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Protein Page:
RUVBL2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RUVBL2 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. Forms homohexameric rings (Probable). Can form a dodecamer with RUVBL1 made of two stacked hexameric rings; however, even though RUVBL1 and RUVBL2 are present in equimolar ratio, the oligomeric status of each hexamer is not known. Oligomerization may regulate binding to nucleic acids and conversely, binding to nucleic acids may affect the dodecameric assembly. Interacts with the transcriptional activation domain of MYC. Interacts With ATF2. Component of the RNA polymerase II holoenzyme complex. May also act to bridge the LEF1/TCF1-CTNNB1 complex and TBP. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC and the adenovirus E1A protein. RUVBL2 interacts with EP400. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. Interacts with NPAT. Component of the chromatin- remodeling INO80 complex; specifically part of a complex module associated with the helicase ATP-binding and the helicase C- terminal domain of INO80. Component of some MLL1/MLL complex, at least composed of the core components MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components C17orf49, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with IGHMBP2. Interacts with TELO2. Ubiquitously expressed. Highly expressed in testis and thymus. Belongs to the RuvB family. Note: This description may include information from UniProtKB.
Protein type: EC 3.6.4.12; EC 3.6.1.-; Helicase
Cellular Component: nucleoplasm; NuA4 histone acetyltransferase complex; nuclear matrix; membrane; cytoplasm; nucleolus; intracellular; ribonucleoprotein complex; nucleus
Molecular Function: ATP-dependent DNA helicase activity; identical protein binding; DNA helicase activity; protein binding; chromatin DNA binding; ATP-dependent 5'-3' DNA helicase activity; ATPase activity; unfolded protein binding; damaged DNA binding; ATP binding
Biological Process: chromatin remodeling; ATP catabolic process; establishment and/or maintenance of chromatin architecture; transcription, DNA-dependent; protein folding; regulation of growth; positive regulation of histone acetylation; positive regulation of transcription from RNA polymerase II promoter; DNA repair; DNA duplex unwinding; DNA recombination
Reference #:  Q9Y230 (UniProtKB)
Alt. Names/Synonyms: 48 kDa TATA box-binding protein-interacting protein; 48 kDa TBP-interacting protein; 51 kDa erythrocyte cytosolic protein; CGI-46; ECP-51; ECP51; erythrocyte cytosolic protein, 51-KD; INO80 complex subunit J; INO80J; Repressing pontin 52; REPTIN; Reptin 52; Reptin52; RuvB (E coli homolog)-like 2; RuvB-like 2; RuvB-like 2 (E. coli); RUVB2; RUVBL2; RVB2; TAP54-beta; TBP-interacting protein, 48-KD; TIH2; TIP48; TIP49B; TIP60-associated protein 54-beta
Gene Symbols: RUVBL2
Molecular weight: 51,157 Da
Basal Isoelectric point: 5.49  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RUVBL2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K9-ub ATVTATTkVPEIRDV
0 1 S26-p IERIGAHsHIRGLGL
0 1 T81-p LIAGQPGtGKTAIAM
0 1 S110-p IAGSEIFsLEMSKTE
0 1 K164-ub KVGKLTLkTTEMETI
0 39 Y172-p TTEMETIyDLGTKMI
0 1 K184-ub KMIESLTkDkVQAGD
0 1 K186-ub IESLTkDkVQAGDVI
0 2 K197-ub GDVITIDkATGKISK
0 157 Y215-p SFTRARDyDAMGsQt
0 11 S220-p RDyDAMGsQtkFVQC
0 9 T222-p yDAMGsQtkFVQCPD
0 1 K223-ub DAMGsQtkFVQCPDG
0 2 K234-ac CPDGELQkRKEVVHT
0 3 K234-ub CPDGELQkRKEVVHT
0 1 T254-p IDVINSRtQGFLALF
0 3 K269-ub SGDTGEIkSEVREQI
0 1 K279-ub VREQINAkVAEWREE
0 1 S318-p FLNRALEsDMAPVLI
0 1 S342-p IRGTSYQsPHGIPID
0 1 S358-p LDRLLIVsTTPYSEk
0 1 K365-ac sTTPYSEkDTkQILR
0 1 K365-ub sTTPYSEkDTkQILR
0 1 K365-sc sTTPYSEkDTkQILR
0 1 K368-ub PYSEkDTkQILRIRC
0 1 K417-ac SLVCRKRkGtEVQVD
0 1 K417-ub SLVCRKRkGtEVQVD
0 1 T419-p VCRKRkGtEVQVDDI
0 1 K427-ac EVQVDDIkRVysLFL
0 7 K427-ub EVQVDDIkRVysLFL
0 1 K427-sc EVQVDDIkRVysLFL
0 7 Y430-p VDDIkRVysLFLDEs
0 5 S431-p DDIkRVysLFLDEsR
0 2 S437-p ysLFLDEsRSTQYMk
0 1 K444-ub sRSTQYMkEYQDAFL
0 1 K456-ub AFLFNELkGEtMDTS
1 0 K456-sm AFLFNELkGEtMDTS
0 1 T459-p FNELkGEtMDTS___
  mouse

 
K9 ATVAATTKVPEIRDV
S26 IERIGAHSHIRGLGL
T81 LIAGQPGTGKTAIAM
S110 IAGSEIFSLEMSKTE
K164 KVGKLTLKTTEMETI
Y172 TTEMETIYDLGTKMI
K184 KMIESLTKDKVQAGD
K186 IESLTKDKVQAGDVI
K197 GDVITIDKATGKISK
Y215-p SFTRARDyDAMGSQT
S220 RDyDAMGSQTKFVQC
T222 yDAMGSQTKFVQCPD
K223 DAMGSQTKFVQCPDG
K234 CPDGELQKRKEVVHT
K234 CPDGELQKRKEVVHT
T254 IDVINSRTQGFLALF
K269 SGDTGEIKSEVREQI
K279 VREQINAKVAEWREE
S318 FLNRALESDMAPVLI
S342 IRGTSYQSPHGIPID
S358 LDRLLIVSTSPYSEk
K365-ac STSPYSEkDTKQILR
K365 STSPYSEKDTKQILR
K365-sc STSPYSEkDTKQILR
K368 PYSEkDTKQILRIRC
K417 SLVCRKRKGTEVQVD
K417 SLVCRKRKGTEVQVD
T419 VCRKRKGTEVQVDDI
K427-ac EVQVDDIkRVYSLFL
K427-ub EVQVDDIkRVYSLFL
K427 EVQVDDIKRVYSLFL
Y430 VDDIkRVYSLFLDES
S431 DDIkRVYSLFLDESR
S437 YSLFLDESRSTQYMK
K444 SRSTQYMKEYQDAFL
K456 AFLFNELKGETMDTS
K456 AFLFNELKGETMDTS
T459 FNELKGETMDTS___
  rat

 
K9 ATVAATTKVPEIRDV
S26 IERIGAHSHIRGLGL
T81 LIAGQPGTGKTAIAM
S110 IAGSEIFSLEMSKTE
K164 KVGKLTLKTTEMETI
Y172 TTEMETIYDLGTKMI
K184 KMIESLTKDKVQAGD
K186 IESLTKDKVQAGDVI
K197 GDVITIDKATGKISK
Y215 SFTRARDYDAMGSQT
S220 RDYDAMGSQTKFVQC
T222 YDAMGSQTKFVQCPD
K223 DAMGSQTKFVQCPDG
K234 CPDGELQKRKEVVHT
K234 CPDGELQKRKEVVHT
T254 IDVINSRTQGFLALF
K269 SGDTGEIKSEVREQI
K279 VREQINAKVAEWREE
S318 FLNRALESDMAPVLI
S342 IRGTSYQSPHGIPID
S358 LDRLLIVSTSPYSEK
K365 STSPYSEKDTKQILR
K365 STSPYSEKDTKQILR
K365 STSPYSEKDTKQILR
K368 PYSEKDTKQILRIRC
K417 SLVCRKRKGTEVQVD
K417 SLVCRKRKGTEVQVD
T419 VCRKRKGTEVQVDDI
K427 EVQVDDIKRVYSLFL
K427 EVQVDDIKRVYSLFL
K427 EVQVDDIKRVYSLFL
Y430 VDDIKRVYSLFLDES
S431 DDIKRVYSLFLDESR
S437 YSLFLDESRSTQYMK
K444 SRSTQYMKEYQDAFL
K456 AFLFNELKGETMDTS
K456 AFLFNELKGETMDTS
T459 FNELKGETMDTS___
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