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UniProtKB - Q12873 (CHD3_HUMAN)

>sp|Q12873|CHD3_HUMAN Chromodomain-helicase-DNA-binding protein 3 OS=Homo sapiens OX=9606 GN=CHD3 PE=1 SV=3
MKAADTVILWARSKNDQLRISFPPGLCWGDRMPDKDDIRLLPSALGVKKRKRGPKKQKEN
KPGKPRKRKKRDSEEEFGSERDEYREKSESGGSEYGTGPGRKRRRKHREKKEKKTKRRKK
GEGDGGQKQVEQKSSATLLLTWGLEDVEHVFSEEDYHTLTNYKAFSQFMRPLIAKKNPKI
PMSKMMTILGAKWREFSANNPFKGSAAAVAAAAAAAAAAVAEQVSAAVSSATPIAPSGPP
ALPPPPAADIQPPPIRRAKTKEGKGPGHKRRSKSPRVPDGRKKLRGKKMAPLKIKLGLLG
GKRKKGGSYVFQSDEGPEPEAEESDLDSGSVHSASGRPDGPVRTKKLKRGRPGRKKKKVL
GCPAVAGEEEVDGYETDHQDYCEVCQQGGEIILCDTCPRAYHLVCLDPELDRAPEGKWSC
PHCEKEGVQWEAKEEEEEYEEEGEEEGEKEEEDDHMEYCRVCKDGGELLCCDACISSYHI
HCLNPPLPDIPNGEWLCPRCTCPVLKGRVQKILHWRWGEPPVAVPAPQQADGNPDVPPPR
PLQGRSEREFFVKWVGLSYWHCSWAKELQLEIFHLVMYRNYQRKNDMDEPPPLDYGSGED
DGKSDKRKVKDPHYAEMEEKYYRFGIKPEWMTVHRIINHSVDKKGNYHYLVKWRDLPYDQ
STWEEDEMNIPEYEEHKQSYWRHRELIMGEDPAQPRKYKKKKKELQGDGPPSSPTNDPTV
KYETQPRFITATGGTLHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYK
EGHTKGPFLVSAPLSTIINWEREFQMWAPKFYVVTYTGDKDSRAIIRENEFSFEDNAIKG
GKKAFKMKREAQVKFHVLLTSYELITIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLN
GYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLL
GPHMLRRLKADVFKNMPAKTELIVRVELSPMQKKYYKYILTRNFEALNSRGGGNQVSLLN
IMMDLKKCCNHPYLFPVAAMESPKLPSGAYEGGALIKSSGKLMLLQKMLRKLKEQGHRVL
IFSQMTKMLDLLEDFLDYEGYKYERIDGGITGALRQEAIDRFNAPGAQQFCFLLSTRAGG
LGINLATADTVIIFDSDWNPHNDIQAFSRAHRIGQANKVMIYRFVTRASVEERITQVAKR
KMMLTHLVVRPGLGSKAGSMSKQELDDILKFGTEELFKDENEGENKEEDSSVIHYDNEAI
ARLLDRNQDATEDTDVQNMNEYLSSFKVAQYVVREEDKIEEIEREIIKQEENVDPDYWEK
LLRHHYEQQQEDLARNLGKGKRVRKQVNYNDAAQEDQDNQSEYSVGSEEEDEDFDERPEG
RRQSKRQLRNEKDKPLPPLLARVGGNIEVLGFNTRQRKAFLNAVMRWGMPPQDAFTTQWL
VRDLRGKTEKEFKAYVSLFMRHLCEPGADGSETFADGVPREGLSRQQVLTRIGVMSLVKK
KVQEFEHINGRWSMPELMPDPSADSKRSSRASSPTKTSPTTPEASATNSPCTSKPATPAP
SEKGEGIRTPLEKEEAENQEEKPEKNSRIGEKMETEADAPSPAPSLGERLEPRKIPLEDE
VPGVPGEMEPEPGYRGDREKSATESTPGERGEEKPLDGQEHRERPEGETGDLGKREDVKG
DRELRPGPRDEPRSNGRREEKTEKPRFMFNIADGGFTELHTLWQNEERAAISSGKLNEIW
HRRHDYWLLAGIVLHGYARWQDIQNDAQFAIINEPFKTEANKGNFLEMKNKFLARRFKLL
EQALVIEEQLRRAAYLNLSQEPAHPAMALHARFAEAECLAESHQHLSKESLAGNKPANAV
LHKVLNQLEELLSDMKADVTRLPATLSRIPPIAARLQMSERSILSRLASKGTEPHPTPAY
PPGPYATPPGYGAAFSAAPVGALAAAGANYSQMPAGSFITAATNGPPVLVKKEKEMVGAL
VSDGLDRKEPRAGEVICIDD

Entry version 222 (25 May 2022)
Sequence version 3 (07 Feb 2006)
Previous versions | rss

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Protein

Chromodomain-helicase-DNA-binding protein 3

Gene

CHD3

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones (PubMed:9804427, PubMed:30397230).

Involved in transcriptional repressiobn as part of the NuRD complex (PubMed:27068747).

Required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity (PubMed:17626165).

