Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  RuvB-like 2  

UniProtKB / Swiss-Prot ID :  RUVB2_HUMAN

Gene Name (Synonyms) : 
RUVBL2, INO80J, TIP48, TIP49B CGI-46  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus matrix. Nucleus, nucleoplasm. Cytoplasm. Membrane. Note=Mainly localized in the nucleus, associated with nuclear matrix or in the nuclear cytosol. Although it is also present in the cytoplasm and associated with the cell membranes. 

Protein Function :  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. 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. 

Protein Sequence MATVTATTKVPEIRDVTRIERIGAHSHIRGLGLDDALEPRQASQGMVGQLAARRAAGVVLEMIREGKIAG...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCHHHEEEECCCCCCCCCCCCCCEECCCCCCCHHHHHHHHHHHHHHHHCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MATVTA
---CCCCCC
15.69UniProtKB
Link-
3Phosphothreonine--MATVTAT
--CCCCCCC
19.66HPRD
Link-
9Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TATTKVPEI
CCCCCCCCC
51.98Phosphositeplus
Link-
26PhosphoserineIGAHSHIRG
EEEECCCCC
21.78HPRD
Link-
26PhosphoserineIGAHSHIRG
EEEECCCCC
21.78Phosphositeplus
Link-
81PhosphothreonineGQPGTGKTA
CCCCCHHHH
42.03Phosphositeplus
Link-
164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KLTLKTTEM
EEEEEEECC
48.44Phosphositeplus
Link
184Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ESLTKDKVQ
HHHHHCEEE
61.93Phosphositeplus
Link
186Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LTKDKVQAG
HHHCEEEEC
37.49Phosphositeplus
Link
197Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ITIDKATGK
EEEECCCCC
43.95Phosphositeplus
Link
215PhosphotyrosineRARDYDAMG
CCCCCCCCC
10.47Phosphositeplus
Link-
220PhosphoserineDAMGSQTKF
CCCCCCCCE
22.92HPRD
Link-
220PhosphoserineDAMGSQTKF
CCCCCCCCE
22.92PhosphoELM
Link-
220PhosphoserineDAMGSQTKF
CCCCCCCCE
22.92Phosphositeplus
Link-
220Phosphoserine.DAMGSQTKF
CCCCCCCCE
22.92UniProtKB
Link-
234Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GELQKRKEV
CHHHHHHHH
77.41Phosphositeplus
Link-
262PhosphoserineLALFSGDTG
HEECCCCCC
36.29HPRD
Link-
265PhosphothreonineFSGDTGEIK
CCCCCCCCC
39.99HPRD
Link-
269Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TGEIKSEVR
CCCCCHHHH
35.94Phosphositeplus
Link-
279Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QINAKVAEW
HHHHHHHHH
37.17Phosphositeplus
Link-
338PhosphothreonineRIRGTSYQS
EEECCCCCC
17.89HPRD
Link-
339PhosphoserineIRGTSYQSP
EECCCCCCC
24.81HPRD
Link-
340PhosphotyrosineRGTSYQSPH
ECCCCCCCC
16.91HPRD
Link-
365Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PYSEKDTKQ
CCCHHHHHH
65.83Phosphositeplus
Link-
368Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EKDTKQILR
HHHHHHHHH
45.54Phosphositeplus
Link-
417Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)CRKRKGTEV
HHHCCCCEE
73.54Phosphositeplus
Link-
427Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VDDIKRVYS
HHHHHHHHH
42.69Phosphositeplus
Link-
430PhosphotyrosineIKRVYSLFL
HHHHHHHHC
12.04Phosphositeplus
Link-
431PhosphoserineKRVYSLFLD
HHHHHHHCC
15.13Phosphositeplus
Link-
444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TQYMKEYQD
HHHHHHHHH
48.62Phosphositeplus
Link-
456Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)FNELKGETM
CCCCCCCCC
48.82Phosphositeplus
Link-
456Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FNELKGETM
