DTX3L_HUMAN - dbPTM
DTX3L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DTX3L_HUMAN
UniProt AC Q8TDB6
Protein Name E3 ubiquitin-protein ligase DTX3L
Gene Name DTX3L
Organism Homo sapiens (Human).
Sequence Length 740
Subcellular Localization Cytoplasm . Nucleus . Early endosome membrane
Peripheral membrane protein
Cytoplasmic side . Lysosome membrane
Peripheral membrane protein
Cytoplasmic side . Translocates to the nucleus in response to IFNG or IFNB1 stimulation (PubMed:2647978
Protein Description E3 ubiquitin-protein ligase which, in association with ADP-ribosyltransferase PARP9, plays a role in DNA damage repair and in interferon-mediated antiviral responses. [PubMed: 12670957]
Protein Sequence MASHLRPPSPLLVRVYKSGPRVRRKLESYFQSSKSSGGGECTVSTQEHEAPGTFRVEFSERAAKERVLKKGEHQILVDEKPVPIFLVPTENSIKKNTRPQISSLTQSQAETPSGDMHQHEGHIPNAVDSCLQKIFLTVTADLNCNLFSKEQRAYITTLCPSIRKMEGHDGIEKVCGDFQDIERIHQFLSEQFLESEQKQQFSPSMTERKPLSQQERDSCISPSEPETKAEQKSNYFEVPLPYFEYFKYICPDKINSIEKRFGVNIEIQESSPNMVCLDFTSSRSGDLEAARESFASEFQKNTEPLKQECVSLADSKQANKFKQELNHQFTKLLIKEKGGELTLLGTQDDISAAKQKISEAFVKIPVKLFAANYMMNVIEVDSAHYKLLETELLQEISEIEKRYDICSKVSEKGQKTCILFESKDRQVDLSVHAYASFIDAFQHASCQLMREVLLLKSLGKERKHLHQTKFADDFRKRHPNVHFVLNQESMTLTGLPNHLAKAKQYVLKGGGMSSLAGKKLKEGHETPMDIDSDDSKAASPPLKGSVSSEASELDKKEKGICVICMDTISNKKVLPKCKHEFCAPCINKAMSYKPICPTCQTSYGIQKGNQPEGSMVFTVSRDSLPGYESFGTIVITYSMKAGIQTEEHPNPGKRYPGIQRTAYLPDNKEGRKVLKLLYRAFDQKLIFTVGYSRVLGVSDVITWNDIHHKTSRFGGPEMYGYPDPSYLKRVKEELKAKGIE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MASHLRPPS
------CCCCCCCCC
12.9819369195
3Phosphorylation-----MASHLRPPSP
-----CCCCCCCCCC
23.0429255136
9PhosphorylationASHLRPPSPLLVRVY
CCCCCCCCCCEEEEE
30.7529255136
16PhosphorylationSPLLVRVYKSGPRVR
CCCEEEEECCCHHHH
6.7224719451
18PhosphorylationLLVRVYKSGPRVRRK
CEEEEECCCHHHHHH
36.0224719451
25AcetylationSGPRVRRKLESYFQS
CCHHHHHHHHHHHHC
46.1523954790
25MalonylationSGPRVRRKLESYFQS
CCHHHHHHHHHHHHC
46.1526320211
28PhosphorylationRVRRKLESYFQSSKS
HHHHHHHHHHHCCCC
41.5029978859
29PhosphorylationVRRKLESYFQSSKSS
HHHHHHHHHHCCCCC
9.0323312004
32PhosphorylationKLESYFQSSKSSGGG
HHHHHHHCCCCCCCC
29.8129978859
33PhosphorylationLESYFQSSKSSGGGE
HHHHHHCCCCCCCCC
26.2723312004
34UbiquitinationESYFQSSKSSGGGEC
HHHHHCCCCCCCCCC
54.6229967540
35PhosphorylationSYFQSSKSSGGGECT
HHHHCCCCCCCCCCE
35.8428857561
36PhosphorylationYFQSSKSSGGGECTV
HHHCCCCCCCCCCEE
45.2328857561
44PhosphorylationGGGECTVSTQEHEAP
CCCCCEEECCCCCCC
13.2522468782
45PhosphorylationGGECTVSTQEHEAPG
CCCCEEECCCCCCCC
33.3722468782
80UbiquitinationHQILVDEKPVPIFLV
CEEEECCCCCCEEEE
47.0229967540
89PhosphorylationVPIFLVPTENSIKKN
CCEEEEECCCCCCCC
40.0827251275
