CKAP5_HUMAN
ID CKAP5_HUMAN Reviewed; 2032 AA.
AC Q14008; Q05D70; Q0VAX7; Q0VAX8; Q14668; Q2TA89; Q6NSH4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Cytoskeleton-associated protein 5;
DE AltName: Full=Colonic and hepatic tumor overexpressed gene protein;
DE Short=Ch-TOG;
GN Name=CKAP5; Synonyms=KIAA0097;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain tumor;
RX PubMed=8536682; DOI=10.1111/j.1432-1033.1995.406_b.x;
RA Charrasse S., Mazel M., Taviaux S., Berta P., Chow T., Larroque C.;
RT "Characterization of the cDNA and pattern of expression of a new gene over-
RT expressed in human hepatomas and colonic tumors.";
RL Eur. J. Biochem. 234:406-413(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=8832653; DOI=10.1016/0304-3940(96)12789-0;
RA Charrasse S., Coubes P., Arrancibia S., Larroque C.;
RT "Expression of the tumor over-expressed ch-TOG gene in human and baboon
RT brain.";
RL Neurosci. Lett. 212:119-122(1996).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9570755; DOI=10.1242/jcs.111.10.1371;
RA Charrasse S., Schroeder M., Gauthier-Rouviere C., Ango F., Cassimeris L.,
RA Gard D.L., Larroque C.;
RT "The TOGp protein is a new human microtubule-associated protein homologous
RT to the Xenopus XMAP215.";
RL J. Cell Sci. 111:1371-1383(1998).
RN [7]
RP INTERACTION WITH TACC1.
RX PubMed=11903063; DOI=10.1042/0264-6021:3630195;
RA Lauffart B., Howell S.J., Tasch J.E., Cowell J.K., Still I.H.;
RT "Interaction of the transforming acidic coiled-coil 1 (TACC1) protein with
RT ch-TOG and GAS41/NuBI1 suggests multiple TACC1-containing protein complexes
RT in human cells.";
RL Biochem. J. 363:195-200(2002).
RN [8]
RP FUNCTION.
RX PubMed=12569123; DOI=10.1101/gad.245603;
RA Gergely F., Draviam V.M., Raff J.W.;
RT "The ch-TOG/XMAP215 protein is essential for spindle pole organization in
RT human somatic cells.";
RL Genes Dev. 17:336-341(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [10]
RP INTERACTION WITH HNRNPA2B1.
RX PubMed=15703215; DOI=10.1091/mbc.e04-08-0709;
RA Kosturko L.D., Maggipinto M.J., D'Sa C., Carson J.H., Barbarese E.;
RT "The microtubule-associated protein tumor overexpressed gene binds to the
RT RNA trafficking protein heterogeneous nuclear ribonucleoprotein A2.";
RL Mol. Biol. Cell 16:1938-1947(2005).
RN [11]
RP FUNCTION.
RX PubMed=18809577; DOI=10.1128/mcb.01040-08;
RA Barr A.R., Gergely F.;
RT "MCAK-independent functions of ch-Tog/XMAP215 in microtubule plus-end
RT dynamics.";
RL Mol. Cell. Biol. 28:7199-7211(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP INTERACTION WITH TACC3 AND CLATHRIN, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21297582; DOI=10.1038/emboj.2011.15;
RA Booth D.G., Hood F.E., Prior I.A., Royle S.J.;
RT "A TACC3/ch-TOG/clathrin complex stabilises kinetochore fibres by inter-
RT microtubule bridging.";
RL EMBO J. 30:906-919(2011).
RN [17]
RP FUNCTION, INTERACTION WITH SLAIN2 AND SLAIN1, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21646404; DOI=10.1083/jcb.201012179;
RA van der Vaart B., Manatschal C., Grigoriev I., Olieric V., Gouveia S.M.,
RA Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C., Steinmetz M.O.,
RA Akhmanova A.;
RT "SLAIN2 links microtubule plus end-tracking proteins and controls
RT microtubule growth in interphase.";
RL J. Cell Biol. 193:1083-1099(2011).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=23251535; DOI=10.1371/journal.pone.0051442;
RA Nakamura S., Grigoriev I., Nogi T., Hamaji T., Cassimeris L.,
RA Mimori-Kiyosue Y.;
RT "Dissecting the nanoscale distributions and functions of microtubule-end-
RT binding proteins EB1 and ch-TOG in interphase HeLa cells.";
RL PLoS ONE 7:E51442-E51442(2012).
RN [19]
RP FUNCTION OF THE TACC3/CH-TOG/CLATHRIN COMPLEX.
RX PubMed=23532825; DOI=10.1242/jcs.124834;
RA Cheeseman L.P., Harry E.F., McAinsh A.D., Prior I.A., Royle S.J.;
RT "Specific removal of TACC3-ch-TOG-clathrin at metaphase deregulates
RT kinetochore fiber tension.";
RL J. Cell Sci. 126:2102-2113(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816; SER-845 AND SER-1469,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1861, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP INTERACTION WITH TACC3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-1939
RP AND LEU-1942.
RX PubMed=25596274; DOI=10.1242/bio.201410843;
RA Gutierrez-Caballero C., Burgess S.G., Bayliss R., Royle S.J.;
RT "TACC3-ch-TOG track the growing tips of microtubules independently of
RT clathrin and Aurora-A phosphorylation.";
RL Biol. Open 4:170-179(2015).
RN [23]
RP FUNCTION, AND INTERACTION WITH NDC80.
RX PubMed=27156448; DOI=10.1016/j.cell.2016.04.030;
RA Miller M.P., Asbury C.L., Biggins S.;
RT "A TOG protein confers tension sensitivity to kinetochore-microtubule
RT attachments.";
RL Cell 165:1428-1439(2016).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 846-1081, AND TOG DOMAIN.
RX PubMed=24966168; DOI=10.1091/mbc.e13-08-0501;
RA Fox J.C., Howard A.E., Currie J.D., Rogers S.L., Slep K.C.;
RT "The XMAP215 family drives microtubule polymerization using a structurally
RT diverse TOG array.";
RL Mol. Biol. Cell 25:2375-2392(2014).
CC -!- FUNCTION: Binds to the plus end of microtubules and regulates
CC microtubule dynamics and microtubule organization. Acts as processive
CC microtubule polymerase. Promotes cytoplasmic microtubule nucleation and
CC elongation. Plays a major role in organizing spindle poles. In spindle
CC formation protects kinetochore microtubules from depolymerization by
CC KIF2C and has an essential role in centrosomal microtubule assembly
CC independently of KIF2C activity. Contributes to centrosome integrity.
CC Acts as component of the TACC3/ch-TOG/clathrin complex proposed to
CC contribute to stabilization of kinetochore fibers of the mitotic
CC spindle by acting as inter-microtubule bridge. The TACC3/ch-
CC TOG/clathrin complex is required for the maintenance of kinetochore
CC fiber tension (PubMed:23532825). Enhances the strength of NDC80
CC complex-mediated kinetochore-tip microtubule attachments
CC (PubMed:27156448). {ECO:0000269|PubMed:12569123,
CC ECO:0000269|PubMed:18809577, ECO:0000269|PubMed:21297582,
CC ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:23532825,
CC ECO:0000269|PubMed:27156448, ECO:0000269|PubMed:9570755}.
CC -!- SUBUNIT: Interacts with TACC1 (PubMed:11903063). Interacts with SLAIN2
CC and SLAIN1 (PubMed:21646404). Interacts with HNRNPA2B1
CC (PubMed:15703215). Interacts with TACC3 independently of clathrin
CC (PubMed:25596274). Interacts with TACC3 and clathrin forming the
CC TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules
CC bridges (PubMed:21297582, PubMed:23532825). Interacts with NDC80;
CC indicative for an association with the NDC80 complex (PubMed:27156448).
CC {ECO:0000269|PubMed:11903063, ECO:0000269|PubMed:15703215,
CC ECO:0000269|PubMed:21297582, ECO:0000269|PubMed:21646404,
CC ECO:0000269|PubMed:23532825, ECO:0000269|PubMed:25596274,
CC ECO:0000269|PubMed:27156448}.
CC -!- INTERACTION:
CC Q14008; P16333: NCK1; NbExp=3; IntAct=EBI-310585, EBI-389883;
CC Q14008; Q9P270: SLAIN2; NbExp=4; IntAct=EBI-310585, EBI-3959887;
CC Q14008; O75410: TACC1; NbExp=4; IntAct=EBI-310585, EBI-624237;
CC Q14008; O75410-1: TACC1; NbExp=3; IntAct=EBI-310585, EBI-624252;
CC Q14008; O75410-6: TACC1; NbExp=2; IntAct=EBI-310585, EBI-624278;
CC Q14008; Q9Y6A5: TACC3; NbExp=7; IntAct=EBI-310585, EBI-2554984;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:25596274,
CC ECO:0000269|PubMed:9570755}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:21646404}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:21297582, ECO:0000269|PubMed:25596274,
CC ECO:0000269|PubMed:9570755}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:25596274}. Note=Detected on centrosomes and
CC kinetochores during interphase and mitosis independently from TACC3 and
CC clathrin. Located to spindle poles and microtubules during mitosis. In
CC complex with TACC3 localized to microtubule plus-ends in mitosis and
CC interphase. In complex with TACC3 and clathrin localized to inter-
CC microtubule bridges in mitotic spindles. Accumulation sites at
CC microtubule plus ends protruded approximately 100 nm from MAPRE1/EB1
CC sites in interphase cells. {ECO:0000269|PubMed:21646404,
CC ECO:0000269|PubMed:23251535, ECO:0000269|PubMed:25596274}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q14008-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14008-2; Sequence=VSP_035668;
CC Name=3;
CC IsoId=Q14008-3; Sequence=VSP_036400;
CC -!- TISSUE SPECIFICITY: Overexpressed in hepatomas and colonic tumors. Also
CC expressed in skeletal muscle, brain, heart, placenta, lung, liver,
CC kidney and pancreas. Expression is elevated in the brain; highly
CC expressed in the Purkinje cell bodies of the cerebellum.
CC {ECO:0000269|PubMed:8536682, ECO:0000269|PubMed:8832653}.
CC -!- DOMAIN: The TOG (tumor overexpressed gene) domains are arranged in a N-
CC terminal pentameric array with each domain composed of six (for the
CC most part non-canonical) HEAT repeats forming a oblong paddle-like
CC structure. Intra-HEAT loops are positioned along a face of the TOG
CC domain and bind to a single alpha/beta-tubulin heterodimer. The TOG
CC domains in the array seem to be structurally and functionally
CC polarized. Differential functions may range from microtubule (MT)
CC lattice binding and/or free tubulin heterodimer binding to potentiating
CC stable incorporation of tubulin into the MT lattice.
CC {ECO:0000305|PubMed:24966168}.
CC -!- SIMILARITY: Belongs to the TOG/XMAP215 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17856.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH70136.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI11044.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI20871.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA07892.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X92474; CAA63212.1; -; mRNA.
DR EMBL; D43948; BAA07892.2; ALT_INIT; mRNA.
DR EMBL; AC115088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017856; AAH17856.1; ALT_SEQ; mRNA.
DR EMBL; BC070136; AAH70136.1; ALT_SEQ; mRNA.
DR EMBL; BC111043; AAI11044.1; ALT_SEQ; mRNA.
DR EMBL; BC120869; AAI20870.1; -; mRNA.
DR EMBL; BC120870; AAI20871.1; ALT_FRAME; mRNA.
DR CCDS; CCDS31477.1; -. [Q14008-1]
DR CCDS; CCDS7924.1; -. [Q14008-2]
DR PIR; S68176; S68176.
DR RefSeq; NP_001008938.1; NM_001008938.3. [Q14008-1]
DR RefSeq; NP_055571.2; NM_014756.3. [Q14008-2]
DR PDB; 4QMI; X-ray; 1.90 A; A/B=846-1081.
DR PDB; 4QMJ; X-ray; 2.50 A; A=846-1081.
