Q9Y265 (RUVB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RuvB-like 1
EC=3.6.4.12

Alternative name(s):
49 kDa TATA box-binding protein-interacting protein
Short name=49 kDa TBP-interacting protein
54 kDa erythrocyte cytosolic protein
Short name=ECP-54
INO80 complex subunit H
Nuclear matrix protein 238
Short name=NMP 238
Pontin 52
TIP49a
TIP60-associated protein 54-alpha
Short name=TAP54-alpha

Gene names

Name:	RUVBL1
Synonyms:	INO80H, NMP238, TIP49, TIP49A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6 Ref.18 Ref.20 Ref.22 Ref.23 Ref.26 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.6 Ref.18 Ref.20 Ref.22 Ref.23 Ref.26 Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Ref.6 Ref.18 Ref.20 Ref.22 Ref.23 Ref.26 Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. Essential for cell proliferation. Ref.6 Ref.18 Ref.20 Ref.22 Ref.23 Ref.26 May be able to bind plasminogen at cell surface and enhance plasminogen activation. Ref.6 Ref.18 Ref.20 Ref.22 Ref.23 Ref.26
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Forms homohexameric rings. Can form a dodecamer with RUVBL2 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. 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. 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. 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 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. Associates with alpha and gamma tubulins, particularly during metaphase and early anaphase. 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. Interacts with IGHMBP2. Interacts with OFD1. Interacts with HINT1. Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.34 Ref.35
Subcellular location	Nucleus matrix. Nucleus › nucleoplasm. Cytoplasm. Membrane. Cytoplasm › cytoskeleton › centrosome. 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. In prophase and prometaphase it is located at the centrosome and the branching microtubule spindles. After mitotic nuclear membrane disintigration it accumulates at the centrosome and sites of tubulin polymerization. As cells pass through metaphase and into telophase it is located close to the centrosome at the early phase of tubulin polymerization. In anaphase it accumulates at the zone of tubule interdigitation. In telophase it is found at polar tubule overlap, and it reappears at the site of chromosomal decondensation in the daughter cells. Ref.18 Ref.26
Tissue specificity	Ubiquitously expressed with high expression in heart, skeletal muscle and testis.
Domain	Binding to MYC is dependent on a Myc domain essential for oncogenic activity.
Miscellaneous	High level of autoantibodies against RUVBL1 are detected in sera of patients with autoimmune diseases such as polymyositis/dermatomyosistis and autoimmune hepatitis.
Sequence similarities	Belongs to the RuvB family.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA damage DNA recombination DNA repair Growth regulation Mitosis Transcription Transcription regulation
Cellular component	Cytoplasm Cytoskeleton Membrane Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator Chromatin regulator Helicase Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	CENP-A containing nucleosome assembly at centromere Traceable author statement. Source: Reactome DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA repair Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW histone H2A acetylation Inferred from direct assay Ref.23. Source: UniProtKB histone H4 acetylation Inferred from direct assay Ref.23. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription from RNA polymerase II promoter Traceable author statement Ref.2. Source: ProtInc spermatogenesis Traceable author statement Ref.1. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA Ino80 complex Inferred from direct assay Ref.29Ref.34. Source: UniProtKB MLL1 complex Inferred from direct assay Ref.24. Source: UniProtKB NuA4 histone acetyltransferase complex Inferred from direct assay Ref.17Ref.23. Source: UniProtKB membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule organizing center 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 DNA helicase activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DKC1	O60832	5	EBI-353675,EBI-713091
RUVBL2	Q9Y230	21	EBI-353675,EBI-352939
TERT	O14746	11	EBI-353675,EBI-1772203
VPS72	Q15906	6	EBI-353675,EBI-399189
YY1	P25490	4	EBI-353675,EBI-765538

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y265-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9Y265-2)

The sequence of this isoform differs from the canonical sequence as follows:
     374-386: IIKIRAQTEGINI → VLSAAADPGQLAC
     387-456: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 456

456

RuvB-like 1

PRO_0000165639

Regions

Nucleotide binding

70 – 77

8

ATP By similarity

Amino acid modifications

Modified residue

453

1

N6-acetyllysine Ref.32

Natural variations

Alternative sequence

374 – 386

13

IIKIR…EGINI → VLSAAADPGQLAC in isoform 2.

VSP_021387

Alternative sequence

387 – 456

70

Missing in isoform 2.

VSP_021388

Experimental info

Mutagenesis

302

1

D → N: Abolishes ATPase activity; inhibition of MYC- and CTNNB1-mediated transformation. Ref.15 Ref.22 Ref.27 Ref.35

Sequence conflict

52

1

I → T in BAD96283. Ref.12

Sequence conflict

145

1

N → D in BAD96295. Ref.12

Sequence conflict

285

1

K → R in ABF13334. Ref.8

Sequence conflict

353

1

D → P in ABF13334. Ref.8

Secondary structure

1

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456

Helix Strand Turn

Details...

