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Cytoskeleton-associated protein 5 (Colonic and hepatic tumor overexpressed gene protein) (Ch-TOG)

 CKAP5_HUMAN             Reviewed;        2032 AA.
Q14008; Q05D70; Q0VAX7; Q0VAX8; Q14668; Q2TA89; Q6NSH4;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
04-NOV-2008, sequence version 3.
27-SEP-2017, entry version 171.
RecName: Full=Cytoskeleton-associated protein 5;
AltName: Full=Colonic and hepatic tumor overexpressed gene protein;
Short=Ch-TOG;
Name=CKAP5; Synonyms=KIAA0097;
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), AND TISSUE SPECIFICITY.
TISSUE=Brain tumor;
PubMed=8536682; DOI=10.1111/j.1432-1033.1995.406_b.x;
Charrasse S., Mazel M., Taviaux S., Berta P., Chow T., Larroque C.;
"Characterization of the cDNA and pattern of expression of a new gene
over-expressed in human hepatomas and colonic tumors.";
Eur. J. Biochem. 234:406-413(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=7788527; DOI=10.1093/dnares/2.1.37;
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. III.
The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:37-43(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Uterus;
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).
[5]
TISSUE SPECIFICITY.
PubMed=8832653; DOI=10.1016/0304-3940(96)12789-0;
Charrasse S., Coubes P., Arrancibia S., Larroque C.;
"Expression of the tumor over-expressed ch-TOG gene in human and
baboon brain.";
Neurosci. Lett. 212:119-122(1996).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9570755;
Charrasse S., Schroeder M., Gauthier-Rouviere C., Ango F.,
Cassimeris L., Gard D.L., Larroque C.;
"The TOGp protein is a new human microtubule-associated protein
homologous to the Xenopus XMAP215.";
J. Cell Sci. 111:1371-1383(1998).
[7]
INTERACTION WITH TACC1.
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).
[8]
FUNCTION.
PubMed=12569123; DOI=10.1101/gad.245603;
Gergely F., Draviam V.M., Raff J.W.;
"The ch-TOG/XMAP215 protein is essential for spindle pole organization
in human somatic cells.";
Genes Dev. 17:336-341(2003).
[9]
INTERACTION WITH HNRNPA2B1.
PubMed=15703215; DOI=10.1091/mbc.E04-08-0709;
Kosturko L.D., Maggipinto M.J., D'Sa C., Carson J.H., Barbarese E.;
"The microtubule-associated protein tumor overexpressed gene binds to
the RNA trafficking protein heterogeneous nuclear ribonucleoprotein
A2.";
Mol. Biol. Cell 16:1938-1947(2005).
[10]
FUNCTION.
PubMed=18809577; DOI=10.1128/MCB.01040-08;
Barr A.R., Gergely F.;
"MCAK-independent functions of ch-Tog/XMAP215 in microtubule plus-end
dynamics.";
Mol. Cell. Biol. 28:7199-7211(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816, 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).
[12]
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).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[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]
INTERACTION WITH TACC3 AND CLATHRIN, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=21297582; DOI=10.1038/emboj.2011.15;
Booth D.G., Hood F.E., Prior I.A., Royle S.J.;
"A TACC3/ch-TOG/clathrin complex stabilises kinetochore fibres by
inter-microtubule bridging.";
EMBO J. 30:906-919(2011).
[16]
FUNCTION, INTERACTION WITH SLAIN2, AND SUBCELLULAR LOCATION.
PubMed=21646404; DOI=10.1083/jcb.201012179;
van der Vaart B., Manatschal C., Grigoriev I., Olieric V.,
Gouveia S.M., Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C.,
Steinmetz M.O., Akhmanova A.;
"SLAIN2 links microtubule plus end-tracking proteins and controls
microtubule growth in interphase.";
J. Cell Biol. 193:1083-1099(2011).
[17]
SUBCELLULAR LOCATION.
PubMed=23251535; DOI=10.1371/journal.pone.0051442;
Nakamura S., Grigoriev I., Nogi T., Hamaji T., Cassimeris L.,
Mimori-Kiyosue Y.;
"Dissecting the nanoscale distributions and functions of microtubule-
end-binding proteins EB1 and ch-TOG in interphase HeLa cells.";
PLoS ONE 7:E51442-E51442(2012).
[18]
FUNCTION OF THE TACC3/CH-TOG/CLATHRIN COMPLEX.
PubMed=23532825; DOI=10.1242/jcs.124834;
Cheeseman L.P., Harry E.F., McAinsh A.D., Prior I.A., Royle S.J.;
"Specific removal of TACC3-ch-TOG-clathrin at metaphase deregulates
kinetochore fiber tension.";
J. Cell Sci. 126:2102-2113(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816; SER-845 AND
SER-1469, 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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1861, 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).
[21]
INTERACTION WITH TACC3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
LEU-1939 AND LEU-1942.
PubMed=25596274; DOI=10.1242/bio.201410843;
Gutierrez-Caballero C., Burgess S.G., Bayliss R., Royle S.J.;
"TACC3-ch-TOG track the growing tips of microtubules independently of
clathrin and Aurora-A phosphorylation.";
Biol. Open 4:170-179(2015).
[22]
FUNCTION, AND INTERACTION WITH NDC80.
PubMed=27156448; DOI=10.1016/j.cell.2016.04.030;
Miller M.P., Asbury C.L., Biggins S.;
"A TOG protein confers tension sensitivity to kinetochore-microtubule
attachments.";
Cell 165:1428-1439(2016).
[23]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 846-1081, AND TOG DOMAIN.
PubMed=24966168; DOI=10.1091/mbc.E13-08-0501;
Fox J.C., Howard A.E., Currie J.D., Rogers S.L., Slep K.C.;
"The XMAP215 family drives microtubule polymerization using a
structurally diverse TOG array.";
Mol. Biol. Cell 25:2375-2392(2014).
-!- FUNCTION: Binds to the plus end of microtubules and regulates
microtubule dynamics and microtubule organization. Acts as
processive microtubule polymerase. Promotes cytoplasmic
microtubule nucleation and elongation. Plays a major role in
organizing spindle poles. In spindle formation protects
kinetochore microtubules from depolymerization by KIF2C and has an
essential role in centrosomal microtubule assembly independently
of KIF2C activity. Contributes to centrosome integrity. Acts as
component of the TACC3/ch-TOG/clathrin complex proposed to
contribute to stabilization of kinetochore fibers of the mitotic
spindle by acting as inter-microtubule bridge. The TACC3/ch-
TOG/clathrin complex is required for the maintenance of
kinetochore fiber tension (PubMed:23532825). Enhances the strength
of NDC80 complex-mediated kinetochore-tip microtubule attachments
(PubMed:27156448). {ECO:0000269|PubMed:12569123,
ECO:0000269|PubMed:18809577, ECO:0000269|PubMed:21297582,
ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:23532825,
ECO:0000269|PubMed:27156448, ECO:0000269|PubMed:9570755}.
-!- SUBUNIT: Interacts with TACC1 (PubMed:11903063). Interacts with
SLAIN2 (PubMed:21646404). Interacts with HNRNPA2B1
(PubMed:15703215). Interacts with TACC3 independently of clathrin.
Interacts with TACC3 and clathrin forming the TACC3/ch-
TOG/clathrin complex located at spindle inter-microtubules bridges
(PubMed:21297582). Interacts with NDC80; indicative for an
association with the NDC80 comnplex (PubMed:27156448).
{ECO:0000269|PubMed:11903063, ECO:0000269|PubMed:15703215,
ECO:0000269|PubMed:21297582, ECO:0000269|PubMed:21646404,
ECO:0000269|PubMed:27156448}.
-!- INTERACTION:
P16333:NCK1; NbExp=3; IntAct=EBI-310585, EBI-389883;
Q9P270:SLAIN2; NbExp=4; IntAct=EBI-310585, EBI-3959887;
O75410:TACC1; NbExp=4; IntAct=EBI-310585, EBI-624237;
O75410-1:TACC1; NbExp=3; IntAct=EBI-310585, EBI-624252;
O75410-6:TACC1; NbExp=2; IntAct=EBI-310585, EBI-624278;
Q9Y6A5:TACC3; NbExp=7; IntAct=EBI-310585, EBI-2554984;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:21646404,
ECO:0000269|PubMed:25596274, ECO:0000269|PubMed:9570755}.
Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:21646404}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:21297582, ECO:0000269|PubMed:25596274,
ECO:0000269|PubMed:9570755}. Chromosome, centromere, kinetochore
{ECO:0000269|PubMed:25596274}. Note=Detected on centrosomes and
kinetochores during interphase and mitosis independently from
TACC3 and clathrin. Located to spindle poles and microtubules
during mitosis. In complex with TACC3 localized to microtubule
plus-ends in mitosis and interphase. In complex with TACC3 and
clathrin localized to inter-microtubule bridges in mitotic
spindles. Accumulation sites at microtubule plus ends protruded
approximately 100 nm from MAPRE1/EB1 sites in interphase cells.
{ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:23251535,
ECO:0000269|PubMed:25596274}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q14008-1; Sequence=Displayed;
Name=2;
IsoId=Q14008-2; Sequence=VSP_035668;
Name=3;
IsoId=Q14008-3; Sequence=VSP_036400;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Overexpressed in hepatomas and colonic tumors.
Also expressed in skeletal muscle, brain, heart, placenta, lung,
liver, kidney and pancreas. Expression is elevated in the brain;
highly expressed in the Purkinje cell bodies of the cerebellum.
{ECO:0000269|PubMed:8536682, ECO:0000269|PubMed:8832653}.
-!- DOMAIN: The TOG (tumor overexpressed gene) domains are arranged in
a N-terminal pentameric array with each domain composed of six
(for the most part non-canonical) HEAT repeats forming a oblong
paddle-like structure. Intra-HEAT loops are positioned along a
face of the TOG domain and bind to a single alpha/beta-tubulin
heterodimer. The TOG domains in the array seem to be structurally
and functionally polarized. Differential functions may range from
microtubule (MT) lattice binding and/or free tubulin heterodimer
binding to potentiating stable incorporation of tubulin into the
MT lattice. {ECO:0000305|PubMed:24966168}.
-!- SIMILARITY: Belongs to the TOG/XMAP215 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH17856.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH70136.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAI11044.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAI20871.1; Type=Frameshift; Positions=18; Evidence={ECO:0000305};
Sequence=BAA07892.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X92474; CAA63212.1; -; mRNA.
EMBL; D43948; BAA07892.2; ALT_INIT; mRNA.
EMBL; AC115088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC017856; AAH17856.1; ALT_SEQ; mRNA.
EMBL; BC070136; AAH70136.1; ALT_SEQ; mRNA.
EMBL; BC111043; AAI11044.1; ALT_SEQ; mRNA.
EMBL; BC120869; AAI20870.1; -; mRNA.
EMBL; BC120870; AAI20871.1; ALT_FRAME; mRNA.
CCDS; CCDS31477.1; -. [Q14008-1]
CCDS; CCDS7924.1; -. [Q14008-2]
PIR; S68176; S68176.
RefSeq; NP_001008938.1; NM_001008938.3. [Q14008-1]
RefSeq; NP_055571.2; NM_014756.3. [Q14008-2]
UniGene; Hs.201253; -.
UniGene; Hs.737795; -.
PDB; 4QMI; X-ray; 1.90 A; A/B=846-1081.
PDB; 4QMJ; X-ray; 2.50 A; A=846-1081.
PDBsum; 4QMI; -.
PDBsum; 4QMJ; -.
ProteinModelPortal; Q14008; -.
SMR; Q14008; -.
BioGrid; 115137; 105.
CORUM; Q14008; -.
IntAct; Q14008; 66.
MINT; MINT-5002817; -.
STRING; 9606.ENSP00000432768; -.
iPTMnet; Q14008; -.
PhosphoSitePlus; Q14008; -.
SwissPalm; Q14008; -.
BioMuta; CKAP5; -.
DMDM; 212276513; -.
