RUVB2_BOVIN
ID RUVB2_BOVIN Reviewed; 463 AA.
AC Q2TBU9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=RuvB-like 2;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q9Y230};
GN Name=RUVBL2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP-
CC dependent DNA helicase (5' to 3') activity; hexamerization is thought
CC to be critical for ATP hydrolysis and adjacent subunits in the ring-
CC like structure contribute to the ATPase activity (By similarity).
CC Component of the NuA4 histone acetyltransferase complex which is
CC involved in transcriptional activation of select genes principally by
CC acetylation of nucleosomal histones H4 and H2A (By similarity). This
CC modification may both alter nucleosome-DNA interactions and promote
CC interaction of the modified histones with other proteins which
CC positively regulate transcription (By similarity). This complex may be
CC required for the activation of transcriptional programs associated with
CC oncogene and proto-oncogene mediated growth induction, tumor suppressor
CC mediated growth arrest and replicative senescence, apoptosis, and DNA
CC repair (By similarity). The NuA4 complex ATPase and helicase activities
CC seem to be, at least in part, contributed by the association of RUVBL1
CC and RUVBL2 with EP400 (By similarity). NuA4 may also play a direct role
CC in DNA repair when recruited to sites of DNA damage (By similarity).
CC Component of a SWR1-like complex that specifically mediates the removal
CC of histone H2A.Z/H2AZ1 from the nucleosome (By similarity). Proposed
CC core component of the chromatin remodeling INO80 complex which exhibits
CC DNA- and nucleosome-activated ATPase activity and catalyzes ATP-
CC dependent nucleosome sliding (By similarity). Plays an essential role
CC in oncogenic transformation by MYC and also modulates transcriptional
CC activation by the LEF1/TCF1-CTNNB1 complex (By similarity). May also
CC inhibit the transcriptional activity of ATF2 (By similarity). Involved
CC in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway
CC where it negatively regulates expression of ER stress response genes
CC (By similarity). May play a role in regulating the composition of the
CC U5 snRNP complex (By similarity). {ECO:0000250|UniProtKB:Q9Y230}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q9Y230};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q9Y230};
CC -!- SUBUNIT: Forms homohexameric rings (Probable). Can form a dodecamer
CC with RUVBL1 made of two stacked hexameric rings; however, even though
CC RUVBL1 and RUVBL2 are present in equimolar ratio, the oligomeric status
CC of each hexamer is not known. Oligomerization may regulate binding to
CC nucleic acids and conversely, binding to nucleic acids may affect the
CC dodecameric assembly. Interaction of the complex with DHX34 results in
CC conformational changes of the N-terminus of the RUVBL2 subunits,
CC resulting in loss of nucleotide binding ability and ATP hydrolysis of
CC the complex (By similarity). Interacts with the transcriptional
CC activation domain of MYC. Interacts With ATF2. Component of the RNA
CC polymerase II holoenzyme complex. May also act to bridge the LEF1/TCF1-
CC CTNNB1 complex and TBP. Component of the NuA4 histone acetyltransferase
CC complex which contains the catalytic subunit KAT5/TIP60 and the
CC subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
CC RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15,
CC MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4
CC complex interacts with MYC and the adenovirus E1A protein. RUVBL2
CC interacts with EP400. Component of a NuA4-related complex which
CC contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
CC RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41.
CC Interacts with NPAT. Component of the chromatin-remodeling INO80
CC complex; specifically part of a complex module associated with the
CC helicase ATP-binding and the helicase C-terminal domain of INO80.
CC Component of some MLL1/MLL complex, at least composed of the core
CC components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as
CC the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
CC LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10. Interacts with IGHMBP2. Interacts with TELO2. Interacts with
CC HINT1. Component of a SWR1-like complex. Component of the R2TP complex
CC composed at least of RUVBL1, RUVBL2, RPAP3 and PIHD1. Component of the
CC PAQosome complex which is responsible for the biogenesis of several
CC protein complexes and which consists of R2TP complex members RUVBL1,
CC RUVBL2, RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT
CC and URI1 as well as ASDURF, POLR2E and DNAAF10/WDR92. Interacts with
CC ITFG1. Interacts with ZMYND10. Interacts with WAC; WAC positively
CC regulates MTOR activity by promoting the assembly of the TTT complex
CC composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of
CC RUVBL1 and RUVBL2 into the TTT-RUVBL complex which leads to the
CC dimerization of the mTORC1 complex and its subsequent activation. Forms
CC a complex with APPL1 and APPL2 (By similarity). Interacts with ZNHIT2
CC (via HIT-type zinc finger) in the presence of ATP or ADP; shows a
CC stronger interaction in the presence of ADP (By similarity). The
CC RUVBL1/RUVBL2 complex interacts with ZNHIT1 (via HIT-type zinc finger),
CC ZNHIT3 (via HIT-type zinc finger), ZNHIT6 (via HIT-type zinc finger)
CC and DDX59/ZNHIT5 (via HIT-type zinc finger) in the presence of ADP (By
CC similarity). Interacts with NOPCHAP1; the interaction is direct and
CC disrupted upon ATP binding (By similarity). Interacts with SMG1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y230, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:Q9Y230}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9Y230}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y230}. Membrane
CC {ECO:0000250|UniProtKB:Q9Y230}. Dynein axonemal particle
CC {ECO:0000250|UniProtKB:Q9DE27}. Note=Mainly localized in the nucleus,
CC associated with nuclear matrix or in the nuclear cytosol. Although it
CC is also present in the cytoplasm and associated with the cell
CC membranes. {ECO:0000250|UniProtKB:Q9Y230}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC109612; AAI09613.1; -; mRNA.
DR RefSeq; NP_001033615.1; NM_001038526.2.
DR AlphaFoldDB; Q2TBU9; -.
DR SMR; Q2TBU9; -.
DR STRING; 9913.ENSBTAP00000031853; -.
DR PaxDb; Q2TBU9; -.
DR PRIDE; Q2TBU9; -.
DR GeneID; 511048; -.
DR KEGG; bta:511048; -.
DR CTD; 10856; -.
DR eggNOG; KOG2680; Eukaryota.
DR InParanoid; Q2TBU9; -.
DR OrthoDB; 752343at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0097255; C:R2TP complex; ISS:UniProtKB.
DR GO; GO:0000812; C:Swr1 complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.40.50.360; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR027238; RuvB-like.
DR InterPro; IPR041048; RuvB-like_C.
DR InterPro; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR InterPro; IPR037942; RUVBL2.
DR InterPro; IPR010339; TIP49_P-loop.
DR PANTHER; PTHR11093; PTHR11093; 1.
DR PANTHER; PTHR11093:SF2; PTHR11093:SF2; 1.
DR Pfam; PF06068; TIP49; 1.
DR Pfam; PF17856; TIP49_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; ATP-binding; Chromatin regulator; Cytoplasm;
KW DNA damage; DNA recombination; DNA repair; Helicase; Hydrolase;
KW Isopeptide bond; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y230"
FT CHAIN 2..463
FT /note="RuvB-like 2"
FT /id="PRO_0000253730"
FT BINDING 77..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y230"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y230"
FT CROSSLNK 9
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y230"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y230"
FT CROSSLNK 456
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y230"
SQ SEQUENCE 463 AA; 51170 MW; 3701BBFF0E4E57CE CRC64;
MATVTATTKV 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
PYSEKDKKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR YAIQLITAAS LVCRKRKGTE
VQVDDIKRVY SLFLDESRST QYMKEYQDAF LFNELKGETM DTS
