CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019709
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cell division cycle 5-like protein 
Protein Synonyms/Alias
 Cdc5-like protein; Pombe cdc5-related protein 
Gene Name
 CDC5L 
Gene Synonyms/Alias
 KIAA0432; PCDC5RP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
59EWLDPSIKKTEWSREubiquitination[1]
70WSREEEEKLLHLAKLubiquitination[2, 3]
165RLANTQGKKAKRKARmethylation[4]
380TNVDTPLKGGLNTPLubiquitination[1]
466YSDPSYVKQMERESRubiquitination[1]
623LEHNPYEKFSKEELKacetylation[5]
623LEHNPYEKFSKEELKubiquitination[2, 3]
626NPYEKFSKEELKKAQacetylation[6]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 DNA-binding protein involved in cell cycle control. May act as a transcription activator. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. 
Sequence Annotation
 DOMAIN 1 56 HTH myb-type 1.
 DOMAIN 57 108 HTH myb-type 2.
 DNA_BIND 31 54 H-T-H motif (By similarity).
 DNA_BIND 82 104 H-T-H motif (By similarity).
 REGION 165 271 Nuclear localization signal (Potential).
 REGION 200 206 Required for interaction with CTNNBL1 (By
 REGION 260 606 Interaction with PPP1R8.
 REGION 501 659 Interaction with DAPK3 (By similarity).
 REGION 706 800 Interaction with PLRG1.
 MOD_RES 227 227 Phosphothreonine.
 MOD_RES 303 303 Phosphoserine.
 MOD_RES 358 358 Phosphoserine.
 MOD_RES 377 377 Phosphothreonine.
 MOD_RES 385 385 Phosphothreonine.
 MOD_RES 396 396 Phosphothreonine.
 MOD_RES 404 404 Phosphothreonine.
 MOD_RES 411 411 Phosphothreonine.
 MOD_RES 415 415 Phosphothreonine.
 MOD_RES 417 417 Phosphoserine.
 MOD_RES 424 424 Phosphothreonine.
 MOD_RES 430 430 Phosphothreonine.
 MOD_RES 437 437 Phosphoserine.
 MOD_RES 438 438 Phosphothreonine.
 MOD_RES 442 442 Phosphothreonine.  
Keyword
 3D-structure; Activator; Cell cycle; Chromosomal rearrangement; Coiled coil; Complete proteome; Cytoplasm; DNA-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding; Spliceosome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 802 AA 
Protein Sequence
MPRIMIKGGV WRNTEDEILK AAVMKYGKNQ WSRIASLLHR KSAKQCKARW YEWLDPSIKK 60
TEWSREEEEK LLHLAKLMPT QWRTIAPIIG RTAAQCLEHY EFLLDKAAQR DNEEETTDDP 120
RKLKPGEIDP NPETKPARPD PIDMDEDELE MLSEARARLA NTQGKKAKRK AREKQLEEAR 180
RLAALQKRRE LRAAGIEIQK KRKRKRGVDY NAEIPFEKKP ALGFYDTSEE NYQALDADFR 240
KLRQQDLDGE LRSEKEGRDR KKDKQHLKRK KESDLPSAIL QTSGVSEFTK KRSKLVLPAP 300
QISDAELQEV VKVGQASEIA RQTAEESGIT NSASSTLLSE YNVTNNSVAL RTPRTPASQD 360
RILQEAQNLM ALTNVDTPLK GGLNTPLHES DFSGVTPQRQ VVQTPNTVLS TPFRTPSNGA 420
EGLTPRSGTT PKPVINSTPG RTPLRDKLNI NPEDGMADYS DPSYVKQMER ESREHLRLGL 480
LGLPAPKNDF EIVLPENAEK ELEEREIDDT YIEDAADVDA RKQAIRDAER VKEMKRMHKA 540
VQKDLPRPSE VNETILRPLN VEPPLTDLQK SEELIKKEMI TMLHYDLLHH PYEPSGNKKG 600
KTVGFGTNNS EHITYLEHNP YEKFSKEELK KAQDVLVQEM EVVKQGMSHG ELSSEAYNQV 660
WEECYSQVLY LPGQSRYTRA NLASKKDRIE SLEKRLEINR GHMTTEAKRA AKMEKKMKIL 720
LGGYQSRAMG LMKQLNDLWD QIEQAHLELR TFEELKKHED SAIPRRLECL KEDVQRQQER 780
EKELQHRYAD LLLEKETLKS KF 802 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016607; C:nuclear speck; IDA:BHF-UCL.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0000974; C:Prp19 complex; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; IEA:InterPro.
 GO:0003677; F:DNA binding; NAS:UniProtKB.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0071987; F:WD40-repeat domain binding; IDA:UniProtKB.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; NAS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR021786; DUF3351.
 IPR009057; Homeodomain-like.
 IPR017930; Myb_dom.
 IPR001005; SANT/Myb. 
Pfam
 PF11831; Myb_Cef 
SMART
 SM00717; SANT 
PROSITE
 PS51294; HTH_MYB 
PRINTS