CK5P2_PANTR
ID CK5P2_PANTR Reviewed; 1893 AA.
AC Q19UN5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 29-SEP-2021, entry version 66.
DE RecName: Full=CDK5 regulatory subunit-associated protein 2;
GN Name=CDK5RAP2;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16631324; DOI=10.1016/j.gene.2006.02.019;
RA Evans P.D., Vallender E.J., Lahn B.T.;
RT "Molecular evolution of the brain size regulator genes CDK5RAP2 and
RT CENPJ.";
RL Gene 375:75-79(2006).
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; DQ430802; ABF83588.1; -; mRNA.
DR RefSeq; NP_001035901.1; NM_001042436.1.
DR STRING; 9598.ENSPTRP00000054333; -.
DR PaxDb; Q19UN5; -.
DR PRIDE; Q19UN5; -.
DR GeneID; 464695; -.
DR KEGG; ptr:464695; -.
DR CTD; 55755; -.
DR eggNOG; ENOG502QTI7; Eukaryota.
DR InParanoid; Q19UN5; -.
DR OrthoDB; 1046642at2759; -.
DR Proteomes; UP000002277; 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: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; IPR012943; Cnn_1N.
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..1893
FT /note="CDK5 regulatory subunit-associated protein 2"
FT /id="PRO_0000251160"
FT REGION 58..196
FT /note="Interaction with NCKAP5L"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
FT REGION 926..1208
FT /note="Interaction with MAPRE1"
FT /evidence="ECO:0000250"
FT REGION 1002..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1893
FT /note="Interaction with PCNT and AKAP9"
FT /evidence="ECO:0000250"
FT REGION 1343..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1651..1701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1726..1768
FT /note="Interaction with CDK5R1"
FT /evidence="ECO:0000250"
FT REGION 1752..1774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1861..1870
FT /note="Required for centrosomal attachment, Golgi
FT localization and CALM1 interaction"
FT /evidence="ECO:0000250"
FT REGION 1874..1893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1666..1701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1752..1768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
FT MOD_RES 1001
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
FT MOD_RES 1238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
FT MOD_RES 1490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
FT MOD_RES 1663
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLH5"
FT MOD_RES 1666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLH5"
FT MOD_RES 1893
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
SQ SEQUENCE 1893 AA; 214938 MW; E582AE1A3228BE17 CRC64;
MMDSVLEEDV TVPGTLSGCS GLVPSVPDDL DGINPNAGLG NGVLPNVSEE TVSPTRARNM
KDFENQITEL KKENFNLKLR IYFLEERMQQ EFHGPTEHIY KTNIELKVEV ESLKRELQER
EQLLIKASKA VESLAEAGGS EIQRVKEDAR KKVQQVEDLL TKRILLLEKD VTAAQAELEK
AFAGTETEKA LRLRLESKLS EMKKMHEGDL AMALVLDEKD RLIEELKLSL KSKEALIQCL
KEEKSQMASP DENVSSGELR GLCAAPREEK XRETEAAQME HQKERNSFEE RIQALEEDLR
EKEREIATEK KNSLKRDKAI QGLTMALKSK EKXVEELNSE IEKLXAAFAK AREALQKAQT
QEFQGSEDYE TALSGKEALS AALRSQNLTK STENHRLRRS IKKITQELSD LQQERERLEK
DLEEAHREKS KGDCTIRDLR NEVEKLRNEV NEREKAMENR YKSLLSESNK KLHNQEQVVK
HLTESTNQKD VLLQKFNEKD LEVIQQNHYL MAAEDLELRS ESLITEKCSS QQPPGSKTIF
SKEKKQSSDY EELIQVLKKE QDIYTHLVKS LQESDSINNL QAELNNIFAL RKQLEQDVLS
YQNLRKTLEE QISXIRRREE ESFSLYSDQT SYLSICLEEN NRFQVEHFSQ EELKKKVSDL
IQLVKELYTD NQHLKKTIFD LSCMGFQGNG FPDRLASTEQ TELLASKEDE DTIKIGEDDE
INFLSDEHLQ QSNEIMKDLS KGGCKNGYLR HTESKISDCD GAHAPGCLEE GAFINLLAPL
FNEKATLLLE SRPDLLKVVR ELLLGQLFLT EQEVSGEHLD GKTEKTPKQK GELVHFVQTN
SFSKPHDELK LSCEAQLVKA GEVPKVGLKD ASVQTVATEG DLLRFKHEAT REAWEEKPIN
TALSAEHRPE NLHGVPGWQA ALLSLPGVTN REAKKSRLPI LIKPSRSLGN MYRLPATQEV
VTQLQSQILE LQGELKEFKT CNKQLHQKLI LAEAVMEGRP TPDKTLLNAQ PPVGAAYQDS
PGEQKGIKTT SSVWRDKEMD SDQQTSYEID SEICPPDDLA SLPSCKENPE DVLSPTSVAT
YLSSKSQPSA KVSVMGTDQS ESINTSNETE YLKQKIHDLE TELEAYQNFI FQLQKHSQCS
EAIITVLCGT EGAQDGLSKP KSGSDGEEMT FSSLHQVRYV KHVKILGPLA PEMIDSRVLE
NLKQQLEEQE YKLQKEQNLN MQLFSEIHNL QNKFRDLSPP RYDSLVQSQA RELSLQRQQI
KDGHGICVIS RQHMNTMIKA FEELLQASDV DYCVAEGFQE QLNQCAELLE KLEKLFLNGK
SVGVEMNTQI ELMERIEEDN LTYQHLLPES PEPSASHALS DYETSEKSFF SQDQKQDNET
EKTSVMVNNF SQDLLMEHIQ EIRTLRKRLE ESIKTNEKLR KQLERQGSEF DQGSTNIFAS
GSELHSSLTS EIHFLRKQNQ ALNAMLIKGS RDKQKENDKL RESLSRKTVS LEHLQREYAS
VKEENERLQK EGSEKERHNQ QLIQEVRCSG QELSRVQEEV KLRQQLLSQN DKLLQSLRVE
LKAYEKLDEE HRRLREASGE GWKGQDPFRD LHSLLMEIQA LRLQLERSIE TSSTLQGRLE
EQLARGAEKA QEGALTLAVQ AVSIPEVPLQ LDKHDGDKYP MESDNSFDLF DSSQAVTPKS
VSETPPLSGN DTDSLSCDSG SSATSTPCVS RLVTGHHLWA SKNGRHVLGL IEDYEALLKQ
ISQGQRLLAE MDVQTQEAPS STSQELGTKG PHPAPLSKFV SSVSTAKLTL EEAYRRLKLL
WRVSLPEDGQ CPLHCEQIGE MKAEVTKLHK KLFEQEKKLQ NTMKLLQLSK RQEKVIFDQL
VVTHKILRKA RGNLELRPGG SHPGTCSPSR PGS
