CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018024
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase DTX3L 
Protein Synonyms/Alias
 B-lymphoma- and BAL-associated protein; Protein deltex-3-like; Rhysin-2; Rhysin2 
Gene Name
 DTX3L 
Gene Synonyms/Alias
 BBAP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
25SGPRVRRKLESYFQSacetylation[1]
95PTENSIKKNTRPQISubiquitination[2]
228SPSEPETKAEQKSNYubiquitination[2, 3, 4]
232PETKAEQKSNYFEVPubiquitination[2]
253FKYICPDKINSIEKRubiquitination[2]
259DKINSIEKRFGVNIEubiquitination[2]
300SFASEFQKNTEPLKQubiquitination[2]
306QKNTEPLKQECVSLAubiquitination[2]
316CVSLADSKQANKFKQubiquitination[1, 2, 3, 4]
322SKQANKFKQELNHQFubiquitination[2]
331ELNHQFTKLLIKEKGubiquitination[2]
337TKLLIKEKGGELTLLubiquitination[1, 2]
354QDDISAAKQKISEAFubiquitination[2, 3]
356DISAAKQKISEAFVKubiquitination[2]
363KISEAFVKIPVKLFAubiquitination[1, 2, 3]
401QEISEIEKRYDICSKubiquitination[2, 4]
408KRYDICSKVSEKGQKubiquitination[2, 4]
412ICSKVSEKGQKTCILubiquitination[2]
415KVSEKGQKTCILFESubiquitination[2]
423TCILFESKDRQVDLSubiquitination[1, 2]
456MREVLLLKSLGKERKubiquitination[1, 2, 5]
463KSLGKERKHLHQTKFubiquitination[2]
469RKHLHQTKFADDFRKubiquitination[2]
503PNHLAKAKQYVLKGGubiquitination[2]
508KAKQYVLKGGGMSSLubiquitination[2]
519MSSLAGKKLKEGHETubiquitination[2]
521SLAGKKLKEGHETPMubiquitination[2]
543KAASPPLKGSVSSEAubiquitination[2]
556EASELDKKEKGICVIubiquitination[2]
558SELDKKEKGICVICMubiquitination[2]
593INKAMSYKPICPTCQubiquitination[2, 4]
607QTSYGIQKGNQPEGSubiquitination[2, 3]
653EEHPNPGKRYPGIQRubiquitination[2, 3, 4]
668TAYLPDNKEGRKVLKubiquitination[2, 4, 5]
672PDNKEGRKVLKLLYRubiquitination[2, 5]
675KEGRKVLKLLYRAFDubiquitination[2, 5, 6, 7]
709TWNDIHHKTSRFGGPubiquitination[2, 4, 6, 7]
728YPDPSYLKRVKEELKubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
Reference
 [1] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] 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]
 [7] 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]
 [8] 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] 
Functional Description
 Ubiquitin ligase that mediates monoubiquitination of 'Lys-91' of histone H4 (H4K91ub1), in response to DNA damage. Protects cells exposed to DNA-damaging agents. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post- translational modifications such as H4 'Lys-20' methylation (H4K20me). Involved in the recruitment of 53BP1/TP53BP1 to sites of DNA damage by mediating H4K91ub1 formation. In concert with PARP9, plays a role in PARP1-dependent DNA damage repair. PARP1- dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. 
Sequence Annotation
 ZN_FING 561 600 RING-type.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 9 9 Phosphoserine.
 MOD_RES 202 202 Phosphoserine.
 MOD_RES 221 221 Phosphoserine.
 MOD_RES 532 532 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; Complete proteome; Cytoplasm; DNA damage; DNA repair; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 740 AA 
Protein Sequence
MASHLRPPSP LLVRVYKSGP RVRRKLESYF QSSKSSGGGE CTVSTQEHEA PGTFRVEFSE 60
RAAKERVLKK GEHQILVDEK PVPIFLVPTE NSIKKNTRPQ ISSLTQSQAE TPSGDMHQHE 120
GHIPNAVDSC LQKIFLTVTA DLNCNLFSKE QRAYITTLCP SIRKMEGHDG IEKVCGDFQD 180
IERIHQFLSE QFLESEQKQQ FSPSMTERKP LSQQERDSCI SPSEPETKAE QKSNYFEVPL 240
PYFEYFKYIC PDKINSIEKR FGVNIEIQES SPNMVCLDFT SSRSGDLEAA RESFASEFQK 300
NTEPLKQECV SLADSKQANK FKQELNHQFT KLLIKEKGGE LTLLGTQDDI SAAKQKISEA 360
FVKIPVKLFA ANYMMNVIEV DSAHYKLLET ELLQEISEIE KRYDICSKVS EKGQKTCILF 420
ESKDRQVDLS VHAYASFIDA FQHASCQLMR EVLLLKSLGK ERKHLHQTKF ADDFRKRHPN 480
VHFVLNQESM TLTGLPNHLA KAKQYVLKGG GMSSLAGKKL KEGHETPMDI DSDDSKAASP 540
PLKGSVSSEA SELDKKEKGI CVICMDTISN KKVLPKCKHE FCAPCINKAM SYKPICPTCQ 600
TSYGIQKGNQ PEGSMVFTVS RDSLPGYESF GTIVITYSMK AGIQTEEHPN PGKRYPGIQR 660
TAYLPDNKEG RKVLKLLYRA FDQKLIFTVG YSRVLGVSDV ITWNDIHHKT SRFGGPEMYG 720
YPDPSYLKRV KEELKAKGIE 740 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0042393; F:histone binding; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006302; P:double-strand break repair; IMP:UniProtKB.
 GO:0010390; P:histone monoubiquitination; IDA:UniProtKB. 
Interpro
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
  
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS