DTX2_HUMAN - dbPTM
DTX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DTX2_HUMAN
UniProt AC Q86UW9
Protein Name Probable E3 ubiquitin-protein ligase DTX2
Gene Name DTX2
Organism Homo sapiens (Human).
Sequence Length 622
Subcellular Localization Cytoplasm . Nucleus . Predominantly cytoplasmic. Partially nuclear.
Protein Description Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Probably acts both as a positive and negative regulator of Notch, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Functions as a ubiquitin ligase protein in vitro, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity..
Protein Sequence MAMAPSPSLVQVYTSPAAVAVWEWQDGLGTWHPYSATVCSFIEQQFVQQKGQRFGLGSLAHSIPLGQADPSLAPYIIDLPSWTQFRQDTGTMRAVRRHLFPQHSAPGRGVVWEWLSDDGSWTAYEASVCDYLEQQVARGNQLVDLAPLGYNYTVNYTTHTQTNKTSSFCRSVRRQAGPPYPVTTIIAPPGHTGVACSCHQCLSGSRTGPVSGRYRHSMTNLPAYPVPQHPPHRTASVFGTHQAFAPYNKPSLSGARSAPRLNTTNAWGAAPPSLGSQPLYRSSLSHLGPQHLPPGSSTSGAVSASLPSGPSSSPGSVPATVPMQMPKPSRVQQALAGMTSVLMSAIGLPVCLSRAPQPTSPPASRLASKSHGSVKRLRKMSVKGATPKPEPEPEQVIKNYTEELKVPPDEDCIICMEKLSTASGYSDVTDSKAIGSLAVGHLTKCSHAFHLLCLLAMYCNGNKDGSLQCPSCKTIYGEKTGTQPQGKMEVLRFQMSLPGHEDCGTILIVYSIPHGIQGPEHPNPGKPFTARGFPRQCYLPDNAQGRKVLELLKVAWKRRLIFTVGTSSTTGETDTVVWNEIHHKTEMDRNITGHGYPDPNYLQNVLAELAAQGVTEDCLEQQ
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
6Phosphorylation--MAMAPSPSLVQVY
--CCCCCCCCEEEEE		19.9923663014
8PhosphorylationMAMAPSPSLVQVYTS
CCCCCCCCEEEEEEC		45.5723663014
13PhosphorylationSPSLVQVYTSPAAVA
CCCEEEEEECCCEEE		5.6123663014
14PhosphorylationPSLVQVYTSPAAVAV
CCEEEEEECCCEEEE		29.4023663014
75PhosphorylationADPSLAPYIIDLPSW
CCHHHCCEEEECCCH		12.6122817900
152PhosphorylationLAPLGYNYTVNYTTH
EECCCCEEEEEEEEC		11.9928152594
153PhosphorylationAPLGYNYTVNYTTHT
ECCCCEEEEEEEECC		9.9128152594
156PhosphorylationGYNYTVNYTTHTQTN
CCEEEEEEEECCCCC		14.5328152594
157PhosphorylationYNYTVNYTTHTQTNK
CEEEEEEEECCCCCC		13.6028152594
158PhosphorylationNYTVNYTTHTQTNKT
EEEEEEEECCCCCCC		16.7428152594
160PhosphorylationTVNYTTHTQTNKTSS
EEEEEECCCCCCCCH		34.6928152594
162PhosphorylationNYTTHTQTNKTSSFC
EEEECCCCCCCCHHH		39.5828152594
213MethylationRTGPVSGRYRHSMTN
CCCCCCCCCCCCCCC		20.1524129315
213Asymmetric dimethylarginineRTGPVSGRYRHSMTN
CCCCCCCCCCCCCCC		20.15-
214PhosphorylationTGPVSGRYRHSMTNL
CCCCCCCCCCCCCCC		19.0627251275
215MethylationGPVSGRYRHSMTNLP
CCCCCCCCCCCCCCC		17.6524129315
215Asymmetric dimethylarginineGPVSGRYRHSMTNLP
CCCCCCCCCCCCCCC		17.65-
217PhosphorylationVSGRYRHSMTNLPAY
CCCCCCCCCCCCCCC		20.5027422710