EPD; Q14008; -.
MaxQB; Q14008; -.
PaxDb; Q14008; -.
PeptideAtlas; Q14008; -.
PRIDE; Q14008; -.
Ensembl; ENST00000312055; ENSP00000310227; ENSG00000175216. [Q14008-2]
Ensembl; ENST00000354558; ENSP00000346566; ENSG00000175216. [Q14008-2]
Ensembl; ENST00000529230; ENSP00000432768; ENSG00000175216. [Q14008-1]
GeneID; 9793; -.
KEGG; hsa:9793; -.
UCSC; uc001ndi.3; human. [Q14008-1]
CTD; 9793; -.
DisGeNET; 9793; -.
EuPathDB; HostDB:ENSG00000175216.14; -.
GeneCards; CKAP5; -.
H-InvDB; HIX0022364; -.
HGNC; HGNC:28959; CKAP5.
HPA; HPA039377; -.
HPA; HPA040375; -.
MIM; 611142; gene.
neXtProt; NX_Q14008; -.
OpenTargets; ENSG00000175216; -.
PharmGKB; PA142672107; -.
eggNOG; KOG1820; Eukaryota.
eggNOG; ENOG410XPTW; LUCA.
GeneTree; ENSGT00390000014757; -.
HOVERGEN; HBG050955; -.
InParanoid; Q14008; -.
KO; K16803; -.
OMA; TEMPCQA; -.
OrthoDB; EOG091G00YR; -.
PhylomeDB; Q14008; -.
TreeFam; TF105639; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
ChiTaRS; CKAP5; human.
GeneWiki; CKAP5; -.
GenomeRNAi; 9793; -.
PRO; PR:Q14008; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000175216; -.
CleanEx; HS_CKAP5; -.
ExpressionAtlas; Q14008; baseline and differential.
Genevisible; Q14008; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007098; P:centrosome cycle; IMP:HGNC.
GO; GO:0051298; P:centrosome duplication; IBA:GO_Central.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IMP:HGNC.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0046785; P:microtubule polymerization; IBA:GO_Central.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0050658; P:RNA transport; ISS:HGNC.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
Gene3D; 1.25.10.10; -; 3.
Gene3D; 1.25.40.90; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR024395; CLASP_N_dom.
InterPro; IPR008942; ENTH_VHS.
InterPro; IPR021133; HEAT_type_2.
InterPro; IPR034085; TOG.
Pfam; PF12348; CLASP_N; 3.
SMART; SM01349; TOG; 5.
SUPFAM; SSF48371; SSF48371; 10.
PROSITE; PS50077; HEAT_REPEAT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Cell division; Centromere; Chromosome; Complete proteome; Cytoplasm;
Cytoskeleton; Kinetochore; Mitosis; Phosphoprotein; Polymorphism;
Reference proteome; Repeat.
CHAIN 1 2032 Cytoskeleton-associated protein 5.
/FTId=PRO_0000089663.
REPEAT 159 197 HEAT 1.
REPEAT 356 394 HEAT 2.
REPEAT 434 472 HEAT 3.
REPEAT 750 788 HEAT 4.
REPEAT 855 893 HEAT 5.
REPEAT 936 974 HEAT 6.
REPEAT 1013 1051 HEAT 7.
REPEAT 1284 1322 HEAT 8.
REPEAT 1324 1357 HEAT 9.
REPEAT 1361 1399 HEAT 10.
REGION 1 223 TOG 1. {ECO:0000305|PubMed:24966168}.
REGION 268 502 TOG 2. {ECO:0000305|PubMed:24966168}.
REGION 588 817 TOG 3. {ECO:0000305|PubMed:24966168}.
REGION 853 1081 TOG 4. {ECO:0000305|PubMed:24966168}.
REGION 1193 1428 TOG 5. {ECO:0000305|PubMed:24966168}.
REGION 1932 1957 Interaction with TACC3.
{ECO:0000269|PubMed:25596274}.
MOD_RES 48 48 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 816 816 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 845 845 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1469 1469 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1861 1861 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1564 1623 Missing (in isoform 2).
