ID CKAP2_HUMAN Reviewed; 683 AA. AC Q8WWK9; A2BDE0; A5YM58; Q3KRA5; Q5VXB4; Q8IWV5; Q8IWV6; Q96FH9; AC Q9H012; Q9H0D0; Q9H988; Q9HC49; Q9NVG4; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 05-OCT-2010, entry version 66. DE RecName: Full=Cytoskeleton-associated protein 2; DE AltName: Full=CTCL tumor antigen se20-10; DE AltName: Full=Tumor- and microtubule-associated protein; GN Name=CKAP2; Synonyms=LB1, TMAP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND VARIANT VAL-323. RC TISSUE=T-cell; RX MEDLINE=98442964; PubMed=9771967; DOI=10.1038/sj.onc.1202048; RA Maouche-Chretien L., Deleu N., Badoual C., Fraissignes P., Berger R., RA Gaulard P., Romeo P.H., Leroy-Viard K.; RT "Identification of a novel cDNA, encoding a cytoskeletal associated RT protein, differentially expressed in diffuse large B-cell lymphomas."; RL Oncogene 17:1245-1251(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX MEDLINE=21130086; PubMed=11234418; RA Udina I.G., Baranova A.V., Kompaniytsev A.A., Sulimova G.E.; RT "Evolutionarily-conserved gene CKAP2,located in region 13q14.3 of the RT human genome, is frequently rearranged in various tumors."; RL Genetika 37:120-123(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION, RP AND INDUCTION. RC TISSUE=Cervix carcinoma; RX PubMed=12942315; DOI=10.1007/s00432-003-0484-0; RA Bae C.-D., Sung Y.-S., Jeon S.-M., Suh Y., Yang H.-K., Kim Y.-I., RA Park K.-H., Choi J., Ahn G., Park J.; RT "Up-regulation of cytoskeletal-associated protein 2 in primary human RT gastric adenocarcinomas."; RL J. Cancer Res. Clin. Oncol. 129:621-630(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP VAL-323. RC TISSUE=Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T., RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 218-683 (ISOFORM 3), AND VARIANT RP VAL-323. RC TISSUE=Bone marrow, Cerebellum, and Testis; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-683 (ISOFORM 1), AND VARIANTS LYS-236 RP AND VAL-323. RC TISSUE=Testis; RX MEDLINE=21143360; PubMed=11149944; DOI=10.1073/pnas.021386498; RA Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., RA Schadendorf D.; RT "Serological detection of cutaneous T-cell lymphoma-associated RT antigens."; RL Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 135-683 (ISOFORM 1), AND RP VARIANT VAL-323. RC TISSUE=Testis; RX MEDLINE=21154917; PubMed=11230166; DOI=10.1101/gr.GR1547R; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., RA Wambutt R., Korn B., Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and RT analysis of 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [10] RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX PubMed=17376772; DOI=10.1074/jbc.M701688200; RA Seki A., Fang G.; RT "CKAP2 is a spindle-associated protein degraded by APC/C-Cdh1 during RT mitotic exit."; RL J. Biol. Chem. 282:15103-15113(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534; THR-579; THR-582; RP THR-597; SER-602 AND THR-623, AND MASS SPECTROMETRY. RC TISSUE=Cervix adenocarcinoma; RX PubMed=16565220; DOI=10.1073/pnas.0507066103; RA Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; RT "Phosphoproteome analysis of the human mitotic spindle."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa RT cells and high confident phosphopeptide identification by cross- RT validation of MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69; SER-209; THR-211; RP SER-276; THR-280; SER-304; SER-305; SER-328; SER-534; THR-597 AND RP SER-614, AND MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=19007248; DOI=10.1021/ac801708p; RA Wang B., Malik R., Nigg E.A., Korner R.; RT "Evaluation of the low-specificity protease elastase for large-scale RT phosphoproteome analysis."; RL Anal. Chem. 80:9526-9533(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-579; THR-582; SER-595; RP THR-596; THR-597; TYR-599 AND SER-602, AND MASS SPECTROMETRY. 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-597 AND SER-602, AND RP MASS SPECTROMETRY. 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). CC -!- FUNCTION: Possesses microtubule stabilizing properties. Involved CC in regulating aneuploidy, cell cycling, and cell death in a CC p53/TP53-dependent manner (By similarity). CC -!- SUBUNIT: Associates with alpha- and beta-tubulins (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, CC cytoskeleton. Cytoplasm, cytoskeleton, spindle. Cytoplasm, CC cytoskeleton, spindle pole. Note=Contrary to the ectopically CC expressed protein, endogenous CKAP2 does not colocalize with CC microtubules in G1, S and early G2. At late G2 and prophase after CC separation of duplicated centrosomes, colocalizes with gamma- CC tubulin and centrosome-proximal microtubules. From prometaphase CC through anaphase B, colocalizes with mitotic spindle poles and CC spindle microtubules. During cytokinesis, absent from midbody CC microtubules. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8WWK9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WWK9-2; Sequence=VSP_052093, VSP_052094; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q8WWK9-3; Sequence=VSP_052094; CC -!- TISSUE SPECIFICITY: Abundant in testis, thymus, and in tumor CC derived cell lines, while barely detectable in liver, prostate, CC and kidney. CC -!- DEVELOPMENTAL STAGE: Present at the G1/S boundary. Accumulates as CC cells progress from S to G2 into mitosis. Rapidly degraded during CC mitosis exit by CDH1-activated anaphase promoting CC complex/cyclosome (APC/C). CC -!- INDUCTION: Up-regulated in primary human gastric cancers. CC -!- SIMILARITY: Belongs to the CKAP2 family. CC -!- SEQUENCE CAUTION: CC Sequence=AAG33675.1; Type=Frameshift; Positions=607; CC Sequence=AAH10901.1; Type=Erroneous initiation; CC Sequence=AAI05807.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence; CC Sequence=BAA91788.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y15758; CAC17466.1; -; mRNA. DR EMBL; AJ429398; CAD22295.1; -; Genomic_DNA. DR EMBL; AY062261; AAL47212.1; -; mRNA. DR EMBL; AY062262; AAL47213.1; -; mRNA. DR EMBL; AK001611; BAA91788.1; ALT_INIT; mRNA. DR EMBL; AK022982; BAB14345.1; -; mRNA. DR EMBL; EF560732; ABQ59042.1; -; mRNA. DR EMBL; AL359513; CAH71660.2; -; Genomic_DNA. DR EMBL; AL359513; CAH71661.2; -; Genomic_DNA. DR EMBL; BC010901; AAH10901.1; ALT_INIT; mRNA. DR EMBL; BC105806; AAI05807.1; ALT_SEQ; mRNA. DR EMBL; BC130296; AAI30297.1; -; mRNA. DR EMBL; AF177227; AAG33675.1; ALT_FRAME; mRNA. DR EMBL; AL136848; CAB66782.2; -; mRNA. DR IPI; IPI00071824; -. DR IPI; IPI00640794; -. DR IPI; IPI00946815; -. DR RefSeq; NP_001091995.1; -. DR RefSeq; NP_060674.3; -. DR