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Reviewed, UniProtKB/Swiss-Prot P60123 (RUVB1_RAT)

Last modified November 3, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    RuvB-like 1
    EC=3.6.1.-
Alternative name(s):
    49 kDa TATA box-binding protein-interacting protein
      Short name=49 kDa TBP-interacting protein
    TIP49a
    Pontin 52
    DNA helicase p50
Gene names
Name: Ruvbl1
Synonyms: Tip49, Tip49a
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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 By similarity.

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

Essential for cell proliferation By similarity.

Subunit structure

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. 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. 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 By similarity. Interacts with IGHMBP2 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.

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
P60123-1 [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

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.
UniGeneRn.86410

3D structure databases

SMRP60123. Positions 9-449.
ModBaseSearch...

Protein-protein interaction databases

STRINGP60123.

Proteomic databases

PRIDEP60123.

Genome annotation databases

EnsemblENSRNOT00000018339; ENSRNOP00000018339; ENSRNOG00000013195; Rattus norvegicus. [Genome view]
GeneID65137.
KEGGrno:65137.
UCSCNM_147177. rat.

Organism-specific databases

CTD65137.
RGD68373. Ruvbl1.

Phylogenomic databases

HOVERGENP60123.
OMAKRVGRSD.

Gene expression databases

ArrayExpressP60123.
GenevestigatorP60123.
GermOnlineENSRNOG00000013195. Rattus norvegicus.

Family and domain databases

InterProIPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR010339. TIP49_C.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF06068. TIP49. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

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: November 3, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents