ID   CKAP2_BOVIN             Reviewed;         625 AA.
AC   A5D7U0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Cytoskeleton-associated protein 2;
GN   Name=CKAP2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal lung;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CKAP2 family. {ECO:0000305}.
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DR   EMBL; BC140680; AAI40681.1; -; mRNA.
DR   RefSeq; NP_001091501.1; NM_001098032.2.
DR   AlphaFoldDB; A5D7U0; -.
DR   SMR; A5D7U0; -.
DR   STRING; 9913.ENSBTAP00000051947; -.
DR   PaxDb; A5D7U0; -.
DR   PRIDE; A5D7U0; -.
DR   GeneID; 515249; -.
DR   KEGG; bta:515249; -.
DR   CTD; 26586; -.
DR   eggNOG; ENOG502RUSI; Eukaryota.
DR   InParanoid; A5D7U0; -.
DR   OrthoDB; 417608at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR   InterPro; IPR029197; CKAP2_C.
DR   InterPro; IPR026165; CKAP2_fam.
DR   PANTHER; PTHR16076; PTHR16076; 2.
DR   Pfam; PF15297; CKAP2_C; 2.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cell cycle; Cytoplasm; Cytoskeleton; Microtubule;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..625
FT                   /note="Cytoskeleton-associated protein 2"
FT                   /id="PRO_0000324337"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..521
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..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..514
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         190
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         518
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         521
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         534
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         535
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         536
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         538
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         541
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
SQ   SEQUENCE   625 AA;  70085 MW;  C4703197377351E9 CRC64;
     MSTPAIPQDL QLNPSQRTQS AFREQRRQKL KEHLLKRKTS FACKQENQML LSDGDQRVRT
     SEGQIQEGKK VLKIKTEMAD KENVGRPTGI KNNLTVEKNC IPLKPSNELT NSTLATDPPN
     SEDNNQTLPL LPVKDDPQSQ HRTLSQTFHL KNNSKKKPVI TEKPKHDANV PKKPVLGAYR
     GQIVQSKINS FRKPLQVKDE SSATTKKLPA TVSKATKPQP GDVSSITVKS DRASHMTSTT
     KFASTTSQIR HLVRPPIRSQ HNKAQDAMKP GNSRMSANVT VQKGPREKEL NTVLSGIKTS
     SSQDIKGDKT LSKSMAAGMV VRPASSSNTK LIEKSKSAGQ RSHTTVKAAV DSRWTQPKET
     AEERKARLSE WKAGKGRILK RPPSSAVTRP EPETQNEQPV GSFWTTMAEE DEQRLFTEKV
     NKTFSECLNL INEPIEEMRH TIVDILTRKS QEKLKFGENI EETSAAEEKI QEAHTDDTGV
     DLESGKLEME NNPPRNVFQD CEKEQDDKVK DPTSDVKTPS TNTRAGCLIK YNVSTTPYLQ
     SVKKKMQFDE TNSAYKELKF LTPVRRSRRL QEKTSKLPDM LKDHYPCVSS LEQLTELGCE
     TDAFVCRPNT ALCGMFSEPD PTEEE