Skip Header

Contribute Send feedback
Read comments (?) or add your own

P60123 (RUVB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ruvbl1
Synonyms:Tip49, Tip49a
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 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.

May be able to bind plasminogen at cell surface and enhance plasminogen activation By similarity.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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 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; 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 By similarity.

Subcellular location

Nucleus By similarity.

Tissue specificity

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. Ref.4

Sequence similarities

Belongs to the RuvB family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA recombination
DNA repair
Growth regulation
Mitosis
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionActivator
Chromatin regulator
Helicase
Hydrolase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processDNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

histone H2A acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H4 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentMLL1 complex

Inferred from sequence or structural similarity. Source: UniProtKB

NuA4 histone acetyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA helicase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456RuvB-like 1
PRO_0000165641

Regions

Nucleotide binding70 – 778ATP

Amino acid modifications

Modified residue21N6-acetyllysine By similarity
Modified residue4531N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P60123 [UniParc].

Last modified November 28, 2003. Version 1.
Checksum: 9AE73EFFBA194BA1

FASTA45650,214
        10         20         30         40         50         60 
MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG VIVELIKSKK 

        70         80         90        100        110        120 
MAGRAVLLAG PPGTGKTALA LAIAQELGSK VPFCPMVGSE VYSTEIKKTE VLMENFRRAI 

       130        140        150        160        170        180 
GLRIKETKEV YEGEVTELTP CETENPMGGY GKTISHVIIG LKTAKGTKQL KLDPSIFESL 

       190        200        210        220        230        240 
QKERVEAGDV IYIEANSGAV KRQGRCDTYA TEFDLEAEEY VPLPKGDVHK KKEIIQDVTL 

       250        260        270        280        290        300 
HDLDVANARP QGGQDILSMM GQLMKPKKTE ITDKLRGEIN KVVNKYIDQG VAELVPGVLF 

       310        320        330        340        350        360 
VDEVHMLDIE CFTYLHRALE SSIAPIVIFA SNRGNCVIRG TEDITSPHGI PLDLLDRVMI 

       370        380        390        400        410        420 
IRTMLYTPQE MKQIIKIRAQ TEGINISEEA LNHLGEIGTK TTLRYSVQLL TPANLLAKIN 

       430        440        450 
GKDSIEKEHV EEISELFYDA KSSAKILADQ QDKYMK 

« Hide

References

« Hide 'large scale' references
[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: 9196036] [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: 10050036] [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: 15489334] [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: 10336418] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB002406 mRNA. Translation: BAA20875.1.
AB001581 mRNA. Translation: BAA76313.1.
BC072511 mRNA. Translation: AAH72511.1.
BC086531 mRNA. Translation: AAH86531.1.
IPIIPI00212268.
PIRJC5521.
RefSeqNP_671706.1. NM_147177.1.
UniGeneRn.86410.

3D structure databases

ProteinModelPortalP60123.
SMRP60123. Positions 7-453.
ModBaseSearch...

Protein-protein interaction databases

IntActP60123. 1 interaction.
MINTMINT-4133484.
STRINGP60123.

2D gel databases

World-2DPAGE0004:P60123.

Proteomic databases

PRIDEP60123.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000018339; ENSRNOP00000018339; ENSRNOG00000013195.
GeneID65137.
KEGGrno:65137.
UCSCNM_147177. rat.

Organism-specific databases

CTD8607.
RGD68373. Ruvbl1.

Phylogenomic databases

eggNOGmaNOG08882.
GeneTreeENSGT00550000075043.
HOVERGENHBG054186.
InParanoidP60123.
OMAVHKKKEV.
OrthoDBEOG46Q6SH.
PhylomeDBP60123.

Gene expression databases

ArrayExpressP60123.
GenevestigatorP60123.
GermOnlineENSRNOG00000013195. Rattus norvegicus.

Family and domain databases

InterProIPR003593. ATPase_AAA+_core.
IPR016027. NA-bd_OB-fold-like.
IPR010339. TIP49_C.
[Graphical view]
KOK04499.
PfamPF06068. TIP49. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
ProtoNetSearch...

Other

NextBio613955.

Entry information

Entry nameRUVB1_RAT
AccessionPrimary (citable) accession number: P60123
Secondary accession number(s): O35753
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 28, 2003
Last modified: January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families