4 Publications

Miscellaneous

One of the main antigens reacting with anti-MI-2 positive sera of dermatomyositis.1 Publication

Catalytic activityⁱ

ATP
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See the description of this molecule in ChEBI.
+
H₂O
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See the description of this molecule in ChEBI.
=
ADP
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See the description of this molecule in ChEBI.
+
H⁺
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+
phosphate
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See the description of this molecule in ChEBI.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.25
  "CHD3 helicase domain mutations cause a neurodevelopmental syndrome with macrocephaly and impaired speech and language."
  Snijders Blok L., Rousseau J., Twist J., Ehresmann S., Takaku M., Venselaar H., Rodan L.H., Nowak C.B., Douglas J., Swoboda K.J., Steeves M.A., Sahai I., Stumpel C.T.R.M., Stegmann A.P.A., Wheeler P., Willing M., Fiala E., Kochhar A.
  Campeau P.M.
  Nat. Commun. 9:4619-4619(2018) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, INVOLVEMENT IN SNIBCPS, VARIANTS SNIBCPS 457-GLU--ASP-2000 DEL; ARG-886; PHE-915; LYS-921; GLU-961; GLN-985; TRP-985; GLY-1109 DEL; HIS-1120; PRO-1121; ILE-1136; ARG-1158; LYS-1159; ARG-1161; TRP-1169; ARG-1171; GLN-1172; PRO-1187; PRO-1236; GLN-1342 AND LEU-1881, CHARACTERIZATION OF VARIANTS SNIBCPS PHE-915; PRO-1121; ARG-1158; LYS-1159; GLN-1172 AND PRO-1187.
EC:
3.6.4.12
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.25
  "CHD3 helicase domain mutations cause a neurodevelopmental syndrome with macrocephaly and impaired speech and language."
  Snijders Blok L., Rousseau J., Twist J., Ehresmann S., Takaku M., Venselaar H., Rodan L.H., Nowak C.B., Douglas J., Swoboda K.J., Steeves M.A., Sahai I., Stumpel C.T.R.M., Stegmann A.P.A., Wheeler P., Willing M., Fiala E., Kochhar A.
  Campeau P.M.
  Nat. Commun. 9:4619-4619(2018) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, INVOLVEMENT IN SNIBCPS, VARIANTS SNIBCPS 457-GLU--ASP-2000 DEL; ARG-886; PHE-915; LYS-921; GLU-961; GLN-985; TRP-985; GLY-1109 DEL; HIS-1120; PRO-1121; ILE-1136; ARG-1158; LYS-1159; ARG-1161; TRP-1169; ARG-1171; GLN-1172; PRO-1187; PRO-1236; GLN-1342 AND LEU-1881, CHARACTERIZATION OF VARIANTS SNIBCPS PHE-915; PRO-1121; ARG-1158; LYS-1159; GLN-1172 AND PRO-1187.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
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ATP
+
H₂O
=
ADP
+
H⁺
+
phosphate
zoom

Regions

Feature key	Position(s)	DescriptionActions	Length
Zinc fingerⁱ	379 – 426	PHD-type 1PROSITE-ProRule annotationAdd BLAST	48
Zinc fingerⁱ	456 – 503	PHD-type 2PROSITE-ProRule annotationAdd BLAST	48
Nucleotide bindingⁱ	761 – 768	ATPPROSITE-ProRule annotation	8

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chromatin regulator, DNA-binding, Helicase, Hydrolase
Biological process	Host-virus interaction, Transcription, Transcription regulation
Ligand	ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

PathwayCommonsⁱ	Q12873
Reactomeⁱ	R-HSA-3214815, HDACs deacetylate histones R-HSA-427389, ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression R-HSA-4551638, SUMOylation of chromatin organization proteins R-HSA-6804758, Regulation of TP53 Activity through Acetylation R-HSA-73762, RNA Polymerase I Transcription Initiation R-HSA-8943724, Regulation of PTEN gene transcription R-HSA-9679191, Potential therapeutics for SARS
SignaLinkⁱ	Q12873
SIGNORⁱ	Q12873

Protein family/group databases

MoonDBⁱ	Q12873, Predicted

MoonDBⁱ

Q12873, Predicted

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Chromodomain-helicase-DNA-binding protein 3 (EC:3.6.4.121 Publication) Short name: CHD-3 Alternative name(s): ATP-dependent helicase CHD3 Mi-2 autoantigen 240 kDa protein Mi2-alpha Zinc finger helicase Short name: hZFH
Gene namesⁱ	Name:CHD3
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 17

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:1918, CHD3
MIMⁱ	602120, gene
neXtProtⁱ	NX_Q12873
VEuPathDBⁱ	HostDB:ENSG00000170004

Keywords - Cellular componentⁱ

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Snijders Blok-Campeau syndrome (SNIBCPS)2 Publications

