RUVBL2

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.

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.

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.

Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway where it negatively regulates expression of ER stress response genes.1 Publication

Catalytic activityⁱ

ATP + H₂O = ADP + phosphate.

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	77 – 84	ATP		8

GO - Molecular functionⁱ

ADP binding Source: Ensembl
ATPase binding Source: Ensembl
ATP binding Source: UniProtKB-KW
ATP-dependent 5'-3' DNA helicase activity Source: InterPro
ATP-dependent DNA helicase activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
beta-catenin binding
Source: UniProtKB
Inferred from direct assayⁱ
- 11080158
chromatin DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 23637611
DNA helicase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 10524211
identical protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- 10966108
protein homodimerization activity Source: Ensembl
RNA polymerase II core promoter sequence-specific DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 23637611
RNA polymerase II distal enhancer sequence-specific DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 23637611
TBP-class protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- 11080158
TFIID-class transcription factor complex binding Source: Ensembl
transcription corepressor activity
Source: UniProtKB
Inferred from direct assayⁱ
- 11080158
unfolded protein binding
Source: ProtInc
Traceable author statementⁱ
- 10524211

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

box C/D snoRNP assembly
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cellular response to estradiol stimulus
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23637611
cellular response to UV
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 18026119
chromatin remodeling
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23637611
DNA recombination
Source: ProtInc
Traceable author statementⁱ
- 10428817
DNA repair
Source: ProtInc
Traceable author statementⁱ
- 10428817
establishment of protein localization to chromatin
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23637611
histone acetylation
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
histone H2A acetylation
Source: UniProtKB
Inferred from direct assayⁱ
- 14966270
histone H4 acetylation
Source: UniProtKB
Inferred from direct assayⁱ
- 14966270
negative regulation of canonical Wnt signaling pathway
Source: UniProtKB
Inferred from direct assayⁱ
- 11080158
negative regulation of estrogen receptor binding
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23637611
positive regulation of histone acetylation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23637611
positive regulation of telomerase RNA localization to Cajal body
Source: BHF-UCL
Inferred from high throughput mutant phenotypeⁱ
- 25467444
positive regulation of transcription by RNA polymerase II
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23637611
protein folding
Source: ProtInc
Traceable author statementⁱ
- 10524211
regulation of growth Source: UniProtKB-KW
regulation of transcription by RNA polymerase II
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
transcriptional activation by promoter-enhancer looping
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23637611

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Activator, Chromatin regulator, Helicase, Hydrolase
Biological process	DNA damage, DNA recombination, DNA repair, Growth regulation, Transcription, Transcription regulation
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactomeⁱ	R-HSA-171319 Telomere Extension By Telomerase R-HSA-3214847 HATs acetylate histones

Reactomeⁱ

R-HSA-171319 Telomere Extension By Telomerase
R-HSA-3214847 HATs acetylate histones

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 19

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000183207.12
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:10475 RUVBL2
MIMⁱ	604788 gene
neXtProtⁱ	NX_Q9Y230

Keywords - Cellular componentⁱ

Cytoplasm, Membrane, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	299	D → N: Abolishes ATPase activity. 1 Publication		1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	10856
Open Targets More...OpenTargetsⁱ	ENSG00000183207
PharmGKBⁱ	PA34888

Chemistry databases

ChEMBLⁱ	CHEMBL2062349

ChEMBLⁱ

CHEMBL2062349

Polymorphism and mutation databases

BioMutaⁱ	RUVBL2
DMDMⁱ	28201890

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources2 Publications
ChainⁱPRO_0000165644	2 – 463	RuvB-like 2Add BLAST		462

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylalanineCombined sources1 Publication	1
Cross-linkⁱ	9	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	437	PhosphoserineCombined sources	1
Cross-linkⁱ	444	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linkⁱ	456	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q9Y230
PaxDbⁱ	Q9Y230
PeptideAtlas More...PeptideAtlasⁱ	Q9Y230
PRIDEⁱ	Q9Y230
ProteomicsDBⁱ	85619

2D gel databases

REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	IPI00009104

REPRODUCTION-2DPAGEⁱ

IPI00009104

PTM databases

iPTMnetⁱ	Q9Y230
PhosphoSitePlusⁱ	Q9Y230
SwissPalmⁱ	Q9Y230

Expressionⁱ

Tissue specificityⁱ

Ubiquitously expressed. Highly expressed in testis and thymus.

Gene expression databases

Bgeeⁱ	ENSG00000183207 Expressed in 225 organ(s), highest expression level in testis
CleanExⁱ	HS_RUVBL2
ExpressionAtlasⁱ	Q9Y230 baseline and differential
Genevisibleⁱ	Q9Y230 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB012432 HPA042880 HPA067966

HPAⁱ

CAB012432
HPA042880
HPA067966

Interactionⁱ

Subunit structureⁱ

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 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. Component of the R2TP complex composed at least of PIHD1, RUVBL1, RUVBL2 and RPAP3 (PubMed:20864032). Interacts with ITFG1 (PubMed:25437307). Interacts with ZMYND10 (PubMed:29601588). Interacts with WAC; WAC positively regulates MTOR activity by promoting the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex which leads to the dimerization of the mTORC1 complex and its subsequent activation (PubMed:26812014).Curated20 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
itself		3	EBI-352939,EBI-352939
CCDC103	Q8IW40	3	EBI-352939,EBI-10261970
DPCD	Q9BVM2	6	EBI-352939,EBI-749988
LNX1	Q8TBB1	5	EBI-352939,EBI-739832
RUVBL1	Q9Y265	29	EBI-352939,EBI-353675
YY1	P25490	6	EBI-352939,EBI-765538

GO - Molecular functionⁱ

ATPase binding Source: Ensembl
beta-catenin binding
Source: UniProtKB
Inferred from direct assayⁱ
- 11080158
identical protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- 10966108
protein homodimerization activity Source: Ensembl
TBP-class protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- 11080158
TFIID-class transcription factor complex binding Source: Ensembl
unfolded protein binding
Source: ProtInc
Traceable author statementⁱ
- 10524211

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	116067, 281 interactors
ComplexPortalⁱ	CPX-846 INO80 chromatin remodeling complex CPX-974 SRCAP histone exchanging complex CPX-978 NuA4 histone acetyltransferase complex
CORUMⁱ	Q9Y230
Database of interacting proteins More...DIPⁱ	DIP-28153N
IntActⁱ	Q9Y230, 127 interactors
Molecular INTeraction database More...MINTⁱ	Q9Y230
STRINGⁱ	9606.ENSP00000473172

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	19 – 22	Combined sources	4
Turnⁱ	24 – 27	Combined sources	4
Beta strandⁱ	41 – 43	Combined sources	3
Beta strandⁱ	46 – 48	Combined sources	3
Helixⁱ	50 – 65	Combined sources	16
Turnⁱ	66 – 70	Combined sources	5
Beta strandⁱ	72 – 77	Combined sources	6
Helixⁱ	83 – 94	Combined sources	12
Beta strandⁱ	100 – 104	Combined sources	5
Helixⁱ	105 – 108	Combined sources	4
Beta strandⁱ	111 – 113	Combined sources	3
Helixⁱ	115 – 125	Combined sources	11
Beta strandⁱ	126 – 145	Combined sources	20
Beta strandⁱ	152 – 156	Combined sources	5
Beta strandⁱ	161 – 164	Combined sources	4
Beta strandⁱ	169 – 172	Combined sources	4
Helixⁱ	176 – 183	Combined sources	8
Beta strandⁱ	191 – 194	Combined sources	4
Turnⁱ	197 – 200	Combined sources	4
Beta strandⁱ	201 – 206	Combined sources	6
Beta strandⁱ	232 – 243	Combined sources	12
Helixⁱ	244 – 251	Combined sources	8
Helixⁱ	259 – 262	Combined sources	4
Helixⁱ	270 – 285	Combined sources	16
Beta strandⁱ	288 – 293	Combined sources	6
Beta strandⁱ	295 – 300	Combined sources	6
Helixⁱ	301 – 303	Combined sources	3
Helixⁱ	306 – 315	Combined sources	10
Beta strandⁱ	318 – 320	Combined sources	3
Beta strandⁱ	323 – 328	Combined sources	6
Beta strandⁱ	331 – 334	Combined sources	4
Beta strandⁱ	341 – 343	Combined sources	3
Helixⁱ	348 – 351	Combined sources	4
Beta strandⁱ	354 – 359	Combined sources	6
Helixⁱ	364 – 378	Combined sources	15
Helixⁱ	384 – 396	Combined sources	13
Helixⁱ	399 – 415	Combined sources	17
Beta strandⁱ	419 – 421	Combined sources	3
Helixⁱ	423 – 432	Combined sources	10
Helixⁱ	436 – 439	Combined sources	4
Turnⁱ	440 – 443	Combined sources	4
Helixⁱ	444 – 454	Combined sources	11

Show more details

3D structure databases

ProteinModelPortalⁱ	Q9Y230
SMRⁱ	Q9Y230
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9Y230

EvolutionaryTraceⁱ

Q9Y230

Family & Domainsⁱ

Domainⁱ

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

Sequence similaritiesⁱ

Belongs to the RuvB family.Curated

Phylogenomic databases

eggNOGⁱ	KOG2680 Eukaryota COG1224 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00890000139527
HOGENOMⁱ	HOG000190885
HOVERGENⁱ	HBG054186
InParanoidⁱ	Q9Y230
KEGG Orthology (KO) More...KOⁱ	K11338
OMAⁱ	VPFTMIA
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G07C9
PhylomeDBⁱ	Q9Y230
TreeFamⁱ	TF300469

Family and domain databases

InterProⁱ	View protein in InterPro IPR003593 AAA+_ATPase IPR027417 P-loop_NTPase IPR027238 RuvB-like IPR037942 RUVBL2 IPR010339 TIP49_C
PANTHERⁱ	PTHR11093 PTHR11093, 1 hit PTHR11093:SF2 PTHR11093:SF2, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF06068 TIP49, 1 hit
SMARTⁱ	View protein in SMART SM00382 AAA, 1 hit
SUPFAMⁱ	SSF52540 SSF52540, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

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

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 8 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q9Y230-1) [UniParc]FASTA Add to basket

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.

« Hide

        10         20         30         40         50
MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL 
        60         70         80         90        100
AARRAAGVVL EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF 
       110        120        130        140        150
TAIAGSEIFS LEMSKTEALT QAFRRSIGVR IKEETEIIEG EVVEIQIDRP 
       160        170        180        190        200
ATGTGSKVGK LTLKTTEMET IYDLGTKMIE SLTKDKVQAG DVITIDKATG 
       210        220        230        240        250
KISKLGRSFT RARDYDAMGS QTKFVQCPDG ELQKRKEVVH TVSLHEIDVI 
       260        270        280        290        300
NSRTQGFLAL FSGDTGEIKS EVREQINAKV AEWREEGKAE IIPGVLFIDE 
       310        320        330        340        350
VHMLDIESFS FLNRALESDM APVLIMATNR GITRIRGTSY QSPHGIPIDL 
       360        370        380        390        400
LDRLLIVSTT PYSEKDTKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR 
       410        420        430        440        450
YAIQLITAAS LVCRKRKGTE VQVDDIKRVY SLFLDESRST QYMKEYQDAF 
       460 
LFNELKGETM DTS

Length:463

Mass (Da):51,157

Last modified:January 23, 2007 - v3

Checksum:ⁱ54C78E9C587D975A

GO

Isoform 2 (identifier: Q9Y230-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-45: Missing.

« Hide

        10         20         30         40         50
MVGQLAARRA AGVVLEMIRE GKIAGRAVLI AGQPGTGKTA IAMGMAQALG 
        60         70         80         90        100
PDTPFTAIAG SEIFSLEMSK TEALTQAFRR SIGVRIKEET EIIEGEVVEI 
       110        120        130        140        150
QIDRPATGTG SKVGKLTLKT TEMETIYDLG TKMIESLTKD KVQAGDVITI 
       160        170        180        190        200
DKATGKISKL GRSFTRARDY DAMGSQTKFV QCPDGELQKR KEVVHTVSLH 
       210        220        230        240        250
EIDVINSRTQ GFLALFSGDT GEIKSEVREQ INAKVAEWRE EGKAEIIPGV 
       260        270        280        290        300
LFIDEVHMLD IESFSFLNRA LESDMAPVLI MATNRGITRI RGTSYQSPHG 
       310        320        330        340        350
IPIDLLDRLL IVSTTPYSEK DTKQILRIRC EEEDVEMSED AYTVLTRIGL 
       360        370        380        390        400
ETSLRYAIQL ITAASLVCRK RKGTEVQVDD IKRVYSLFLD ESRSTQYMKE 
       410 
YQDAFLFNEL KGETMDTS

Note: No experimental confirmation available.

Show »

Length:418

Mass (Da):46,306

Checksum:ⁱ64C304B804D86B2E

GO

Computationally mapped potential isoform sequencesⁱ

There are 8 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

M0R0Y3	M0R0Y3_HUMAN	RuvB-like helicase RuvB-like helicase, EC 3.6.4.12	RUVBL2	354	Annotation score:
M0QXI6	M0QXI6_HUMAN	RuvB-like helicase RuvB-like helicase, EC 3.6.4.12	RUVBL2	109	Annotation score:
X6R2L4	X6R2L4_HUMAN	RuvB-like helicase RuvB-like helicase, EC 3.6.4.12	RUVBL2	259	Annotation score:
M0R0Z0	M0R0Z0_HUMAN	RuvB-like helicase RuvB-like helicase, EC 3.6.4.12	RUVBL2	50	Annotation score:
A0A1W2PS48	A0A1W2PS48_HUMAN	RuvB-like helicase RuvB-like helicase, EC 3.6.4.12	RUVBL2	50	Annotation score:
M0QXZ7	M0QXZ7_HUMAN	RuvB-like 2 (E. coli), isoform CRA_... RuvB-like 2 (E. coli), isoform CRA_b	RUVBL2 hCG_16214	39	Annotation score:
M0QYD8	M0QYD8_HUMAN	RuvB-like 2 (E. coli), isoform CRA_... RuvB-like 2 (E. coli), isoform CRA_c	RUVBL2 hCG_16214	44	Annotation score:
A0A1W2PS22	A0A1W2PS22_HUMAN	RuvB-like 2 RuvB-like 2	RUVBL2	39	Annotation score:

Sequence cautionⁱ

The sequence AAD34041 differs from that shown. Reason: Frameshift at position 401.Curated

The sequence AAH08355 differs from that shown. Reason: Frameshift at position 191.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	214	D → N in AAD34041 (PubMed:10810093).Curated		1
Sequence conflictⁱ	257 – 258	FL → YV AA sequence (PubMed:10882073).Curated		2

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_056584	1 – 45	Missing in isoform 2. 1 PublicationAdd BLAST		45

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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 AK057498 mRNA Translation: BAG51921.1 AK074542 mRNA Translation: BAC11048.1 CR533507 mRNA Translation: CAG38538.1 AC008687 Genomic DNA No translation available. CH471177 Genomic DNA Translation: EAW52426.1 CH471177 Genomic DNA Translation: EAW52430.1 BC000428 mRNA Translation: AAH00428.1 BC004531 mRNA Translation: AAH04531.1 BC008355 mRNA Translation: AAH08355.1 Frameshift.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS42588.1 [Q9Y230-1]
PIRⁱ	T46313
NCBI Reference Sequences More...RefSeqⁱ	NP_001308120.1, NM_001321191.1 [Q9Y230-2] NP_006657.1, NM_006666.2 [Q9Y230-1] XP_011524632.1, XM_011526330.1 [Q9Y230-2]
UniGeneⁱ	Hs.515846

Genome annotation databases

Ensemblⁱ	ENST00000595090; ENSP00000473172; ENSG00000183207 [Q9Y230-1]
GeneIDⁱ	10856
KEGGⁱ	hsa:10856
UCSC genome browser More...UCSCⁱ	uc002plr.2 human [Q9Y230-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9Y230	RuvB-like helicase		MACMU		463	UniRef100_Q9Y230
RuvB-like helicase		PANTR		463
RuvB-like helicase		MACNE		463
RuvB-like helicase		COLAP		463
RuvB-like helicase		PONAB		463
+10
Q9Y230-2	RuvB-like helicase		PONAB		418	UniRef100_H2NZJ4
RuvB-like helicase (Fragment)		CALJA		210
RuvB-like helicase		PANTR		296
RuvB-like helicase		TARSY		418
UPI0005F45094		CERAT		374
+3

Protein	Similar proteins		Species	Score	Length	Source
Q9Y230	RuvB-like 2		MOUSE		463	UniRef90_Q9Y230
RuvB-like 2		BOVIN		463
RuvB-like 2		XENLA		462
RuvB-like helicase		MACMU		463
RuvB-like helicase		PANTR		463
+121
Q9Y230-2	RuvB-like helicase		BOVIN		463	UniRef90_F1MSD2
ruvB-like 2		BALAS		538
RuvB-like helicase (Fragment)		XENLA		31
RuvB-like helicase (Fragment)		HUMAN		109
RuvB-like helicase (Fragment)		PONAB		109
+49

Protein	Similar proteins		Species	Score	Length	Source
Q9Y230	RuvB-like 2		MOUSE		463	UniRef50_Q9Y230
RuvB-like 2		BOVIN		463
RuvB-like 2		XENLA		462
RuvB-like helicase		MACMU		463
RuvB-like helicase		PANTR		463
+156
Q9Y230-2	RuvB-like 2		DANRE		463	UniRef50_P83571
RuvB-like helicase		FUNHE		526
RuvB-like helicase		Austrofundulus limnaeus		481
RuvB-like helicase		GASAC		469
RuvB-like helicase		ICTPU		463
+225

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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 AK057498 mRNA Translation: BAG51921.1 AK074542 mRNA Translation: BAC11048.1 CR533507 mRNA Translation: CAG38538.1 AC008687 Genomic DNA No translation available. CH471177 Genomic DNA Translation: EAW52426.1 CH471177 Genomic DNA Translation: EAW52430.1 BC000428 mRNA Translation: AAH00428.1 BC004531 mRNA Translation: AAH04531.1 BC008355 mRNA Translation: AAH08355.1 Frameshift.
CCDSⁱ	CCDS42588.1 [Q9Y230-1]
PIRⁱ	T46313
RefSeqⁱ	NP_001308120.1, NM_001321191.1 [Q9Y230-2] NP_006657.1, NM_006666.2 [Q9Y230-1] XP_011524632.1, XM_011526330.1 [Q9Y230-2]
UniGeneⁱ	Hs.515846

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	5OAF	electron microscopy	4.06	B/D/F	1-463	[»]
	6ETX	electron microscopy	4.80	B/D/F	1-463	[»]
	6FO1	electron microscopy	3.57	D/E/F	1-463	[»]
	6H7X	X-ray	2.89	A	1-463	[»]
ProteinModelPortalⁱ	Q9Y230
SMRⁱ	Q9Y230
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	116067, 281 interactors
ComplexPortalⁱ	CPX-846 INO80 chromatin remodeling complex CPX-974 SRCAP histone exchanging complex CPX-978 NuA4 histone acetyltransferase complex
CORUMⁱ	Q9Y230
DIPⁱ	DIP-28153N
IntActⁱ	Q9Y230, 127 interactors
MINTⁱ	Q9Y230
STRINGⁱ	9606.ENSP00000473172

Chemistry databases

ChEMBLⁱ	CHEMBL2062349

ChEMBLⁱ

CHEMBL2062349

PTM databases

iPTMnetⁱ	Q9Y230
PhosphoSitePlusⁱ	Q9Y230
SwissPalmⁱ	Q9Y230

Polymorphism and mutation databases

BioMutaⁱ	RUVBL2
DMDMⁱ	28201890

2D gel databases

REPRODUCTION-2DPAGEⁱ	IPI00009104

REPRODUCTION-2DPAGEⁱ

IPI00009104

Proteomic databases

EPDⁱ	Q9Y230
PaxDbⁱ	Q9Y230
PeptideAtlasⁱ	Q9Y230
PRIDEⁱ	Q9Y230
ProteomicsDBⁱ	85619

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	10856
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000595090; ENSP00000473172; ENSG00000183207 [Q9Y230-1]
GeneIDⁱ	10856
KEGGⁱ	hsa:10856
UCSCⁱ	uc002plr.2 human [Q9Y230-1]

Organism-specific databases

CTDⁱ	10856
DisGeNETⁱ	10856
EuPathDBⁱ	HostDB:ENSG00000183207.12
GeneCardsⁱ	RUVBL2
HGNCⁱ	HGNC:10475 RUVBL2
HPAⁱ	CAB012432 HPA042880 HPA067966
MIMⁱ	604788 gene
neXtProtⁱ	NX_Q9Y230
OpenTargetsⁱ	ENSG00000183207
PharmGKBⁱ	PA34888
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2680 Eukaryota COG1224 LUCA
GeneTreeⁱ	ENSGT00890000139527
HOGENOMⁱ	HOG000190885
HOVERGENⁱ	HBG054186
InParanoidⁱ	Q9Y230
KOⁱ	K11338
OMAⁱ	VPFTMIA
OrthoDBⁱ	EOG091G07C9
PhylomeDBⁱ	Q9Y230
TreeFamⁱ	TF300469

Enzyme and pathway databases

Reactomeⁱ	R-HSA-171319 Telomere Extension By Telomerase R-HSA-3214847 HATs acetylate histones

Reactomeⁱ

R-HSA-171319 Telomere Extension By Telomerase
R-HSA-3214847 HATs acetylate histones

Miscellaneous databases

ChiTaRSⁱ	RUVBL2 human
EvolutionaryTraceⁱ	Q9Y230
GeneWikiⁱ	RUVBL2
GenomeRNAiⁱ	10856
Protein Ontology More...PROⁱ	PR:Q9Y230
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000183207 Expressed in 225 organ(s), highest expression level in testis
CleanExⁱ	HS_RUVBL2
ExpressionAtlasⁱ	Q9Y230 baseline and differential
Genevisibleⁱ	Q9Y230 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR003593 AAA+_ATPase IPR027417 P-loop_NTPase IPR027238 RuvB-like IPR037942 RUVBL2 IPR010339 TIP49_C
PANTHERⁱ	PTHR11093 PTHR11093, 1 hit PTHR11093:SF2 PTHR11093:SF2, 1 hit
Pfamⁱ	View protein in Pfam PF06068 TIP49, 1 hit
SMARTⁱ	View protein in SMART SM00382 AAA, 1 hit
SUPFAMⁱ	SSF52540 SSF52540, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RUVB2_HUMAN
Accessionⁱ	Q9Y230Primary (citable) accession number: Q9Y230 Secondary accession number(s): B3KQ59 , E7ETE5, Q6FIB9, Q6PK27, Q9Y361
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 1, 2003
	Last sequence update:	January 23, 2007
	Last modified:	November 7, 2018
	This is version 211 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

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

Documents

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

UniProtKB

UniParc

Help

UniRef

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Supporting data

UniProtKB - Q9Y230 (RUVB2_HUMAN)

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RuvB-like 2

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Cytoskeleton

Cytosol

Extracellular region or secreted

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