Q9Y230 (RUVB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	RUVBL2
Synonyms:	INO80J, TIP48, TIP49B
ORF Names:	CGI-46

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.16 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. Ref.16 Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Ref.16 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. Ref.16
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Forms homohexameric rings Probable. 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 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. Interacts with IGHMBP2. Interacts with TELO2. Ref.2 Ref.5 Ref.15 Ref.19 Ref.20 Ref.22 Ref.24 Ref.25
Subcellular location	Nucleus matrix. Nucleus › nucleoplasm. 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.
Tissue specificity	Ubiquitously expressed. Highly expressed in testis and thymus.
Domain	The C-terminal domain is required for association with ATF2.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.21
Sequence similarities	Belongs to the RuvB family.
Sequence caution	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.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair Growth regulation Transcription Transcription regulation
Cellular component	Cytoplasm Membrane Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator Chromatin regulator Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA recombination Traceable author statement. Source: ProtInc DNA repair Traceable author statement. Source: ProtInc cellular response to UV Inferred from mutant phenotype Ref.20. Source: UniProtKB histone H2A acetylation Inferred from direct assay Ref.16. Source: UniProtKB histone H4 acetylation Inferred from direct assay Ref.16. Source: UniProtKB protein folding Traceable author statement. Source: ProtInc 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 component	Ino80 complex Inferred from direct assay Ref.20Ref.27. Source: UniProtKB MLL1 complex Inferred from direct assay Ref.17. Source: UniProtKB NuA4 histone acetyltransferase complex Inferred from direct assay Ref.13Ref.16. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent DNA helicase activity Traceable author statement. Source: ProtInc damaged DNA binding Inferred from electronic annotation. Source: InterPro identical protein binding Inferred from direct assay Ref.13. Source: UniProtKB unfolded protein binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-352939,EBI-352939
RUVBL1	Q9Y265	21	EBI-352939,EBI-353675
YY1	P25490	5	EBI-352939,EBI-765538

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.11 Ref.12

Chain

2 – 463

462

RuvB-like 2

PRO_0000165644

Regions

Nucleotide binding

77 – 84

8

ATP

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.12 Ref.23

Modified residue

220

1

Phosphoserine Ref.21

Experimental info

Mutagenesis

299

1

D → N: Abolishes ATPase activity. Ref.19

Sequence conflict

214

1

D → N in AAD34041. Ref.6

Sequence conflict

257 – 258

2

FL → YV AA sequence Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

463

Helix Strand Turn

Details...