DR PDBsum; 4QMI; -.
DR PDBsum; 4QMJ; -.
DR AlphaFoldDB; Q14008; -.
DR SMR; Q14008; -.
DR BioGRID; 115137; 231.
DR CORUM; Q14008; -.
DR IntAct; Q14008; 104.
DR MINT; Q14008; -.
DR STRING; 9606.ENSP00000432768; -.
DR CarbonylDB; Q14008; -.
DR GlyGen; Q14008; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q14008; -.
DR MetOSite; Q14008; -.
DR PhosphoSitePlus; Q14008; -.
DR SwissPalm; Q14008; -.
DR BioMuta; CKAP5; -.
DR DMDM; 212276513; -.
DR EPD; Q14008; -.
DR jPOST; Q14008; -.
DR MassIVE; Q14008; -.
DR MaxQB; Q14008; -.
DR PaxDb; Q14008; -.
DR PeptideAtlas; Q14008; -.
DR PRIDE; Q14008; -.
DR ProteomicsDB; 59791; -. [Q14008-1]
DR ProteomicsDB; 59792; -. [Q14008-2]
DR ProteomicsDB; 59793; -. [Q14008-3]
DR Antibodypedia; 26445; 152 antibodies from 26 providers.
DR DNASU; 9793; -.
DR Ensembl; ENST00000312055.9; ENSP00000310227.5; ENSG00000175216.15. [Q14008-2]
DR Ensembl; ENST00000354558.7; ENSP00000346566.3; ENSG00000175216.15. [Q14008-2]
DR Ensembl; ENST00000529230.6; ENSP00000432768.1; ENSG00000175216.15. [Q14008-1]
DR GeneID; 9793; -.
DR KEGG; hsa:9793; -.
DR MANE-Select; ENST00000529230.6; ENSP00000432768.1; NM_001008938.4; NP_001008938.1.
DR UCSC; uc001ndi.3; human. [Q14008-1]
DR CTD; 9793; -.
DR DisGeNET; 9793; -.
DR GeneCards; CKAP5; -.
DR HGNC; HGNC:28959; CKAP5.
DR HPA; ENSG00000175216; Low tissue specificity.
DR MIM; 611142; gene.
DR neXtProt; NX_Q14008; -.
DR OpenTargets; ENSG00000175216; -.
DR PharmGKB; PA142672107; -.
DR VEuPathDB; HostDB:ENSG00000175216; -.
DR eggNOG; KOG1820; Eukaryota.
DR GeneTree; ENSGT00390000014757; -.
DR HOGENOM; CLU_000539_2_1_1; -.
DR InParanoid; Q14008; -.
DR OMA; HMVPRQM; -.
DR OrthoDB; 33681at2759; -.
DR PhylomeDB; Q14008; -.
DR TreeFam; TF105639; -.
DR PathwayCommons; Q14008; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q14008; -.
DR BioGRID-ORCS; 9793; 789 hits in 1085 CRISPR screens.
DR ChiTaRS; CKAP5; human.
DR GeneWiki; CKAP5; -.
DR GenomeRNAi; 9793; -.
DR Pharos; Q14008; Tbio.
DR PRO; PR:Q14008; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q14008; protein.
DR Bgee; ENSG00000175216; Expressed in ventricular zone and 214 other tissues.
DR ExpressionAtlas; Q14008; baseline and differential.
DR Genevisible; Q14008; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0061863; F:microtubule plus end polymerase; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; IMP:HGNC-UCL.
DR GO; GO:0051298; P:centrosome duplication; IBA:GO_Central.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IMP:HGNC-UCL.
DR GO; GO:0007019; P:microtubule depolymerization; TAS:ARUK-UCL.
DR GO; GO:0046785; P:microtubule polymerization; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; IDA:CACAO.
DR GO; GO:0050658; P:RNA transport; ISS:HGNC-UCL.
DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 5.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR045110; XMAP215.
DR PANTHER; PTHR12609; PTHR12609; 1.
DR Pfam; PF12348; CLASP_N; 3.