The disease is caused by variants affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant neurodevelopmental disorder characterized by intellectual disability with a wide range of severity, developmental delay, and impaired speech and language skills. Speech-related problems include dysarthria, speech apraxia, oromotor problems, and stuttering. Additional clinical features are macrocephaly, characteristic facial features such as prominent forehead and hypertelorism, hypotonia, and joint laxity.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_081506	457 – 2000	Missing in SNIBCPS. 1 PublicationAdd BLAST	1544
Natural variantⁱVAR_081507	886	H → R in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567855081EnsemblClinVar.	1
Natural variantⁱVAR_081508	915	L → F in SNIBCPS; increased function in chromatin remodeling. 1 PublicationCorresponds to variant dbSNP:rs1567855669EnsemblClinVar.	1
Natural variantⁱVAR_081509	921	E → K in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567855704EnsemblClinVar.	1
Natural variantⁱVAR_081510	961	G → E in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567856045EnsemblClinVar.	1
Natural variantⁱVAR_081511	985	R → Q in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567856331EnsemblClinVar.	1
Natural variantⁱVAR_081512	985	R → W in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1555611722EnsemblClinVar.	1
Natural variantⁱVAR_081513	1109	Missing in SNIBCPS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1567859975Ensembl.	1
Natural variantⁱVAR_081514	1120	D → H in SNIBCPS; the patient also carries a truncating variant in CIC; both variants may contribute to disease phenotype. 1 Publication	1
Natural variantⁱVAR_081515	1121	R → P in SNIBCPS; decreased function in chromatin remodeling; decreased ATPase activity. 1 PublicationCorresponds to variant dbSNP:rs1567860112EnsemblClinVar.	1
Natural variantⁱVAR_081516	1136	T → I in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567860640EnsemblClinVar.	1
Natural variantⁱVAR_081517	1158	W → R in SNIBCPS; highly decreased function in chromatin remodeling. 1 PublicationCorresponds to variant dbSNP:rs1567860891EnsemblClinVar.	1
Natural variantⁱVAR_081518	1159	N → K in SNIBCPS; highly decreased function in chromatin remodeling. 1 PublicationCorresponds to variant dbSNP:rs754919272EnsemblClinVar.	1
Natural variantⁱVAR_081519	1161	H → R in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567860919EnsemblClinVar.	1
Natural variantⁱVAR_081520	1169	R → W in SNIBCPS. 2 PublicationsCorresponds to variant dbSNP:rs1567861468EnsemblClinVar.	1
Natural variantⁱVAR_081521	1171	H → R in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567861489EnsemblClinVar.	1
Natural variantⁱVAR_081522	1172	R → Q in SNIBCPS; decreased function in chromatin remodeling; decreased ATPase activity. 1 PublicationCorresponds to variant dbSNP:rs1567861501EnsemblClinVar.	1
Natural variantⁱVAR_081523	1187	R → P in SNIBCPS; unknown pathological significance; does not affect function in chromatin remodeling; no effect on ATPase activity. 1 PublicationCorresponds to variant dbSNP:rs1567861571EnsemblClinVar.	1
Natural variantⁱVAR_081524	1236	L → P in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567861894EnsemblClinVar.	1
Natural variantⁱVAR_081525	1342	R → Q in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567863732EnsemblClinVar.	1
Natural variantⁱVAR_081526	1881	R → L in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567877108EnsemblClinVar.	1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	1971	K → R: Abolishes sumoylation by ZBED1/hDREF and increases binding to chromatin. 1 Publication		1

Keywords - Diseaseⁱ

Disease variant, Mental retardation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	1107
MalaCards human disease database More...MalaCardsⁱ	CHD3
MIMⁱ	618205, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000170004
PharmGKBⁱ	PA26454

Miscellaneous databases

Pharosⁱ	Q12873, Tbio

Pharosⁱ

Q12873, Tbio

Genetic variation databases

BioMutaⁱ	CHD3
DMDMⁱ	88911273

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000080227	1 – 2000	Chromodomain-helicase-DNA-binding protein 3Add BLAST		2000

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	79	PhosphoserineCombined sources	1
Cross-linkⁱ	120	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linkⁱ	163	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linkⁱ	295	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linkⁱ	302	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residueⁱ	308	PhosphoserineBy similarity	1
Modified residueⁱ	324	PhosphoserineCombined sources	1
Modified residueⁱ	376	PhosphothreonineBy similarity	1
Modified residueⁱ	597	PhosphoserineCombined sources	1
Cross-linkⁱ	627	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	713	PhosphoserineCombined sources	1
Cross-linkⁱ	721	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linkⁱ	721	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residueⁱ	1219	PhosphoserineBy similarity	1
Cross-linkⁱ	1222	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linkⁱ	1238	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linkⁱ	1246	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linkⁱ	1308	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	1367	PhosphoserineCombined sources	1
Modified residueⁱ	1532	PhosphoserineBy similarity	1
Modified residueⁱ	1538	PhosphoserineBy similarity	1
Cross-linkⁱ	1573	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linkⁱ	1585	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residueⁱ	1601	PhosphoserineCombined sources	1
Modified residueⁱ	1605	PhosphoserineCombined sources	1
Modified residueⁱ	1646	PhosphothreonineCombined sources	1
Cross-linkⁱ	1876	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linkⁱ	1971	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Cross-linkⁱ	1988	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationⁱ

Sumoylation at Lys-1971 results in dissociation from chromatin and suppression of transcriptional repression.1 Publication

Keywords - PTMⁱ

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q12873
jPOSTⁱ	Q12873
MassIVEⁱ	Q12873
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q12873
PaxDbⁱ	Q12873
PeptideAtlas More...PeptideAtlasⁱ	Q12873
PRIDEⁱ	Q12873
ProteomicsDBⁱ	20268 58995 [Q12873-1] 58996 [Q12873-2]

PTM databases

GlyGenⁱ	Q12873, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	Q12873
MetOSiteⁱ	Q12873
PhosphoSitePlusⁱ	Q12873
SwissPalmⁱ	Q12873

Expressionⁱ

Tissue specificityⁱ

Widely expressed.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000170004, Expressed in cortical plate and 228 other tissues
ExpressionAtlasⁱ	Q12873, baseline and differential
Genevisibleⁱ	Q12873, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000170004, Low tissue specificity

HPAⁱ

ENSG00000170004, Low tissue specificity

Interactionⁱ

Subunit structureⁱ

Central component of the nucleosome remodeling and histone deacetylase (NuRD) repressive complex (PubMed:9804427, PubMed:27068747).

Interacts with TRIM28 (PubMed:11230151).

Interacts with SERBP1 (PubMed:12505151).

Interacts (via its C-terminal) with HABP4 (PubMed:12505151).

Interacts with PCNT; the interaction regulates centrosome integrity (PubMed:17626165).

Interacts with ZBED1/hDREF (PubMed:27068747).

5 Publications

(Microbial infection) Interacts with Hantaan hantavirus nucleoprotein.

1 Publication

(Microbial infection) Interacts with Seoul hantavirus nucleoprotein.

1 Publication

Binary interactionsⁱ

Hide details

Q12873

With	#Exp.	IntAct
BARD1 [Q99728]	2	EBI-523590,EBI-473181
DDX5 [P17844]	4	EBI-523590,EBI-351962
GIT1 [Q9Y2X7]	2	EBI-523590,EBI-466061
HTT [P42858]	3	EBI-523590,EBI-466029
KDM1A [O60341]	4	EBI-523590,EBI-710124
PRPF40A [O75400]	2	EBI-523590,EBI-473291
SERBP1 [Q8NC51]	5	EBI-523590,EBI-523558
SUMO2 [P61956]	3	EBI-523590,EBI-473220
TRIM28 [Q13263]	4	EBI-523590,EBI-78139
ZBTB7A [O95365]	2	EBI-523590,EBI-2795384

Protein-protein interaction databases

BioGRIDⁱ	107532, 715 interactors
ComplexPortalⁱ	CPX-880, MBD2/NuRD nucleosome remodeling and deacetylase complex CPX-922, MBD3/NuRD nucleosome remodeling and deacetylase complex
CORUMⁱ	Q12873
Database of interacting proteins More...DIPⁱ	DIP-32496N
ELMⁱ	Q12873
IntActⁱ	Q12873, 157 interactors
Molecular INTeraction database More...MINTⁱ	Q12873
STRINGⁱ	9606.ENSP00000369716

Miscellaneous databases

RNActⁱ	Q12873, protein

RNActⁱ

Q12873, protein

Structureⁱ

3D structure databases

AlphaFoldDBⁱ	Q12873
SMRⁱ	Q12873
ModBaseⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	494 – 594	Chromo 1PROSITE-ProRule annotationAdd BLAST	101
Domainⁱ	631 – 673	Chromo 2PROSITE-ProRule annotationAdd BLAST	43
Domainⁱ	748 – 932	Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST	185
Domainⁱ	1064 – 1229	Helicase C-terminalPROSITE-ProRule annotationAdd BLAST	166

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	23 – 133	DisorderedSequence analysisAdd BLAST	111
Regionⁱ	231 – 359	DisorderedSequence analysisAdd BLAST	129
Regionⁱ	431 – 452	DisorderedSequence analysisAdd BLAST	22
Regionⁱ	523 – 542	DisorderedSequence analysisAdd BLAST	20
Regionⁱ	587 – 611	DisorderedSequence analysisAdd BLAST	25
Regionⁱ	692 – 721	DisorderedSequence analysisAdd BLAST	30
Regionⁱ	1349 – 1399	DisorderedSequence analysisAdd BLAST	51
Regionⁱ	1513 – 1707	DisorderedSequence analysisAdd BLAST	195
Regionⁱ	1566 – 1966	Required for interaction with PCNT1 PublicationAdd BLAST	401

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	883 – 886	DEAH box		4

Compositional bias

Feature key	Position(s)	DescriptionActions	Length
Compositional biasⁱ	30 – 44	Basic and acidic residuesSequence analysisAdd BLAST	15
Compositional biasⁱ	45 – 67	Basic residuesSequence analysisAdd BLAST	23
Compositional biasⁱ	68 – 90	Basic and acidic residuesSequence analysisAdd BLAST	23
Compositional biasⁱ	100 – 117	Basic residuesSequence analysisAdd BLAST	18
Compositional biasⁱ	236 – 252	Pro residuesSequence analysisAdd BLAST	17
Compositional biasⁱ	262 – 290	Basic residuesSequence analysisAdd BLAST	29
Compositional biasⁱ	433 – 452	Acidic residuesSequence analysisAdd BLAST	20
Compositional biasⁱ	692 – 707	Basic and acidic residuesSequence analysisAdd BLAST	16
Compositional biasⁱ	1376 – 1396	Basic and acidic residuesSequence analysisAdd BLAST	21
Compositional biasⁱ	1525 – 1556	Polar residuesSequence analysisAdd BLAST	32
Compositional biasⁱ	1566 – 1595	Basic and acidic residuesSequence analysisAdd BLAST	30
Compositional biasⁱ	1631 – 1707	Basic and acidic residuesSequence analysisAdd BLAST	77

Sequence similaritiesⁱ

Belongs to the SNF2/RAD54 helicase family.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	379 – 426	PHD-type 1PROSITE-ProRule annotationAdd BLAST		48
Zinc fingerⁱ	456 – 503	PHD-type 2PROSITE-ProRule annotationAdd BLAST		48

Keywords - Domainⁱ

Repeat, Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG0383, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000158001
HOGENOMⁱ	CLU_000315_22_2_1
InParanoidⁱ	Q12873
OMAⁱ	MIRKPVE
Database of Orthologous Groups More...OrthoDBⁱ	54215at2759
PhylomeDBⁱ	Q12873
TreeFamⁱ	TF106448

