CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023593
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chromodomain Y-like protein 
Protein Synonyms/Alias
 CDY-like 
Gene Name
 CDYL 
Gene Synonyms/Alias
 CDYL1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
135TSPNNARKQISRSTNmethylation[1, 2]
157PKALVIGKDHESKNSmethylation[3]
172QLFAASQKFRKNTAPubiquitination[4, 5]
538QEVMVRIKELASCNPubiquitination[4, 5, 6, 7, 8]
560ALVRCNMKMELEQANubiquitination[6]
576RECEVLKKIWGSAQGubiquitination[4, 5]
589QGMDSMLKYLQRKIDubiquitination[4, 5]
Reference
 [1] Protein lysine methyltransferase G9a acts on non-histone targets.
 Rathert P, Dhayalan A, Murakami M, Zhang X, Tamas R, Jurkowska R, Komatsu Y, Shinkai Y, Cheng X, Jeltsch A.
 Nat Chem Biol. 2008 Jun;4(6):344-6. [PMID: 18438403]
 [2] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681]
 [3] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [4] 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]
 [5] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [8] 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
 Acts as repressor of transcription (By similarity). Has histone acetyltransferase activity, with a preference for histone H4. 
Sequence Annotation
 DOMAIN 61 121 Chromo.
 MOD_RES 88 88 Phosphoserine.
 MOD_RES 135 135 N6,N6,N6-trimethyllysine; by EHMT2;
 MOD_RES 135 135 N6,N6-dimethyllysine; by EHMT2;
 MOD_RES 135 135 N6-methyllysine; by EHMT2; alternate.
 MOD_RES 201 201 Phosphoserine.
 MOD_RES 216 216 Phosphoserine.  
Keyword
 3D-structure; Acyltransferase; Alternative splicing; Complete proteome; Methylation; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 598 AA 
Protein Sequence
MTFQASHRSA WGKSRKKNWQ YEGPTQKLFL KRNNVSAPDG PSDPSISVSS EQSGAQQPPA 60
LQVERIVDKR KNKKGKTEYL VRWKGYDSED DTWEPEQHLV NCEEYIHDFN RRHTEKQKES 120
TLTRTNRTSP NNARKQISRS TNSNFSKTSP KALVIGKDHE SKNSQLFAAS QKFRKNTAPS 180
LSSRKNMDLA KSGIKILVPK SPVKSRTAVD GFQSESPEKL DPVEQGQEDT VAPEVAAEKP 240
VGALLGPGAE RARMGSRPRI HPLVPQVPGP VTAAMATGLA VNGKGTSPFM DALTANGTTN 300
IQTSVTGVTA SKRKFIDDRR DQPFDKRLRF SVRQTESAYR YRDIVVRKQD GFTHILLSTK 360
SSENNSLNPE VMREVQSALS TAAADDSKLV LLSAVGSVFC CGLDFIYFIR RLTDDRKRES 420
TKMAEAIRNF VNTFIQFKKP IIVAVNGPAI GLGASILPLC DVVWANEKAW FQTPYTTFGQ 480
SPDGCSTVMF PKIMGGASAN EMLLSGRKLT AQEACGKGLV SQVFWPGTFT QEVMVRIKEL 540
ASCNPVVLEE SKALVRCNMK MELEQANERE CEVLKKIWGS AQGMDSMLKY LQRKIDEF 598 
Gene Ontology
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0004402; F:histone acetyltransferase activity; IEA:EC.
 GO:0016573; P:histone acetylation; IEA:GOC.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0007283; P:spermatogenesis; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR023780; Chromo_domain.
 IPR000953; Chromo_domain/shadow.
 IPR016197; Chromodomain-like.
 IPR023779; Chromodomain_CS.
 IPR001753; Crotonase_core_superfam. 
Pfam
 PF00385; Chromo
 PF00378; ECH 
SMART
 SM00298; CHROMO 
PROSITE
 PS00598; CHROMO_1
 PS50013; CHROMO_2 
PRINTS