DR SMART; SM01349; TOG; 5.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Centromere; Chromosome; Cytoplasm; Cytoskeleton; Kinetochore; Mitosis;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..2032
FT /note="Cytoskeleton-associated protein 5"
FT /id="PRO_0000089663"
FT REPEAT 159..197
FT /note="HEAT 1"
FT REPEAT 356..394
FT /note="HEAT 2"
FT REPEAT 434..472
FT /note="HEAT 3"
FT REPEAT 750..788
FT /note="HEAT 4"
FT REPEAT 855..893
FT /note="HEAT 5"
FT REPEAT 936..974
FT /note="HEAT 6"
FT REPEAT 1013..1051
FT /note="HEAT 7"
FT REPEAT 1284..1322
FT /note="HEAT 8"
FT REPEAT 1324..1357
FT /note="HEAT 9"
FT REPEAT 1361..1399
FT /note="HEAT 10"
FT REGION 1..223
FT /note="TOG 1"
FT /evidence="ECO:0000305|PubMed:24966168"
FT REGION 268..502
FT /note="TOG 2"
FT /evidence="ECO:0000305|PubMed:24966168"
FT REGION 516..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..817
FT /note="TOG 3"
FT /evidence="ECO:0000305|PubMed:24966168"
FT REGION 811..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..1081
FT /note="TOG 4"
FT /evidence="ECO:0000305|PubMed:24966168"
FT REGION 1077..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1428
FT /note="TOG 5"
FT /evidence="ECO:0000305|PubMed:24966168"
FT REGION 1422..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1801..1822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1932..1957
FT /note="Interaction with TACC3"
FT /evidence="ECO:0000269|PubMed:25596274"
FT REGION 1949..2032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1966..1981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1982..1997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1998..2017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1861
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1564..1623
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8536682"
FT /id="VSP_035668"
FT VAR_SEQ 1774
FT /note="K -> KSCMCLPQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036400"
FT VARIANT 785
FT /note="Y -> C (in dbSNP:rs11038988)"
FT /id="VAR_045627"
FT MUTAGEN 1939
FT /note="L->A,R: Disrupts interaction with TACC3."
FT /evidence="ECO:0000269|PubMed:25596274"
FT MUTAGEN 1939
FT /note="L->A: Abolishes localization to spindle
FT microtubules, no effect on localization to centrosomes and
FT kinetochores; when associated with A-1942."
FT /evidence="ECO:0000269|PubMed:25596274"
FT MUTAGEN 1942
FT /note="L->A,R: Disrupts interaction with TACC3."
FT /evidence="ECO:0000269|PubMed:25596274"
FT MUTAGEN 1942
FT /note="L->A: Abolishes localization to spindle
FT microtubules, no effect on localization to centrosomes and
FT kinetochores; when associated with A-1939."
FT /evidence="ECO:0000269|PubMed:25596274"
FT CONFLICT 476
FT /note="N -> K (in Ref. 1; CAA63212 and 2; BAA07892)"
FT /evidence="ECO:0000305"
FT CONFLICT 1814
FT /note="E -> A (in Ref. 1; CAA63212)"
FT /evidence="ECO:0000305"
FT CONFLICT 1822
FT /note="E -> A (in Ref. 1; CAA63212)"
FT /evidence="ECO:0000305"
FT HELIX 858..860
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 863..869
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 874..891
FT /evidence="ECO:0007829|PDB:4QMI"
FT STRAND 892..894
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 901..906
FT /evidence="ECO:0007829|PDB:4QMI"
FT TURN 907..910
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 914..931
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 932..938
FT /evidence="ECO:0007829|PDB:4QMI"
FT TURN 939..942
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 943..948
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 949..951
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 955..972
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 975..978
FT /evidence="ECO:0007829|PDB:4QMI"
FT STRAND 979..981
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 982..987
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 992..1005
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 1006..1008
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 1016..1019
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 1020..1027
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 1032..1049
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 1051..1056
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 1057..1060
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 1063..1076
FT /evidence="ECO:0007829|PDB:4QMI"
FT HELIX 1077..1079
FT /evidence="ECO:0007829|PDB:4QMI"
SQ 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