Family and domain databases

Gene3Dⁱ	1.10.30.10, 1 hit 3.30.40.10, 2 hits 3.40.50.10810, 1 hit 3.40.50.300, 1 hit
InterProⁱ	View protein in InterPro IPR012957, CHD_C2 IPR009462, CHD_II_SANT-like IPR012958, CHD_N IPR016197, Chromo-like_dom_sf IPR000953, Chromo/chromo_shadow_dom IPR023780, Chromo_domain IPR023779, Chromodomain_CS IPR002464, DNA/RNA_helicase_DEAH_CS IPR009463, DUF1087 IPR014001, Helicase_ATP-bd IPR001650, Helicase_C IPR036910, HMG_box_dom_sf IPR027417, P-loop_NTPase IPR038718, SNF2-like_sf IPR000330, SNF2_N IPR019786, Zinc_finger_PHD-type_CS IPR011011, Znf_FYVE_PHD IPR001965, Znf_PHD IPR019787, Znf_PHD-finger IPR013083, Znf_RING/FYVE/PHD
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08074, CHDCT2, 1 hit PF08073, CHDNT, 1 hit PF00385, Chromo, 1 hit PF06461, DUF1086, 1 hit PF06465, DUF1087, 1 hit PF00271, Helicase_C, 1 hit PF00628, PHD, 2 hits PF00176, SNF2-rel_dom, 1 hit
SMARTⁱ	View protein in SMART SM00298, CHROMO, 2 hits SM00487, DEXDc, 1 hit SM01146, DUF1086, 1 hit SM01147, DUF1087, 1 hit SM00490, HELICc, 1 hit SM00249, PHD, 2 hits
SUPFAMⁱ	SSF47095, SSF47095, 1 hit SSF52540, SSF52540, 2 hits SSF54160, SSF54160, 2 hits SSF57903, SSF57903, 1 hit
PROSITEⁱ	View protein in PROSITE PS00598, CHROMO_1, 1 hit PS50013, CHROMO_2, 2 hits PS00690, DEAH_ATP_HELICASE, 1 hit PS51192, HELICASE_ATP_BIND_1, 1 hit PS51194, HELICASE_CTER, 1 hit PS01359, ZF_PHD_1, 2 hits PS50016, ZF_PHD_2, 2 hits

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 8 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q12873-1) [UniParc]FASTA Add to basket

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

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        10         20         30         40         50
MKAADTVILW ARSKNDQLRI SFPPGLCWGD RMPDKDDIRL LPSALGVKKR 
        60         70         80         90        100
KRGPKKQKEN KPGKPRKRKK RDSEEEFGSE RDEYREKSES GGSEYGTGPG 
       110        120        130        140        150
RKRRRKHREK KEKKTKRRKK GEGDGGQKQV EQKSSATLLL TWGLEDVEHV 
       160        170        180        190        200
FSEEDYHTLT NYKAFSQFMR PLIAKKNPKI PMSKMMTILG AKWREFSANN 
       210        220        230        240        250
PFKGSAAAVA AAAAAAAAAV AEQVSAAVSS ATPIAPSGPP ALPPPPAADI 
       260        270        280        290        300
QPPPIRRAKT KEGKGPGHKR RSKSPRVPDG RKKLRGKKMA PLKIKLGLLG 
       310        320        330        340        350
GKRKKGGSYV FQSDEGPEPE AEESDLDSGS VHSASGRPDG PVRTKKLKRG 
       360        370        380        390        400
RPGRKKKKVL GCPAVAGEEE VDGYETDHQD YCEVCQQGGE IILCDTCPRA 
       410        420        430        440        450
YHLVCLDPEL DRAPEGKWSC PHCEKEGVQW EAKEEEEEYE EEGEEEGEKE 
       460        470        480        490        500
EEDDHMEYCR VCKDGGELLC CDACISSYHI HCLNPPLPDI PNGEWLCPRC 
       510        520        530        540        550
TCPVLKGRVQ KILHWRWGEP PVAVPAPQQA DGNPDVPPPR PLQGRSEREF 
       560        570        580        590        600
FVKWVGLSYW HCSWAKELQL EIFHLVMYRN YQRKNDMDEP PPLDYGSGED 
       610        620        630        640        650
