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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
40 | Dimethylation | AEKIRHFREFLDSWR HHHHHHHHHHHHHHH | 27.86 | - | |
40 | Methylation | AEKIRHFREFLDSWR HHHHHHHHHHHHHHH | 27.86 | 24379783 | |
47 | Dimethylation | REFLDSWRKFHDALH HHHHHHHHHHHHHHH | 35.40 | - | |
47 | Methylation | REFLDSWRKFHDALH HHHHHHHHHHHHHHH | 35.40 | 24379793 | |
55 | Ubiquitination | KFHDALHKNHKDVTD HHHHHHHHCCCCCHH | 62.69 | - | |
85 | Ubiquitination | ERMAYGIKETMLAKL HHHHHCCHHHHHHHH | 42.65 | - | |
87 | Phosphorylation | MAYGIKETMLAKLYI HHHCCHHHHHHHHHH | 16.69 | 24719451 | |
164 | Ubiquitination | SNNSAKRKDLIKKSL CCCHHHHHHHHHHHH | 57.06 | - | |
169 | Ubiquitination | KRKDLIKKSLLQLIT HHHHHHHHHHHHHHH | 39.06 | - | |
170 | Phosphorylation | RKDLIKKSLLQLITQ HHHHHHHHHHHHHHC | 29.34 | 24114839 | |
199 | Phosphorylation | KDLKLGVSQQTIFSV HHHCCCCCHHHHHHH | 18.12 | 10608806 | |
267 | Phosphorylation | EKDMKHQSFYIETKL HHHHCCCCEEEEEEE | 21.53 | 29214152 | |
269 | Phosphorylation | DMKHQSFYIETKLDG HHCCCCEEEEEEECC | 11.77 | 22210691 | |
273 | Ubiquitination | QSFYIETKLDGERMQ CCEEEEEEECCCEEE | 31.61 | - | |
283 | Ubiquitination | GERMQMHKDGDVYKY CCEEEECCCCCHHHH | 59.05 | - | |
288 | Phosphorylation | MHKDGDVYKYFSRNG ECCCCCHHHHHCCCC | 12.52 | 22817900 | |
289 | Ubiquitination | HKDGDVYKYFSRNGY CCCCCHHHHHCCCCC | 39.40 | - | |
347 | Phosphorylation | QTFMQKGTKFDIKRM HHHHCCCCCCCHHHH | 35.26 | 22817900 | |
358 | Phosphorylation | IKRMVEDSDLQTCYC HHHHHCCCCHHHHHH | 27.07 | 24719451 | |
362 | Phosphorylation | VEDSDLQTCYCVFDV HCCCCHHHHHHHEEE | 16.85 | 24719451 | |
376 | Ubiquitination | VLMVNNKKLGHETLR EEEECCCCCCHHHHH | 62.92 | - | |
411 | Ubiquitination | QKTQAHTKNEVIDAL ECCCCCCHHHHHHHH | 41.04 | - | |
424 | Ubiquitination | ALNEAIDKREEGIMV HHHHHHHHCCCCCCC | 56.44 | - | |
432 | Methylation | REEGIMVKQPLSIYK CCCCCCCCCCCEECC | 28.90 | - | |
432 | Ubiquitination | REEGIMVKQPLSIYK CCCCCCCCCCCEECC | 28.90 | - | |
439 | Ubiquitination | KQPLSIYKPDKRGEG CCCCEECCCCCCCCC | 45.10 | - | |
442 | Methylation | LSIYKPDKRGEGWLK CEECCCCCCCCCCEE | 71.48 | - | |
454 | Phosphorylation | WLKIKPEYVSGLMDE CEECCHHHHCCCCCC | 14.40 | - | |
513 | Ubiquitination | VGSGCTMKELYDLGL CCCCCCHHHHHHHHH | 26.81 | - | |
521 | Ubiquitination | ELYDLGLKLAKYWKP HHHHHHHHHHHHCCC | 44.60 | - | |
571 | Ubiquitination | IVPSDMYKTGCTLRF ECCHHHHCCCCEEEC | 31.63 | - | |
588 | Ubiquitination | IEKIRDDKEWHECMT HHHCCCCCCHHHCCC | 67.97 | - | |
613 | Ubiquitination | ASGKLASKHLYIGGD HHCCCCCCCEECCCC | 31.83 | - | |
626 | Ubiquitination | GDDEPQEKKRKAAPK CCCCHHHHHHHHCHH | 53.26 | - | |
645 | Ubiquitination | IGIIEHLKAPNLTNV HHHHHHHCCCCCCCH | 64.80 | - | |
650 | Phosphorylation | HLKAPNLTNVNKISN HHCCCCCCCHHHHHH | 43.70 | 22817900 | |
710 | Ubiquitination | GSENIRVKNIILSNK CCCCEEEEEEEECCC | 32.36 | - | |
722 | Ubiquitination | SNKHDVVKPAWLLEC CCCCCCCCHHHHHHH | 28.94 | - | |
733 | Ubiquitination | LLECFKTKSFVPWQP HHHHHCCCCCCCCCC | 42.35 | - | |
765 | Phosphorylation | YDCYGDSYFIDTDLN CCCCCCEEEEECCHH | 14.86 | 23879269 | |
769 | Phosphorylation | GDSYFIDTDLNQLKE CCEEEEECCHHHHHH | 37.25 | 23879269 | |
775 | Ubiquitination | DTDLNQLKEVFSGIK ECCHHHHHHHHHCCC | 41.91 | - | |
788 | Phosphorylation | IKNSNEQTPEEMASL CCCCCCCCHHHHHHH | 26.87 | 26714015 | |
841 | Ubiquitination | EGTRLAIKALELRFH HHHHHHHHHHHHHHC | 41.11 | - | |
876 | Ubiquitination | HSRVADFKAFRRTFK CHHHHHHHHHHHHHH | 47.35 | - | |
890 | Ubiquitination | KRKFKILKESWVTDS HHHHHHHHHHHCCCC | 53.85 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
199 | S | Phosphorylation | Kinase | ATM | Q13315 | PhosphoELM |
650 | T | Phosphorylation | Kinase | PRKDC | P78527 | PhosphoELM |
- | K | Ubiquitination | E3 ubiquitin ligase | N/A#E4 | P03243#Q6VGT3 | PMID:22199232 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DNLI4_HUMAN !! |
* 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 !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
606593 | LIG4 syndrome (LIG4S) | |||||
602450 | Severe 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. |
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Phosphorylation | |
Reference | PubMed |
"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. |