DNLI4_HUMAN - dbPTM
DNLI4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNLI4_HUMAN
UniProt AC P49917
Protein Name DNA ligase 4
Gene Name LIG4
Organism Homo sapiens (Human).
Sequence Length 911
Subcellular Localization Nucleus.
Protein Description Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends..
Protein Sequence MAASQTSQTVASHVPFADLCSTLERIQKSKGRAEKIRHFREFLDSWRKFHDALHKNHKDVTDSFYPAMRLILPQLERERMAYGIKETMLAKLYIELLNLPRDGKDALKLLNYRTPTGTHGDAGDFAMIAYFVLKPRCLQKGSLTIQQVNDLLDSIASNNSAKRKDLIKKSLLQLITQSSALEQKWLIRMIIKDLKLGVSQQTIFSVFHNDAAELHNVTTDLEKVCRQLHDPSVGLSDISITLFSAFKPMLAAIADIEHIEKDMKHQSFYIETKLDGERMQMHKDGDVYKYFSRNGYNYTDQFGASPTEGSLTPFIHNAFKADIQICILDGEMMAYNPNTQTFMQKGTKFDIKRMVEDSDLQTCYCVFDVLMVNNKKLGHETLRKRYEILSSIFTPIPGRIEIVQKTQAHTKNEVIDALNEAIDKREEGIMVKQPLSIYKPDKRGEGWLKIKPEYVSGLMDELDILIVGGYWGKGSRGGMMSHFLCAVAEKPPPGEKPSVFHTLSRVGSGCTMKELYDLGLKLAKYWKPFHRKAPPSSILCGTEKPEVYIEPCNSVIVQIKAAEIVPSDMYKTGCTLRFPRIEKIRDDKEWHECMTLDDLEQLRGKASGKLASKHLYIGGDDEPQEKKRKAAPKMKKVIGIIEHLKAPNLTNVNKISNIFEDVEFCVMSGTDSQPKPDLENRIAEFGGYIVQNPGPDTYCVIAGSENIRVKNIILSNKHDVVKPAWLLECFKTKSFVPWQPRFMIHMCPSTKEHFAREYDCYGDSYFIDTDLNQLKEVFSGIKNSNEQTPEEMASLIADLEYRYSWDCSPLSMFRRHTVYLDSYAVINDLSTKNEGTRLAIKALELRFHGAKVVSCLAEGVSHVIIGEDHSRVADFKAFRRTFKRKFKILKESWVTDSIDKCELQEENQYLI
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
40DimethylationAEKIRHFREFLDSWR
HHHHHHHHHHHHHHH
27.86-
40MethylationAEKIRHFREFLDSWR
HHHHHHHHHHHHHHH
27.8624379783
47DimethylationREFLDSWRKFHDALH
HHHHHHHHHHHHHHH
35.40-
47MethylationREFLDSWRKFHDALH
HHHHHHHHHHHHHHH
35.4024379793
55UbiquitinationKFHDALHKNHKDVTD
HHHHHHHHCCCCCHH
62.69-
85UbiquitinationERMAYGIKETMLAKL
HHHHHCCHHHHHHHH
42.65-
87PhosphorylationMAYGIKETMLAKLYI
HHHCCHHHHHHHHHH
16.6924719451
164UbiquitinationSNNSAKRKDLIKKSL
CCCHHHHHHHHHHHH
57.06-
169UbiquitinationKRKDLIKKSLLQLIT
HHHHHHHHHHHHHHH
39.06-
170PhosphorylationRKDLIKKSLLQLITQ
HHHHHHHHHHHHHHC
29.3424114839
199PhosphorylationKDLKLGVSQQTIFSV
HHHCCCCCHHHHHHH
18.1210608806
267PhosphorylationEKDMKHQSFYIETKL
HHHHCCCCEEEEEEE
21.5329214152
269PhosphorylationDMKHQSFYIETKLDG
HHCCCCEEEEEEECC
11.7722210691
273UbiquitinationQSFYIETKLDGERMQ
CCEEEEEEECCCEEE
31.61-
283UbiquitinationGERMQMHKDGDVYKY
CCEEEECCCCCHHHH
59.05-
288PhosphorylationMHKDGDVYKYFSRNG
ECCCCCHHHHHCCCC
12.5222817900
289UbiquitinationHKDGDVYKYFSRNGY
CCCCCHHHHHCCCCC
39.40-
347PhosphorylationQTFMQKGTKFDIKRM
HHHHCCCCCCCHHHH
35.2622817900
358PhosphorylationIKRMVEDSDLQTCYC
HHHHHCCCCHHHHHH
27.0724719451
362PhosphorylationVEDSDLQTCYCVFDV
HCCCCHHHHHHHEEE
16.8524719451
376UbiquitinationVLMVNNKKLGHETLR
EEEECCCCCCHHHHH
62.92-
411UbiquitinationQKTQAHTKNEVIDAL
ECCCCCCHHHHHHHH
41.04-
424UbiquitinationALNEAIDKREEGIMV
HHHHHHHHCCCCCCC
56.44-
432MethylationREEGIMVKQPLSIYK
CCCCCCCCCCCEECC
28.90-
432UbiquitinationREEGIMVKQPLSIYK
CCCCCCCCCCCEECC
28.90-
439UbiquitinationKQPLSIYKPDKRGEG
CCCCEECCCCCCCCC
45.10-
442MethylationLSIYKPDKRGEGWLK
CEECCCCCCCCCCEE
71.48-
454PhosphorylationWLKIKPEYVSGLMDE
