CK5P2_RAT
ID CK5P2_RAT Reviewed; 1903 AA.
AC Q9JLH5; K7QQW0;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=CDK5 regulatory subunit-associated protein 2;
DE AltName: Full=CDK5 activator-binding protein C48;
GN Name=Cdk5rap2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Brown Norway;
RA Park J.S.Y., Lee M.-K.R., Jin Y., Fu S.-B., Rosales J.L., Lee K.-Y.;
RT "Human and rat express full length and alternatively spliced variant 1 of
RT cdk5rap2.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1686-1903, INTERACTION WITH CDK5R1, AND
RP PHOSPHORYLATION.
RC TISSUE=Brain;
RX PubMed=10721722; DOI=10.1016/s0378-1119(99)00499-0;
RA Ching Y.-P., Qi Z., Wang J.H.;
RT "Cloning of three novel neuronal Cdk5 activator binding proteins.";
RL Gene 242:285-294(2000).
RN [3]
RP LACK OF INTERACTION WITH MAPRE1.
RX PubMed=19553473; DOI=10.1091/mbc.e09-01-0009;
RA Fong K.W., Hau S.Y., Kho Y.S., Jia Y., He L., Qi R.Z.;
RT "Interaction of CDK5RAP2 with EB1 to track growing microtubule tips and to
RT regulate microtubule dynamics.";
RL Mol. Biol. Cell 20:3660-3670(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485; THR-1193; SER-1241;
RP SER-1495; SER-1673 AND SER-1676, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Required for the recruitment of AKAP9
CC to centrosomes (By similarity). Plays a role in neurogenesis. Contrary
CC to higher mammalian orthologs, including human, chimpanzee, bovine and
CC dog, does not interact with EB1/MAPRE1, therefore its function in the
CC regulation of microtubule dynamics is unclear (By similarity).
CC {ECO:0000250|UniProtKB:Q8K389, ECO:0000250|UniProtKB:Q96SN8}.
CC -!- SUBUNIT: Interacts with CDK5R1 (p35 form) (PubMed:10721722). CDK5RAP1,
CC CDK5RAP2 and CDK5RAP3 show competitive binding to CDK5R1. May form a
CC complex with CDK5R1 and CDK5. Interacts (via C-terminus) with PCNT; the
CC interaction is leading to centrosomal localization of CDK5RAP2 and PCNT
CC (By similarity). Interacts with AKAP9; the interaction is leading to
CC Golgi localization of CDK5RAP2 and AKAP9. Interacts with TUBG1; the
CC interaction is leading to the centrosomal localization of CDK5RAP2 and
CC TUBG1. Interacts with TUBGCP3. Interacts with CALM1. Interacts with
CC CDC20. Interacts with CEP68; degradation of CEP68 in early mitosis
CC leads to removal of CDK5RAP2 from the centrosome which promotes
CC centriole disengagement and subsequent centriole separation. Interacts
CC with NCKAP5L. Interacts with LGALS3BP; this interaction may connect the
CC pericentrosomal complex to the gamma-tubulin ring complex (gamma-TuRC)
CC to promote microtubule assembly and acetylation (By similarity).
CC Contrary to human, chimpanzee, bovine and dog orthologous proteins,
CC does not interact with EB1/MAPRE1, possibly due to a divergence at the
CC level of the critical residue 939, which is a proline in MAPRE1-binding
CC orthologs and a leucine in mouse and rat (Probable).
CC {ECO:0000250|UniProtKB:Q8K389, ECO:0000250|UniProtKB:Q96SN8,
CC ECO:0000269|PubMed:10721722, ECO:0000305|PubMed:19553473}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q8K389}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q96SN8}. Cytoplasm
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. Localization to centrosomes versus Golgi
CC apparatus may be cell type-dependent. Due to the probable lack of
CC interaction with EB1/MAPRE1, its localization to microtubule plus ends
CC may not be conserved in rats. {ECO:0000250|UniProtKB:Q96SN8,
CC ECO:0000305|PubMed:19553473}.
CC -!- PTM: Phosphorylated in vitro by CDK5. {ECO:0000269|PubMed:10721722}.
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DR EMBL; JX524852; AFV70628.1; -; mRNA.
DR EMBL; AF177478; AAF60224.1; -; mRNA.
DR AlphaFoldDB; Q9JLH5; -.
DR SMR; Q9JLH5; -.
DR IntAct; Q9JLH5; 2.
DR STRING; 10116.ENSRNOP00000007710; -.
DR iPTMnet; Q9JLH5; -.
DR PhosphoSitePlus; Q9JLH5; -.
DR PaxDb; Q9JLH5; -.
DR PeptideAtlas; Q9JLH5; -.
DR PRIDE; Q9JLH5; -.
DR Ensembl; ENSRNOT00000007710; ENSRNOP00000007710; ENSRNOG00000005788.
DR UCSC; RGD:708451; rat.
DR RGD; 708451; Cdk5rap2.
DR eggNOG; ENOG502QTI7; Eukaryota.
DR GeneTree; ENSGT00950000183190; -.
DR InParanoid; Q9JLH5; -.
DR PhylomeDB; Q9JLH5; -.
DR PRO; PR:Q9JLH5; -.
DR Proteomes; UP000002494; Chromosome 5.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000931; C:gamma-tubulin large complex; IEA:Ensembl.
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:0097431; C:mitotic spindle pole; ISO:RGD.
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:0043015; F:gamma-tubulin binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; ISO:RGD.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0007099; P:centriole replication; ISO:RGD.