92PhosphorylationFLVPTENSIKKNTRP
EEEECCCCCCCCCCH
29.5627251275
95UbiquitinationPTENSIKKNTRPQIS
ECCCCCCCCCCHHHH
62.98-
148PhosphorylationDLNCNLFSKEQRAYI
CCCCCCCCHHHHHHH
38.1524719451
163 (in isoform 2)Ubiquitination-36.2821890473
164UbiquitinationTLCPSIRKMEGHDGI
HHCHHHHHHCCCCCH
39.3729967540
173UbiquitinationEGHDGIEKVCGDFQD
CCCCCHHHHHCCHHH
40.6929967540
189PhosphorylationERIHQFLSEQFLESE
HHHHHHHHHHHHHHH
30.5524732914
195PhosphorylationLSEQFLESEQKQQFS
HHHHHHHHHHHHCCC
47.6926074081
197 (in isoform 2)Ubiquitination-59.1321890473
198UbiquitinationQFLESEQKQQFSPSM
HHHHHHHHHCCCCCC
41.8529967540
202PhosphorylationSEQKQQFSPSMTERK
HHHHHCCCCCCCCCC
16.2429255136
204PhosphorylationQKQQFSPSMTERKPL
HHHCCCCCCCCCCCC
36.8229255136
206PhosphorylationQQFSPSMTERKPLSQ
HCCCCCCCCCCCCCH
36.6626329039
209UbiquitinationSPSMTERKPLSQQER
CCCCCCCCCCCHHHH
44.0429967540
212PhosphorylationMTERKPLSQQERDSC
CCCCCCCCHHHHHCC
38.0426074081
216 (in isoform 2)Ubiquitination-36.4821890473
218PhosphorylationLSQQERDSCISPSEP
CCHHHHHCCCCCCCC
21.4120058876
221PhosphorylationQERDSCISPSEPETK
HHHHCCCCCCCCCCH
27.0525159151
223PhosphorylationRDSCISPSEPETKAE
HHCCCCCCCCCCHHH
60.0230183078
227PhosphorylationISPSEPETKAEQKSN
CCCCCCCCHHHHHCC
46.3923403867
228UbiquitinationSPSEPETKAEQKSNY
CCCCCCCHHHHHCCC
48.5421963094
232UbiquitinationPETKAEQKSNYFEVP
CCCHHHHHCCCEECC
31.9722817900
233PhosphorylationETKAEQKSNYFEVPL
CCHHHHHCCCEECCC
36.1328348404
235PhosphorylationKAEQKSNYFEVPLPY
HHHHHCCCEECCCHH
14.2822817900
248PhosphorylationPYFEYFKYICPDKIN
HHHHHHHHHCHHHHH
9.6122817900
253AcetylationFKYICPDKINSIEKR
HHHHCHHHHHHHHHH
29.0025953088
253UbiquitinationFKYICPDKINSIEKR
HHHHCHHHHHHHHHH
29.0029967540
256PhosphorylationICPDKINSIEKRFGV
HCHHHHHHHHHHHCC
35.2823401153
259UbiquitinationDKINSIEKRFGVNIE
HHHHHHHHHHCCCEE
51.89-
293PhosphorylationDLEAARESFASEFQK
CHHHHHHHHHHHHHH
22.1327499020
300UbiquitinationSFASEFQKNTEPLKQ
HHHHHHHHCCHHHHH
71.7729967540
306AcetylationQKNTEPLKQECVSLA
HHCCHHHHHHHHHHH
55.5626051181
306UbiquitinationQKNTEPLKQECVSLA
HHCCHHHHHHHHHHH
55.5629967540
311PhosphorylationPLKQECVSLADSKQA
HHHHHHHHHHHHHHH
29.5130108239
315PhosphorylationECVSLADSKQANKFK
HHHHHHHHHHHHHHH
22.5130108239
316UbiquitinationCVSLADSKQANKFKQ
HHHHHHHHHHHHHHH
54.7121963094
320UbiquitinationADSKQANKFKQELNH
HHHHHHHHHHHHHHH
57.8822817900
322UbiquitinationSKQANKFKQELNHQF
HHHHHHHHHHHHHHH
44.4629967540
331UbiquitinationELNHQFTKLLIKEKG
HHHHHHHHHHHHCCC
42.4529967540
337UbiquitinationTKLLIKEKGGELTLL
HHHHHHCCCCEEEEE
68.1829967540
354UbiquitinationQDDISAAKQKISEAF
HHHHHHHHHHHHHHH
52.4121963094
356UbiquitinationDISAAKQKISEAFVK
HHHHHHHHHHHHHHH
47.7122817900
