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RuvB-like 2 (EC 3.6.4.12) (p47 protein)

 RUVB2_MOUSE             Reviewed;         463 AA.
Q9WTM5;
28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 152.
RecName: Full=RuvB-like 2;
EC=3.6.4.12;
AltName: Full=p47 protein;
Name=Ruvbl2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=10220587; DOI=10.1093/oxfordjournals.jbchem.a022372;
Gohshi T., Simada M., Kawahire S., Imai N., Ichimura T., Omata S.,
Horigome T.;
"Molecular cloning of mouse p47, a second group mammalian RuvB DNA
helicase-like protein: homology with those from human and
Saccharomyces cerevisiae.";
J. Biochem. 125:939-946(1999).
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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.
{ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: Proposed core component of the chromatin remodeling
INO80 complex which is involved in transcriptional regulation, DNA
replication and probably DNA repair. {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: Involved in the endoplasmic reticulum (ER)-associated
degradation (ERAD) pathway where it negatively regulates
expression of ER stress response genes.
{ECO:0000250|UniProtKB:Q9Y230}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: 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 KMT2A/MLL1, ASH2L,
HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components
BAP18, 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. Interacts with HINT1. Component of
a SWR1-like complex. Component of the R2TP complex composed at
least of PIHD1, RUVBL1, RUVBL2 and RPAP3. Interacts with ITFG1.
Interacts with WAC; WAC positively regulates MTOR activity by
promoting the assembly of the TTT complex composed of TELO2, TTI1
and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into
the TTT-RUVBL complex which leads to the dimerization of the
mTORC1 complex and its subsequent activation.
{ECO:0000250|UniProtKB:Q9Y230, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB013912; BAA76297.1; -; mRNA.
CCDS; CCDS21243.1; -.
RefSeq; NP_035434.1; NM_011304.3.
RefSeq; XP_006540785.1; XM_006540722.1.
RefSeq; XP_006540786.1; XM_006540723.3.
UniGene; Mm.34410; -.
ProteinModelPortal; Q9WTM5; -.
SMR; Q9WTM5; -.
BioGrid; 203037; 65.
IntAct; Q9WTM5; 68.
MINT; MINT-4133502; -.
STRING; 10090.ENSMUSP00000033087; -.
iPTMnet; Q9WTM5; -.
PhosphoSitePlus; Q9WTM5; -.
REPRODUCTION-2DPAGE; Q9WTM5; -.
EPD; Q9WTM5; -.
MaxQB; Q9WTM5; -.
PaxDb; Q9WTM5; -.
PRIDE; Q9WTM5; -.
Ensembl; ENSMUST00000107771; ENSMUSP00000103400; ENSMUSG00000003868.
Ensembl; ENSMUST00000211214; ENSMUSP00000147502; ENSMUSG00000003868.
GeneID; 20174; -.
KEGG; mmu:20174; -.
UCSC; uc009gvc.1; mouse.
CTD; 10856; -.
MGI; MGI:1342299; Ruvbl2.
eggNOG; KOG2680; Eukaryota.
eggNOG; COG1224; LUCA.
GeneTree; ENSGT00890000139527; -.
HOGENOM; HOG000190885; -.
HOVERGEN; HBG054186; -.
InParanoid; Q9WTM5; -.
KO; K11338; -.
OMA; VPFTMIA; -.
OrthoDB; EOG091G07C9; -.
PhylomeDB; Q9WTM5; -.
TreeFam; TF300469; -.
PRO; PR:Q9WTM5; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000003868; -.
CleanEx; MM_RUVBL2; -.
ExpressionAtlas; Q9WTM5; baseline and differential.
Genevisible; Q9WTM5; MM.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031011; C:Ino80 complex; ISO:MGI.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:MGI.
GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
GO; GO:0005719; C:nuclear euchromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0097255; C:R2TP complex; ISO:MGI.
GO; GO:0000812; C:Swr1 complex; ISS:UniProtKB.
GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0043141; F:ATP-dependent 5'-3' DNA helicase activity; IEA:InterPro.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; IBA:GO_Central.
GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
GO; GO:0003678; F:DNA helicase activity; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; ISO:MGI.
GO; GO:0001094; F:TFIID-class transcription factor binding; IPI:UniProtKB.
GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:MGI.
GO; GO:0034644; P:cellular response to UV; ISO:MGI.
GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0071169; P:establishment of protein localization to chromatin; ISO:MGI.
GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
GO; GO:0071899; P:negative regulation of estrogen receptor binding; ISO:MGI.
GO; GO:0035066; P:positive regulation of histone acetylation; ISO:MGI.
GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0071733; P:transcriptional activation by promoter-enhancer looping; ISO:MGI.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR027238; RuvB-like.
InterPro; IPR010339; TIP49_C.
PANTHER; PTHR11093; PTHR11093; 1.
Pfam; PF06068; TIP49; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
Acetylation; Activator; ATP-binding; Chromatin regulator;
Complete proteome; DNA damage; DNA recombination; DNA repair;
Helicase; Hydrolase; Isopeptide bond; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9Y230}.
CHAIN 2 463 RuvB-like 2.
/FTId=PRO_0000165645.
NP_BIND 77 84 ATP. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q9Y230}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y230}.
CROSSLNK 9 9 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9Y230}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9Y230}.
CROSSLNK 456 456 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9Y230}.
SEQUENCE 463 AA; 51113 MW; 419D779972933308 CRC64;
MATVAATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL
EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF TAIAGSEIFS LEMSKTEALT
QAFRRSIGVR IKEETEIIEG EVVEIQIDRP ATGTGSKVGK LTLKTTEMET IYDLGTKMIE
SLTKDKVQAG DVITIDKATG KISKLGRSFT RARDYDAMGS QTKFVQCPDG ELQKRKEVVH
TVSLHEIDVI NSRTQGFLAL FSGDTGEIKS EVREQINAKV AEWREEGKAE IIPGVLFIDE
VHMLDIESFS FLNRALESDM APVLIMATNR GITRIRGTSY QSPHGIPIDL LDRLLIVSTS
PYSEKDTKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR YAIQLITAAS LVCRKRKGTE
VQVDDIKRVY SLFLDESRST QYMKEYQDAF LFNELKGETM DTS


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