Helix

10 – 16

7

Turn

17 – 20

4

Beta strand

28 – 30

3

Beta strand

34 – 36

3

Beta strand

39 – 41

3

Helix

43 – 57

15

Beta strand

65 – 69

5

Beta strand

72 – 75

4

Helix

76 – 87

12

Beta strand

93 – 97

5

Helix

98 – 101

4

Beta strand

104 – 106

3

Helix

108 – 118

11

Beta strand

119 – 140

22

Beta strand

157 – 163

7

Beta strand

166 – 172

7

Helix

174 – 182

9

Beta strand

189 – 194

6

Turn

195 – 197

3

Beta strand

200 – 206

7

Beta strand

216 – 221

6

Beta strand

228 – 239

12

Helix

240 – 245

6

Helix

278 – 288

11

Beta strand

291 – 296

6

Beta strand

298 – 303

6

Helix

304 – 306

3

Helix

309 – 318

10

Beta strand

326 – 331

6

Beta strand

334 – 337

4

Beta strand

345 – 347

3

Helix

352 – 355

4

Beta strand

358 – 362

5

Helix

368 – 382

15

Helix

388 – 400

13

Helix

403 – 408

6

Helix

410 – 419

10

Beta strand

423 – 425

3

Helix

427 – 436

10

Helix

440 – 448

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 6095ADE692B1482B	FASTA	456	50,228
	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 IAELVPGVLF 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
	Isoform 2 [UniParc]. Checksum: 6F19852DA93A435A	FASTA	386	42,127
	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 IAELVPGVLF 310 320 330 340 350 360 VDEVHMLDIE CFTYLHRALE SSIAPIVIFA SNRGNCVIRG TEDITSPHGI PLDLLDRVMI 370 380 IRTMLYTPQE MKQVLSAAAD PGQLAC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"TIP49, homologous to the bacterial DNA helicase RuvB, acts as an autoantigen in human." Makino Y., Mimori T., Koike C., Kanemaki M., Kurokawa Y., Inoue S., Kishimoto T., Tamura T.-A. Biochem. Biophys. Res. Commun. 245:819-823(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[2]	"Identification and characterization of the ubiquitously occurring nuclear matrix protein NMP 238." Holzmann K., Gerner C., Korosec T., Poeltl A., Grimm R., Sauermann G. Biochem. Biophys. Res. Commun. 252:39-45(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 1-7. Tissue: Pancreas.
[3]	"An eukaryotic RuvB-like protein (RUVBL1) essential for growth." Qiu X.-B., Lin Y.-L., Thome K.C., Pian P., Schlegel B.P., Weremowicz S., Parvin J.D., Dutta A. J. Biol. Chem. 273:27786-27793(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[4]	"Pontin52, an interaction partner of beta-catenin, binds to the TATA box binding protein." Bauer A., Huber O., Kemler R. Proc. Natl. Acad. Sci. U.S.A. 95:14787-14792(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Colon adenocarcinoma.
[5]	"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] (ISOFORM 1), PROTEIN SEQUENCE OF 34-46; 108-118; 169-177; 207-219 AND 446-456. Tissue: Bone marrow.
[6]	"Purification, cloning, and characterization of a profibrinolytic plasminogen-binding protein, TIP49a." Hawley S.B., Tamura T.-A., Miles L.A. J. Biol. Chem. 276:179-186(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 172-182 AND 184-201, FUNCTION.
[7]	"The genomic structure of the human pontin 52 gene." Huber O., Orso S. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[8]	"RUVBL1-FK- splice variant." Koc F., Gartner W., Birkenkamp-Demtroeder K., Altenberger T., Daneva T., Wagner L. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[9]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[10]	"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] (ISOFORM 1). Tissue: Cerebellum.
[11]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Adipose tissue and Coronary artery.
[12]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[13]	"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] (ISOFORM 1). Tissue: Lung.
[14]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 23-33; 65-90; 153-162; 172-182; 318-333; 340-357; 363-372 AND 379-400, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[15]	"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: PROTEIN SEQUENCE OF 23-33 AND 77-90, INTERACTION WITH MYC, MUTAGENESIS OF ASP-302.
[16]	"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 23-33; 34-46; 77-90; 172-182; 185-201; 340-357 AND 405-418 (ISOFORM 1), IDENTIFICATION IN NUA4 COMPLEX, MASS SPECTROMETRY.
[17]	"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 34-46 AND 108-117, IDENTIFICATION IN NUA4 COMPLEX, MASS SPECTROMETRY.
[18]	"The ATP-dependent helicase RUVBL1/TIP49a associates with tubulin during mitosis." Gartner W., Rossbacher J., Zierhut B., Daneva T., Base W., Weissel M., Waldhausl W., Pasternack M.S., Wagner L. Cell Motil. Cytoskeleton 56:79-93(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 34-46, FUNCTION, INTERACTION WITH TUBULIN, SUBCELLULAR LOCATION. Tissue: Monocyte.
[19]	"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: INTERACTION WITH RUVBL2.
[20]	"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: FUNCTION.
[21]	"BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation." Park J., Wood M.A., Cole M.D. Mol. Cell. Biol. 22:1307-1316(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN BAF53 COMPLEX WITH ACTL6A; SMARCA2 AND TRRAP.
[22]	"TIP49 regulates beta-catenin-mediated neoplastic transformation and T-cell factor target gene induction via effects on chromatin remodeling." Feng Y., Lee N., Fearon E.R. Cancer Res. 63:8726-8734(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-302.
[23]	"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.
[24]	"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.
[25]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[26]	"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, SUBCELLULAR LOCATION.
[27]	"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-302, ELECTRON MICROSCOPY OF THE RUVBL1-RUVBL2 HETEROMER.
[28]	"Functional characterization of the OFD1 protein reveals a nuclear localization and physical interaction with subunits of a chromatin remodeling complex." Giorgio G., Alfieri M., Prattichizzo C., Zullo A., Cairo S., Franco B. Mol. Biol. Cell 18:4397-4404(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH OFD1.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-453, MASS SPECTROMETRY.
[33]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]	"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.
[35]	"Crystal structure of the human AAA+ protein RuvBL1." Matias P.M., Gorynia S., Donner P., Carrondo M.A. J. Biol. Chem. 281:38918-38929(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, MUTAGENESIS OF ASP-302.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB012122 mRNA. Translation: BAA28169.1.
AJ010058 mRNA. Translation: CAA08986.1.
AF070735 mRNA. Translation: AAC77819.1.
AF099084 mRNA. Translation: AAD04427.1.
Y18418 mRNA. Translation: CAB46271.1.
AF380344, AF380343 Genomic DNA. Translation: AAM45570.1.
DQ469310 mRNA. Translation: ABF13334.1.
BT007057 mRNA. Translation: AAP35706.1.
AK222563 mRNA. Translation: BAD96283.1.
AK222575 mRNA. Translation: BAD96295.1.
AK312290 mRNA. Translation: BAG35217.1.
AB451224 mRNA. Translation: BAG70038.1.
BC002993 mRNA. Translation: AAH02993.1.
BC012886 mRNA. Translation: AAH12886.1.