219PhosphorylationGRYRHSMTNLPAYPV
CCCCCCCCCCCCCCC		36.3027251275
224PhosphorylationSMTNLPAYPVPQHPP
CCCCCCCCCCCCCCC		11.6527251275
233MethylationVPQHPPHRTASVFGT
CCCCCCCCCCCCCCC		37.4524129315
233Asymmetric dimethylarginineVPQHPPHRTASVFGT
CCCCCCCCCCCCCCC		37.45-
234PhosphorylationPQHPPHRTASVFGTH
CCCCCCCCCCCCCCC		21.9128152594
236PhosphorylationHPPHRTASVFGTHQA
CCCCCCCCCCCCCCC		19.8428152594
240PhosphorylationRTASVFGTHQAFAPY
CCCCCCCCCCCCCCC		10.1929978859
247PhosphorylationTHQAFAPYNKPSLSG
CCCCCCCCCCCCCCC		32.1829978859
249UbiquitinationQAFAPYNKPSLSGAR
CCCCCCCCCCCCCCC		30.0921890473
249UbiquitinationQAFAPYNKPSLSGAR
CCCCCCCCCCCCCCC		30.0923000965
249UbiquitinationQAFAPYNKPSLSGAR
CCCCCCCCCCCCCCC		30.0921890473
249 (in isoform 2)Ubiquitination-30.0921890473
249AcetylationQAFAPYNKPSLSGAR
CCCCCCCCCCCCCCC		30.0919608861
249 (in isoform 1)Ubiquitination-30.0921890473
251PhosphorylationFAPYNKPSLSGARSA
CCCCCCCCCCCCCCC		36.4629978859
253PhosphorylationPYNKPSLSGARSAPR
CCCCCCCCCCCCCCC		34.4429978859
256MethylationKPSLSGARSAPRLNT
CCCCCCCCCCCCCCC		36.5624129315
257PhosphorylationPSLSGARSAPRLNTT
CCCCCCCCCCCCCCC		41.9322777824
280PhosphorylationSLGSQPLYRSSLSHL
CCCCCCCCCCCCHHC		18.35-
281MethylationLGSQPLYRSSLSHLG
CCCCCCCCCCCHHCC		27.70-
339PhosphorylationQQALAGMTSVLMSAI
HHHHHHHHHHHHHHH		18.1124043423
340PhosphorylationQALAGMTSVLMSAIG
HHHHHHHHHHHHHHC		12.3624043423
341 (in isoform 2)Sumoylation-3.70-
344PhosphorylationGMTSVLMSAIGLPVC
HHHHHHHHHHCCCCH		16.7524043423
353PhosphorylationIGLPVCLSRAPQPTS
HCCCCHHCCCCCCCC		22.6724043423
359PhosphorylationLSRAPQPTSPPASRL
HCCCCCCCCCCHHHH		48.9330266825
360PhosphorylationSRAPQPTSPPASRLA
CCCCCCCCCCHHHHH		35.2512670957
364PhosphorylationQPTSPPASRLASKSH
CCCCCCHHHHHHCCC		33.3327794612
368PhosphorylationPPASRLASKSHGSVK
CCHHHHHHCCCCHHH		39.0029083192
369UbiquitinationPASRLASKSHGSVKR
CHHHHHHCCCCHHHH		40.64-
370PhosphorylationASRLASKSHGSVKRL
HHHHHHCCCCHHHHH		30.5029083192
373PhosphorylationLASKSHGSVKRLRKM
HHHCCCCHHHHHHHC		21.0229083192
379AcetylationGSVKRLRKMSVKGAT
CHHHHHHHCCCCCCC		39.877427345
381PhosphorylationVKRLRKMSVKGATPK
HHHHHHCCCCCCCCC		24.5824719451
383AcetylationRLRKMSVKGATPKPE
HHHHCCCCCCCCCCC		35.217427355
386PhosphorylationKMSVKGATPKPEPEP
HCCCCCCCCCCCCCH		40.2825159151
398UbiquitinationPEPEQVIKNYTEELK
CCHHHHHHHHHHHHC		45.0729967540
425PhosphorylationKLSTASGYSDVTDSK
ECHHCCCCCCCCCCH		10.1318083107
426UbiquitinationLSTASGYSDVTDSKA
CHHCCCCCCCCCCHH		29.1829967540
432UbiquitinationYSDVTDSKAIGSLAV