DGKSDKRKVK DPHYAEMEEK YYRFGIKPEW MTVHRIINHS VDKKGNYHYL 
       660        670        680        690        700
VKWRDLPYDQ STWEEDEMNI PEYEEHKQSY WRHRELIMGE DPAQPRKYKK 
       710        720        730        740        750
KKKELQGDGP PSSPTNDPTV KYETQPRFIT ATGGTLHMYQ LEGLNWLRFS 
       760        770        780        790        800
WAQGTDTILA DEMGLGKTIQ TIVFLYSLYK EGHTKGPFLV SAPLSTIINW 
       810        820        830        840        850
EREFQMWAPK FYVVTYTGDK DSRAIIRENE FSFEDNAIKG GKKAFKMKRE 
       860        870        880        890        900
AQVKFHVLLT SYELITIDQA ALGSIRWACL VVDEAHRLKN NQSKFFRVLN 
       910        920        930        940        950
GYKIDHKLLL TGTPLQNNLE ELFHLLNFLT PERFNNLEGF LEEFADISKE 
       960        970        980        990       1000
DQIKKLHDLL GPHMLRRLKA DVFKNMPAKT ELIVRVELSP MQKKYYKYIL 
      1010       1020       1030       1040       1050
TRNFEALNSR GGGNQVSLLN IMMDLKKCCN HPYLFPVAAM ESPKLPSGAY 
      1060       1070       1080       1090       1100
EGGALIKSSG KLMLLQKMLR KLKEQGHRVL IFSQMTKMLD LLEDFLDYEG 
      1110       1120       1130       1140       1150
YKYERIDGGI TGALRQEAID RFNAPGAQQF CFLLSTRAGG LGINLATADT 
      1160       1170       1180       1190       1200
VIIFDSDWNP HNDIQAFSRA HRIGQANKVM IYRFVTRASV EERITQVAKR 
      1210       1220       1230       1240       1250
KMMLTHLVVR PGLGSKAGSM SKQELDDILK FGTEELFKDE NEGENKEEDS 
      1260       1270       1280       1290       1300
SVIHYDNEAI ARLLDRNQDA TEDTDVQNMN EYLSSFKVAQ YVVREEDKIE 
      1310       1320       1330       1340       1350
EIEREIIKQE ENVDPDYWEK LLRHHYEQQQ EDLARNLGKG KRVRKQVNYN 
      1360       1370       1380       1390       1400
DAAQEDQDNQ SEYSVGSEEE DEDFDERPEG RRQSKRQLRN EKDKPLPPLL 
      1410       1420       1430       1440       1450
ARVGGNIEVL GFNTRQRKAF LNAVMRWGMP PQDAFTTQWL VRDLRGKTEK 
      1460       1470       1480       1490       1500
EFKAYVSLFM RHLCEPGADG SETFADGVPR EGLSRQQVLT RIGVMSLVKK 
      1510       1520       1530       1540       1550
KVQEFEHING RWSMPELMPD PSADSKRSSR ASSPTKTSPT TPEASATNSP 
      1560       1570       1580       1590       1600
CTSKPATPAP SEKGEGIRTP LEKEEAENQE EKPEKNSRIG EKMETEADAP 
      1610       1620       1630       1640       1650
SPAPSLGERL EPRKIPLEDE VPGVPGEMEP EPGYRGDREK SATESTPGER 
      1660       1670       1680       1690       1700
GEEKPLDGQE HRERPEGETG DLGKREDVKG DRELRPGPRD EPRSNGRREE 
      1710       1720       1730       1740       1750
KTEKPRFMFN IADGGFTELH TLWQNEERAA ISSGKLNEIW HRRHDYWLLA 
      1760       1770       1780       1790       1800
GIVLHGYARW QDIQNDAQFA IINEPFKTEA NKGNFLEMKN KFLARRFKLL 
      1810       1820       1830       1840       1850
EQALVIEEQL RRAAYLNLSQ EPAHPAMALH ARFAEAECLA ESHQHLSKES 
      1860       1870       1880       1890       1900
LAGNKPANAV LHKVLNQLEE LLSDMKADVT RLPATLSRIP PIAARLQMSE 
      1910       1920       1930       1940       1950
RSILSRLASK GTEPHPTPAY PPGPYATPPG YGAAFSAAPV GALAAAGANY 
      1960       1970       1980       1990       2000
SQMPAGSFIT AATNGPPVLV KKEKEMVGAL VSDGLDRKEP RAGEVICIDD

Length:2,000

Mass (Da):226,592

Last modified:February 7, 2006 - v3

Checksum:ⁱ4494F56E5D0E7083

Isoform 2 (identifier: Q12873-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1642-1675: Missing.

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        10         20         30         40         50
MKAADTVILW ARSKNDQLRI SFPPGLCWGD RMPDKDDIRL LPSALGVKKR 
        60         70         80         90        100
KRGPKKQKEN KPGKPRKRKK RDSEEEFGSE RDEYREKSES GGSEYGTGPG 
       110        120        130        140        150
RKRRRKHREK KEKKTKRRKK GEGDGGQKQV EQKSSATLLL TWGLEDVEHV 
       160        170        180        190        200
FSEEDYHTLT NYKAFSQFMR PLIAKKNPKI PMSKMMTILG AKWREFSANN 
       210        220        230        240        250
PFKGSAAAVA AAAAAAAAAV AEQVSAAVSS ATPIAPSGPP ALPPPPAADI 
       260        270        280        290        300
QPPPIRRAKT KEGKGPGHKR RSKSPRVPDG RKKLRGKKMA PLKIKLGLLG 
       310        320        330        340        350
GKRKKGGSYV FQSDEGPEPE AEESDLDSGS VHSASGRPDG PVRTKKLKRG 
       360        370        380        390        400
RPGRKKKKVL GCPAVAGEEE VDGYETDHQD YCEVCQQGGE IILCDTCPRA 
       410        420        430        440        450
YHLVCLDPEL DRAPEGKWSC PHCEKEGVQW EAKEEEEEYE EEGEEEGEKE 
       460        470        480        490        500
EEDDHMEYCR VCKDGGELLC CDACISSYHI HCLNPPLPDI PNGEWLCPRC 
       510        520        530        540        550
TCPVLKGRVQ KILHWRWGEP PVAVPAPQQA DGNPDVPPPR PLQGRSEREF 
       560        570        580        590        600
FVKWVGLSYW HCSWAKELQL EIFHLVMYRN YQRKNDMDEP PPLDYGSGED 
       610        620        630        640        650
DGKSDKRKVK DPHYAEMEEK YYRFGIKPEW MTVHRIINHS VDKKGNYHYL 
       660        670        680        690        700
VKWRDLPYDQ STWEEDEMNI PEYEEHKQSY WRHRELIMGE DPAQPRKYKK 
       710        720        730        740        750
KKKELQGDGP PSSPTNDPTV KYETQPRFIT ATGGTLHMYQ LEGLNWLRFS 
       760        770        780        790        800
WAQGTDTILA DEMGLGKTIQ TIVFLYSLYK EGHTKGPFLV SAPLSTIINW 
       810        820        830        840        850
EREFQMWAPK FYVVTYTGDK DSRAIIRENE FSFEDNAIKG GKKAFKMKRE 
       860        870        880        890        900
AQVKFHVLLT SYELITIDQA ALGSIRWACL VVDEAHRLKN NQSKFFRVLN 
       910        920        930        940        950
GYKIDHKLLL TGTPLQNNLE ELFHLLNFLT PERFNNLEGF LEEFADISKE 
       960        970        980        990       1000
DQIKKLHDLL GPHMLRRLKA DVFKNMPAKT ELIVRVELSP MQKKYYKYIL 
      1010       1020       1030       1040       1050
TRNFEALNSR GGGNQVSLLN IMMDLKKCCN HPYLFPVAAM ESPKLPSGAY 
      1060       1070       1080       1090       1100
EGGALIKSSG KLMLLQKMLR KLKEQGHRVL IFSQMTKMLD LLEDFLDYEG 
      1110       1120       1130       1140       1150
YKYERIDGGI TGALRQEAID RFNAPGAQQF CFLLSTRAGG LGINLATADT 
      1160       1170       1180       1190       1200
VIIFDSDWNP HNDIQAFSRA HRIGQANKVM IYRFVTRASV EERITQVAKR 
      1210       1220       1230       1240       1250
KMMLTHLVVR PGLGSKAGSM SKQELDDILK FGTEELFKDE NEGENKEEDS 
      1260       1270       1280       1290       1300
SVIHYDNEAI ARLLDRNQDA TEDTDVQNMN EYLSSFKVAQ YVVREEDKIE 
      1310       1320       1330       1340       1350
EIEREIIKQE ENVDPDYWEK LLRHHYEQQQ EDLARNLGKG KRVRKQVNYN 
      1360       1370       1380       1390       1400
DAAQEDQDNQ SEYSVGSEEE DEDFDERPEG RRQSKRQLRN EKDKPLPPLL 
      1410       1420       1430       1440       1450
ARVGGNIEVL GFNTRQRKAF LNAVMRWGMP PQDAFTTQWL VRDLRGKTEK 
      1460       1470       1480       1490       1500
EFKAYVSLFM RHLCEPGADG SETFADGVPR EGLSRQQVLT RIGVMSLVKK 
      1510       1520       1530       1540       1550
KVQEFEHING RWSMPELMPD PSADSKRSSR ASSPTKTSPT TPEASATNSP 
      1560       1570       1580       1590       1600
CTSKPATPAP SEKGEGIRTP LEKEEAENQE EKPEKNSRIG EKMETEADAP 
      1610       1620       1630       1640       1650
SPAPSLGERL EPRKIPLEDE VPGVPGEMEP EPGYRGDREK SEDVKGDREL 
      1660       1670       1680       1690       1700
RPGPRDEPRS NGRREEKTEK PRFMFNIADG GFTELHTLWQ NEERAAISSG 
      1710       1720       1730       1740       1750
KLNEIWHRRH DYWLLAGIVL HGYARWQDIQ NDAQFAIINE PFKTEANKGN 
      1760       1770       1780       1790       1800
FLEMKNKFLA RRFKLLEQAL VIEEQLRRAA YLNLSQEPAH PAMALHARFA 
      1810       1820       1830       1840       1850
EAECLAESHQ HLSKESLAGN KPANAVLHKV LNQLEELLSD MKADVTRLPA 
      1860       1870       1880       1890       1900
TLSRIPPIAA RLQMSERSIL SRLASKGTEP HPTPAYPPGP YATPPGYGAA 
      1910       1920       1930       1940       1950
FSAAPVGALA AAGANYSQMP AGSFITAATN GPPVLVKKEK EMVGALVSDG 
      1960 
LDRKEPRAGE VICIDD

Show »

Length:1,966

Mass (Da):222,861

Checksum:ⁱF8D7B7C132B263A6

Isoform 3 (identifier: Q12873-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-32: MKAADTVILWARSKNDQLRISFPPGLCWGDRM → MASPLRDEEE...PLPPPPPPPP

