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 27-MAR-2024, entry version 163. 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}, TMAP GN {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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) 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; 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; 124. DR ELM; Q8WWK9; -. DR IntAct; Q8WWK9; 42. DR MINT; Q8WWK9; -. DR STRING; 9606.ENSP00000367276; -. DR GlyGen; Q8WWK9; 3 sites, 1 O-linked glycan (3 sites). 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; 9606-ENSP00000367276; -. DR PeptideAtlas; Q8WWK9; -. DR ProteomicsDB; 19610; -. DR ProteomicsDB; 74895; -. [Q8WWK9-1] DR Pumba; Q8WWK9; -. DR Antibodypedia; 1993; 150 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 AGR; HGNC:1990; -. 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; HEPEGQN; -. DR OrthoDB; 5354146at2759; -. DR PhylomeDB; Q8WWK9; -. DR TreeFam; TF333003; -. DR PathwayCommons; Q8WWK9; -. DR SignaLink; Q8WWK9; -. DR SIGNOR; Q8WWK9; -. DR BioGRID-ORCS; 26586; 51 hits in 1166 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 179 other cell types or tissues. DR ExpressionAtlas; Q8WWK9; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:HPA. 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; CYTOSKELETON ASSOCIATED PROTEIN 2-RELATED; 1. DR PANTHER; PTHR16076:SF8; CYTOSKELETON-ASSOCIATED PROTEIN 2; 1. DR Pfam; PF15297; CKAP2_C; 1. DR Genevisible; Q8WWK9; HS. 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 //