CCCCCCCCC
48.82Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
FDFT_HUMANphysical interactionMINT-65797MINT16169070
TRAF2_HUMANphysical interactionMINT-49537MINT14743216
M3K1_HUMANphysical interactionMINT-48286MINT14743216
M3K14_HUMANphysical interactionMINT-48799MINT14743216
TAB2_HUMANphysical interactionMINT-49188MINT14743216
RIPK3_HUMANphysical interactionMINT-49090MINT14743216
MYC_HUMANphysical interactionDIP:56687EDIP12660246
RUVB2_HUMANphysical interactionEBI-449155
intact10966108
FDFT_HUMANphysical interactionEBI-735708
intact16169070
Q9BVM2_HUMANphysical interaction
physical interaction
EBI-757783
EBI-1060104
intact16189514
17353931
ARP6_HUMANphysical interactionEBI-769446
intact16230350
EAF1_HUMANphysical interactionEBI-769446
intact16230350
CCD95_HUMANphysical interaction
physical interaction
EBI-769446
EBI-769712
intact16230350
16230350
SRCAP_HUMANphysical interactionEBI-769446
intact16230350
PLS4_HUMANphysical interactionEBI-769446
intact16230350
INOC1_HUMANphysical interactionEBI-769446
intact16230350
TIP60_HUMANphysical interaction
physical interaction
EBI-769446
EBI-449133
intact16230350
10966108
ARP5_HUMANphysical interactionEBI-769446
intact16230350
ZNHI4_HUMANphysical interaction
physical interaction
EBI-769446
EBI-769582
intact16230350
16230350
POK3_HUMANphysical interactionEBI-769446
intact16230350
EPC1_HUMANphysical interactionEBI-769446
intact16230350
BRD8_HUMANphysical interactionEBI-769446
intact16230350
Q6P198_HUMANphysical interaction
physical interaction
EBI-769446
EBI-769676
intact16230350
16230350
DMAP1_HUMANphysical interactionEBI-769446
intact16230350
YETS4_HUMANphysical interactionEBI-769446
intact16230350
ING3_HUMANphysical interactionEBI-769446
intact16230350
MO4L1_HUMANphysical interactionEBI-769446
intact16230350
EPC2_HUMANphysical interactionEBI-769446
intact16230350
TFE2_HUMANphysical interactionEBI-769446
intact16230350
CB044_HUMANphysical interactionEBI-1060145
intact17353931
UBP7_HUMANphysical interactionEBI-1070205
intact17353931
PLOD2_HUMANphysical interactionEBI-1065434
intact17353931
RS11_HUMANphysical interactionEBI-1063696
intact17353931
ATF2_HUMANin vivo
yeast 2-hybrid
HPRD:16070HPRD11713276
RUVB1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:16070HPRD11080158
10524211
10966108
TBP_HUMANENSP00000221413STRING
TBP_HUMANENSP00000221413STRING
YETS4_HUMANENSP00000221413STRING
YETS4_HUMANENSP00000221413STRING
BRD8_HUMANENSP00000221413STRING
BRD8_HUMANENSP00000221413STRING
ACL6A_HUMANENSP00000221413STRING
ACL6A_HUMANENSP00000221413STRING
EPC1_HUMANENSP00000221413STRING
EPC1_HUMANENSP00000221413STRING
NOL5_HUMANENSP00000221413STRING
NOL5_HUMANENSP00000221413STRING
DMAP1_HUMANENSP00000221413STRING
DMAP1_HUMANENSP00000221413STRING
RUVB1_HUMANENSP00000221413STRING
RUVB1_HUMANENSP00000221413STRING
ING3_HUMANENSP00000221413STRING
ING3_HUMANENSP00000221413STRING
MO4L1_HUMANENSP00000221413STRING
MO4L1_HUMANENSP00000221413STRING
MORF4_HUMANENSP00000221413STRING
MORF4_HUMANENSP00000221413STRING
CTNB1_HUMANENSP00000221413STRING
CTNB1_HUMANENSP00000221413STRING
ACTB_HUMANENSP00000221413STRING
ACTB_HUMANENSP00000221413STRING
TRRAP_HUMANENSP00000221413STRING
TRRAP_HUMANENSP00000221413STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures