQ 2429 2432 Missing (in isoform 2).
{ECO:0000303|PubMed:10749935}.
/FTId=VSP_006368.
VAR_SEQ 2633 2709 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:10749935,
ECO:0000303|PubMed:11161455,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_006369.
VAR_SEQ 2680 2709 Missing (in isoform 6).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022158.
VARIANT 170 170 V -> I (in dbSNP:rs11200385).
/FTId=VAR_053706.
VARIANT 798 798 L -> V (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036381.
VARIANT 830 830 L -> F (in dbSNP:rs10887063).
{ECO:0000269|PubMed:12620397}.
/FTId=VAR_053707.
VARIANT 1103 1103 W -> R (in dbSNP:rs7073433).
{ECO:0000269|PubMed:12620397}.
/FTId=VAR_053708.
VARIANT 1347 1347 A -> S (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036382.
VARIANT 1425 1425 A -> T (in dbSNP:rs4752642).
/FTId=VAR_053709.
VARIANT 1492 1492 P -> L (in dbSNP:rs7920896).
/FTId=VAR_053710.
VARIANT 1916 1916 E -> K (in dbSNP:rs12765679).
/FTId=VAR_053711.
VARIANT 2078 2078 I -> T (in dbSNP:rs7083331).
/FTId=VAR_029803.
VARIANT 2102 2102 N -> S (in dbSNP:rs3750843).
/FTId=VAR_020478.
VARIANT 2197 2197 V -> A (in dbSNP:rs2295873).
/FTId=VAR_020479.
VARIANT 2210 2210 A -> V (in dbSNP:rs2295874).
/FTId=VAR_029804.
VARIANT 2216 2216 P -> L (in dbSNP:rs2295875).
/FTId=VAR_053712.
VARIANT 2261 2261 L -> H (in dbSNP:rs2295876).
/FTId=VAR_020480.
VARIANT 2271 2271 E -> D (in dbSNP:rs11200483).
/FTId=VAR_053713.
VARIANT 2718 2718 V -> I (in dbSNP:rs2295878).
/FTId=VAR_020481.
VARIANT 2732 2732 A -> T (in dbSNP:rs2295879).
{ECO:0000269|PubMed:17974005}.
/FTId=VAR_020482.
VARIANT 2900 2900 Q -> K (in dbSNP:rs1063627).
{ECO:0000269|PubMed:12620397}.
/FTId=VAR_029805.
CONFLICT 2896 2896 R -> Q (in Ref. 3; AAO62629/AAO62630).
{ECO:0000305}.
CONFLICT 2909 2909 S -> T (in Ref. 5; AAH39311).
{ECO:0000305}.
SEQUENCE 2948 AA; 309427 MW; 9DC4CC5231A5ADBD CRC64;
MGNENSTSDN QRTLSAQTPR SAQPPGNSQN IKRKQQDTPG SPDHRDASSI GSVGLGGFCT
ASESSASLDP CLVSPEVTEP RKDPQGARGP EGSLLPSPPP SQEREHPSSS MPFAECPPEG
CLASPAAAPE DGPQTQSPRR EPAPNAPGDI AAAFPAERDS STPYQEIAAV PSAGRERQPK
EEGQKSSFSF SSGIDQSPGM SPVPLREPMK APLCGEGDQP GGFESQEKEA AGGFPPAESR
QGVASVQVTP EAPAAAQQGT ESSAVLEKSP LKPMAPIPQD PAPRASDRER GQGEAPPQYL
TDDLEFLRAC HLPRSNSGAA PEAEVNAASQ ESCQQPVGAY LPHAELPWGL PSPALVPEAG
GSGKEALDTI DVQGHPQTGM RGTKPNQVVC VAAGGQPEGG LPVSPEPSLL TPTEEAHPAS
SLASFPAAQI PIAVEEPGSS SRESVSKAGM PVSADAAKEV VDAGLVGLER QVSDLGSKGE
HPEGDPGEVP APSPQERGEH LNTEQSHEVQ PGVPPPPLPK EQSHEVQPGA PPPPLPKAPS
ESARGPPGPT DGAKVHEDST SPAVAKEGSR SPGDSPGGKE EAPEPPDGGD PGNLQGEDSQ
AFSSKRDPEV GKDELSKPSS DAESRDHPSS HSAQPPRKGG AGHTDGPHSQ TAEADASGLP
HKLGEEDPVL PPVPDGAGEP TVPEGAIWEG SGLQPKCPDT LQSREGLGRM ESFLTLESEK
SDFPPTPVAE VAPKAQEGES TLEIRKMGSC DGEGLLTSPD QPRGPACDAS RQEFHAGVPH
PPQGENLAAD LGLTALILDQ DQQGIPSCPG EGWIRGAASE WPLLSSEKHL QPSQAQPETS
IFDVLKEQAQ PPENGKETSP SHPGFKDQGA DSSQIHVPVE PQEDNNLPTH GGQEQALGSE
LQSQLPKGTL SDTPTSSPTD MVWESSLTEE SELSAPTRQK LPALGEKRPE GACGDGQSSR
VSPPAADVLK DFSLAGNFSR KETCCTGQGP NKSQQALADA LEEGSQHEEA CQRHPGASEA
ADGCSPLWGL SKREMASGNT GEAPPCQPDS VALLDAVPCL PALAPASPGV TPTQDAPETE
ACDETQEGRQ QPVPAPQQKM ECWATSDAES PKLLASFPSA GEQGGEAGAA ETGGSAGAGD
PGKQQAPEKP GEATLSCGLL QTEHCLTSGE EASTSALRES CQAEHPMASC QDALLPAREL
GGIPRSTMDF STHQAVPDPK ELLLSGPPEV AAPDTPYLHV DSAAQRGAED SGVKAVSSAD
PRAPGESPCP VGEPPLALEN AASLKLFAGS LAPLLQPGAA GGEIPAVQAS SGSPKARTTE
GPVDSMPCLD RMPLLAKGKQ ATGEEKAATA PGAGAKASGE GMAGDAAGET EGSMERMGEP
SQDPKQGTSG GVDTSSEQIA TLTGFPDFRE HIAKIFEKPV LGALATPGEK AGAGRSAVGK
DLTRPLGPEK LLDGPPGVDV TLLPAPPARL QVEKKQQLAG EAEISHLALQ DPASDKLLGP
AGLTWERNLP GAGVGKEMAG VPPTLREDER PEGPGAAWPG LEGQAYSQLE RSRQELASGL
PSPAATQELP VERAAAFQVA PHSHGEEAVA QDRIPSGKQH QETSACDSPH GEDGPGDFAH
TGVPGHVPRS TCAPSPQREV LTVPEANSEP WTLDTLGGER RPGVTAGILE MRNALGNQST
PAPPTGEVAD TPLEPGKVAG AAGEAEGDIT LSTAETQACA SGDLPEAGTT RTFSVVAGDL
VLPGSCQDPA CSDKAPGMEG TAALHGDSPA RPQQAKEQPG PERPIPAGDG KVCVSSPPEP
DETHDPKLQH LAPEELHTDR ESPRPGPSML PSVPKKDAPR VMDKVTSDET RGAEGTESSP
VADDIIQPAA PADLESPTLA ASSYHGDVVG QVSTDLIAQS ISPAAAHAGL PPSAAEHIVS
PSAPAGDRVE ASTPSCPDPA KDLSRSSDSE EAFETPESTT PVKAPPAPPP PPPEVIPEPE
VSTQPPPEEP GCGSETVPVP DGPRSDSVEG SPFRPPSHSF SAVFDEDKPI ASSGTYNLDF
DNIELVDTFQ TLEPRASDAK NQEGKVNTRR KSTDSVPISK STLSRSLSLQ ASDFDGASSS
GNPEAVALAP DAYSTGSSSA SSTLKRTKKP RPPSLKKKQT TKKPTETPPV KETQQEPDEE
SLVPSGENLA SETKTESAKT EGPSPALLEE TPLEPAVGPK AACPLDSESA EGVVPPASGG
GRVQNSPPVG RKTLPLTTAP EAGEVTPSDS GGQEDSPAKG LSVRLEFDYS EDKSSWDNQQ
ENPPPTKKIG KKPVAKMPLR RPKMKKTPEK LDNTPASPPR SPAEPNDIPI AKGTYTFDID
KWDDPNFNPF SSTSKMQESP KLPQQSYNFD PDTCDESVDP FKTSSKTPSS PSKSPASFEI
PASAMEANGV DGDGLNKPAK KKKTPLKTDT FRVKKSPKRS PLSDPPSQDP TPAATPETPP
VISAVVHATD EEKLAVTNQK WTCMTVDLEA DKQDYPQPSD LSTFVNETKF SSPTEELDYR
NSYEIEYMEK IGSSLPQDDD APKKQALYLM FDTSQESPVK SSPVRMSESP TPCSGSSFEE
TEALVNTAAK NQHPVPRGLA PNQESHLQVP EKSSQKELEA MGLGTPSEAI EITAPEGSFA
SADALLSRLA HPVSLCGALD YLEPDLAEKN PPLFAQKLQE ELEFAIMRIE ALKLARQIAL
ASRSHQDAKR EAAHPTDVSI SKTALYSRIG TAEVEKPAGL LFQQPDLDSA LQIARAEIIT
KEREVSEWKD KYEESRREVM EMRKIVAEYE KTIAQMIEDE QREKSVSHQT VQQLVLEKEQ
ALADLNSVEK SLADLFRRYE KMKEVLEGFR KNEEVLKRCA QEYLSRVKKE EQRYQALKVH
AEEKLDRANA EIAQVRGKAQ QEQAAHQASL RKEQLRVDAL ERTLEQKNKE IEELTKICDE
LIAKMGKS


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