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Protein

RuvB-like 1

Gene

Ruvbl1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity.By similarity
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).By similarity
Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.By similarity
Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. Essential for cell proliferation (By similarity).By similarity
May be able to bind plasminogen at cell surface and enhance plasminogen activation.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi70 – 778ATP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA recombination, DNA repair, Growth regulation, Mitosis, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-5696394. DNA Damage Recognition in GG-NER.
R-RNO-606279. Deposition of new CENPA-containing nucleosomes at the centromere.

Names & Taxonomyi

Protein namesi
Recommended name:
RuvB-like 1 (EC:3.6.4.12)
Alternative name(s):
49 kDa TATA box-binding protein-interacting protein
Short name:
49 kDa TBP-interacting protein
DNA helicase p50
Pontin 52
TIP49a
Gene namesi
Name:Ruvbl1
Synonyms:Tip49, Tip49a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi68373. Ruvbl1.

Subcellular locationi

GO - Cellular componenti

  • MLL1 complex Source: UniProtKB
  • NuA4 histone acetyltransferase complex Source: UniProtKB
  • nuclear matrix Source: RGD
  • nucleus Source: RGD
  • protein complex Source: RGD
  • Swr1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456RuvB-like 1PRO_0000165641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki2 – 2Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei453 – 4531N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP60123.
PRIDEiP60123.

2D gel databases

World-2DPAGE0004:P60123.

PTM databases

iPTMnetiP60123.

Expressioni

Tissue specificityi

Abundantly expressed in testes and moderately in spleen, thymus, and lung. In mouse seminiferous tubules, is specifically localized in germ cells from late pachytene spermatocytes to round spermatids.1 Publication

Gene expression databases

GenevisibleiP60123. RN.

Interactioni

Subunit structurei

Forms homohexameric rings. Can form a dodecamer with RUVBL2 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. 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 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. Associates with alpha and gamma tubulins, particularly during metaphase and early anaphase. 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. Interacts with IGHMBP2. Interacts with OFD1. Interacts with HINT1. Component of a complex with USP49 and PSMC5. Component of a SWR1-like complex. Component of the R2TP complex composed at least of PIHD1, RUVBL1, RUVBL2 and RPAP3. Interacts with PIH1D1. Interacts with ITFG1.By similarity

Protein-protein interaction databases

BioGridi249258. 1 interaction.
IntActiP60123. 2 interactions.
MINTiMINT-4133484.
STRINGi10116.ENSRNOP00000018339.

Structurei

3D structure databases

ProteinModelPortaliP60123.
SMRiP60123. Positions 7-453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuvB family.Curated

Phylogenomic databases

eggNOGiKOG1942. Eukaryota.
COG1224. LUCA.
GeneTreeiENSGT00550000075043.
HOGENOMiHOG000190885.
HOVERGENiHBG054186.
InParanoidiP60123.
KOiK04499.
OMAiYSTSDME.
OrthoDBiEOG70KGPD.
PhylomeDBiP60123.
TreeFamiTF300457.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR027238. RuvB-like.
IPR010339. TIP49_C.
[Graphical view]
PANTHERiPTHR11093. PTHR11093. 1 hit.
PfamiPF06068. TIP49. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

P60123-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG
60 70 80 90 100
VIVELIKSKK MAGRAVLLAG PPGTGKTALA LAIAQELGSK VPFCPMVGSE
110 120 130 140 150
VYSTEIKKTE VLMENFRRAI GLRIKETKEV YEGEVTELTP CETENPMGGY
160 170 180 190 200
GKTISHVIIG LKTAKGTKQL KLDPSIFESL QKERVEAGDV IYIEANSGAV
210 220 230 240 250
KRQGRCDTYA TEFDLEAEEY VPLPKGDVHK KKEIIQDVTL HDLDVANARP
260 270 280 290 300
QGGQDILSMM GQLMKPKKTE ITDKLRGEIN KVVNKYIDQG VAELVPGVLF
310 320 330 340 350
VDEVHMLDIE CFTYLHRALE SSIAPIVIFA SNRGNCVIRG TEDITSPHGI
360 370 380 390 400
PLDLLDRVMI IRTMLYTPQE MKQIIKIRAQ TEGINISEEA LNHLGEIGTK
410 420 430 440 450
TTLRYSVQLL TPANLLAKIN GKDSIEKEHV EEISELFYDA KSSAKILADQ

QDKYMK
Length:456
Mass (Da):50,214
Last modified:November 28, 2003 - v1
Checksum:i9AE73EFFBA194BA1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002406 mRNA. Translation: BAA20875.1.
AB001581 mRNA. Translation: BAA76313.1.
BC072511 mRNA. Translation: AAH72511.1.
BC086531 mRNA. Translation: AAH86531.1.
PIRiJC5521.
RefSeqiNP_671706.1. NM_147177.1.
XP_006236927.1. XM_006236865.2.
UniGeneiRn.86410.

