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Q9Y230

- RUVB2_HUMAN

UniProt

Q9Y230 - RUVB2_HUMAN

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Protein
RuvB-like 2
Gene
RUVBL2, INO80J, TIP48, TIP49B, CGI-46
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications
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.3 Publications
Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.3 Publications
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 ATF2.3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi77 – 848ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent 5'-3' DNA helicase activity Source: InterPro
  3. ATP-dependent DNA helicase activity Source: ProtInc
  4. DNA helicase activity Source: UniProtKB
  5. RNA polymerase II core promoter sequence-specific DNA binding Source: UniProt
  6. RNA polymerase II distal enhancer sequence-specific DNA binding Source: UniProt
  7. chromatin DNA binding Source: UniProt
  8. damaged DNA binding Source: InterPro
  9. identical protein binding Source: UniProtKB
  10. protein binding Source: UniProtKB
  11. unfolded protein binding Source: ProtInc

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. DNA duplex unwinding Source: GOC
  3. DNA recombination Source: ProtInc
  4. DNA repair Source: ProtInc
  5. cellular response to UV Source: UniProtKB
  6. cellular response to estradiol stimulus Source: UniProt
  7. chromatin organization Source: Reactome
  8. chromatin remodeling Source: UniProt
  9. establishment of protein localization to chromatin Source: UniProt
  10. histone H2A acetylation Source: UniProtKB
  11. histone H4 acetylation Source: UniProtKB
  12. negative regulation of estrogen receptor binding Source: UniProt
  13. positive regulation of histone acetylation Source: UniProt
  14. positive regulation of transcription from RNA polymerase II promoter Source: UniProt
  15. protein folding Source: ProtInc
  16. regulation of growth Source: UniProtKB-KW
  17. transcription, DNA-templated Source: UniProtKB-KW
  18. transcriptional activation by promoter-enhancer looping Source: UniProt
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, Growth regulation, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.
REACT_197820. HATs acetylate histones.
REACT_7974. Telomere Extension By Telomerase.

Names & Taxonomyi

Protein namesi
Recommended name:
RuvB-like 2 (EC:3.6.4.12)
Alternative name(s):
48 kDa TATA box-binding protein-interacting protein
Short name:
48 kDa TBP-interacting protein
51 kDa erythrocyte cytosolic protein
Short name:
ECP-51
INO80 complex subunit J
Repressing pontin 52
Short name:
Reptin 52
TIP49b
TIP60-associated protein 54-beta
Short name:
TAP54-beta
Gene namesi
Name:RUVBL2
Synonyms:INO80J, TIP48, TIP49B
ORF Names:CGI-46
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:10475. RUVBL2.

Subcellular locationi

Nucleus matrix. Nucleusnucleoplasm. Cytoplasm. Membrane
Note: Mainly localized in the nucleus, associated with nuclear matrix or in the nuclear cytosol. Although it is also present in the cytoplasm and associated with the cell membranes.

GO - Cellular componenti

  1. Ino80 complex Source: UniProtKB
  2. MLL1 complex Source: UniProtKB
  3. NuA4 histone acetyltransferase complex Source: UniProtKB
  4. Swr1 complex Source: UniProtKB
  5. cytoplasm Source: HPA
  6. extracellular vesicular exosome Source: UniProt
  7. intracellular Source: LIFEdb
  8. membrane Source: UniProtKB-SubCell
  9. nuclear euchromatin Source: UniProt
  10. nuclear matrix Source: UniProtKB-SubCell
  11. nucleoplasm Source: Reactome
  12. nucleus Source: UniProtKB
  13. ribonucleoprotein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi299 – 2991D → N: Abolishes ATPase activity. 1 Publication

Organism-specific databases

PharmGKBiPA34888.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 463462RuvB-like 2
PRO_0000165644Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y230.
PaxDbiQ9Y230.
PeptideAtlasiQ9Y230.
PRIDEiQ9Y230.

2D gel databases

REPRODUCTION-2DPAGEIPI00009104.

PTM databases

PhosphoSiteiQ9Y230.

Expressioni

Tissue specificityi

Ubiquitously expressed. Highly expressed in testis and thymus.

Gene expression databases

ArrayExpressiQ9Y230.
BgeeiQ9Y230.
CleanExiHS_RUVBL2.
GenevestigatoriQ9Y230.

Organism-specific databases

HPAiCAB012432.
HPA042880.

