CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019643
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 CDK5 regulatory subunit-associated protein 2 
Protein Synonyms/Alias
 CDK5 activator-binding protein C48; Centrosome-associated protein 215 
Gene Name
 CDK5RAP2 
Gene Synonyms/Alias
 CEP215; KIAA1633 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
78KKENFNLKLRIYFLEubiquitination[1]
129QLLIKASKAVESLAEubiquitination[1]
480HNQEQVIKHLTESTNubiquitination[1]
489LTESTNQKDVLLQKFubiquitination[1]
495QKDVLLQKFNEKDLEubiquitination[1]
527SEGLITEKCSSQQPPubiquitination[1]
537SQQPPGSKTIFSKEKubiquitination[1]
542GSKTIFSKEKKQSSDubiquitination[1]
544KTIFSKEKKQSSDYEubiquitination[1]
558EELIQVLKKEQDIYTubiquitination[1]
559ELIQVLKKEQDIYTHubiquitination[1]
569DIYTHLVKSLQESDSubiquitination[1]
586NLQAELNKIFALRKQubiquitination[1]
592NKIFALRKQLEQDVLubiquitination[1]
606LSYQNLRKTLEEQISubiquitination[1]
655FSQEELKKKVSDLIQubiquitination[1]
656SQEELKKKVSDLIQLubiquitination[1]
665SDLIQLVKELYTDNQubiquitination[1]
675YTDNQHLKKTIFDLSubiquitination[1]
676TDNQHLKKTIFDLSCubiquitination[1]
705TEQTEIMKDLSKGGCubiquitination[1]
713DLSKGGCKNGYLRHTubiquitination[1]
723YLRHTESKISDCDGAubiquitination[1]
765ESRPDLLKVVRELLLubiquitination[1]
796GKTEKTPKQKGELVHubiquitination[1]
798TEKTPKQKGELVHFVubiquitination[1]
827SCEAQLVKAGEVPKVubiquitination[1]
837EVPKVGLKDASVQTVubiquitination[1]
911SRLPILIKPSRSLGNubiquitination[1]
972EGRPTPDKTLLNAQPubiquitination[1]
996PGEQKGIKTTSSVWRubiquitination[1]
1053VATYLSSKSQPSAKVubiquitination[1]
1059SKSQPSAKVSVMGTDubiquitination[1]
1081SNETEYLKQKIHDLEubiquitination[1]
1083ETEYLKQKIHDLETEubiquitination[1]
1127GAQDGLSKPKNGSDGubiquitination[1]
1129QDGLSKPKNGSDGEEubiquitination[1]
1152VRYVKHVKILGPLAPubiquitination[1]
1171SRVLENLKQQLEEQEubiquitination[1]
1180QLEEQEYKLQKEQNLubiquitination[1]
1183EQEYKLQKEQNLNMQubiquitination[1]
1201EIHNLQNKFRDLSPPubiquitination[1]
1229SLQRQQIKDGHGICVubiquitination[1]
1288EKLFLNGKSVGVEMNubiquitination[1]
1425SEIHFLRKQNQALNAubiquitination[1]
1455LRESLSRKTVSLEHLubiquitination[1]
1509SRVQEEVKLRQQLLSubiquitination[1]
1530QSLRVELKAYEKLDEubiquitination[1]
1534VELKAYEKLDEEHRRubiquitination[1]
1588STLQSRLKEQLARGAubiquitination[1]
1690GHHLWASKNGRHVLGubiquitination[1]
1737TSQELGTKGPHPAPLubiquitination[1]
1766EEAYRRLKLLWRVSLubiquitination[1]
1833DQLVVTHKILRKARGubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
Functional Description
 Potential regulator of CDK5 activity via its interaction with CDK5R1. Negative regulator of centriole disengagement (licensing) which maintains centriole engagement and cohesion. Involved in regulation of mitotic spindle orientation (By similarity). Plays a role in the spindle checkpoint activation by acting as a transcriptional regulator of both BUBR1 and MAD2 promoter. Together with MAPRE1, it may promote microtubule polymerization, bundle formation, growth and dynamics at the plus ends. 
Sequence Annotation
 REGION 926 1208 Interaction with MAPRE1.
 REGION 1726 1893 Interaction with PCNT and AKAP9.
 REGION 1726 1768 Interaction with CDK5R1 (By similarity).
 REGION 1861 1870 Required for centrosomal attachment,
 MOD_RES 547 547 Phosphoserine.
 MOD_RES 1001 1001 Phosphothreonine.
 MOD_RES 1238 1238 Phosphoserine.
 MOD_RES 1893 1893 Phosphoserine.  
Keyword
 Alternative splicing; Calmodulin-binding; Complete proteome; Cytoplasm; Cytoskeleton; Golgi apparatus; Microtubule; Phosphoprotein; Polymorphism; Primary microcephaly; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1893 AA 
Protein Sequence
MMDLVLEEDV TVPGTLSGCS GLVPSVPDDL DGINPNAGLG NGLLPNVSEE TVSPTRARNM 60
KDFENQITEL KKENFNLKLR IYFLEERMQQ EFHGPTEHIY KTNIELKVEV ESLKRELQER 120
EQLLIKASKA VESLAEAGGS EIQRVKEDAR KKVQQVEDLL TKRILLLEKD VTAAQAELEK 180
AFAGTETEKA LRLRLESKLS EMKKMHEGDL AMALVLDEKD RLIEELKLSL KSKEALIQCL 240
KEEKSQMACP DENVSSGELR GLCAAPREEK ERETEAAQME HQKERNSFEE RIQALEEDLR 300
EKEREIATEK KNSLKRDKAI QGLTMALKSK EKKVEELNSE IEKLSAAFAK AREALQKAQT 360
QEFQGSEDYE TALSGKEALS AALRSQNLTK STENHRLRRS IKKITQELSD LQQERERLEK 420
DLEEAHREKS KGDCTIRDLR NEVEKLRNEV NEREKAMENR YKSLLSESNK KLHNQEQVIK 480
HLTESTNQKD VLLQKFNEKD LEVIQQNCYL MAAEDLELRS EGLITEKCSS QQPPGSKTIF 540
SKEKKQSSDY EELIQVLKKE QDIYTHLVKS LQESDSINNL QAELNKIFAL RKQLEQDVLS 600
YQNLRKTLEE QISEIRRREE ESFSLYSDQT SYLSICLEEN NRFQVEHFSQ EELKKKVSDL 660
IQLVKELYTD NQHLKKTIFD LSCMGFQGNG FPDRLASTEQ TEIMKDLSKG GCKNGYLRHT 720
ESKISDCDGA HAPGCLEEGA FINLLAPLFN EKATLLLESR PDLLKVVREL LLGQLFLTEQ 780
EVSGEHLDGK TEKTPKQKGE LVHFVQTNSF SKPHDELKLS CEAQLVKAGE VPKVGLKDAS 840
VQTVATEGDL LRFKHEATRE AWEEKPINTA LSAEHRPENL HGVPGWQAAL LSLPGITNRE 900
AKKSRLPILI KPSRSLGNMY RLPATQEVVT QLQSQILELQ GELKEFKTCN KQLHQKLILA 960
EAVMEGRPTP DKTLLNAQPP VGAAYQDSPG EQKGIKTTSS VWRDKEMDSD QQRSYEIDSE 1020
ICPPDDLASL PSCKENPEDV LSPTSVATYL SSKSQPSAKV SVMGTDQSES INTSNETEYL 1080
KQKIHDLETE LEGYQNFIFQ LQKHSQCSEA IITVLCGTEG AQDGLSKPKN GSDGEEMTFS 1140
SLHQVRYVKH VKILGPLAPE MIDSRVLENL KQQLEEQEYK LQKEQNLNMQ LFSEIHNLQN 1200
KFRDLSPPRY DSLVQSQARE LSLQRQQIKD GHGICVISRQ HMNTMIKAFE ELLQASDVDY 1260
CVAEGFQEQL NQCAELLEKL EKLFLNGKSV GVEMNTQNEL MERIEEDNLT YQHLLPESPE 1320
PSASHALSDY ETSEKSFFSR DQKQDNETEK TSVMVNSFSQ DLLMEHIQEI RTLRKRLEES 1380
IKTNEKLRKQ LERQGSEFVQ GSTSIFASGS ELHSSLTSEI HFLRKQNQAL NAMLIKGSRD 1440
KQKENDKLRE SLSRKTVSLE HLQREYASVK EENERLQKEG SEKERHNQQL IQEVRCSGQE 1500
LSRVQEEVKL RQQLLSQNDK LLQSLRVELK AYEKLDEEHR RLREASGEGW KGQDPFRDLH 1560
SLLMEIQALR LQLERSIETS STLQSRLKEQ LARGAEKAQE GALTLAVQAV SIPEVPLQPD 1620
KHDGDKYPME SDNSFDLFDS SQAVTPKSVS ETPPLSGNDT DSLSCDSGSS ATSTPCVSRL 1680
VTGHHLWASK NGRHVLGLIE DYEALLKQIS QGQRLLAEMD IQTQEAPSST SQELGTKGPH 1740
PAPLSKFVSS VSTAKLTLEE AYRRLKLLWR VSLPEDGQCP LHCEQIGEMK AEVTKLHKKL 1800
FEQEKKLQNT MKLLQLSKRQ EKVIFDQLVV THKILRKARG NLELRPGGAH PGTCSPSRPG 1860
S 1861 
Gene Ontology
 GO:0030054; C:cell junction; IDA:HPA.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0000242; C:pericentriolar material; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0000922; C:spindle pole; IDA:UniProtKB.
 GO:0008017; F:microtubule binding; IDA:UniProtKB.
 GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
 GO:0007420; P:brain development; ISS:UniProtKB.
 GO:0051297; P:centrosome organization; IMP:UniProtKB.
 GO:0007059; P:chromosome segregation; IMP:UniProtKB.
 GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0001578; P:microtubule bundle formation; IDA:UniProtKB.
 GO:0046600; P:negative regulation of centriole replication; ISS:UniProtKB.
 GO:0045665; P:negative regulation of neuron differentiation; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0045664; P:regulation of neuron differentiation; NAS:UniProtKB.
 GO:0090231; P:regulation of spindle checkpoint; IDA:UniProtKB. 
Interpro
 IPR012943; Spindle_assoc. 
Pfam
 PF07989; Microtub_assoc 
SMART
  
PROSITE
  
PRINTS