CKAP2_MOUSE
ID CKAP2_MOUSE Reviewed; 664 AA.
AC Q3V1H1; A6H5W7; Q66LN2; Q8BSF0;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cytoskeleton-associated protein 2;
GN Name=Ckap2 {ECO:0000312|MGI:MGI:1931797};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAU06608.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ASSOCIATION WITH ALPHA-TUBULINS AND
RP BETA-TUBULINS, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=NIH Swiss {ECO:0000312|EMBL:AAU06608.1};
RX PubMed=15504249; DOI=10.1111/j.1349-7006.2004.tb02187.x;
RA Jin Y., Murakumo Y., Ueno K., Hashimoto M., Watanabe T., Shimoyama Y.,
RA Ichihara M., Takahashi M.;
RT "Identification of a mouse cytoskeleton-associated protein, CKAP2, with
RT microtubule-stabilizing properties.";
RL Cancer Sci. 95:815-821(2004).
RN [2] {ECO:0000312|EMBL:BAE21180.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE21180.1};
RC TISSUE=Skin {ECO:0000312|EMBL:BAE21180.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=16061649; DOI=10.1158/0008-5472.can-04-4223;
RA Tsuchihara K., Lapin V., Bakal C., Okada H., Brown L.,
RA Hirota-Tsuchihara M., Zaugg K., Ho A., Itie-Youten A., Harris-Brandts M.,
RA Rottapel R., Richardson C.D., Benchimol S., Mak T.W.;
RT "Ckap2 regulates aneuploidy, cell cycling, and cell death in a p53-
RT dependent manner.";
RL Cancer Res. 65:6685-6691(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-561, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Possesses microtubule stabilizing properties. Involved in
CC regulating aneuploidy, cell cycling, and cell death in a p53-dependent
CC manner. {ECO:0000269|PubMed:15504249, ECO:0000269|PubMed:16061649}.
CC -!- SUBUNIT: Associates with alpha- and beta-tubulins.
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 (By
CC similarity). {ECO:0000250}.
CC -!- INDUCTION: By constitutively activated RET proteins. By p53/TP53.
CC {ECO:0000269|PubMed:15504249, ECO:0000269|PubMed:16061649}.
CC -!- SIMILARITY: Belongs to the CKAP2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28747.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY692438; AAU06608.1; -; mRNA.
DR EMBL; AK034534; BAC28747.1; ALT_INIT; mRNA.
DR EMBL; AK132463; BAE21180.1; -; mRNA.
DR EMBL; BC145666; AAI45667.1; -; mRNA.
DR EMBL; BC146023; AAI46024.1; -; mRNA.
DR CCDS; CCDS22170.1; -.
DR RefSeq; NP_001004140.2; NM_001004140.2.
DR AlphaFoldDB; Q3V1H1; -.
DR STRING; 10090.ENSMUSP00000039518; -.
DR iPTMnet; Q3V1H1; -.
DR PhosphoSitePlus; Q3V1H1; -.
DR EPD; Q3V1H1; -.
DR MaxQB; Q3V1H1; -.
DR PaxDb; Q3V1H1; -.
DR PeptideAtlas; Q3V1H1; -.
DR PRIDE; Q3V1H1; -.
DR ProteomicsDB; 279090; -.
DR Antibodypedia; 1993; 130 antibodies from 24 providers.
DR Ensembl; ENSMUST00000046916; ENSMUSP00000039518; ENSMUSG00000037725.
DR GeneID; 80986; -.
DR KEGG; mmu:80986; -.
DR UCSC; uc009lcs.2; mouse.
DR CTD; 26586; -.
DR MGI; MGI:1931797; Ckap2.
DR VEuPathDB; HostDB:ENSMUSG00000037725; -.
DR eggNOG; ENOG502RUSI; Eukaryota.
DR GeneTree; ENSGT00530000063691; -.
DR HOGENOM; CLU_026552_0_0_1; -.
DR InParanoid; Q3V1H1; -.
DR OMA; HHRNLLF; -.
DR OrthoDB; 417608at2759; -.
DR PhylomeDB; Q3V1H1; -.
DR TreeFam; TF333003; -.
DR BioGRID-ORCS; 80986; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Ckap2; mouse.
DR PRO; PR:Q3V1H1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3V1H1; protein.
DR Bgee; ENSMUSG00000037725; Expressed in secondary oocyte and 164 other tissues.
DR Genevisible; Q3V1H1; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
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:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO: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 Apoptosis; Cell cycle; Cytoplasm; Cytoskeleton; Microtubule;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..664
FT /note="Cytoskeleton-associated protein 2"
FT /id="PRO_0000245775"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..319
FT /note="Association with alpha- and beta-tubulin"
FT /evidence="ECO:0000269|PubMed:15504249"
FT REGION 254..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT MOD_RES 561
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT MOD_RES 579
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT CONFLICT 124
FT /note="A -> S (in Ref. 2; BAC28747)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="V -> A (in Ref. 1; AAU06608)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 664 AA; 74029 MW; 198278F62F5AE75E CRC64;
MAESRKRFLG RAARNPLPVT RDLQLPPTRR DQPAFREQRK QKLKEYLLIR KTVFPYKQEN
QISRDQKMIT SEDRVQEGKK VVKLKTEVAD KENIESTVEK NCIPLKAGEV TSSEIHNSKD
NVQAVQLLST RDDLPGQTVT LDPACHHKDN KKMQMTAEKP KQDSNVSKKR VLGYYHGQIV
QSKINSFRKL PSVKGESLTT TKKLPTTVSK AMKAQSEPAN TVSVKASTTA AATKFADAKP
VSTASKDTLV RPPIRSLHSS SHGAAKQGLS RPLANVTVRK GMLDKESHRS EPVVSVVKAG
SSQAPSRSIA SKDAARTDSS NTRLMVKPKD TDQRRYTIAG ASVHRSAQLK DTTAERKAQM
TEWRTGKGKG LKRPPHSVVT QAEPKGQSEN PVGSFWTTMA EEDEQRLFTE KVNKTISECL
NLINEGCPKE EILATLNDLI HNIPDAKKLV KYWICLVRIE PITSPIENII SIYEKAILAG
AQPIEEMRHI IIDILTTKSQ EKVNLGENIE EAHATKEPIQ EVNADANVGS GKPGEENEHH
GKVEVYEDDQ DNKIKDPDLT TPDSKTEAGC IIRYNVSSTP RLQSMKKMQH DKNSTLKELK
FLTPVRRSRR IQDKTSRLPA MLKDHDPSVS SLEQLSELGG DAFVCRPNAA LCPLFFETDV
AEEE