Interactioni

Subunit structurei

Forms homohexameric rings Inferred. Can form a dodecamer with RUVBL1 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. Interacts With ATF2. 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. RUVBL2 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. 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. 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. Interacts with IGHMBP2. Interacts with TELO2. Interacts with HINT1. Component of a SWR1-like complex.16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-352939,EBI-352939
RUVBL1Q9Y26521EBI-352939,EBI-353675
YY1P254905EBI-352939,EBI-765538

Protein-protein interaction databases

BioGridi116067. 182 interactions.
DIPiDIP-28153N.
IntActiQ9Y230. 79 interactions.
MINTiMINT-1136527.
STRINGi9606.ENSP00000221413.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni24 – 274
Beta strandi41 – 433
Beta strandi46 – 483
Helixi50 – 6415
Beta strandi72 – 787
Helixi83 – 9412
Beta strandi100 – 1045
Helixi105 – 1084
Beta strandi111 – 1133
Helixi115 – 12511
Beta strandi126 – 1294
Beta strandi136 – 14813
Beta strandi152 – 1565
Beta strandi158 – 1647
Beta strandi166 – 1749
Helixi177 – 1848
Beta strandi191 – 1966
Turni197 – 2004
Beta strandi201 – 2066
Beta strandi241 – 2433
Helixi244 – 2507
Helixi270 – 28617
Beta strandi290 – 2934
Beta strandi295 – 3006
Helixi301 – 3033
Helixi306 – 31510
Beta strandi323 – 3297
Beta strandi331 – 3344
Beta strandi341 – 3433
Helixi348 – 3514
Beta strandi354 – 3596
Helixi364 – 37714
Helixi384 – 39613
Helixi399 – 41517
Beta strandi419 – 4213
Helixi423 – 43210
Helixi436 – 4438

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQANMR-A132-213[»]
2XSZX-ray3.00D/E/F2-133[»]
D/E/F238-463[»]
3UK6X-ray2.95A/B/C/D/E/F/G/H/I/J/K/L1-132[»]
A/B/C/D/E/F/G/H/I/J/K/L239-463[»]
ProteinModelPortaliQ9Y230.
SMRiQ9Y230. Positions 24-219, 241-444.

Miscellaneous databases

EvolutionaryTraceiQ9Y230.

Family & Domainsi

Domaini

The C-terminal domain is required for association with ATF2.

Sequence similaritiesi

Belongs to the RuvB family.

Phylogenomic databases

eggNOGiCOG1224.
HOGENOMiHOG000190885.
HOVERGENiHBG054186.
InParanoidiQ9Y230.
KOiK11338.
OMAiGHKQGKL.
OrthoDBiEOG75TMBR.
PhylomeDBiQ9Y230.
TreeFamiTF300469.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR003593. AAA+_ATPase.
IPR004504. DNA_repair_RadA.
IPR027417. P-loop_NTPase.
IPR027238. RuvB-like.
IPR010339. TIP49_C.
[Graphical view]
PANTHERiPTHR11093. PTHR11093. 1 hit.
PfamiPF06068. TIP49. 1 hit.
[Graphical view]
PRINTSiPR01874. DNAREPAIRADA.
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y230-1 [UniParc]FASTAAdd to Basket

« Hide

MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL    50
AARRAAGVVL EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF 100
TAIAGSEIFS LEMSKTEALT QAFRRSIGVR IKEETEIIEG EVVEIQIDRP 150
ATGTGSKVGK LTLKTTEMET IYDLGTKMIE SLTKDKVQAG DVITIDKATG 200
KISKLGRSFT RARDYDAMGS QTKFVQCPDG ELQKRKEVVH TVSLHEIDVI 250
NSRTQGFLAL FSGDTGEIKS EVREQINAKV AEWREEGKAE IIPGVLFIDE 300
VHMLDIESFS FLNRALESDM APVLIMATNR GITRIRGTSY QSPHGIPIDL 350
LDRLLIVSTT PYSEKDTKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR 400
YAIQLITAAS LVCRKRKGTE VQVDDIKRVY SLFLDESRST QYMKEYQDAF 450
LFNELKGETM DTS 463
Length:463
Mass (Da):51,157
Last modified:January 23, 2007 - v3
Checksum:i54C78E9C587D975A
GO

Sequence cautioni

The sequence AAD34041.1 differs from that shown. Reason: Frameshift at position 401.
The sequence AAH08355.1 differs from that shown. Reason: Frameshift at position 191.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti214 – 2141D → N in AAD34041. 1 Publication
Sequence conflicti257 – 2582FL → YV AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y18417 mRNA. Translation: CAB46270.1.
AB024301 mRNA. Translation: BAA76708.1.
AF155138 mRNA. Translation: AAD38073.1.
AF124607 mRNA. Translation: AAF87087.1.
AF151804 mRNA. Translation: AAD34041.1. Frameshift.
AL136743 mRNA. Translation: CAB66677.1.
AK074542 mRNA. Translation: BAC11048.1.
CR533507 mRNA. Translation: CAG38538.1.
BC000428 mRNA. Translation: AAH00428.1.
BC004531 mRNA. Translation: AAH04531.1.
BC008355 mRNA. Translation: AAH08355.1. Frameshift.
CCDSiCCDS42588.1.
PIRiT46313.
RefSeqiNP_006657.1. NM_006666.1.
UniGeneiHs.515846.

Genome annotation databases

EnsembliENST00000595090; ENSP00000473172; ENSG00000183207.
GeneIDi10856.
KEGGihsa:10856.
UCSCiuc002plr.1. human.

Polymorphism databases

DMDMi28201890.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y18417 mRNA. Translation: CAB46270.1 .
AB024301 mRNA. Translation: BAA76708.1 .
AF155138 mRNA. Translation: AAD38073.1 .
AF124607 mRNA. Translation: AAF87087.1 .
AF151804 mRNA. Translation: AAD34041.1 . Frameshift.
AL136743 mRNA. Translation: CAB66677.1 .
AK074542 mRNA. Translation: BAC11048.1 .
CR533507 mRNA. Translation: CAG38538.1 .
BC000428 mRNA. Translation: AAH00428.1 .
BC004531 mRNA. Translation: AAH04531.1 .
BC008355 mRNA. Translation: AAH08355.1 . Frameshift.
CCDSi CCDS42588.1.
PIRi T46313.
RefSeqi NP_006657.1. NM_006666.1.
UniGenei Hs.515846.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CQA NMR - A 132-213 [» ]
2XSZ X-ray 3.00 D/E/F 2-133 [» ]
D/E/F 238-463 [» ]
3UK6 X-ray 2.95 A/B/C/D/E/F/G/H/I/J/K/L 1-132 [» ]
A/B/C/D/E/F/G/H/I/J/K/L 239-463 [» ]
ProteinModelPortali Q9Y230.
SMRi Q9Y230. Positions 24-219, 241-444.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116067. 182 interactions.
DIPi DIP-28153N.
IntActi Q9Y230. 79 interactions.
MINTi MINT-1136527.
STRINGi 9606.ENSP00000221413.

Chemistry

ChEMBLi CHEMBL2062349.

PTM databases

PhosphoSitei Q9Y230.

Polymorphism databases

DMDMi 28201890.

2D gel databases

REPRODUCTION-2DPAGE IPI00009104.

Proteomic databases

MaxQBi Q9Y230.
PaxDbi Q9Y230.
PeptideAtlasi Q9Y230.
PRIDEi Q9Y230.

Protocols and materials databases

DNASUi 10856.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000595090 ; ENSP00000473172 ; ENSG00000183207 .
GeneIDi 10856.
KEGGi hsa:10856.
UCSCi uc002plr.1. human.

Organism-specific databases

CTDi 10856.
GeneCardsi GC19P049497.
HGNCi HGNC:10475. RUVBL2.
HPAi CAB012432.
HPA042880.
MIMi 604788. gene.
neXtProti NX_Q9Y230.
PharmGKBi PA34888.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1224.
HOGENOMi HOG000190885.
HOVERGENi HBG054186.
InParanoidi Q9Y230.
KOi K11338.
OMAi GHKQGKL.
OrthoDBi EOG75TMBR.
PhylomeDBi Q9Y230.
TreeFami TF300469.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.
REACT_197820. HATs acetylate histones.
REACT_7974. Telomere Extension By Telomerase.

Miscellaneous databases

ChiTaRSi RUVBL2. human.
EvolutionaryTracei Q9Y230.
GeneWikii RUVBL2.
GenomeRNAii 10856.
NextBioi 41211.
PROi Q9Y230.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y230.
Bgeei Q9Y230.
CleanExi HS_RUVBL2.
Genevestigatori Q9Y230.

Family and domain databases

Gene3Di 3.40.50.300. 3 hits.
InterProi IPR003593. AAA+_ATPase.
IPR004504. DNA_repair_RadA.
IPR027417. P-loop_NTPase.
IPR027238. RuvB-like.
IPR010339. TIP49_C.
[Graphical view ]
PANTHERi PTHR11093. PTHR11093. 1 hit.
Pfami PF06068. TIP49. 1 hit.
[Graphical view ]
PRINTSi PR01874. DNAREPAIRADA.
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation, molecular characterization, and tissue-specific expression of ECP-51 and ECP-54 (TIP49), two homologous, interacting erythroid cytosolic proteins."
    Salzer U., Kubicek M., Prohaska R.
    Biochim. Biophys. Acta 1446:365-370(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 72-83; 131-144; 212-223; 369-372 AND 440-457.
    Tissue: Bone marrow.
  2. "TIP49b, a new RuvB-like DNA helicase, is included in a complex together with another RuvB-like DNA helicase, TIP49a."
    Kanemaki M., Kurokawa Y., Matsu-ura T., Makino Y., Masani A., Okazaki K., Morishita T., Tamura T.-A.
    J. Biol. Chem. 274:22437-22444(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INTERACTION WITH RUVBL1.
    Tissue: Liver.
  3. "Human TIP49b/RUVBL2 gene: genomic structure, expression pattern, physical link to the human CGB/LHB gene cluster on chromosome 19q13.3."
    Parfait B., Giovangrandi Y., Asheuer M., Laurendeau I., Olivi M., Vodovar N., Vidaud D., Vidaud M., Bieche I.
    Ann. Genet. 43:69-74(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary gland.
  4. "Pontin52 and reptin52 function as antagonistic regulators of beta-catenin signalling activity."
    Bauer A., Chauvet S., Huber O., Usseglio F., Rothbaecher U., Aragnol D., Kemler R., Pradel J.
    EMBO J. 19:6121-6130(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal liver.
  5. "An ATPase/helicase complex is an essential cofactor for oncogenic transformation by c-Myc."
    Wood M.A., McMahon S.B., Cole M.D.
    Mol. Cell 5:321-330(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 73-83; 116-124; 237-253 AND 254-269, INTERACTION WITH MYC.
  6. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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 T.-O., 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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  9. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  10. "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: Colon and Lung.
  11. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-14.
    Tissue: Platelet.
  12. Bienvenut W.V., Heiserich L., Gottlieb E.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-18; 30-53; 55-64; 72-83; 116-124; 165-177; 237-269; 335-368; 393-400 AND 418-438, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  13. "Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis."
    Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J., Horikoshi M., Scully R., Qin J., Nakatani Y.
    Cell 102:463-473(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-40; 185-197; 354-365 AND 417-427, IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  14. "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
    Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
    J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-40; 72-83; 165-177; 187-197; 254-269; 354-365; 418-438 AND 445-463, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  15. "TIP49b, a regulator of activating transcription factor 2 response to stress and DNA damage."
    Cho S.-G., Bhoumik A., Broday L., Ivanov V., Rosenstein B., Ronai Z.
    Mol. Cell. Biol. 21:8398-8413(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATF2.
  16. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
    Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
    Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION IN A NUA4-RELATED SRCAP-CONTAINING COMPLEX.
  17. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
    Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
    Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
  18. Cited for: IDENTIFICATION IN INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  19. "The histidine triad protein Hint1 interacts with Pontin and Reptin and inhibits TCF-beta-catenin-mediated transcription."
    Weiske J., Huber O.
    J. Cell Sci. 118:3117-3129(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HINT1, FUNCTION.
  20. "Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex."
    Puri T., Wendler P., Sigala B., Saibil H., Tsaneva I.R.
    J. Mol. Biol. 366:179-192(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, MUTAGENESIS OF ASP-299, ELECTRON MICROSCOPY OF THE RUVBL1-RUVBL2 HETEROMER.
  21. "A YY1-INO80 complex regulates genomic stability through homologous recombination-based repair."
    Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H., Wang W., Nickoloff J.A., Wu C., Shi Y.
    Nat. Struct. Mol. Biol. 14:1165-1172(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE INO80 COMPLEX, PROTEIN INTERACTION.
  22. "Transcriptional activation of histone genes requires NPAT-dependent recruitment of TRRAP-Tip60 complex to histone promoters during the G1/S phase transition."
    DeRan M., Pulvino M., Greene E., Su C., Zhao J.
    Mol. Cell. Biol. 28:435-447(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NPAT.
  23. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Biochemical and genetic evidence for a role of IGHMBP2 in the translational machinery."
    de Planell-Saguer M., Schroeder D.G., Rodicio M.C., Cox G.A., Mourelatos Z.
    Hum. Mol. Genet. 18:2115-2126(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGHMBP2.
  25. "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes."
    Takai H., Xie Y., de Lange T., Pavletich N.P.
    Genes Dev. 24:2019-2030(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TELO2.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Subunit organization of the human INO80 chromatin remodeling complex: An evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling."
    Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P., Conaway J.W., Conaway R.C.
    J. Biol. Chem. 286:11283-11289(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE INO80 COMPLEX.
  28. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
  30. "Solution structure of RSGI RUH-039, a fragment of C-terminal domain of RuvB-like 2 from human cDNA."
    Mycobacterium tuberculosis structural genomics consortium (TB)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 132-213.

Entry informationi

Entry nameiRUVB2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y230
Secondary accession number(s): Q6FIB9, Q6PK27, Q9Y361
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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