CKAP2_HUMAN
ID CKAP2_HUMAN Reviewed; 683 AA.
AC Q8WWK9; A2BDE0; A5YM58; B4DR35; E9PD90; Q3KRA5; Q5VXB4; Q8IWV5; Q8IWV6;
AC Q96FH9; Q9H012; Q9H0D0; Q9H988; Q9HC49; Q9NVG4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 154.
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 {ECO:0000312|HGNC:HGNC:1990};
GN Synonyms=LB1 {ECO:0000312|EMBL:CAC17466.1},
GN TMAP {ECO:0000312|EMBL:AAL47212.1};
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] {ECO:0000305, ECO:0000312|EMBL:CAC17466.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND VARIANT VAL-323.
RC TISSUE=T-cell {ECO:0000312|EMBL:CAC17466.1};
RX 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] {ECO:0000305, ECO:0000312|EMBL:CAD22295.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX 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] {ECO:0000305, ECO:0000312|EMBL:AAL47212.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, AND
RP INDUCTION.
RC TISSUE=Cervix carcinoma {ECO:0000312|EMBL:AAL47212.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAB14345.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
RP VAL-323.
RC TISSUE=Teratocarcinoma {ECO:0000312|EMBL:BAB14345.1};
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6] {ECO:0000305}
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., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., 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., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., 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., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [7] {ECO:0000305, ECO:0000312|EMBL:AAH10901.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT VAL-323.
RC TISSUE=Bone marrow {ECO:0000312|EMBL:AAH10901.1}, Cerebellum, and
RC Testis {ECO:0000312|EMBL:AAI05807.1};
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 [8] {ECO:0000305, ECO:0000312|EMBL:AAG33675.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-683 (ISOFORM 1), AND VARIANTS LYS-236 AND
RP VAL-323.
RC TISSUE=Testis {ECO:0000312|EMBL:AAG33675.1};
RX PubMed=11149944; DOI=10.1073/pnas.98.2.629;
RA Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.;
RT "Serological detection of cutaneous T-cell lymphoma-associated antigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001).
RN [9] {ECO:0000305, ECO:0000312|EMBL:CAB66782.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 135-683 (ISOFORM 1), AND VARIANT
RP VAL-323.
RC TISSUE=Testis {ECO:0000312|EMBL:CAB66782.2};
RX 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., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 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 THR-579; THR-582; SER-595;
RP THR-596; THR-597; TYR-599 AND SER-602, AND IDENTIFICATION BY MASS
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-597 AND SER-602, AND
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534; SER-595; THR-597 AND
RP SER-602, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-190, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Possesses microtubule stabilizing properties. Involved in
CC regulating aneuploidy, cell cycling, and cell death in a p53/TP53-
CC dependent manner (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Associates with alpha- and beta-tubulins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Contrary to the
CC ectopically expressed protein, endogenous CKAP2 does not colocalize
CC with microtubules in G1, S and early G2. At late G2 and prophase after
CC separation of duplicated centrosomes, colocalizes with gamma-tubulin
CC and centrosome-proximal microtubules. From prometaphase through
CC anaphase B, colocalizes with mitotic spindle poles and spindle
CC microtubules. During cytokinesis, absent from midbody microtubules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:11149944, ECO:0000269|PubMed:12942315,
CC ECO:0000269|PubMed:9771967};
CC IsoId=Q8WWK9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WWK9-4; Sequence=VSP_047100, VSP_047101, VSP_047102;
CC Name=4;
CC IsoId=Q8WWK9-6; Sequence=VSP_055686;
CC Name=3;
CC IsoId=Q8WWK9-5; Sequence=VSP_047100;
CC -!- TISSUE SPECIFICITY: Abundant in testis, thymus, and in tumor derived
CC cell lines, while barely detectable in liver, prostate, and kidney.
CC {ECO:0000269|PubMed:9771967}.
CC -!- DEVELOPMENTAL STAGE: Present at the G1/S boundary. Accumulates as cells
CC progress from S to G2 into mitosis. Rapidly degraded during mitosis
CC exit by CDH1-activated anaphase promoting complex/cyclosome (APC/C).
CC {ECO:0000269|PubMed:17376772}.
CC -!- INDUCTION: Up-regulated in primary human gastric cancers.
CC {ECO:0000269|PubMed:12942315}.
CC -!- SIMILARITY: Belongs to the CKAP2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG33675.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH10901.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI05807.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA91788.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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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; AK299083; BAG61147.1; -; mRNA.
DR EMBL; EF560732; ABQ59042.1; -; mRNA.
DR EMBL; AL359513; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS41893.1; -. [Q8WWK9-1]
DR CCDS; CCDS66557.1; -. [Q8WWK9-6]
DR CCDS; CCDS73578.1; -. [Q8WWK9-4]
DR CCDS; CCDS9435.1; -. [Q8WWK9-5]
DR RefSeq; NP_001091995.1; NM_001098525.2. [Q8WWK9-1]
DR RefSeq; NP_001273615.1; NM_001286686.1. [Q8WWK9-6]
DR RefSeq; NP_001273616.1; NM_001286687.1. [Q8WWK9-4]
DR RefSeq; NP_060674.3; NM_018204.4. [Q8WWK9-5]
DR AlphaFoldDB; Q8WWK9; -.
DR BioGRID; 117755; 95.
DR ELM; Q8WWK9; -.
DR IntAct; Q8WWK9; 39.
DR MINT; Q8WWK9; -.
DR STRING; 9606.ENSP00000367276; -.
DR GlyGen; Q8WWK9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WWK9; -.
DR PhosphoSitePlus; Q8WWK9; -.
DR SwissPalm; Q8WWK9; -.
DR BioMuta; CKAP2; -.
DR DMDM; 74751579; -.
DR EPD; Q8WWK9; -.
DR jPOST; Q8WWK9; -.
DR MassIVE; Q8WWK9; -.
DR MaxQB; Q8WWK9; -.
DR PaxDb; Q8WWK9; -.
DR PeptideAtlas; Q8WWK9; -.
DR PRIDE; Q8WWK9; -.
DR ProteomicsDB; 19610; -.
DR ProteomicsDB; 74895; -. [Q8WWK9-1]
DR Antibodypedia; 1993; 130 antibodies from 24 providers.
DR DNASU; 26586; -.
DR Ensembl; ENST00000258607.10; ENSP00000258607.5; ENSG00000136108.15. [Q8WWK9-5]
DR Ensembl; ENST00000378034.7; ENSP00000367273.2; ENSG00000136108.15. [Q8WWK9-4]
DR Ensembl; ENST00000378037.9; ENSP00000367276.4; ENSG00000136108.15. [Q8WWK9-1]
DR Ensembl; ENST00000490903.5; ENSP00000417830.1; ENSG00000136108.15. [Q8WWK9-6]
DR GeneID; 26586; -.
DR KEGG; hsa:26586; -.
DR MANE-Select; ENST00000258607.10; ENSP00000258607.5; NM_018204.5; NP_060674.3. [Q8WWK9-5]
DR UCSC; uc001vgt.4; human. [Q8WWK9-1]
DR CTD; 26586; -.
DR DisGeNET; 26586; -.
DR GeneCards; CKAP2; -.
DR HGNC; HGNC:1990; CKAP2.
DR HPA; ENSG00000136108; Tissue enhanced (bone).
DR MIM; 611569; gene.
DR neXtProt; NX_Q8WWK9; -.
DR OpenTargets; ENSG00000136108; -.
DR PharmGKB; PA26526; -.
DR VEuPathDB; HostDB:ENSG00000136108; -.
DR eggNOG; ENOG502RUSI; Eukaryota.
DR GeneTree; ENSGT00530000063691; -.
DR HOGENOM; CLU_026552_0_0_1; -.
DR InParanoid; Q8WWK9; -.
DR OMA; HHRNLLF; -.
DR OrthoDB; 417608at2759; -.
DR PhylomeDB; Q8WWK9; -.
DR TreeFam; TF333003; -.
DR PathwayCommons; Q8WWK9; -.
DR SignaLink; Q8WWK9; -.
DR SIGNOR; Q8WWK9; -.
DR BioGRID-ORCS; 26586; 50 hits in 1088 CRISPR screens.
DR ChiTaRS; CKAP2; human.
DR GeneWiki; CKAP2; -.
DR GenomeRNAi; 26586; -.
DR Pharos; Q8WWK9; Tbio.
DR PRO; PR:Q8WWK9; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q8WWK9; protein.
DR Bgee; ENSG00000136108; Expressed in ventricular zone and 178 other tissues.
DR ExpressionAtlas; Q8WWK9; baseline and differential.
DR Genevisible; Q8WWK9; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000281; P:mitotic cytokinesis; IGI:MGI.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR InterPro; IPR029197; CKAP2_C.
DR InterPro; IPR026165; CKAP2_fam.
DR PANTHER; PTHR16076; PTHR16076; 1.
DR Pfam; PF15297; CKAP2_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cell cycle; Cytoplasm; Cytoskeleton;
KW Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..683
FT /note="Cytoskeleton-associated protein 2"
FT /id="PRO_0000245774"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 579
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 582
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 596
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 597
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 599
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..51
FT /note="MSTPAVPQDLQLPPSQRAQSAFKEQRRQKLKEHLLRRKTLFAYKQENEMLS
FT -> ML (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055686"
FT VAR_SEQ 53
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12942315,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_047100"
FT VAR_SEQ 494..495
FT /note="PI -> VR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12942315"
FT /id="VSP_047101"
FT VAR_SEQ 496..683
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12942315"
FT /id="VSP_047102"
FT VARIANT 236
FT /note="M -> K (in dbSNP:rs35975899)"
FT /evidence="ECO:0000269|PubMed:11149944"
FT /id="VAR_054018"
FT VARIANT 323
FT /note="I -> V (in dbSNP:rs7335867)"
FT /evidence="ECO:0000269|PubMed:11149944,
FT ECO:0000269|PubMed:11230166, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9771967"
FT /id="VAR_069359"
FT CONFLICT 402
FT /note="P -> L (in Ref. 9; CAB66782)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="K -> Q (in Ref. 4; BAA91788)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="K -> R (in Ref. 4; BAB14345)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="F -> L (in Ref. 4; BAB14345)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="V -> A (in Ref. 4; BAB14345)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="K -> R (in Ref. 4; BAA91788)"
FT /evidence="ECO:0000305"
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
