RUVB1_MOUSE - dbPTM
RUVB1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RUVB1_MOUSE
UniProt AC P60122
Protein Name RuvB-like 1
Gene Name Ruvbl1
Organism Mus musculus (Mouse).
Sequence Length 456
Subcellular Localization Nucleus.
Protein Description Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') 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. Essential for cell proliferation (By similarity).; May be able to bind plasminogen at cell surface and enhance plasminogen activation..
Protein Sequence MKIEEVKSTTKTQRIASHSHVKGLGLDESGLAKQAASGLVGQENAREACGVIVELIKSKKMAGRAVLLAGPPGTGKTALALAIAQELGSKVPFCPMVGSEVYSTEIKKTEVLMENFRRAIGLRIKETKEVYEGEVTELTPCETENPMGGYGKTISHVIIGLKTAKGTKQLKLDPSIFESLQKERVEAGDVIYIEANSGAVKRQGRCDTYATEFDLEAEEYVPLPKGDVHKKKEIIQDVTLHDLDVANARPQGGQDILSMMGQLMKPKKTEITDKLRGEINKVVNKYIDQGVAELVPGVLFVDEVHMLDIECFTYLHRALESSIAPIVIFASNRGNCVIRGTEDITSPHGIPLDLLDRVMIIRTMLYTPQEMKQIIKIRAQTEGINISEEALNHLGEIGTKTTLRYSVQLLTPANLLAKINGKDSIEKEHVEEISELFYDAKSSAKILADQQDKYMK
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
8PhosphorylationMKIEEVKSTTKTQRI
CCHHHCCCCCCHHHH
46.6225338131
22AcetylationIASHSHVKGLGLDES
HHHCCCCCCCCCCCC
42.896568897
102PhosphorylationPMVGSEVYSTEIKKT
CCCCCEEEECCCCHH
13.0628576409
104PhosphorylationVGSEVYSTEIKKTEV
CCCEEEECCCCHHHH
24.8428576409
109PhosphorylationYSTEIKKTEVLMENF
EECCCCHHHHHHHHH
26.7327180971
131PhosphorylationIKETKEVYEGEVTEL
EEECCEEECCCCEEE
21.22-
141GlutathionylationEVTELTPCETENPMG
CCEEECCCCCCCCCC
9.4724333276
155PhosphorylationGGYGKTISHVIIGLK
CCCCHHHEEEEEEEC
19.55-
171UbiquitinationAKGTKQLKLDPSIFE
CCCCCEEECCHHHHH
48.6422790023
171AcetylationAKGTKQLKLDPSIFE
CCCCCEEECCHHHHH
48.6423236377
281UbiquitinationKLRGEINKVVNKYID
HHHHHHHHHHHHHHH
53.90-
281MalonylationKLRGEINKVVNKYID
HHHHHHHHHHHHHHH
53.9026320211
336GlutathionylationFASNRGNCVIRGTED
EECCCCCEEEECCCC
2.7624333276
363PhosphorylationDRVMIIRTMLYTPQE
HHHHHHHHHHCCHHH
10.9125293948
366PhosphorylationMIIRTMLYTPQEMKQ
HHHHHHHCCHHHHHH
12.9325293948
367PhosphorylationIIRTMLYTPQEMKQI
HHHHHHCCHHHHHHH
17.9725293948
387PhosphorylationQTEGINISEEALNHL
HCCCCCCCHHHHHHH
25.54-
453AcetylationILADQQDKYMK----
HHHHHHHHHCC----
42.7923806337
456AcetylationDQQDKYMK-------
HHHHHHCC-------
54.8461241

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 RUVB1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RUVB1_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 RUVB1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACL6A_HUMANACTL6Aphysical
26496610
ATP5E_HUMANATP5Ephysical
26496610
RPC4_HUMANPOLR3Dphysical
26496610
ZNHI2_HUMANZNHIT2physical
26496610
CPSM_HUMANCPS1physical
26496610
NDUB5_HUMANNDUFB5physical
26496610
NFRKB_HUMANNFRKBphysical
26496610
CHM1A_HUMANCHMP1Aphysical
26496610
PFD2_HUMANPFDN2physical
26496610
RPB1_HUMANPOLR2Aphysical
26496610
RPB2_HUMANPOLR2Bphysical
26496610
RPAB1_HUMANPOLR2Ephysical
26496610
PRKDC_HUMANPRKDCphysical
26496610
PRS4_HUMANPSMC1physical
26496610
GLYM_HUMANSHMT2physical
26496610
SPT6H_HUMANSUPT6Hphysical
26496610
SURF4_HUMANSURF4physical
26496610
VPS72_HUMANVPS72physical
26496610
UBF1_HUMANUBTFphysical
26496610
TYY1_HUMANYY1physical
26496610
YETS4_HUMANYEATS4physical
26496610
TRRAP_HUMANTRRAPphysical
26496610
UXT_HUMANUXTphysical
26496610
YBOX3_HUMANYBX3physical
26496610
RMP_HUMANURI1physical
26496610
ZNHI3_HUMANZNHIT3physical
26496610
TTI1_HUMANTTI1physical
26496610
TELO2_HUMANTELO2physical
26496610
TSSC4_HUMANTSSC4physical
26496610
TBB4A_HUMANTUBB4Aphysical
26496610
ZNHI1_HUMANZNHIT1physical
26496610
PFD6_HUMANPFDN6physical
26496610
KAT5_HUMANKAT5physical
26496610
TBL3_HUMANTBL3physical
26496610
SRCAP_HUMANSRCAPphysical
26496610
RUVB2_HUMANRUVBL2physical
26496610
BRD8_HUMANBRD8physical
26496610
MO4L1_HUMANMORF4L1physical
26496610
ECD_HUMANECDphysical
26496610
GPN1_HUMANGPN1physical
26496610
DPCD_HUMANDPCDphysical
26496610
AAR2_HUMANAAR2physical
26496610
IBTK_HUMANIBTKphysical
26496610
EPC2_HUMANEPC2physical
26496610
AATF_HUMANAATFphysical
26496610
NUFP1_HUMANNUFIP1physical
26496610
TFPT_HUMANTFPTphysical
26496610
UCHL5_HUMANUCHL5physical
26496610
NOP58_HUMANNOP58physical
26496610
RPC10_HUMANPOLR3Kphysical
26496610
STK26_HUMANSTK26physical
26496610
ING3_HUMANING3physical
26496610
INO80_HUMANINO80physical
26496610
BCD1_HUMANZNHIT6physical
26496610
MBTD1_HUMANMBTD1physical
26496610
IN80D_HUMANINO80Dphysical
26496610
PINX1_HUMANPINX1physical
26496610
PK1IP_HUMANPAK1IP1physical
26496610
PIHD1_HUMANPIH1D1physical
26496610
PTCD3_HUMANPTCD3physical
26496610
MRGBP_HUMANMRGBPphysical
26496610
RPC2_HUMANPOLR3Bphysical
26496610
RPC5_HUMANPOLR3Ephysical
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
TBRG1_HUMANTBRG1physical
26496610
TM263_HUMANTMEM263physical
26496610
ARP8_HUMANACTR8physical
26496610
CL045_HUMANC12orf45physical
26496610
IN80C_HUMANINO80Cphysical
26496610
CHM4B_HUMANCHMP4Bphysical
26496610
JAZF1_HUMANJAZF1physical
26496610
IN80E_HUMANINO80Ephysical
26496610
WDR92_HUMANWDR92physical
26496610
MCRS1_HUMANMCRS1physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RUVB1_MOUSE

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Related Literatures of Post-Translational Modification

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