UniProt ID | ELP3_MOUSE | |
---|---|---|
UniProt AC | Q9CZX0 | |
Protein Name | Elongator complex protein 3 | |
Gene Name | Elp3 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 547 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | Catalytic histone acetyltransferase subunit of the RNA polymerase II elongator complex, which is a component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. Involved in acetylation of alpha-tubulin (By similarity). May also have a methyltransferase activity. Involved in cell migration. Involved in neurogenesis. Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation. [PubMed: 19185337] | |
Protein Sequence | MRQKRKGDLSPAELMMLTIGDVIKQLVEAHEQGKDVDLNKMKTKTAAKYGLASQPRLVDIIAAVPPHYRKILIPKLKAKPVRTASGIAVVAVMCKPHRCPHISFTGNICIYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRSLHDALSGHTSNNIHEAIKYSERSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESFHLAKDSGFKVVTHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPYQVELVRRDYVANGGWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMEEAERIAREEHGSGKMAVISGVGTRNYYRKIGYRLQGPYMVKMLK | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
34 (in isoform 2) | Ubiquitination | - | 55.03 | 22790023 | |
34 | Ubiquitination | VEAHEQGKDVDLNKM HHHHHCCCCCCHHHH | 55.03 | 22790023 | |
40 (in isoform 2) | Ubiquitination | - | 49.42 | 22790023 | |
40 | Ubiquitination | GKDVDLNKMKTKTAA CCCCCHHHHHHHHHH | 49.42 | 22790023 | |
48 | Ubiquitination | MKTKTAAKYGLASQP HHHHHHHHHCCCCCC | 37.07 | 22790023 | |
48 (in isoform 2) | Ubiquitination | - | 37.07 | 22790023 | |
53 | Phosphorylation | AAKYGLASQPRLVDI HHHHCCCCCCEEHHH | 45.84 | 23737553 | |
53 (in isoform 2) | Ubiquitination | - | 45.84 | - | |
59 (in isoform 2) | Ubiquitination | - | 31.04 | - | |
67 (in isoform 2) | Ubiquitination | - | 29.03 | - | |
161 | Phosphorylation | QLKQLGHSVDKVEFI HHHHHCCCCCEEEEE | 30.16 | 22817900 | |
229 | Methylation | TRPDYCMKRHLSDML CCCCHHHHHHHHHHH | 32.86 | - | |
280 | Acetylation | LAKDSGFKVVTHMMP CCCCCCCEEEEEECC | 39.04 | 23236377 | |
329 | Phosphorylation | VIRGTGLYELWKSGR EEECCCHHHHHHCCC | 15.43 | 19605366 | |
333 | Ubiquitination | TGLYELWKSGRYRSY CCHHHHHHCCCCCCC | 56.51 | 22790023 | |
333 (in isoform 2) | Ubiquitination | - | 56.51 | 22790023 | |
352 (in isoform 2) | Ubiquitination | - | 1.58 | - | |
392 (in isoform 2) | Ubiquitination | - | 44.22 | 22790023 | |
392 | Ubiquitination | ELAFARMKDLGIQCR HHHHHHHHHHCCEEE | 44.22 | 22790023 | |
411 (in isoform 2) | Ubiquitination | - | 1.58 | - | |
470 | Phosphorylation | FELGGGVSIVRELHV EEECCCEEEEEEEEE | 20.74 | 25619855 |
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 ELP3_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ELP3_MOUSE !! |
* 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 ELP3_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ELP3_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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