Hmdb loader

Showing Protein RuvB-like 2 (HMDBP07373)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 7 metabolites
Identification
HMDB Protein ID HMDBP07373
Secondary Accession Numbers
  • 13027
Name RuvB-like 2
Synonyms
  1. 48 kDa TATA box-binding protein-interacting protein
  2. 48 kDa TBP-interacting protein
  3. 51 kDa erythrocyte cytosolic protein
  4. ECP-51
  5. INO80 complex subunit J
  6. Repressing pontin 52
  7. Reptin 52
  8. TAP54-beta
  9. TIP49b
  10. TIP60-associated protein 54-beta
Gene Name RUVBL2
Protein Type Enzyme
Biological Properties
General Function Involved in nucleotide binding
Specific Function Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (5' to 3') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase 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. Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. May also inhibit the transcriptional activity of ATF2.
Pathways
  • Pterine Biosynthesis
Reactions
Adenosine triphosphate + Water → ADP + Phosphate details
GO Classification
Biological Process
histone H2A acetylation
protein folding
DNA repair
histone H4 acetylation
cellular response to UV
regulation of transcription, DNA-dependent
transcription, DNA-dependent
regulation of growth
DNA recombination
Cellular Component
NuA4 histone acetyltransferase complex
cytoplasm
nuclear matrix
Ino80 complex
MLL1 complex
membrane
ribonucleoprotein complex
Function
binding
nucleotide binding
catalytic activity
hydrolase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
dna helicase activity
damaged dna binding
nucleic acid binding
dna binding
nucleoside-triphosphatase activity
helicase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
pyrophosphatase activity
Molecular Function
unfolded protein binding
ATP binding
ATP-dependent DNA helicase activity
damaged DNA binding
identical protein binding
Process
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
dna metabolic process
dna repair
Cellular Location
  1. Nucleus
  2. Cytoplasm
  3. Membrane
  4. nucleoplasm
  5. Nucleus matrix
Gene Properties
Chromosome Location 19
Locus 19q13.3
SNPs RUVBL2
Gene Sequence 
>1392 bp
ATGGCAACCGTTACAGCCACAACCAAAGTCCCGGAGATCCGTGATGTAACAAGGATTGAG
CGAATCGGTGCCCACTCCCACATCCGGGGACTGGGGCTGGACGATGCCTTGGAGCCTCGG
CAGGCTTCGCAAGGCATGGTGGGTCAGCTGGCGGCACGGCGGGCGGCTGGCGTGGTGCTG
GAGATGATCCGGGAAGGGAAGATTGCCGGTCGGGCAGTCCTTATTGCTGGCCAGCCGGGC
ACGGGGAAGACGGCCATCGCCATGGGCATGGCGCAGGCCCTGGGCCCTGACACGCCATTC
ACAGCCATCGCCGGCAGTGAAATCTTCTCCCTGGAGATGAGCAAGACCGAGGCGCTGACG
CAGGCCTTCCGGCGGTCCATCGGCGTTCGCATCAAGGAGGAGACGGAGATCATCGAAGGG
GAGGTGGTGGAGATCCAGATTGATCGACCAGCAACAGGGACGGGCTCCAAGGTGGGCAAA
CTGACCCTCAAGACCACAGAGATGGAGACCATCTACGACCTGGGCACCAAGATGATTGAG
TCCCTGACCAAGGACAAGGTCCAGGCCGGGGACGTGATCACCATCGACAAGGCGACGGGC
AAGATCTCCAAGCTGGGCCGCTCCTTCACACGCGCCCGCGACTACGACGCTATGGGCTCC
CAGACCAAGTTCGTGCAGTGCCCAGATGGGGAGCTCCAGAAACGCAAGGAGGTGGTGCAC
ACCGTGTCCCTGCACGAGATCGACGTCATCAACTCTCGCACCCAGGGCTTCCTGGCGCTC
TTCTCAGGTGACACAGGGGAGATCAAGTCAGAAGTCCGTGAGCAGATCAATGCCAAGGTG
GCTGAGTGGCGCGAGGAGGGCAAGGCGGAGATCATCCCTGGAGTGCTGTTCATCGACGAG
GTCCACATGCTGGACATCGAGAGCTTCTCCTTCCTCAACCGGGCCCTGGAGAGTGACATG
GCGCCTGTCCTGATCATGGCCACCAACCGTGGCATCACGCGAATCCGGGGCACCAGCTAC
CAGAGCCCTCACGGCATCCCCATAGACCTGCTGGACCGGCTGCTTATCGTCTCCACCACC
CCCTACAGCGAGAAAGACACGAAGCAGATCCTCCGCATCCGGTGCGAGGAAGAAGATGTG
GAGATGAGTGAGGACGCCTACACGGTGCTGACCCGCATCGGGCTGGAGACGTCACTGCGC
TACGCCATCCAGCTCATCACAGCTGCCAGCTTGGTGTGCCGGAAACGCAAGGGTACAGAA
GTGCAGGTGGATGACATCAAGCGGGTCTACTCACTCTTCCTGGACGAGTCCCGCTCCACG
CAGTACATGAAGGAGTACCAGGACGCCTTCCTCTTCAACGAACTCAAAGGCGAGACCATG
GACACCTCCTGA
Protein Properties
Number of Residues 463
Molecular Weight 51156.08
Theoretical pI 5.642
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>RuvB-like 2
MATVTATTKVPEIRDVTRIERIGAHSHIRGLGLDDALEPRQASQGMVGQLAARRAAGVVL
EMIREGKIAGRAVLIAGQPGTGKTAIAMGMAQALGPDTPFTAIAGSEIFSLEMSKTEALT
QAFRRSIGVRIKEETEIIEGEVVEIQIDRPATGTGSKVGKLTLKTTEMETIYDLGTKMIE
SLTKDKVQAGDVITIDKATGKISKLGRSFTRARDYDAMGSQTKFVQCPDGELQKRKEVVH
TVSLHEIDVINSRTQGFLALFSGDTGEIKSEVREQINAKVAEWREEGKAEIIPGVLFIDE
VHMLDIESFSFLNRALESDMAPVLIMATNRGITRIRGTSYQSPHGIPIDLLDRLLIVSTT
PYSEKDTKQILRIRCEEEDVEMSEDAYTVLTRIGLETSLRYAIQLITAASLVCRKRKGTE
VQVDDIKRVYSLFLDESRSTQYMKEYQDAFLFNELKGETMDTS
GenBank ID Protein 4587311
UniProtKB/Swiss-Prot ID Q9Y230
UniProtKB/Swiss-Prot Entry Name RUVB2_HUMAN
PDB IDs
GenBank Gene ID AB024301
GeneCard ID RUVBL2
GenAtlas ID RUVBL2
HGNC ID HGNC:10475
References
General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  4. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed:11230166 ]
  5. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed:17525332 ]
  6. Cai Y, Jin J, Tomomori-Sato C, Sato S, Sorokina I, Parmely TJ, Conaway RC, Conaway JW: Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex. J Biol Chem. 2003 Oct 31;278(44):42733-6. Epub 2003 Sep 8. [PubMed:12963728 ]
  7. Ikura T, Ogryzko VV, Grigoriev M, Groisman R, Wang J, Horikoshi M, Scully R, Qin J, Nakatani Y: Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell. 2000 Aug 18;102(4):463-73. [PubMed:10966108 ]
  8. Doyon Y, Selleck W, Lane WS, Tan S, Cote J: Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans. Mol Cell Biol. 2004 Mar;24(5):1884-96. [PubMed:14966270 ]
  9. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed:12665801 ]
  10. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed:10810093 ]
  11. Dou Y, Milne TA, Tackett AJ, Smith ER, Fukuda A, Wysocka J, Allis CD, Chait BT, Hess JL, Roeder RG: Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell. 2005 Jun 17;121(6):873-85. [PubMed:15960975 ]
  12. Salzer U, Kubicek M, Prohaska R: Isolation, molecular characterization, and tissue-specific expression of ECP-51 and ECP-54 (TIP49), two homologous, interacting erythroid cytosolic proteins. Biochim Biophys Acta. 1999 Sep 3;1446(3):365-70. [PubMed:10524211 ]
  13. Kanemaki M, Kurokawa Y, Matsu-ura T, Makino Y, Masani A, Okazaki K, Morishita T, Tamura TA: TIP49b, a new RuvB-like DNA helicase, is included in a complex together with another RuvB-like DNA helicase, TIP49a. J Biol Chem. 1999 Aug 6;274(32):22437-44. [PubMed:10428817 ]
  14. Parfait B, Giovangrandi Y, Asheuer M, Laurendeau I, Olivi M, Vodovar N, Vidaud D, Vidaud M, Bieche I: Human TIP49b/RUVBL2 gene: genomic structure, expression pattern, physical link to the human CGB/LHB gene cluster on chromosome 19q13.3. Ann Genet. 2000 Apr-Jun;43(2):69-74. [PubMed:10998447 ]
  15. Bauer A, Chauvet S, Huber O, Usseglio F, Rothbacher U, Aragnol D, Kemler R, Pradel J: Pontin52 and reptin52 function as antagonistic regulators of beta-catenin signalling activity. EMBO J. 2000 Nov 15;19(22):6121-30. [PubMed:11080158 ]
  16. Wood MA, McMahon SB, Cole MD: An ATPase/helicase complex is an essential cofactor for oncogenic transformation by c-Myc. Mol Cell. 2000 Feb;5(2):321-30. [PubMed:10882073 ]
  17. Cho SG, Bhoumik A, Broday L, Ivanov V, Rosenstein B, Ronai Z: TIP49b, a regulator of activating transcription factor 2 response to stress and DNA damage. Mol Cell Biol. 2001 Dec;21(24):8398-413. [PubMed:11713276 ]
  18. Jin J, Cai Y, Yao T, Gottschalk AJ, Florens L, Swanson SK, Gutierrez JL, Coleman MK, Workman JL, Mushegian A, Washburn MP, Conaway RC, Conaway JW: A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex. J Biol Chem. 2005 Dec 16;280(50):41207-12. Epub 2005 Oct 17. [PubMed:16230350 ]
  19. DeRan M, Pulvino M, Greene E, Su C, Zhao J: Transcriptional activation of histone genes requires NPAT-dependent recruitment of TRRAP-Tip60 complex to histone promoters during the G1/S phase transition. Mol Cell Biol. 2008 Jan;28(1):435-47. Epub 2007 Oct 29. [PubMed:17967892 ]
  20. de Planell-Saguer M, Schroeder DG, Rodicio MC, Cox GA, Mourelatos Z: Biochemical and genetic evidence for a role of IGHMBP2 in the translational machinery. Hum Mol Genet. 2009 Jun 15;18(12):2115-26. doi: 10.1093/hmg/ddp134. Epub 2009 Mar 19. [PubMed:19299493 ]