CK5P2_MACFA
ID CK5P2_MACFA Reviewed; 862 AA.
AC Q9BE52;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=CDK5 regulatory subunit-associated protein 2;
DE AltName: Full=CDK5 activator-binding protein C48;
GN Name=CDK5RAP2; ORFNames=QflA-15432;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Potential regulator of CDK5 activity via its interaction with
CC CDK5R1. Negative regulator of centriole disengagement (licensing) which
CC maintains centriole engagement and cohesion. Involved in regulation of
CC mitotic spindle orientation (By similarity). Plays a role in the
CC spindle checkpoint activation by acting as a transcriptional regulator
CC of both BUBR1 and MAD2 promoter. Together with EB1/MAPRE1, may promote
CC microtubule polymerization, bundle formation, growth and dynamics at
CC the plus ends. Regulates centrosomal maturation by recruitment of the
CC gamma-tubulin ring complex (gamma-TuRC) onto centrosomes (By
CC similarity). In complex with PDE4DIP, MAPRE1 and AKAP9, contributes to
CC microtubules nucleation and extension from the centrosome to the cell
CC periphery. Required for the recruitment of AKAP9 to centrosomes (By
CC similarity). Plays a role in neurogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q8K389, ECO:0000250|UniProtKB:Q96SN8}.
CC -!- SUBUNIT: Interacts with CDK5R1 (p35 form). CDK5RAP1, CDK5RAP2 and
CC CDK5RAP3 show competitive binding to CDK5R1. May form a complex with
CC CDK5R1 and CDK5 (By similarity). Interacts with pericentrin/PCNT; the
CC interaction is leading to centrosomal and Golgi localization of
CC CDK5RAP2 and PCNT. Interacts with AKAP9; the interaction targets
CC CDK5RAP2 and AKAP9 to Golgi apparatus. Interacts with MAPRE1; the
CC interaction is direct and targets CDK5RAP2 and EB1/MAPRE1 to
CC microtubule plus ends. Interacts with TUBG1; the interaction is leading
CC to the centrosomal localization of CDK5RAP2 and TUBG1. Interacts with
CC TUBGCP3. Interacts with CALM1. Interacts with CDC20. Interacts with
CC CEP68; degradation of CEP68 in early mitosis leads to removal of
CC CDK5RAP2 from the centrosome which promotes centriole disengagement and
CC subsequent centriole separation. Interacts with NCKAP5L. Forms a
CC pericentrosomal complex with AKAP9, MAPRE1 and PDE4DIP; within this
CC complex, MAPRE1 binding to CDK5RAP2 may be mediated by PDE4DIP.
CC Interaction with PDE4DIP is PDE4DIP isoform-specific. Interacts with
CC LGALS3BP; this interaction may connect the pericentrosomal complex to
CC the gamma-tubulin ring complex (gamma-TuRC) to promote microtubule
CC assembly and acetylation (By similarity).
CC {ECO:0000250|UniProtKB:Q96SN8, ECO:0000250|UniProtKB:Q9JLH5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q96SN8}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q96SN8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96SN8}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q96SN8}. Note=Found in the pericentriolar region
CC adhering to the surface of the centrosome and in the region of the
CC centrosomal appendages. Localizes to microtubule plus ends in the
CC presence of EB1/MAPRE1. Localization to centrosomes versus Golgi
CC apparatus may be cell type-dependent. {ECO:0000250|UniProtKB:Q96SN8}.
CC -!- PTM: Phosphorylated in vitro by CDK5. {ECO:0000250|UniProtKB:Q9JLH5}.
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DR EMBL; AB056817; BAB39343.1; -; mRNA.
DR AlphaFoldDB; Q9BE52; -.
DR SMR; Q9BE52; -.
DR STRING; 9541.XP_005580988.1; -.
DR eggNOG; ENOG502QTI7; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0000242; C:pericentriolar material; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
DR GO; GO:0046600; P:negative regulation of centriole replication; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR InterPro; IPR042791; CDK5RAP2.
DR InterPro; IPR012943; Cnn_1N.
DR PANTHER; PTHR46930; PTHR46930; 2.
DR Pfam; PF07989; Cnn_1N; 1.
PE 2: Evidence at transcript level;
KW Calmodulin-binding; Cytoplasm; Cytoskeleton; Golgi apparatus; Microtubule;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..862
FT /note="CDK5 regulatory subunit-associated protein 2"
FT /id="PRO_0000089836"
FT REGION 58..196
FT /note="Interaction with NCKAP5L"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
FT REGION 830..839
FT /note="Required for centrosomal attachment, Golgi
FT localization and CALM1 interaction"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
SQ SEQUENCE 862 AA; 99105 MW; D6BC4FD33473DDA2 CRC64;
MMDSVLEEDV TLLGTLSGCS GLVPNVPDDL DGINPDARLG NGVLSNVSEE TVSPTRARNM
KDFENQITEL KKENFNLKLR IYFLEERMQQ EFHGPAEHIY KTNIELKVEV ESLKRELQER
ERLLIRASKA VESLAEAGGS EIQRVKEDAR KKVQQVEDLL TKRILLLEKD VKAAQAELEK
AFAGTETEKA LRLSLESKLS EMKKMHKGDL AMALVLDEKD RLIEELKLSL KSKEALIQCL
KEEKSQMASP DENVSSGELR GLCAAPREEK ERETEAAQME HQKERNSFEE RIQALEEDLR
EKEREIATEK KNSLKRDKAI QGLTMALKSK EKKVEELNSE IEKLSAAFAK AREALQKAQT
QEFQGSENYE AALSGKEALL TELRSQNLTK SAENHRLRRS IKKITQELSD LQQERERLEK
DLEEAHREKS RGDCTIRDLR NEVEKLRNEV NERKKAMENR YKNLLSESSK KLHNQEQVIK
HLTERTNHKD MLLQKFNEKD LEVIQQNHYL MTAEDLELRS EGLITEKCPS QQSPGSKTIF
SKEEKQSSDY QELIQVLKKE QDIYTHLVKS LQESDSINNL QAELNNIFAL RKQLERDVLS
YQNLRRTLEE QISEIRRREE ESFSFYSDQT SYLSICLEEN NRFQVEHFSQ EELKKKVSDL
IQLVKELYTD DQHLKKTIFD LSCMGFQGNG FPDRLVSTEQ TEIMKDLSKG GCKNGYLRHT
EPKILESDGA HTPGCLEEGV FINLLAPLFN EKATLLLESR PDLLKVVREL LLGHLCLAEQ
DVSGEHLGGK TEKTPKLHKK LFEQEKKLQN TMKLLQLSKR QEKVIFDQLV VTHKILRKAR
GNLELRPGGA HPGTCSPSRP GS
