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Protein Page:
RUVBL1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RUVBL1 Possesses single-stranded DNA-stimulated ATPase and ATP- dependent DNA helicase (3' to 5') 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. RUVBL1 plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1- CTNNB1 complex. Belongs to the ruvB family. Forms homotypic and heterotypic interactions. Forms a multimeric complex with RUVBL2. Interacts with the transcriptional activation domain of MYC. 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. RUVBL1 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. Component of the BAF53 complex, at least composed of ACTL6A/BAF53A, RUVBL1/TIP49, SMARCA2/BRM, and TRRAP/PAF400. 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, IN80C, KIAA1267, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Associates with alpha and gamma tubulins, particularly during metaphase and early anaphase. Interacts with NPAT. Component of the chromatin-remodeling INO80 complex, at least composed of ACTL6A, ACTR5, ACTR8, RVBL1, RVBL2, INO80, INO80B, INO80C, INO80D and INO80E. Interacts with IGHMBP2. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Helicase; EC 3.6.4.12
Chromosomal Location of Human Ortholog: 3q21
Cellular Component: cytoplasm; Golgi apparatus; intracellular membrane-bound organelle; membrane; microtubule organizing center; NuA4 histone acetyltransferase complex; nuclear matrix; nucleoplasm; nucleus
Molecular Function: ATP binding; ATPase activity; DNA helicase activity; protein binding
Biological Process: cell division; DNA duplex unwinding; DNA recombination; DNA repair; DNA replication-independent nucleosome assembly at centromere; mitosis; regulation of growth; regulation of transcription from RNA polymerase II promoter; spermatogenesis; transcription, DNA-dependent
Reference #:  Q9Y265 (UniProtKB)
Gene Symbols: RUVBL1
Molecular weight: 50,228 Da
Basal Isoelectric point: 6.02  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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RUVBL1

Protein Structure Not Found.
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Sites Implicated In
cell cycle regulation: T239‑p

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


 LTP 

LTP: 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.


 HTP 

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


       human

► Hide Isoforms
 
0 5 K2‑ac ______MkIEEVKST
0 1 K2‑ub ______MkIEEVKST
0 1 K22 IASHSHVKGLGLDEs
0 2 K22‑ub IASHSHVkGLGLDEs
0 2 S29‑p kGLGLDEsGLAkQAA
0 1 K33‑ub LDEsGLAkQAASGLV
0 2 T74‑p LLAGPPGtGktALAL
0 1 K76‑ub AGPPGtGktALALAI
0 1 T77‑p GPPGtGktALALAIA
0 1 S89‑p AIAQELGsKVPFCPM
0 1 Y131 IKETKEVYEGEVTEL
0 1 K152‑ub NPMGGYGkTIsHVII
0 2 S155‑p GGYGkTIsHVIIGLk
0 2 K162‑ub sHVIIGLkTAKGTKQ
0 3 K171‑ac AKGTKQLkLDPSIFE
0 6 K171‑ub AKGTKQLkLDPSIFE
0 1 S179‑p LDPSIFEsLQkERVE
0 3 K182‑ub SIFEsLQkERVEAGD
0 6 Y192‑p VEAGDVIyIEANSGA
0 1 K201‑ub EANSGAVkRQGRCDT
1 0 K225‑sm EEYVPLPkGDVHKKk
0 1 K232‑ac kGDVHKKkEIIQDVt
1 0 T239‑p kEIIQDVtLHDLDVA
0 3 K281‑ub KLRGEINkVVNKYID
0 1 S331‑p APIVIFAsNRGNCVI
0 1 S346‑p RGTEDITsPHGIPLD
0 1 S387‑p QTEGINIsEEALNHL
0 7 K400‑ub HLGEIGTkTTLRYSV
0 1 T411‑p RYSVQLLtPANLLAk
0 2 K418‑ub tPANLLAkINGKDSI
0 1 Y438‑p EEISELFyDAKSSAk
0 1 K445‑ub yDAKSSAkILADQQD
0 4 K453‑ac ILADQQDkyMk____
0 10 Y454‑p LADQQDkyMk_____
0 20 K456‑ac DQQDkyMk_______
  RUVBL1 iso2  
K2 ______MKIEEVKST
K2 ______MKIEEVKST
K22 IASHSHVKGLGLDES
K22 IASHSHVKGLGLDES
S29 KGLGLDESGLAKQAA
K33 LDESGLAKQAASGLV
T74 LLAGPPGTGKTALAL
K76 AGPPGTGKTALALAI
T77 GPPGTGKTALALAIA
S89 AIAQELGSKVPFCPM
Y131 IKETKEVYEGEVTEL
K152 NPMGGYGKTISHVII
S155 GGYGKTISHVIIGLK
K162 SHVIIGLKTAKGTKQ
K171 AKGTKQLKLDPSIFE
K171 AKGTKQLKLDPSIFE
S179 LDPSIFESLQKERVE
K182 SIFESLQKERVEAGD
Y192 VEAGDVIYIEANSGA
K201 EANSGAVKRQGRCDT
K225 EEYVPLPKGDVHKKK
K232 KGDVHKKKEIIQDVT
T239 KEIIQDVTLHDLDVA
K281 KLRGEINKVVNKYID
S331 APIVIFASNRGNCVI
S346 RGTEDITSPHGIPLD
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  mouse

 
K2 ______MKIEEVKST
K2 ______MKIEEVKST
K22‑ac IASHSHVkGLGLDES
K22 IASHSHVKGLGLDES
S29 kGLGLDESGLAKQAA
K33 LDESGLAKQAASGLV
T74 LLAGPPGTGKTALAL
K76 AGPPGTGKTALALAI
T77 GPPGTGKTALALAIA
S89 AIAQELGSKVPFCPM
Y131‑p IKETKEVyEGEVTEL
K152 NPMGGYGKTIsHVII
S155‑p GGYGKTIsHVIIGLK
K162 sHVIIGLKTAKGTKQ
K171 AKGTKQLKLDPSIFE
K171‑ub AKGTKQLkLDPSIFE
S179 LDPSIFESLQKERVE
K182 SIFESLQKERVEAGD
Y192 VEAGDVIYIEANSGA
K201 EANSGAVKRQGRCDT
K225 EEYVPLPKGDVHKKK
K232 KGDVHKKKEIIQDVT
T239 KEIIQDVTLHDLDVA
K281‑ub KLRGEINkVVNKYID
S331 APIVIFASNRGNCVI
S346 RGTEDITSPHGIPLD
S387‑p QTEGINIsEEALNHL
K400 HLGEIGTKTTLRYSV
T411 RYSVQLLTPANLLAK
K418 TPANLLAKINGKDSI
Y438 EEISELFYDAKSSAK
K445 YDAKSSAKILADQQD
K453 ILADQQDKYMk____
Y454 LADQQDKYMk_____
K456‑ac DQQDKYMk_______
  rat

 
K2‑ac ______MkIEEVKST
K2 ______MKIEEVKST
K22 IASHSHVKGLGLDES
K22 IASHSHVKGLGLDES
S29 KGLGLDESGLAKQAA
K33 LDESGLAKQAASGLV
T74 LLAGPPGTGKTALAL
K76 AGPPGTGKTALALAI
T77 GPPGTGKTALALAIA
S89 AIAQELGSKVPFCPM
Y131 IKETKEVYEGEVTEL
K152 NPMGGYGKTISHVII
S155 GGYGKTISHVIIGLK
K162 SHVIIGLKTAKGTKQ
K171‑ac AKGTKQLkLDPSIFE
K171 AKGTKQLKLDPSIFE
S179 LDPSIFESLQKERVE
K182 SIFESLQKERVEAGD
Y192 VEAGDVIYIEANSGA
K201 EANSGAVKRQGRCDT
K225 EEYVPLPKGDVHKKK
K232 KGDVHKKKEIIQDVT
T239 KEIIQDVTLHDLDVA
K281 KLRGEINKVVNKYID
S331 APIVIFASNRGNCVI
S346 RGTEDITSPHGIPLD
S387 QTEGINISEEALNHL
K400 HLGEIGTKTTLRYSV
T411 RYSVQLLTPANLLAK
K418 TPANLLAKINGKDSI
Y438 EEISELFYDAKSSAK
K445 YDAKSSAKILADQQD
K453‑ac ILADQQDkYMK____
Y454 LADQQDkYMK_____
K456 DQQDkYMK_______
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