CEECCHHHHCCCCCC
14.40-
513UbiquitinationVGSGCTMKELYDLGL
CCCCCCHHHHHHHHH
26.81-
521UbiquitinationELYDLGLKLAKYWKP
HHHHHHHHHHHHCCC
44.60-
571UbiquitinationIVPSDMYKTGCTLRF
ECCHHHHCCCCEEEC
31.63-
588UbiquitinationIEKIRDDKEWHECMT
HHHCCCCCCHHHCCC
67.97-
613UbiquitinationASGKLASKHLYIGGD
HHCCCCCCCEECCCC
31.83-
626UbiquitinationGDDEPQEKKRKAAPK
CCCCHHHHHHHHCHH
53.26-
645UbiquitinationIGIIEHLKAPNLTNV
HHHHHHHCCCCCCCH
64.80-
650PhosphorylationHLKAPNLTNVNKISN
HHCCCCCCCHHHHHH
43.7022817900
710UbiquitinationGSENIRVKNIILSNK
CCCCEEEEEEEECCC
32.36-
722UbiquitinationSNKHDVVKPAWLLEC
CCCCCCCCHHHHHHH
28.94-
733UbiquitinationLLECFKTKSFVPWQP
HHHHHCCCCCCCCCC
42.35-
765PhosphorylationYDCYGDSYFIDTDLN
CCCCCCEEEEECCHH
14.8623879269
769PhosphorylationGDSYFIDTDLNQLKE
CCEEEEECCHHHHHH
37.2523879269
775UbiquitinationDTDLNQLKEVFSGIK
ECCHHHHHHHHHCCC
41.91-
788PhosphorylationIKNSNEQTPEEMASL
CCCCCCCCHHHHHHH
26.8726714015
841UbiquitinationEGTRLAIKALELRFH
HHHHHHHHHHHHHHC
41.11-
876UbiquitinationHSRVADFKAFRRTFK
CHHHHHHHHHHHHHH
47.35-
890UbiquitinationKRKFKILKESWVTDS
HHHHHHHHHHHCCCC
53.85-

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
199SPhosphorylationKinaseATMQ13315
PhosphoELM
650TPhosphorylationKinasePRKDCP78527
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseN/A#E4P03243#Q6VGT3
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNLI4_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 DNLI4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC4_HUMANXRCC4physical
11702069
APLF_HUMANAPLFphysical
17396150
SMC2_HUMANSMC2physical
12589063
XRCC4_HUMANXRCC4physical
11809878
ACTG_HUMANACTG1physical
22990118
BTG1_HUMANBTG1physical
22990118
CLUS_HUMANCLUphysical
22990118
CO1A2_HUMANCOL1A2physical
22990118
CBP_HUMANCREBBPphysical
22990118
CATK_HUMANCTSKphysical
22990118
DGUOK_HUMANDGUOKphysical
22990118
EF1A1_HUMANEEF1A1physical
22990118
IF4A1_HUMANEIF4A1physical
22990118
ERF1_HUMANETF1physical
22990118
G3P_HUMANGAPDHphysical
22990118
HXK1_HUMANHK1physical
22990118
HMGN1_HUMANHMGN1physical
22990118
ROA1_HUMANHNRNPA1physical
22990118
ROA2_HUMANHNRNPA2B1physical
22990118
IPP_HUMANIPPphysical
22990118
LDHC_HUMANLDHCphysical
22990118
MCM4_HUMANMCM4physical
22990118
COX1_HUMANCOX1physical
22990118
COX2_HUMANCOX2physical
22990118
COX3_HUMANCOX3physical
22990118
NU1M_HUMANND1physical
22990118
NU4M_HUMANND4physical
22990118
NU5M_HUMANND5physical
22990118
NDUBA_HUMANNDUFB10physical
22990118
NEUR1_HUMANNEU1physical
22990118
PA2G4_HUMANPA2G4physical
22990118
PEX10_HUMANPEX10physical
22990118
MP2K2_HUMANMAP2K2physical
22990118
PSA6_HUMANPSMA6physical
22990118
RL11_HUMANRPL11physical
22990118
SRSF2_HUMANSRSF2physical
22990118
TLE4_HUMANTLE4physical
22990118
TP53B_HUMANTP53BP1physical
22990118
TCTP_HUMANTPT1physical
22990118
UBB_HUMANUBBphysical
22990118
UB2L3_HUMANUBE2L3physical
22990118
SYWC_HUMANWARSphysical
22990118
ALMS1_HUMANALMS1physical
22990118
GPAN1_HUMANGPANK1physical
22990118
THOC5_HUMANTHOC5physical
22990118
EIF3I_HUMANEIF3Iphysical
22990118
IF4G3_HUMANEIF4G3physical
22990118
SNX3_HUMANSNX3physical
22990118
GGH_HUMANGGHphysical
22990118
CPNE1_HUMANCPNE1physical
22990118
U119A_HUMANUNC119physical
22990118
VA0D1_HUMANATP6V0D1physical
22990118
GRHPR_HUMANGRHPRphysical
22990118
DPP3_HUMANDPP3physical
22990118
RBM5_HUMANRBM5physical
22990118
APC10_HUMANANAPC10physical
22990118
MCRS1_HUMANMCRS1physical
22990118
CAP1_HUMANCAP1physical
22990118
NPC2_HUMANNPC2physical
22990118
RUVB2_HUMANRUVBL2physical
22990118
ERD21_HUMANKDELR1physical
22990118
KIF3A_HUMANKIF3Aphysical
22990118
ZWINT_HUMANZWINTphysical
22990118
PALLD_HUMANPALLDphysical
22990118
B9D1_HUMANB9D1physical
22990118
TPPC3_HUMANTRAPPC3physical
22990118
E2AK1_HUMANEIF2AK1physical
22990118
OSTM1_HUMANOSTM1physical
22990118
SYCP3_HUMANSYCP3physical
22990118
RT18C_HUMANMRPS18Cphysical
22990118
AMPL_HUMANLAP3physical
22990118
NDUAD_HUMANNDUFA13physical
22990118
AFTIN_HUMANAFTPHphysical
22990118
WBP1L_HUMANWBP1Lphysical
22990118
OXR1_HUMANOXR1physical
22990118
OGFD1_HUMANOGFOD1physical
22990118
DD19A_HUMANDDX19Aphysical
22990118
UFSP2_HUMANUFSP2physical
22990118
F214A_HUMANFAM214Aphysical
22990118
RHBD2_HUMANRHBDD2physical
22990118
SEM4G_HUMANSEMA4Gphysical
22990118
SWAHC_HUMANSOWAHCphysical
22990118
VKOR1_HUMANVKORC1physical
22990118
BBOF1_HUMANCCDC176physical
22990118
FIP1_HUMANFIP1L1physical
22990118
ZFN2A_HUMANZFAND2Aphysical
22990118
AROS_HUMANRPS19BP1physical
22990118
WDR20_HUMANWDR20physical
22990118
AGAP4_HUMANAGAP4physical
22990118
ZN428_HUMANZNF428physical
22990118
COMD1_HUMANCOMMD1physical
22990118
ASPM_HUMANASPMphysical
22990118
PGP_HUMANPGPphysical
22990118
NOMO3_HUMANNOMO3physical
22990118
ALDOA_HUMANALDOAphysical
22990118
CATD_HUMANCTSDphysical
22990118
FLNA_HUMANFLNAphysical
22990118
XRCC6_HUMANXRCC6physical
22990118
GSTP1_HUMANGSTP1physical
22990118
LDHA_HUMANLDHAphysical
22990118
LDHB_HUMANLDHBphysical
22990118
PROF1_HUMANPFN1physical
22990118
TGM3_HUMANTGM3physical
22990118
TPIS_HUMANTPI1physical
22990118
TAGL2_HUMANTAGLN2physical
22990118
ML12A_HUMANMYL12Aphysical
22990118
HIC2_HUMANHIC2physical
22990118
STRN3_HUMANSTRN3physical
22990118
MICA3_HUMANMICAL3physical
22990118
COA7_HUMANCOA7physical
22990118
PPR18_HUMANPPP1R18physical
22990118
ENOA_HUMANENO1physical
22990118
PPIA_HUMANPPIAphysical
22990118
PRKDC_HUMANPRKDCphysical
15194694
XRCC4_HUMANXRCC4physical
15194694
PHF10_HUMANPHF10physical
21988832
EFTS_HUMANTSFMphysical
21988832
ZSC18_HUMANZSCAN18physical
21988832
XRCC4_HUMANXRCC4physical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
606593LIG4 syndrome (LIG4S)
602450Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-negative/NK-cell-positive with sensitivity to ionizing radiation (RSSCID)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DNLI4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-347, AND MASSSPECTROMETRY.

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