UniGene; Hs.444028; -. DR UniGene; Hs.521482; -. DR UniGene; Hs.706579; -. DR ProteinModelPortal; Q8WWK9; -. DR STRING; Q8WWK9; -. DR PhosphoSite; Q8WWK9; -. DR PRIDE; Q8WWK9; -. DR Ensembl; ENST00000378037; ENSP00000367276; ENSG00000136108. DR GeneID; 26586; -. DR KEGG; hsa:26586; -. DR UCSC; uc001vgt.2; human. DR UCSC; uc001vgv.2; human. DR CTD; 26586; -. DR GeneCards; GC13P053029; -. DR HGNC; HGNC:1990; CKAP2. DR HPA; HPA008410; -. DR HPA; HPA027821; -. DR MIM; 611569; gene. DR PharmGKB; PA26526; -. DR eggNOG; prNOG06748; -. DR HOVERGEN; HBG107703; -. DR InParanoid; Q8WWK9; -. DR OMA; KYWICLA; -. DR OrthoDB; EOG9QC3QW; -. DR NextBio; 48956; -. DR ArrayExpress; Q8WWK9; -. DR Bgee; Q8WWK9; -. DR Genevestigator; Q8WWK9; -. DR GermOnline; ENSG00000136108; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. DR GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Alternative splicing; Apoptosis; Cell cycle; Complete proteome; KW Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein; Polymorphism. FT CHAIN 1 683 Cytoskeleton-associated protein 2. FT /FTId=PRO_0000245774. FT MOD_RES 69 69 Phosphothreonine. FT MOD_RES 209 209 Phosphoserine. FT MOD_RES 211 211 Phosphothreonine. FT MOD_RES 276 276 Phosphoserine. FT MOD_RES 280 280 Phosphothreonine. FT MOD_RES 304 304 Phosphoserine. FT MOD_RES 305 305 Phosphoserine. FT MOD_RES 328 328 Phosphoserine. FT MOD_RES 534 534 Phosphoserine. FT MOD_RES 579 579 Phosphothreonine. FT MOD_RES 582 582 Phosphothreonine. FT MOD_RES 595 595 Phosphoserine. FT MOD_RES 596 596 Phosphothreonine. FT MOD_RES 597 597 Phosphothreonine. FT MOD_RES 599 599 Phosphotyrosine. FT MOD_RES 602 602 Phosphoserine. FT MOD_RES 614 614 Phosphoserine. FT MOD_RES 623 623 Phosphothreonine. FT VAR_SEQ 1 235 Missing (in isoform 2). FT /FTId=VSP_052093. FT VAR_SEQ 496 683 Missing (in isoform 2 and isoform 3). FT /FTId=VSP_052094. FT VARIANT 236 236 M -> K (in dbSNP:rs35975899). FT /FTId=VAR_054018. FT VARIANT 323 323 I -> V (in dbSNP:rs7335867). FT /FTId=VAR_027005. FT CONFLICT 53 53 Missing (in Ref. 3; AAL47212/AAL47213, 4; FT BAA91788/BAB14345, 6; CAH71660/CAH71661 FT and 7; AAI30297). FT CONFLICT 402 402 P -> L (in Ref. 9; CAB66782). FT CONFLICT 494 495 PI -> VR (in Ref. 3; AAL47213, 6; FT CAH71661 and 7; AAH10901). FT CONFLICT 531 531 K -> Q (in Ref. 4; BAA91788). FT CONFLICT 531 531 K -> R (in Ref. 4; BAB14345). FT CONFLICT 559 559 F -> L (in Ref. 4; BAB14345). FT CONFLICT 577 577 V -> A (in Ref. 4; BAB14345). FT CONFLICT 643 643 K -> R (in Ref. 4; BAA91788). SQ SEQUENCE 683 AA; 76987 MW; 15287A7D860A4B23 CRC64; MSTPAVPQDL QLPPSQRAQS AFKEQRRQKL KEHLLRRKTL FAYKQENEML SSSRDQRVVT SEDQVQEGTK VLKLKTKMAD KENMKRPAES KNNTVVGKHC IPLKPSNELT NSTVVIDTHK PKDSNQTPHL LLTEDDPQSQ HMTLSQAFHL KNNSKKKQMT TEKQKQDANM PKKPVLGSYR GQIVQSKINS FRKPLQVKDE SSAATKKLSA TIPKATKPQP VNTSSVTVKS NRSSNMTATT KFVSTTSQNT QLVRPPIRSH HSNTRDTVKQ GISRTSANVT IRKGPHEKEL LQSKTALSSV KTSSSQGIIR NKTLSRSIAS EVIARPASLS NDKLMEKSEP VDQRRHTAGK AIVDSRSAQP KETSEERKAR LSEWKAGKGR VLKRPPNSVV TQHEPAGQNE KPVGSFWTTM AEEDEQRLFT EKVNNTFSEC LNLINEGCPK EDILVTLNDL IKNIPDAKKL VKYWICLALI EPITSPIENI IAIYEKAILA GAQPIEEMRH TIVDILTMKS QEKANLGENM EKSCASKEEV KEVSIEDTGV DVDPEKLEME SKLHRNLLFQ DCEKEQDNKT KDPTHDVKTP NTETRTSCLI KYNVSTTPYL QSVKKKVQFD GTNSAFKELK FLTPVRRSRR LQEKTSKLPD MLKDHYPCVS SLEQLTELGR ETDAFVCRPN AALCRVYYEA DTT //