{ECO:0000303|PubMed:8536682}.
/FTId=VSP_035668.
VAR_SEQ 1774 1774 K -> KSCMCLPQ (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_036400.
VARIANT 785 785 Y -> C (in dbSNP:rs11038988).
/FTId=VAR_045627.
MUTAGEN 1939 1939 L->A,R: Disrupts interaction with TACC3.
{ECO:0000269|PubMed:25596274}.
MUTAGEN 1939 1939 L->A: Abolishes localization to spindle
microtubules, no effect on localization
to centrosomes and kinetochores; when
associated with A-1942.
{ECO:0000269|PubMed:25596274}.
MUTAGEN 1942 1942 L->A,R: Disrupts interaction with TACC3.
{ECO:0000269|PubMed:25596274}.
MUTAGEN 1942 1942 L->A: Abolishes localization to spindle
microtubules, no effect on localization
to centrosomes and kinetochores; when
associated with A-1939.
{ECO:0000269|PubMed:25596274}.
CONFLICT 476 476 N -> K (in Ref. 1; CAA63212 and 2;
BAA07892). {ECO:0000305}.
CONFLICT 1814 1814 E -> A (in Ref. 1; CAA63212).
{ECO:0000305}.
CONFLICT 1822 1822 E -> A (in Ref. 1; CAA63212).
{ECO:0000305}.
HELIX 858 860 {ECO:0000244|PDB:4QMI}.
HELIX 863 869 {ECO:0000244|PDB:4QMI}.
HELIX 874 891 {ECO:0000244|PDB:4QMI}.
STRAND 892 894 {ECO:0000244|PDB:4QMI}.
HELIX 901 906 {ECO:0000244|PDB:4QMI}.
TURN 907 910 {ECO:0000244|PDB:4QMI}.
HELIX 914 931 {ECO:0000244|PDB:4QMI}.
HELIX 932 938 {ECO:0000244|PDB:4QMI}.
TURN 939 942 {ECO:0000244|PDB:4QMI}.
HELIX 943 948 {ECO:0000244|PDB:4QMI}.
HELIX 949 951 {ECO:0000244|PDB:4QMI}.
HELIX 955 972 {ECO:0000244|PDB:4QMI}.
HELIX 975 978 {ECO:0000244|PDB:4QMI}.
STRAND 979 981 {ECO:0000244|PDB:4QMI}.
HELIX 982 987 {ECO:0000244|PDB:4QMI}.
HELIX 992 1005 {ECO:0000244|PDB:4QMI}.
HELIX 1006 1008 {ECO:0000244|PDB:4QMI}.
HELIX 1016 1019 {ECO:0000244|PDB:4QMI}.
HELIX 1020 1027 {ECO:0000244|PDB:4QMI}.
HELIX 1032 1049 {ECO:0000244|PDB:4QMI}.
HELIX 1051 1056 {ECO:0000244|PDB:4QMI}.
HELIX 1057 1060 {ECO:0000244|PDB:4QMI}.
HELIX 1063 1076 {ECO:0000244|PDB:4QMI}.
HELIX 1077 1079 {ECO:0000244|PDB:4QMI}.