363UbiquitinationKISEAFVKIPVKLFA
HHHHHHHHHHHHHHH
34.5321963094
367UbiquitinationAFVKIPVKLFAANYM
HHHHHHHHHHHHHHH
32.3122817900
373PhosphorylationVKLFAANYMMNVIEV
HHHHHHHHHCCEEEE
7.9422817900
385PhosphorylationIEVDSAHYKLLETEL
EEECHHHHHHHHHHH
11.7522817900
401AcetylationQEISEIEKRYDICSK
HHHHHHHHHHCHHHH
63.0226051181
401UbiquitinationQEISEIEKRYDICSK
HHHHHHHHHHCHHHH
63.0222505724
408AcetylationKRYDICSKVSEKGQK
HHHCHHHHHCCCCCE
45.4225953088
408UbiquitinationKRYDICSKVSEKGQK
HHHCHHHHHCCCCCE
45.4222505724
412UbiquitinationICSKVSEKGQKTCIL
HHHHHCCCCCEEEEE
60.17-
415UbiquitinationKVSEKGQKTCILFES
HHCCCCCEEEEEEEC
54.7729967540
423UbiquitinationTCILFESKDRQVDLS
EEEEEECCCCCEEEE
50.13-
456UbiquitinationMREVLLLKSLGKERK
HHHHHHHHHHCHHHH
43.5321890473
460UbiquitinationLLLKSLGKERKHLHQ
HHHHHHCHHHHHHHH
60.6923000965
463UbiquitinationKSLGKERKHLHQTKF
HHHCHHHHHHHHCCC
52.1629967540
469UbiquitinationRKHLHQTKFADDFRK
HHHHHHCCCHHHHHH
31.8029967540
476UbiquitinationKFADDFRKRHPNVHF
CCHHHHHHHCCCEEE
55.8629967540
501UbiquitinationGLPNHLAKAKQYVLK
CCCCHHHHHHHHHHH
63.5829967540
503UbiquitinationPNHLAKAKQYVLKGG
CCHHHHHHHHHHHCC
41.2629967540
508UbiquitinationKAKQYVLKGGGMSSL
HHHHHHHHCCCHHHH
45.5329967540
513PhosphorylationVLKGGGMSSLAGKKL
HHHCCCHHHHCCCCC
26.02-
514PhosphorylationLKGGGMSSLAGKKLK
HHCCCHHHHCCCCCC
17.2228857561
518AcetylationGMSSLAGKKLKEGHE
CHHHHCCCCCCCCCC
49.6925953088
518UbiquitinationGMSSLAGKKLKEGHE
CHHHHCCCCCCCCCC
49.6929967540
519UbiquitinationMSSLAGKKLKEGHET
HHHHCCCCCCCCCCC
64.97-
521UbiquitinationSLAGKKLKEGHETPM
HHCCCCCCCCCCCCC
71.21-
526PhosphorylationKLKEGHETPMDIDSD
CCCCCCCCCCCCCCC
20.4529255136
532PhosphorylationETPMDIDSDDSKAAS
CCCCCCCCCCCCCCC
43.5929255136
535PhosphorylationMDIDSDDSKAASPPL
CCCCCCCCCCCCCCC
29.2330266825
539PhosphorylationSDDSKAASPPLKGSV
CCCCCCCCCCCCCCC
31.7323401153
543UbiquitinationKAASPPLKGSVSSEA
CCCCCCCCCCCCCCH
55.7133845483
545O-linked_GlycosylationASPPLKGSVSSEASE
CCCCCCCCCCCCHHH
19.7629351928
545PhosphorylationASPPLKGSVSSEASE
CCCCCCCCCCCCHHH
19.7626657352
547PhosphorylationPPLKGSVSSEASELD
CCCCCCCCCCHHHCC
24.9423927012
548PhosphorylationPLKGSVSSEASELDK
CCCCCCCCCHHHCCC
34.7226657352
551PhosphorylationGSVSSEASELDKKEK
CCCCCCHHHCCCCCC
34.3424732914
556UbiquitinationEASELDKKEKGICVI
CHHHCCCCCCCEEEE
65.41-
558UbiquitinationSELDKKEKGICVICM
HHCCCCCCCEEEEEE
63.56-
567PhosphorylationICVICMDTISNKKVL
EEEEEECCCCCCCCC
10.2227251275
591PhosphorylationPCINKAMSYKPICPT
HHHHHHHCCCCCCCC
34.5628857561
592PhosphorylationCINKAMSYKPICPTC
HHHHHHCCCCCCCCC
14.0120090780
593UbiquitinationINKAMSYKPICPTCQ
HHHHHCCCCCCCCCC
22.1622505724
601PhosphorylationPICPTCQTSYGIQKG
CCCCCCCHHCCCCCC
26.5127251275