IPI

IPI00021187.
IPI00788942.

PIR

JE0334.

RefSeq

NP_003698.1. NM_003707.2.

UniGene

Hs.272822.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C9O	X-ray	2.20	A/B/C	1-456	[»]
2XSZ	X-ray	3.00	A/B/C	2-456	[»]

ProteinModelPortal

Q9Y265.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29937N.

IntAct

Q9Y265. 61 interactions.

MINT

MINT-1138777.

STRING

9606.ENSP00000318297.

PTM databases

PhosphoSite

Q9Y265.

Polymorphism databases

DMDM

28201891.

2D gel databases

OGP

Q9Y265.

REPRODUCTION-2DPAGE

Q9Y265.

SWISS-2DPAGE

Q9Y265.

Proteomic databases

PaxDb

Q9Y265.

PeptideAtlas

Q9Y265.

PRIDE

Q9Y265.

Protocols and materials databases

DNASU

8607.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000322623; ENSP00000318297; ENSG00000175792.
ENST00000417360; ENSP00000393755; ENSG00000175792.

GeneID

8607.

KEGG

hsa:8607.

UCSC

uc003ekh.3. human.
uc010hss.3. human.

Organism-specific databases

CTD

8607.

GeneCards

GC03M127783.

HGNC

HGNC:10474. RUVBL1.

HPA

HPA019947.
HPA019948.

MIM

603449. gene.

neXtProt

NX_Q9Y265.

PharmGKB

PA34887.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1224.

HOVERGEN

HBG054186.

InParanoid

Q9Y265.

KO

K04499.

OMA

GNKVPFC.

OrthoDB

EOG46Q6SH.

PhylomeDB

Q9Y265.

Enzyme and pathway databases

Reactome

REACT_115566. Cell Cycle.

Gene expression databases

ArrayExpress

Q9Y265.

Bgee

Q9Y265.

CleanEx

HS_RUVBL1.

Genevestigator

Q9Y265.

GermOnline

ENSG00000175792. Homo sapiens.

Family and domain databases

InterPro

IPR003593. AAA+_ATPase.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR027238. RuvB-like.
IPR010339. TIP49_C.
[Graphical view]

PANTHER

PTHR11093. PTHR11093. 1 hit.

Pfam

PF06068. TIP49. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
[Graphical view]

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.
SSF52540. SSF52540. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

RUVBL1. human.

EvolutionaryTrace

Q9Y265.

GenomeRNAi

8607.

NextBio

32249.

SOURCE

Search...

Entry information

Entry name

RUVB1_HUMAN

Accession

Primary (citable) accession number: Q9Y265
Secondary accession number(s): B2R5S0 , P82276, Q1KMR0, Q53HK5, Q53HL7, Q53Y27, Q9BSX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2003
Last sequence update:	November 1, 1999
Last modified:	May 29, 2013
This is version 140 of the entry and version 1 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.