ID   CKAP2_PONAB             Reviewed;         682 AA.
AC   Q5R7F8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Cytoskeleton-associated protein 2;
GN   Name=CKAP2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR860160; CAH92302.1; -; mRNA.
DR   RefSeq; NP_001126347.1; NM_001132875.1.
DR   AlphaFoldDB; Q5R7F8; -.
DR   STRING; 9601.ENSPPYP00000006141; -.
DR   PRIDE; Q5R7F8; -.
DR   GeneID; 100173328; -.
DR   KEGG; pon:100173328; -.
DR   CTD; 26586; -.
DR   eggNOG; ENOG502RUSI; Eukaryota.
DR   InParanoid; Q5R7F8; -.
DR   OrthoDB; 417608at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR029197; CKAP2_C.
DR   InterPro; IPR026165; CKAP2_fam.
DR   PANTHER; PTHR16076; PTHR16076; 1.
DR   Pfam; PF15297; CKAP2_C; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cell cycle; Cytoplasm; Cytoskeleton; Microtubule;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..682
FT                   /note="Cytoskeleton-associated protein 2"
FT                   /id="PRO_0000324338"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          152..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..581
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        154..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..350
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..379
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..578
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         533
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         578
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         581
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         594
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         595
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         596
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         598
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
FT   MOD_RES         601
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWK9"
SQ   SEQUENCE   682 AA;  76840 MW;  0367FD7639ADADB9 CRC64;
     MSTPAVPQDL QLPPSQRAQS AFKEQRRQKL KEHLLRRKTL FAYKQENEVL SSRGQRVVTS
     EDQVQEGTKA LKLKTKMADK ENMKRPAESK NNTVVGKHCI PLKPSNELTN STVVIDTHKP
     KDSNQTPHLL LTEDDPQSQH MTLSQAFHLK NNSKKKQMTT EKQKQDANMP KKPVLGSYRG
     QIVQSKINSF RKPLQVKDES SAATKKLSAT IPKATKPQPV NTSNATVKSN RSSNMTATTK
     FVSTTSQNTQ LVRPPIRSHH SNTQDTVKQG ISRTSANVTI RKGPREKELL QSKTALSSVK
     TSSSQGIIRN KTLSRCIASE VVARPASLSN DKLTEKSEPV DQRRHTAGKA SVDSRSAQPK
     ETSEERKARL NEWKAGKGRV LKRPPNSVVT QHEPEGQNEK PVGSFWTTMA EEDEQRLFTE
     KVNNTFSECL NLINEGCPKG DILITLNDLI KNIPDAKKLV KYWICLALIE PITSPIENII
     AIYEKAILAG AQPIEEMRHT IVDILTMKSQ EKANLGENME KSCASKEEVK EVSIEDTGVD
     VDPEKLEMES KHHRNLLFQD CEKEQDNKTK DPTHDVKTPN TETRTSCLIK YNVSTTPYLQ
     SVKKKVQFDE TNSAFKELKF LTPVRRSRRL QEKTSKLPDM LKDHYPCVSS LEQLTELGRE
     TDAFVCRPNA ALCRVYYEAD TT