DNLI1_MOUSE - dbPTM
DNLI1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNLI1_MOUSE
UniProt AC P37913
Protein Name DNA ligase 1
Gene Name Lig1
Organism Mus musculus (Mouse).
Sequence Length 916
Subcellular Localization Nucleus.
Protein Description DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair..
Protein Sequence MQRSIMSFFQPTKEGKAKKPEKETPSSIREKEPPPKVALKERNQVVPESDSPVKRTGRKVAQVLSCEGEDEDEAPGTPKVQKPVSDSEQSSPPSPDTCPENSPVFNCSSPMDISPSGFPKRRTARKQLPKRTIQDTLEEQNEDKTKTAKKRKKEEETPKESLAEAEDIKQKEEKEGDQLIVPSEPTKSPESVTLTKTENIPVCKAGVKLKPQEEEQSKPPARGAKTLSSFFTPRKPAVKTEVKQEESGTLRKEETKGTLDPANYNPSKNNYHPIEDACWKHGQKVPFLAVARTFEKIEEVSARLKMVETLSNLLRSVVALSPPDLLPVLYLSLNRLGPPQQGLELGVGDGVLLKAVAQATGRQLESIRAEVAEKGDVGLVAENSRSTQRLMLPPPPLTISGVFTKFCDIARLTGSASMAKKMDIIKGLFVACRHSEARYIARSLSGRLRLGLAEQSVLAALAQAVSLTPPGQEFPTVVVDAGKGKTAEARKMWLEEQGMILKQTFCEVPDLDRIIPVLLEHGLERLPEHCKLSPGVPLKPMLAHPTRGVSEVLKRFEEVDFTCEYKYDGQRAQIHVLEGGEVKIFSRNQEDNTGKYPDIISRIPKIKHPSVTSFILDTEAVAWDREKKQIQPFQVLTTRKRKEVDASEIQVQVCLYAFDLIYLNGESLVRQPLSRRRQLLRENFVETEGEFVFTTSLDTKDTEQIAEFLEQSVKDSCEGLMVKTLDVDATYEIAKRSHNWLKLKKDYLDGVGDTLDLVVIGAYLGRGKRAGRYGGFLLAAYDEESEELQAICKLGTGFSDEELEEHHQSLQALVLPTPRPYVRIDGAVAPDHWLDPSIVWEVKCADLSLSPIYPAARGLVDKEKGISLRFPRFIRVRKDKQPEQATTSNQVASLYRKQSQIQNQQSSDLDSDVEDY
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
7Phosphorylation-MQRSIMSFFQPTKE
-CCCCHHHHCCCCCC		22.6527600695
13AcetylationMSFFQPTKEGKAKKP
HHHCCCCCCCCCCCC		71.7622826441
16AcetylationFQPTKEGKAKKPEKE
CCCCCCCCCCCCCCC		59.1115627475
49PhosphorylationRNQVVPESDSPVKRT
CCCCCCCCCCCCCCC		37.0023375375
51PhosphorylationQVVPESDSPVKRTGR
CCCCCCCCCCCCCCC		40.6527087446
56PhosphorylationSDSPVKRTGRKVAQV
CCCCCCCCCCEEEEE		35.3024759943
59UbiquitinationPVKRTGRKVAQVLSC
CCCCCCCEEEEEEEC		43.18-
65PhosphorylationRKVAQVLSCEGEDED
CEEEEEEECCCCCCC		15.9726824392
77PhosphorylationDEDEAPGTPKVQKPV
CCCCCCCCCCCCCCC		20.9127087446
85PhosphorylationPKVQKPVSDSEQSSP
CCCCCCCCCCCCCCC		43.9025266776
87PhosphorylationVQKPVSDSEQSSPPS
CCCCCCCCCCCCCCC		29.9926643407
90PhosphorylationPVSDSEQSSPPSPDT
CCCCCCCCCCCCCCC		40.5426643407
91PhosphorylationVSDSEQSSPPSPDTC
CCCCCCCCCCCCCCC		40.2926643407
94PhosphorylationSEQSSPPSPDTCPEN
CCCCCCCCCCCCCCC		38.5025266776
97PhosphorylationSSPPSPDTCPENSPV
CCCCCCCCCCCCCCC		33.0926643407
102PhosphorylationPDTCPENSPVFNCSS
CCCCCCCCCCCCCCC		22.3026643407
108PhosphorylationNSPVFNCSSPMDISP
CCCCCCCCCCCCCCC		38.2825293948
109PhosphorylationSPVFNCSSPMDISPS
CCCCCCCCCCCCCCC		26.8325293948
114PhosphorylationCSSPMDISPSGFPKR
CCCCCCCCCCCCCCH		14.5626643407
116PhosphorylationSPMDISPSGFPKRRT
CCCCCCCCCCCCHHH		46.4024759943
132PhosphorylationRKQLPKRTIQDTLEE
HHHCCCCCHHHHHHH		29.1729550500
136PhosphorylationPKRTIQDTLEEQNED
CCCCHHHHHHHHCHH		21.5029550500
144AcetylationLEEQNEDKTKTAKKR
HHHHCHHHHHHHHHH		45.8223806337
183PhosphorylationGDQLIVPSEPTKSPE
CCEEECCCCCCCCCC		45.3627742792
186PhosphorylationLIVPSEPTKSPESVT
EECCCCCCCCCCCEE		39.8527742792
188PhosphorylationVPSEPTKSPESVTLT
CCCCCCCCCCCEEEE		36.0627087446
191PhosphorylationEPTKSPESVTLTKTE
CCCCCCCCEEEEECC		24.6427742792
193PhosphorylationTKSPESVTLTKTENI
CCCCCCEEEEECCCC		37.6827742792
195PhosphorylationSPESVTLTKTENIPV
CCCCEEEEECCCCCE		26.9327742792
203GlutathionylationKTENIPVCKAGVKLK
ECCCCCEEECCCCCC		1.7824333276
208AcetylationPVCKAGVKLKPQEEE
CEEECCCCCCCCCHH		50.2922826441
225AcetylationKPPARGAKTLSSFFT
CCCCCCCCCHHHHCC		53.4723806337
226PhosphorylationPPARGAKTLSSFFTP
CCCCCCCCHHHHCCC		31.1928066266
228PhosphorylationARGAKTLSSFFTPRK
CCCCCCHHHHCCCCC		30.2626745281
229PhosphorylationRGAKTLSSFFTPRKP
CCCCCHHHHCCCCCC		27.7326745281
232PhosphorylationKTLSSFFTPRKPAVK
CCHHHHCCCCCCCCC		21.8526824392
239AcetylationTPRKPAVKTEVKQEE
CCCCCCCCCEEEHHH		40.8622826441
354UbiquitinationVGDGVLLKAVAQATG
CCCHHHHHHHHHHHC		36.33-
386PhosphorylationLVAENSRSTQRLMLP
EEEECCCCCCCCCCC		28.8126643407
387PhosphorylationVAENSRSTQRLMLPP
EEECCCCCCCCCCCC		19.3226643407
398PhosphorylationMLPPPPLTISGVFTK
CCCCCCEEEEEHHHH		20.9026643407
400PhosphorylationPPPPLTISGVFTKFC
CCCCEEEEEHHHHHH		24.5426643407
404PhosphorylationLTISGVFTKFCDIAR
EEEEEHHHHHHHHHH		22.3226643407
566AcetylationVDFTCEYKYDGQRAQ
CCEEEEEEECCEEEE		17.9922826441
593PhosphorylationSRNQEDNTGKYPDII
ECCCCCCCCCCCHHH		47.5822817900
601PhosphorylationGKYPDIISRIPKIKH
CCCCHHHHCCCCCCC		25.2122817900
796PhosphorylationQAICKLGTGFSDEEL
HHHHHHCCCCCHHHH		45.55-
799PhosphorylationCKLGTGFSDEELEEH
HHHCCCCCHHHHHHH		45.52-
887PhosphorylationKQPEQATTSNQVASL
CCCCCCCCHHHHHHH		28.7923140645
888PhosphorylationQPEQATTSNQVASLY
CCCCCCCHHHHHHHH		22.4023140645
893PhosphorylationTTSNQVASLYRKQSQ
CCHHHHHHHHHHHHH		27.3823140645
899PhosphorylationASLYRKQSQIQNQQS
HHHHHHHHHHHHHHH		32.0825619855
906PhosphorylationSQIQNQQSSDLDSDV
HHHHHHHHHCCCCCC		18.9627087446
907PhosphorylationQIQNQQSSDLDSDVE
HHHHHHHHCCCCCCC		37.5427087446
911PhosphorylationQQSSDLDSDVEDY--
HHHHCCCCCCCCC--		51.3427087446
916PhosphorylationLDSDVEDY-------
CCCCCCCC-------		13.6225619855
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 DNLI1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNLI1_MOUSE !!
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 DNLI1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UHRF1_HUMANUHRF1physical
28803780
PCNA_HUMANPCNAphysical
28803780
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DNLI1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-188, ANDMASS SPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-77, AND MASSSPECTROMETRY.

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