Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  E3 ubiquitin-protein ligase DTX3L  

UniProtKB / Swiss-Prot ID :  DTX3L_HUMAN

Gene Name (Synonyms) : 
DTX3L, BBAP  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. 

Protein Function :  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. 

Protein Sequence MASHLRPPSPLLVRVYKSGPRVRRKLESYFQSSKSSGGGECTVSTQEHEAPGTFRVEFSERAAKERVLKK...
Predicted Secondary Structure CCCCCCCCCCEEEEECCCCCCHHHHHHHHEECCCCCCCCEEEEECCCCCCCCEEEEEECHHHHHHHHHHC...
Protein Variant
LocationDescription
209K -> N (in a breast cancer sample;somatic mutation).
425R -> K (in dbSNP:rs2332285). VAR_048895
668K -> M (in dbSNP:rs9868175). VAR_048896
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
3Phosphoserine--MASHLRP
--CCCCCCC
23.04HPRD
Link-
9PhosphoserineLRPPSPLLV
CCCCCCEEE
30.75HPRD
Link-
9PhosphoserineLRPPSPLLV
CCCCCCEEE
30.75Phosphositeplus
Link-
9PhosphoserineLRPPSPLLV
CCCCCCEEE
30.75SysPTM
Link-
9Phosphoserine.LRPPSPLLV
CCCCCCEEE
30.75UniProtKB
Link-
202PhosphoserineKQQFSPSMT
HHHCCCCCH
16.24HPRD
Link-
202PhosphoserineKQQFSPSMT
HHHCCCCCH
16.24Phosphositeplus
Link-
202PhosphoserineKQQFSPSMT
HHHCCCCCH
16.24SysPTM
Link-
202Phosphoserine.KQQFSPSMT
HHHCCCCCH
16.24UniProtKB
Link-
218PhosphoserineQERDSCISP
HHHHCCCCC
21.41HPRD
Link-
218PhosphoserineQERDSCISP
HHHHCCCCC
21.41Phosphositeplus
Link-
221PhosphoserineDSCISPSEP
HCCCCCCCC
27.05HPRD
Link-
221PhosphoserineDSCISPSEP
HCCCCCCCC
27.05PhosphoELM
Link-
221PhosphoserineDSCISPSEP
HCCCCCCCC
27.05Phosphositeplus
Link-
221PhosphoserineDSCISPSEP
HCCCCCCCC
27.05SysPTM
Link-
221Phosphoserine.DSCISPSEP
HCCCCCCCC
27.05UniProtKB
Link-
248PhosphotyrosineEYFKYICPD
HHHHHHCCH
9.61Phosphositeplus
Link-
373PhosphotyrosineFAANYMMNV
HHHHHHHHH
7.94Phosphositeplus
Link-
385PhosphotyrosineDSAHYKLLE
HHHHHHHHH
11.75Phosphositeplus
Link-
532PhosphoserineMDIDSDDSK
CCCCCCCCC
43.59HPRD
Link-
532PhosphoserineMDIDSDDSK
CCCCCCCCC
43.59Phosphositeplus
Link-
535PhosphoserineDSDDSKAAS
CCCCCCCCC
29.23HPRD
Link-
592PhosphotyrosineKAMSYKPIC
HHHHCCCCC
14.01Phosphositeplus
Link-
675Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RKVLKLLYR
HHHHHHHHH
39.16Phosphositeplus
Link
709Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DIHHKTSRF
CCCCCCCCC
33.75Phosphositeplus
Link
728Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PSYLKRVKE
CHHHHHHHH
47.08Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
UB2D1_HUMANin vitro
in vivo
HPRD:16843HPRD12670957
UB2D2_HUMANin vitro
in vivo
HPRD:16843HPRD12670957
UB2D3_HUMANin vitro
in vivo
HPRD:16843HPRD12670957
DTX1_HUMANin vitro
in vivo
HPRD:16843HPRD12670957
DTX3L_HUMANin vitro
in vivo
HPRD:16843HPRD12670957
PARP9_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:16843HPRD12670957
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-202, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures