RuvB-like 1 (RUVBL1)

The protein contains 456 amino acids for an estimated molecular weight of 50228 Da.

 

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 (PubMed:17157868). 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 (PubMed:14966270). This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription (PubMed:14966270). 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 (PubMed:14966270). 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 (PubMed:14966270). Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome (PubMed:24463511). Proposed core component of the chromatin remodeling INO80 complex which exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP-dependent nucleosome sliding (PubMed:16230350, PubMed:21303910 (updated: Nov. 13, 2019)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  5. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  6. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  7. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

Interpro domains
Total structural coverage: 100%
Model score: 100
No model available.

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The reference OMIM entry for this protein is 603449

Ruvb, e. coli, homolog-like 1; ruvbl1
Nuclear matrix protein 238; nmp238
Tata box-binding protein-interacting protein, 49-kd; tip49
Tbp-interacting protein, 49-kd
Pontin 52
Pontin
Erythrocyte cytosolic protein, 54-kd; ecp54

CLONING

By 2-dimensional electrophoresis of nuclear matrix proteins from various types of human cells, Holzmann et al. (1998) detected a common nuclear matrix protein that they designated NMP238. Using a partial protein sequence, they searched an EST database and identified a cDNA encoding NMP238. The calculated molecular mass and pI of the predicted 456-amino acid protein were close to the experimentally determined values of 54 kD and 6.5. By immunofluorescence, Holzmann et al. (1998) determined that NMP238 is found primarily in the nucleus, although it is also present in the cytoplasm. The NMP238 staining pattern appeared as punctate signals in both in situ prepared nuclear matrices and in the nucleoplasm of whole cells. Northern blot and RNA dot blot analysis revealed that NMP238 is expressed ubiquitously as an approximately 1.8-kb mRNA. Bacterial RuvB proteins function as DNA helicases that promote branch migration of Holliday junctions that form during genetic recombination. Independently, Qiu et al. (1998) isolated NMP238 cDNAs, designating the protein RUVBL1 (E. coli RuvB-like-1). They reported that RUVBL1 has homology to bacterial RuvB proteins. The regions of homology contained, among other motifs, Walker A and B motifs characteristic of DNA/RNA helicases. Makino et al. (1998) identified RUVBL1 as the human homolog of rat TIP49, a 49-kD TATA box-binding protein (TBP; 600075)-interacting protein. Rat and human TIP49 differ at only 1 amino acid position. Bauer et al. (1998) demonstrated by immunofluorescence microscopy that RUVBL1 is present in small dot-like structures in the nucleus but not in nucleoli.

GENE FUNCTION

Qiu et al. (1998) found that RUVBL1 coimmunoprecipitated with several cellular proteins and was present in the RNA polymerase II holoenzyme complex purified over multiple chromatographic steps. Qiu et al. (1998) identified 2 S. cerevisiae RuvB homologs, scRuvBL1 and scRuvBL2, which share 70% and 42% protein sequence identity with RUVBL1, respectively. They determined that scRuvBL1 is essential for viability in yeast. Wood et al. (2000) used the MYC (190080) transactivation domain to affinity purify tightly associated nuclear proteins. They identified 2 of these proteins as RUVBL1 and a novel related protein, RUVBL2 (604788). RUVBL1 and RUVBL2 are both highly conserved in evolution and contain ATPase/helicase motifs. The authors showed that RUVBL1 and RUVBL2 are complexed with MYC in vivo and that binding is dependent on a MYC domain essential for oncogenic activity. A missense mutation in the RUVBL1 ATPase motif acted as a dominant inhibitor of MYC oncogenic activity but did not inhibit normal cell growth, indicating that functional RUVBL1 protein is an essential mediator of MYC oncogenic transformation. Wood et al. (2000) concluded that the RUVBL1 and RUVBL2 ATPase/helicase proteins represent a class of cofactors recruited by transcriptional activation domains that function in diverse pathways. Using the N-terminal 284 amino acids of beta-catenin (CTNNB1; 116806), Bauer et al. (1998) identified RUVBL1, which they termed pontin-52, as a 52-kD binding partner of CTNNB1. Using binding analysis, they confirmed that RUVBL1 serves as a bridge between CTNNB1 (residues 187-284) and TBP as predicted by sequence analysis. Bauer et al. (1998) also observed interaction between RUVBL1 and the CTNNB1-lymphoid enhancer-binding factor-1 (LEF1; 153245) complex. Hawley et al. (2001) identified TIP49 as a plasm ... More on the omim web site

Subscribe to this protein entry history

Dec. 2, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.

Oct. 27, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 603449 was added.

Jan. 28, 2016: Protein entry updated
Automatic update: model status changed

Jan. 25, 2016: Protein entry updated
Automatic update: model status changed