CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019644
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
489LTESTNQKDVLLQKFubiquitination[1]
1162SRVLENLKQQLEEQEubiquitination[1]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
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 TELLASKEDE DTIKIGEDDE 720
INFLSDQHLQ QSNEIMKDLS KGGCKNGYLR HTESKISDCD GAHAPGCLEE GAFINLLAPL 780
FNEKATLLLE SRPDLLKVVR ELLLGQLFLT EQEVSGEHLD GKTEKTPKQK GELVHFVQTN 840
SFSKPHDELK LSCEAQLVKA GEVPKVGLKD ASVQTVATEG DLLRFKHEAT REAWEEKPIN 900
TALSAEHRPE NLHGVPGWQA ALLSLPGITN REAKKSRLPI LIKPSRSLGN MYRLPATQEV 960
VTQLQSQILE LQGELKEFKT CNKQLHQKLI LAEAVMEGRP TPDKTLLNDS EICPPDDLAS 1020
LPSCKENPED VLSPTSVATY LSSKSQPSAK VSVMGTDQSE SINTSNETEY LKQKIHDLET 1080
ELEGYQNFIF QLQKHSQCSE AIITVLCGTE GAQDGLSKPK NGSDGEEMTF SSLHQVRYVK 1140
HVKILGPLAP EMIDSRVLEN LKQQLEEQEY KLQKEQNLNM QLFSEIHNLQ NKFRDLSPPR 1200
YDSLVQSQAR ELSLQRQQIK DGHGICVISR QHMNTMIKAF EELLQASDVD YCVAEGFQEQ 1260
LNQCAELLEK LEKLFLNGKS VGVEMNTQNE LMERIEEDNL TYQHLLPESP EPSASHALSD 1320
YETSEKSFFS RDQKQDNETE KTSVMVNSFS QDLLMEHIQE IRTLRKRLEE SIKTNEKLRK 1380
QLERQGSEFV QGSTSIFASG SELHSSLTSE IHFLRKQNQA LNAMLIKGSR DKQKENDKLR 1440
ESLSRKTVSL EHLQREYASV KEENERLQKE GSEKERHNQQ LIQEVRCSGQ ELSRVQEEVK 1500
LRQQLLSQND KLLQSLRVEL KAYEKLDEEH RRLREASGEG WKGQDPFRDL HSLLMEIQAL 1560
RLQLERSIET SSTLQSRLKE QLARGAEKAQ EGALTLAVQA VSIPEVPLQP DKHDGDKYPM 1620
ESDNSFDLFD SSQAVTPKSV SETPPLSGND TDSLSCDSGS SATSTPCVSR LVTGHHLWAS 1680
KNGRHVLGLI EDYEALLKQI SQGQRLLAEM DIQTQEAPSS TSQELGTKGP HPAPLSKFVS 1740
SVSTAKLTLE EAYRRLKLLW RVSLPEDGQC PLHCEQIGEM KAEVTKLHKK LFEQEKKLQN 1800
TMKLLQLSKR QEKVIFDQLV VTHKILRKAR GNLELRPGGA HPGTCSPSRP GS 1852 
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