CCCCCCCHHHHHHHH		47.0033845483
440UbiquitinationAIGSLAVGHLTKCSH
HHHHHHHHHHHHHHH		12.4133845483
466PhosphorylationCNGNKDGSLQCPSCK
HCCCCCCCCCCCCCC		25.9622210691
471PhosphorylationDGSLQCPSCKTIYGE
CCCCCCCCCCEEEEC		35.5522210691
473UbiquitinationSLQCPSCKTIYGEKT
CCCCCCCCEEEECCC		42.1529967540
479UbiquitinationCKTIYGEKTGTQPQG
CCEEEECCCCCCCCC		48.1433845483
487UbiquitinationTGTQPQGKMEVLRFQ
CCCCCCCCCEEEEEE		27.0033845483
493UbiquitinationGKMEVLRFQMSLPGH
CCCEEEEEEECCCCC		6.6323000965
499UbiquitinationRFQMSLPGHEDCGTI
EEEECCCCCCCCCEE		41.9521890473
500UbiquitinationFQMSLPGHEDCGTIL
EEECCCCCCCCCEEE		26.2823000965
503UbiquitinationSLPGHEDCGTILIVY
CCCCCCCCCEEEEEE		4.7623000965
506 (in isoform 2)Ubiquitination-1.1821890473
506UbiquitinationGHEDCGTILIVYSIP
CCCCCCEEEEEEECC		1.1823000965
506UbiquitinationGHEDCGTILIVYSIP
CCCCCCEEEEEEECC		1.1821890473
510UbiquitinationCGTILIVYSIPHGIQ
CCEEEEEEECCCCCC		8.2223000965
537UbiquitinationARGFPRQCYLPDNAQ
CCCCCCCCCCCCCHH		3.8833845483
547UbiquitinationPDNAQGRKVLELLKV
CCCHHHHHHHHHHHH		58.9823000965
553UbiquitinationRKVLELLKVAWKRRL
HHHHHHHHHHHHCCE		42.4023000965
553 (in isoform 1)Ubiquitination-42.4021890473
553AcetylationRKVLELLKVAWKRRL
HHHHHHHHHHHHCCE		42.4028641621
553UbiquitinationRKVLELLKVAWKRRL
HHHHHHHHHHHHCCE		42.4021890473
557UbiquitinationELLKVAWKRRLIFTV
HHHHHHHHCCEEEEE		20.2223000965
557AcetylationELLKVAWKRRLIFTV
HHHHHHHHCCEEEEE		20.2228641627
584UbiquitinationVWNEIHHKTEMDRNI
EEEECCCCCCCCCCC		31.8333845483
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 DTX2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DTX2_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 DTX2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFX6_HUMANRFX6physical
16189514
DTX2_HUMANDTX2physical
25416956
GLCTK_HUMANGLYCTKphysical
25416956
KLC3_HUMANKLC3physical
25416956
RFX6_HUMANRFX6physical
25416956
KR261_HUMANKRTAP26-1physical
25416956
ZN641_HUMANZNF641physical
21516116
NCS1_HUMANNCS1physical
21516116
SC22A_HUMANSEC22Aphysical
21516116
SPG21_HUMANSPG21physical
21516116
ALKB4_HUMANALKBH4physical
21516116
4ET_HUMANEIF4ENIF1physical
21516116
SYQ_HUMANQARSphysical
21516116
UB2D1_HUMANUBE2D1physical
21516116
ABHGA_HUMANABHD16Aphysical
21516116
NCALD_HUMANNCALDphysical
21516116
RIM3A_HUMANRIMBP3physical
21516116
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 DTX2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-360, AND MASSSPECTROMETRY.

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