Genome annotation databases

EnsembliENSRNOT00000018339; ENSRNOP00000018339; ENSRNOG00000013195.
ENSRNOT00000090875; ENSRNOP00000075190; ENSRNOG00000013195.
GeneIDi65137.
KEGGirno:65137.
UCSCiRGD:68373. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB002406 mRNA. Translation: BAA20875.1.
AB001581 mRNA. Translation: BAA76313.1.
BC072511 mRNA. Translation: AAH72511.1.
BC086531 mRNA. Translation: AAH86531.1.
PIRiJC5521.
RefSeqiNP_671706.1. NM_147177.1.
XP_006236927.1. XM_006236865.2.
UniGeneiRn.86410.

3D structure databases

ProteinModelPortaliP60123.
SMRiP60123. Positions 7-453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249258. 1 interaction.
IntActiP60123. 2 interactions.
MINTiMINT-4133484.
STRINGi10116.ENSRNOP00000018339.

PTM databases

iPTMnetiP60123.

2D gel databases

World-2DPAGE0004:P60123.

Proteomic databases

PaxDbiP60123.
PRIDEiP60123.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000018339; ENSRNOP00000018339; ENSRNOG00000013195.
ENSRNOT00000090875; ENSRNOP00000075190; ENSRNOG00000013195.
GeneIDi65137.
KEGGirno:65137.
UCSCiRGD:68373. rat.

Organism-specific databases

CTDi8607.
RGDi68373. Ruvbl1.

Phylogenomic databases

eggNOGiKOG1942. Eukaryota.
COG1224. LUCA.
GeneTreeiENSGT00550000075043.
HOGENOMiHOG000190885.
HOVERGENiHBG054186.
InParanoidiP60123.
KOiK04499.
OMAiYSTSDME.
OrthoDBiEOG70KGPD.
PhylomeDBiP60123.
TreeFamiTF300457.

Enzyme and pathway databases

ReactomeiR-RNO-5696394. DNA Damage Recognition in GG-NER.
R-RNO-606279. Deposition of new CENPA-containing nucleosomes at the centromere.

Miscellaneous databases

NextBioi613955.
PROiP60123.

Gene expression databases

GenevisibleiP60123. RN.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR027238. RuvB-like.
IPR010339. TIP49_C.
[Graphical view]
PANTHERiPTHR11093. PTHR11093. 1 hit.
PfamiPF06068. TIP49. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a rat 49-kDa TBP-interacting protein (TIP49) that is highly homologous to the bacterial RuvB."
    Kanemaki M., Makino Y., Yoshida T., Kishimoto T., Koga A., Yamamoto K., Yamamoto M., Moncollin V., Egly J.-M., Muramatsu M., Tamura T.-A.
    Biochem. Biophys. Res. Commun. 235:64-68(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-11; 34-45; 129-138 AND 446-452.
    Tissue: Liver.
  2. "Molecular shape and ATP binding activity of rat p50, a putative mammalian homologue of RuvB DNA helicase."
    Kikuchi N., Gohshi T., Kawahire S., Tachibana T., Yoneda Y., Isobe T., Lim C.R., Kohno K., Ichimura T., Omata S., Horigome T.
    J. Biochem. 125:487-494(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-9; 91-102; 377-398 AND 441.
    Strain: Fischer 344.
    Tissue: Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart and Ovary.
  4. "A rat RuvB-like protein, TIP49a, is a germ cell-enriched novel DNA helicase."
    Makino Y., Kanemaki M., Kurokawa Y., Koji T., Tamura T.-A.
    J. Biol. Chem. 274:15329-15335(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiRUVB1_RAT
AccessioniPrimary (citable) accession number: P60123
Secondary accession number(s): O35753
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 28, 2003
Last modified: January 20, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.