UniProt ID | RUVB2_MOUSE | |
---|---|---|
UniProt AC | Q9WTM5 | |
Protein Name | RuvB-like 2 | |
Gene Name | Ruvbl2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 463 | |
Subcellular Localization | Nucleus. | |
Protein Description | Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (5' to 3') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity.; Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome (By similarity).; Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.; Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. May also inhibit the transcriptional activity of ATF2 (By similarity).; Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway where it negatively regulates expression of ER stress response genes.. | |
Protein Sequence | MATVAATTKVPEIRDVTRIERIGAHSHIRGLGLDDALEPRQASQGMVGQLAARRAAGVVLEMIREGKIAGRAVLIAGQPGTGKTAIAMGMAQALGPDTPFTAIAGSEIFSLEMSKTEALTQAFRRSIGVRIKEETEIIEGEVVEIQIDRPATGTGSKVGKLTLKTTEMETIYDLGTKMIESLTKDKVQAGDVITIDKATGKISKLGRSFTRARDYDAMGSQTKFVQCPDGELQKRKEVVHTVSLHEIDVINSRTQGFLALFSGDTGEIKSEVREQINAKVAEWREEGKAEIIPGVLFIDEVHMLDIESFSFLNRALESDMAPVLIMATNRGITRIRGTSYQSPHGIPIDLLDRLLIVSTSPYSEKDTKQILRIRCEEEDVEMSEDAYTVLTRIGLETSLRYAIQLITAASLVCRKRKGTEVQVDDIKRVYSLFLDESRSTQYMKEYQDAFLFNELKGETMDTS | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MATVAATTK ------CCCCCCCCC | 15.69 | - | |
9 | Acetylation | ATVAATTKVPEIRDV CCCCCCCCCCCHHCC | 51.98 | 23806337 | |
43 | Phosphorylation | ALEPRQASQGMVGQL CCCHHHHCCHHHHHH | 20.94 | 28285833 | |
215 | Phosphorylation | SFTRARDYDAMGSQT CCCCCCCCCCCCCCC | 10.47 | 29514104 | |
227 | Glutathionylation | SQTKFVQCPDGELQK CCCEEEECCCCHHHH | 2.52 | 24333276 | |
358 | Phosphorylation | LDRLLIVSTSPYSEK HCCEEEEECCCCCCC | 19.04 | 28066266 | |
359 | Phosphorylation | DRLLIVSTSPYSEKD CCEEEEECCCCCCCC | 23.87 | 28066266 | |
360 | Phosphorylation | RLLIVSTSPYSEKDT CEEEEECCCCCCCCH | 17.84 | 28066266 | |
363 | Phosphorylation | IVSTSPYSEKDTKQI EEECCCCCCCCHHHH | 41.37 | 28066266 | |
365 | Acetylation | STSPYSEKDTKQILR ECCCCCCCCHHHHEE | 65.83 | 23806337 | |
365 | Succinylation | STSPYSEKDTKQILR ECCCCCCCCHHHHEE | 65.83 | 23954790 | |
365 | Malonylation | STSPYSEKDTKQILR ECCCCCCCCHHHHEE | 65.83 | 26320211 | |
419 | Phosphorylation | VCRKRKGTEVQVDDI HHHHCCCCEEEHHHH | 35.70 | 27841257 | |
427 | Acetylation | EVQVDDIKRVYSLFL EEEHHHHHHHHHHHH | 42.69 | 23954790 | |
427 | Ubiquitination | EVQVDDIKRVYSLFL EEEHHHHHHHHHHHH | 42.69 | - | |
431 | Phosphorylation | DDIKRVYSLFLDESR HHHHHHHHHHHCCHH | 15.13 | 25338131 | |
437 | Phosphorylation | YSLFLDESRSTQYMK HHHHHCCHHCHHHHH | 31.06 | - | |
459 | Phosphorylation | FNELKGETMDTS--- HHHHCCCCCCCC--- | 29.08 | 25338131 | |
462 | Phosphorylation | LKGETMDTS------ HCCCCCCCC------ | 26.05 | 29899451 | |
463 | Phosphorylation | KGETMDTS------- CCCCCCCC------- | 33.68 | 25338131 |
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 RUVB2_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RUVB2_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 RUVB2_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...