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:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:RGD.
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 1: Evidence at protein level;
KW Calmodulin-binding; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1903
FT /note="CDK5 regulatory subunit-associated protein 2"
FT /id="PRO_0000089838"
FT REGION 244..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1736..1903
FT /note="Required for centrosomal attachment, Golgi
FT localization and CALM1 interaction"
FT /evidence="ECO:0000250"
FT REGION 1736..1778
FT /note="Interaction with CDK5R1"
FT /evidence="ECO:0000269|PubMed:10721722"
FT REGION 1871..1880
FT /note="Required for centrosomal attachment, Golgi
FT localization and CALM1 interaction"
FT /evidence="ECO:0000250"
FT REGION 1883..1903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
FT MOD_RES 1193
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K389"
FT MOD_RES 1495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1903
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
SQ SEQUENCE 1903 AA; 215482 MW; 770918B8FFD50B84 CRC64;
MMDSGMEEDV TLPGTLSGCS GLHPVLPSDL DVISDTTGLG NGVLPIMSEE KVSPTRARNM
KDFENQITEL KKENFNLKLR IYFLEERIQQ EFAGPTEHIY KKNIELKVEV ESLKRELQER
DQLLVKASKA VESLAEGGGS EIQRVKEDAR KKVQQVEELL TKRIHLLEED VKAAQAELEK
AFAGTETEKA LRLSLESKLS AMKKMQEGDL EMTLALEEKD RLIEELKLSL KSKEALIQCL
KEEKSQMASP DENVSSGELR GLSATLREEK ERDAEERQKE RNHFEERIQA LQEDLREKER
EIATEKKNSL KRDKAIQGLT MALKSKEKEV EELNSIIKEL TADSTQSREA PLKTQVSEFE
VRESENCEAA LAEKEALLAK LHSENVTKNT ENHRLLRNVK KVTQELNDLK KEKLRLERDL
EEAHREGNRG ARTIHDLRNE VEKLRKEVCE REKAVEKHYK SLPGESSSKF HSQEQVVKGL
TESASQEDLL LQKSNEKDLE AIQQNCYLMT AEELKFGSDG LITEKCSQQS PDSKLIFSKE
KQQSEYEGLT GDLKTEQNVY AHLAKNLQDT DSKLQAELKR VLALRKQLEQ DVLAYRNLQT
ALQEQLSEIR KREEEPFSFY SDQTSYLSIC LEEHSQFQLE HFSQEEIKKK VIDLIQLVKD
LHADNQHLKK TIFDISCMGV QGNDRLESTK QAELMASKAD EDTLKFKADD ENHFQSDQHL
EQSREIMEDY AEGGGKDGYV RHMDSNILDH DGAHTPDTSE DHSLEDELLS LLATFFSKKA
TPSLESRPDL LKALGALLLE RICLAEQGSP GDHSDSKAEK ALEQVAVRLR DELGHSCLAN
SFSKSHSELK SPRGTWLVKT GDEAKVELKS VSVQTMTIED STRGFKPERK REAWAGKPEE
AVFSTELESE ALGEMPGLQA THLSFPSAID KDDQKTGLLI QLKTPELLEN LYNLPASQEV
VAQLQGQVLE LQKELKEYKI RNKQLLDKLI LAEAMMEGMA VPNSTPVNVP AAQAVVRTAF
QGKPGEQEGH ETTHSAGRDK EVDSDQYTSF EIDSEICPPD DLALLPACKE NLEDFLGPPS
IATYLDSKSQ LSVKVSVVGT DQSENINLPD DTEALKQKIH DLQTELEGYR NIIVQLQKHS
QCSEAIITVL CGTEGAQDGL NKPKGHIDEE EMTFSSLHQV RYVKHMKILR PLTPEIIDGK
MLESLKQQLV EQEQELQKEQ DLNLELFGEI HNLQNKFRDL SPSRYDSLVQ SQARELSLQR
QQIKDSHDIC VVCHQHMSTM IKAFEELLQA SDVDSCVAEG FREQLTQCAG LLEQLEKLFL
HGKSARVEPH TQTELLRRLR TEEDNLPYQH LLPESPEPSA SHALSDDEMS EKSFLSREPK
PDSETEKYPT IASRFPQDLL MEHIQEIRTL RKHLEESIKT NEKLRKQLER QGCETDQGST
NVSAYSSELH NSLTSEIQFL RKQNEALSTM LEKGSKEKQK ENEKLRESLA RKTESLEHLQ
LEYASVREEN ERLRRDISEK ERQNQQLTQE VCSSLQELSR VQEEAKSRQQ LLLQKDELLQ
SLQMELKVYE KLAEEHQKLQ QESRGEACGG GQKGQDPFSN LHGLLKEIQV LRDQAERSIQ
TNNTLKSKLE KQLSQGSKQA QEGALTLAVQ ALSVTEWSLQ LDKHDVNKCP EASDNSFDLF
ESTQAMAPKS ASETPVLSGT DVDSLSCDST SSATSPSCMP CLVAGRHLWA SKSGHHMLCL
IEDYDALYKQ ISWGQTLLAK MDIQTQEALS PTSQKLGPKA SFSVPLSKFL SSMNTAKLIL
EKASRLLKLF WRVSVPTNGQ CSLHCDQIGE MKAEITKLHK KLFEQEKKLQ NTAKLLQQSK
HQEKIIFDQL VITHQVLRKA RGNLELRPRA AHPGTSSPSR PGS