SEQUENCE 2032 AA; 225495 MW; B2BBFB1CF2ED688B CRC64;
MGDDSEWLKL PVDQKCEHKL WKARLSGYEE ALKIFQKIKD EKSPEWSKFL GLIKKFVTDS
NAVVQLKGLE AALVYVENAH VAGKTTGEVV SGVVSKVFNQ PKAKAKELGI EICLMYIEIE
KGEAVQEELL KGLDNKNPKI IVACIETLRK ALSEFGSKII LLKPIIKVLP KLFESREKAV
RDEAKLIAVE IYRWIRDALR PPLQNINSVQ LKELEEEWVK LPTSAPRPTR FLRSQQELEA
KLEQQQSAGG DAEGGGDDGD EVPQIDAYEL LEAVEILSKL PKDFYDKIEA KKWQERKEAL
ESVEVLIKNP KLEAGDYADL VKALKKVVGK DTNVMLVALA AKCLTGLAVG LRKKFGQYAG
HVVPTILEKF KEKKPQVVQA LQEAIDAIFL TTTLQNISED VLAVMDNKNP TIKQQTSLFI
ARSFRHCTAS TLPKSLLKPF CAALLKHIND SAPEVRDAAF EALGTALKVV GEKAVNPFLA
DVDKLKLDKI KECSEKVELI HGKKAGLAAD KKEFKPLPGR TAASGAAGDK DTKDISAPKP
GPLKKAPAAK AGGPPKKGKP AAPGGAGNTG TKNKKGLETK EIVEPELSIE VCEEKASAVL
PPTCIQLLDS SNWKERLACM EEFQKAVELM DRTEMPCQAL VRMLAKKPGW KETNFQVMQM
KLHIVALIAQ KGNFSKTSAQ VVLDGLVDKI GDVKCGNNAK EAMTAIAEAC MLPWTAEQVV
SMAFSQKNPK NQSETLNWLS NAIKEFGFSG LNVKAFISNV KTALAATNPA VRTAAITLLG
VMYLYVGPSL RMFFEDEKPA LLSQIDAEFE KMQGQSPPAP TRGISKHSTS GTDEGEDGDE
PDDGSNDVVD LLPRTEISDK ITSELVSKIG DKNWKIRKEG LDEVAGIIND AKFIQPNIGE
LPTALKGRLN DSNKILVQQT LNILQQLAVA MGPNIKQHVK NLGIPIITVL GDSKNNVRAA
ALATVNAWAE QTGMKEWLEG EDLSEELKKE NPFLRQELLG WLAEKLPTLR STPTDLILCV
PHLYSCLEDR NGDVRKKAQD ALPFFMMHLG YEKMAKATGK LKPTSKDQVL AMLEKAKVNM
PAKPAPPTKA TSKPMGGSAP AKFQPASAPA EDCISSSTEP KPDPKKAKAP GLSSKAKSAQ
GKKMPSKTSL KEDEDKSGPI FIVVPNGKEQ RMKDEKGLKV LKWNFTTPRD EYIEQLKTQM
SSCVAKWLQD EMFHSDFQHH NKALAVMVDH LESEKEGVIG CLDLILKWLT LRFFDTNTSV
LMKALEYLKL LFTLLSEEEY HLTENEASSF IPYLVVKVGE PKDVIRKDVR AILNRMCLVY
PASKMFPFIM EGTKSKNSKQ RAECLEELGC LVESYGMNVC QPTPGKALKE IAVHIGDRDN
AVRNAALNTI VTVYNVHGDQ VFKLIGNLSE KDMSMLEERI KRSAKRPSAA PIKQVEEKPQ
RAQNISSNAN MLRKGPAEDM SSKLNQARSM SGHPEAAQMV RREFQLDLDE IENDNGTVRC
EMPELVQHKL DDIFEPVLIP EPKIRAVSPH FDDMHSNTAS TINFIISQVA SGDINTSIQA
LTQIDEVLRQ EDKAEAMSGH IDQFLIATFM QLRLIYNTHM ADEKLEKDEI IKLYSCIIGN
MISLFQIESL AREASTGVLK DLMHGLITLM LDSRIEDLEE GQQVIRSVNL LVVKVLEKSD
QTNILSALLV LLQDSLLATA SSPKFSELVM KCLWRMVRLL PDTINSINLD RILLDIHIFM
KVFPKEKLKQ CKSEFPIRTL KTLLHTLCKL KGPKILDHLT MIDNKNESEL EAHLCRMMKH
SMDQTGSKSD KETEKGASRI DEKSSKAKVN DFLAEIFKKI GSKENTKEGL AELYEYKKKY
SDADIEPFLK NSSQFFQSYV ERGLRVIEME REGKGRISTS TGISPQMEVT CVPTPTSTVS
SIGNTNGEEV GPSVYLERLK ILRQRCGLDN TKQDDRPPLT SLLSKPAVPT VASSTDMLHS
KLSQLRESRE QHQHSDLDSN QTHSSGTVTS SSSTANIDDL KKRLERIKSS RK


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