602PhosphorylationICPTCQTSYGIQKGN
CCCCCCHHCCCCCCC
8.7628857561
603PhosphorylationCPTCQTSYGIQKGNQ
CCCCCHHCCCCCCCC
22.9527251275
607UbiquitinationQTSYGIQKGNQPEGS
CHHCCCCCCCCCCCE
58.8921963094
614PhosphorylationKGNQPEGSMVFTVSR
CCCCCCCEEEEEEEC
15.3127499020
623PhosphorylationVFTVSRDSLPGYESF
EEEEECCCCCCCCCC
35.04-
629PhosphorylationDSLPGYESFGTIVIT
CCCCCCCCCCEEEEE
22.0927251275
632PhosphorylationPGYESFGTIVITYSM
CCCCCCCEEEEEEEE
15.2927251275
653UbiquitinationEEHPNPGKRYPGIQR
CCCCCCCCCCCCCCC
50.4421963094
668UbiquitinationTAYLPDNKEGRKVLK
EEECCCCHHHHHHHH
69.7723000965
672UbiquitinationPDNKEGRKVLKLLYR
CCCHHHHHHHHHHHH
63.8823000965
675AcetylationKEGRKVLKLLYRAFD
HHHHHHHHHHHHHCC
39.1625953088
675UbiquitinationKEGRKVLKLLYRAFD
HHHHHHHHHHHHHCC
39.1623000965
675 (in isoform 1)Ubiquitination-39.1621890473
698PhosphorylationYSRVLGVSDVITWND
CCCCCCCCCEEEHHH
25.1027251275
709UbiquitinationTWNDIHHKTSRFGGP
EHHHHCCCCCCCCCH
33.7522817900
709 (in isoform 1)Ubiquitination-33.7521890473
719PhosphorylationRFGGPEMYGYPDPSY
CCCCHHHHCCCCHHH
16.3123917254
721PhosphorylationGGPEMYGYPDPSYLK
CCHHHHCCCCHHHHH
6.23-
728UbiquitinationYPDPSYLKRVKEELK
CCCHHHHHHHHHHHH
47.0823000965
728 (in isoform 1)Ubiquitination-47.0821890473
731UbiquitinationPSYLKRVKEELKAKG
HHHHHHHHHHHHHCC
49.8823000965

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of DTX3L_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DTX3L_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DTX3L_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2D1_HUMANUBE2D1physical
12670957
UB2D2_HUMANUBE2D2physical
12670957
UB2D3_HUMANUBE2D3physical
12670957
DTX3L_HUMANDTX3Lphysical
12670957
UB2D1_HUMANUBE2D1physical
19818714
UB2D2_HUMANUBE2D2physical
19818714
RN111_HUMANRNF111physical
22493164
TRIM9_HUMANTRIM9physical
22493164
ITCH_HUMANITCHphysical
24790097
HGS_HUMANHGSphysical
24790097
STAM1_HUMANSTAMphysical
24790097
DTX3L_HUMANDTX3Lphysical
24790097
PARP9_HUMANPARP9physical
24886089
PAR14_HUMANPARP14physical
24886089
INGR1_HUMANIFNGR1physical
24886089
JAK1_HUMANJAK1physical
24886089
JAK2_HUMANJAK2physical
24886089
STAT1_HUMANSTAT1physical
24886089
H2B1J_HUMANHIST1H2BJphysical
26479788
H2AV_HUMANH2AFVphysical
26479788
STAT1_HUMANSTAT1physical
26479788
PARP9_HUMANPARP9physical
26479788
PARP9_HUMANPARP9physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DTX3L_HUMAN

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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.
"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.
"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.

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