Beta strand

135 – 147

13

Beta strand

151 – 155

5

Beta strand

157 – 163

7

Beta strand

165 – 173

9

Helix

176 – 183

8

Beta strand

190 – 195

6

Turn

196 – 199

4

Beta strand

200 – 205

6

Sequences

	Sequence		Length	Mass (Da)
	Q9Y230 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 54C78E9C587D975A	FASTA	463	51,157
	10 20 30 40 50 60 MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL 70 80 90 100 110 120 EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF TAIAGSEIFS LEMSKTEALT 130 140 150 160 170 180 QAFRRSIGVR IKEETEIIEG EVVEIQIDRP ATGTGSKVGK LTLKTTEMET IYDLGTKMIE 190 200 210 220 230 240 SLTKDKVQAG DVITIDKATG KISKLGRSFT RARDYDAMGS QTKFVQCPDG ELQKRKEVVH 250 260 270 280 290 300 TVSLHEIDVI NSRTQGFLAL FSGDTGEIKS EVREQINAKV AEWREEGKAE IIPGVLFIDE 310 320 330 340 350 360 VHMLDIESFS FLNRALESDM APVLIMATNR GITRIRGTSY QSPHGIPIDL LDRLLIVSTT 370 380 390 400 410 420 PYSEKDTKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR YAIQLITAAS LVCRKRKGTE 430 440 450 460 VQVDDIKRVY SLFLDESRST QYMKEYQDAF LFNELKGETM DTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10524211] [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: 10428817] [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: 10998447] [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: 11080158] [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: 10882073] [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: 10810093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] 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: 14702039] [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: 15489334] [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: 12665801] [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, 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: 10966108] [Abstract] Cited for: PROTEIN SEQUENCE OF 30-40; 185-197; 354-365 AND 417-427, IDENTIFICATION IN THE NUA4 COMPLEX, 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: 12963728] [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, 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: 11713276] [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: 14966270] [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: 15960975] [Abstract] Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[18]	"A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex." Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K., Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A., Washburn M.P., Conaway R.C., Conaway J.W. J. Biol. Chem. 280:41207-41212(2005) [PubMed: 16230350] [Abstract] Cited for: IDENTIFICATION IN INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[19]	"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: 17157868] [Abstract] Cited for: SUBUNIT, MUTAGENESIS OF ASP-299, ELECTRON MICROSPCOPY OF THE RUVBL1-RUVBL2 HETEROMER.
[20]	"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: 18026119] [Abstract] Cited for: IDENTIFICATION IN THE INO80 COMPLEX, PROTEIN INTERACTION.
[21]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 17967892] [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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 19299493] [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: 20801936] [Abstract] Cited for: INTERACTION WITH TELO2.
[26]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] 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: 21303910] [Abstract] Cited for: IDENTIFICATION IN THE INO80 COMPLEX.
[28]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00009104.

PIR

T46313.

RefSeq

NP_006657.1. NM_006666.1.

UniGene

Hs.515846.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CQA	NMR	-	A	132-212	[»]
2XSZ	X-ray	3.00	D/E/F	2-463	[»]

ProteinModelPortal

Q9Y230.

SMR

Q9Y230. Positions 22-219, 239-456.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-28153N.

IntAct

Q9Y230. 59 interactions.

MINT

MINT-1136527.

STRING

Q9Y230.

PTM databases

PhosphoSite

Q9Y230.

Polymorphism databases

DMDM

28201890.

2D gel databases

REPRODUCTION-2DPAGE

IPI00009104.

Proteomic databases

PeptideAtlas

Q9Y230.

PRIDE

Q9Y230.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000221413; ENSP00000221413; ENSG00000183207.

GeneID

10856.

KEGG

hsa:10856.

UCSC

uc002plr.1. human.

Organism-specific databases

CTD

10856.

GeneCards

GC19P049497.

H-InvDB

HIX0015312.

HGNC

HGNC:10475. RUVBL2.

HPA

CAB012432.

MIM

604788. gene.

neXtProt

NX_Q9Y230.

PharmGKB

PA34888.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07249.

GeneTree

ENSGT00550000075034.

HOGENOM

HBG749829.

HOVERGEN

HBG054186.

InParanoid

Q9Y230.

OMA

TQAFRKS.

OrthoDB

EOG4K0QND.

PhylomeDB

Q9Y230.

Gene expression databases

ArrayExpress

Q9Y230.

Bgee

Q9Y230.

CleanEx

HS_RUVBL2.

Genevestigator

Q9Y230.

GermOnline

ENSG00000183207. Homo sapiens.

Family and domain databases

InterPro

IPR003593. ATPase_AAA+_core.
IPR004504. DNA_repair_RadA.
IPR016027. NA-bd_OB-fold-like.
IPR010339. TIP49_C.
[Graphical view]

KO

K11338.

Pfam

PF06068. TIP49. 1 hit.
[Graphical view]

PRINTS

PR01874. DNAREPAIRADA.

SMART

SM00382. AAA. 1 hit.
[Graphical view]

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.

ProtoNet

Search...

Other

NextBio

41211.

SOURCE

Search...

Entry information

Entry name

RUVB2_HUMAN

Accession

Primary (citable) accession number: Q9Y230
Secondary accession number(s): Q6FIB9, Q6PK27, Q9Y361

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2003
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 136 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.