RUVB2_MOUSE - dbPTM
RUVB2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MATVAATTK
------CCCCCCCCC
15.69-
9AcetylationATVAATTKVPEIRDV
CCCCCCCCCCCHHCC
51.9823806337
43PhosphorylationALEPRQASQGMVGQL
CCCHHHHCCHHHHHH
20.9428285833
215PhosphorylationSFTRARDYDAMGSQT
CCCCCCCCCCCCCCC
10.4729514104
227GlutathionylationSQTKFVQCPDGELQK
CCCEEEECCCCHHHH
2.5224333276
358PhosphorylationLDRLLIVSTSPYSEK
HCCEEEEECCCCCCC
19.0428066266
359PhosphorylationDRLLIVSTSPYSEKD
CCEEEEECCCCCCCC
23.8728066266
360PhosphorylationRLLIVSTSPYSEKDT
CEEEEECCCCCCCCH
17.8428066266
363PhosphorylationIVSTSPYSEKDTKQI
EEECCCCCCCCHHHH
41.3728066266
365AcetylationSTSPYSEKDTKQILR
ECCCCCCCCHHHHEE
65.8323806337
365SuccinylationSTSPYSEKDTKQILR
ECCCCCCCCHHHHEE
65.8323954790
365MalonylationSTSPYSEKDTKQILR
ECCCCCCCCHHHHEE
65.8326320211
419PhosphorylationVCRKRKGTEVQVDDI
HHHHCCCCEEEHHHH
35.7027841257
427AcetylationEVQVDDIKRVYSLFL
EEEHHHHHHHHHHHH
42.6923954790
427UbiquitinationEVQVDDIKRVYSLFL
EEEHHHHHHHHHHHH
42.69-
431PhosphorylationDDIKRVYSLFLDESR
HHHHHHHHHHHCCHH
15.1325338131
437PhosphorylationYSLFLDESRSTQYMK
HHHHHCCHHCHHHHH
31.06-
459PhosphorylationFNELKGETMDTS---
HHHHCCCCCCCC---
29.0825338131
462PhosphorylationLKGETMDTS------
HCCCCCCCC------
26.0529899451
463PhosphorylationKGETMDTS-------
CCCCCCCC-------
33.6825338131

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 RUVB2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RUVB2_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 RUVB2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUVB1_MOUSERuvbl1physical
20211142
ACL6A_HUMANACTL6Aphysical
26496610
ZNHI2_HUMANZNHIT2physical
26496610
NFRKB_HUMANNFRKBphysical
26496610
PFD2_HUMANPFDN2physical
26496610
RPB1_HUMANPOLR2Aphysical
26496610
2ABA_HUMANPPP2R2Aphysical
26496610
PRKDC_HUMANPRKDCphysical
26496610
SPT6H_HUMANSUPT6Hphysical
26496610
VPS72_HUMANVPS72physical
26496610
TYY1_HUMANYY1physical
26496610
YETS4_HUMANYEATS4physical
26496610
TRRAP_HUMANTRRAPphysical
26496610
MRCKA_HUMANCDC42BPAphysical
26496610
RUVB1_HUMANRUVBL1physical
26496610
RMP_HUMANURI1physical
26496610
MO4L2_HUMANMORF4L2physical
26496610
TTI1_HUMANTTI1physical
26496610
ZNHI1_HUMANZNHIT1physical
26496610
PFD6_HUMANPFDN6physical
26496610
KAT5_HUMANKAT5physical
26496610
SRCAP_HUMANSRCAPphysical
26496610
BRD8_HUMANBRD8physical
26496610
DPCD_HUMANDPCDphysical
26496610
EPC2_HUMANEPC2physical
26496610
TFPT_HUMANTFPTphysical
26496610
UCHL5_HUMANUCHL5physical
26496610
NOP58_HUMANNOP58physical
26496610
ING3_HUMANING3physical
26496610
INO80_HUMANINO80physical
26496610
MBTD1_HUMANMBTD1physical
26496610
IN80D_HUMANINO80Dphysical
26496610
PIHD1_HUMANPIH1D1physical
26496610
MRGBP_HUMANMRGBPphysical
26496610
DMAP1_HUMANDMAP1physical
26496610
CHM1B_HUMANCHMP1Bphysical
26496610
EP400_HUMANEP400physical
26496610
ARP6_HUMANACTR6physical
26496610
RPAP3_HUMANRPAP3physical
26496610
RPAP2_HUMANRPAP2physical
26496610
ARP5_HUMANACTR5physical
26496610
TTI2_HUMANTTI2physical
26496610
WDCP_HUMANC2orf44physical
26496610
EPC1_HUMANEPC1physical
26496610
PDRG1_HUMANPDRG1physical
26496610
IN80B_HUMANINO80Bphysical
26496610
ARP8_HUMANACTR8physical
26496610
CL045_HUMANC12orf45physical
26496610
IN80C_HUMANINO80Cphysical
26496610
IN80E_HUMANINO80Ephysical
26496610
WDR92_HUMANWDR92physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RUVB2_MOUSE

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Related Literatures of Post-Translational Modification

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