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        10         20         30         40         50
MASPLRDEEE EEEEMVVSEE EEEEEEEGDE EEEEEVEAAD EDDEEDDDEG 
        60         70         80         90        100
VLGRGPGHDR GRDRHSPPGC HLFPPPPPPP PPLPPPPPPP PPDKDDIRLL 
       110        120        130        140        150
PSALGVKKRK RGPKKQKENK PGKPRKRKKR DSEEEFGSER DEYREKSESG 
       160        170        180        190        200
GSEYGTGPGR KRRRKHREKK EKKTKRRKKG EGDGGQKQVE QKSSATLLLT 
       210        220        230        240        250
WGLEDVEHVF SEEDYHTLTN YKAFSQFMRP LIAKKNPKIP MSKMMTILGA 
       260        270        280        290        300
KWREFSANNP FKGSAAAVAA AAAAAAAAVA EQVSAAVSSA TPIAPSGPPA 
       310        320        330        340        350
LPPPPAADIQ PPPIRRAKTK EGKGPGHKRR SKSPRVPDGR KKLRGKKMAP 
       360        370        380        390        400
LKIKLGLLGG KRKKGGSYVF QSDEGPEPEA EESDLDSGSV HSASGRPDGP 
       410        420        430        440        450
VRTKKLKRGR PGRKKKKVLG CPAVAGEEEV DGYETDHQDY CEVCQQGGEI 
       460        470        480        490        500
ILCDTCPRAY HLVCLDPELD RAPEGKWSCP HCEKEGVQWE AKEEEEEYEE 
       510        520        530        540        550
EGEEEGEKEE EDDHMEYCRV CKDGGELLCC DACISSYHIH CLNPPLPDIP 
       560        570        580        590        600
NGEWLCPRCT CPVLKGRVQK ILHWRWGEPP VAVPAPQQAD GNPDVPPPRP 
       610        620        630        640        650
LQGRSEREFF VKWVGLSYWH CSWAKELQLE IFHLVMYRNY QRKNDMDEPP 
       660        670        680        690        700
PLDYGSGEDD GKSDKRKVKD PHYAEMEEKY YRFGIKPEWM TVHRIINHSV 
       710        720        730        740        750
DKKGNYHYLV KWRDLPYDQS TWEEDEMNIP EYEEHKQSYW RHRELIMGED 
       760        770        780        790        800
PAQPRKYKKK KKELQGDGPP SSPTNDPTVK YETQPRFITA TGGTLHMYQL 
       810        820        830        840        850
EGLNWLRFSW AQGTDTILAD EMGLGKTIQT IVFLYSLYKE GHTKGPFLVS 
       860        870        880        890        900
APLSTIINWE REFQMWAPKF YVVTYTGDKD SRAIIRENEF SFEDNAIKGG 
       910        920        930        940        950
KKAFKMKREA QVKFHVLLTS YELITIDQAA LGSIRWACLV VDEAHRLKNN 
       960        970        980        990       1000
QSKFFRVLNG YKIDHKLLLT GTPLQNNLEE LFHLLNFLTP ERFNNLEGFL 
      1010       1020       1030       1040       1050
EEFADISKED QIKKLHDLLG PHMLRRLKAD VFKNMPAKTE LIVRVELSPM 
      1060       1070       1080       1090       1100
QKKYYKYILT RNFEALNSRG GGNQVSLLNI MMDLKKCCNH PYLFPVAAME 
      1110       1120       1130       1140       1150
SPKLPSGAYE GGALIKSSGK LMLLQKMLRK LKEQGHRVLI FSQMTKMLDL 
      1160       1170       1180       1190       1200
LEDFLDYEGY KYERIDGGIT GALRQEAIDR FNAPGAQQFC FLLSTRAGGL 
      1210       1220       1230       1240       1250
GINLATADTV IIFDSDWNPH NDIQAFSRAH RIGQANKVMI YRFVTRASVE 
      1260       1270       1280       1290       1300
ERITQVAKRK MMLTHLVVRP GLGSKAGSMS KQELDDILKF GTEELFKDEN 
      1310       1320       1330       1340       1350
EGENKEEDSS VIHYDNEAIA RLLDRNQDAT EDTDVQNMNE YLSSFKVAQY 
      1360       1370       1380       1390       1400
VVREEDKIEE IEREIIKQEE NVDPDYWEKL LRHHYEQQQE DLARNLGKGK 
      1410       1420       1430       1440       1450
RVRKQVNYND AAQEDQDNQS EYSVGSEEED EDFDERPEGR RQSKRQLRNE 
      1460       1470       1480       1490       1500
KDKPLPPLLA RVGGNIEVLG FNTRQRKAFL NAVMRWGMPP QDAFTTQWLV 
      1510       1520       1530       1540       1550
RDLRGKTEKE FKAYVSLFMR HLCEPGADGS ETFADGVPRE GLSRQQVLTR 
      1560       1570       1580       1590       1600
IGVMSLVKKK VQEFEHINGR WSMPELMPDP SADSKRSSRA SSPTKTSPTT 
      1610       1620       1630       1640       1650
PEASATNSPC TSKPATPAPS EKGEGIRTPL EKEEAENQEE KPEKNSRIGE 
      1660       1670       1680       1690       1700
KMETEADAPS PAPSLGERLE PRKIPLEDEV PGVPGEMEPE PGYRGDREKS 
      1710       1720       1730       1740       1750
ATESTPGERG EEKPLDGQEH RERPEGETGD LGKREDVKGD RELRPGPRDE 
      1760       1770       1780       1790       1800
PRSNGRREEK TEKPRFMFNI ADGGFTELHT LWQNEERAAI SSGKLNEIWH 
      1810       1820       1830       1840       1850
RRHDYWLLAG IVLHGYARWQ DIQNDAQFAI INEPFKTEAN KGNFLEMKNK 
      1860       1870       1880       1890       1900
FLARRFKLLE QALVIEEQLR RAAYLNLSQE PAHPAMALHA RFAEAECLAE 
      1910       1920       1930       1940       1950
SHQHLSKESL AGNKPANAVL HKVLNQLEEL LSDMKADVTR LPATLSRIPP 
      1960       1970       1980       1990       2000
IAARLQMSER SILSRLASKG TEPHPTPAYP PGPYATPPGY GAAFSAAPVG 
      2010       2020       2030       2040       2050
ALAAAGANYS QMPAGSFITA ATNGPPVLVK KEKEMVGALV SDGLDRKEPR 

AGEVICIDD

Show »

Length:2,059

Mass (Da):233,037

Checksum:ⁱ3C71593E3C788027

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

A0A5F9ZHX5	A0A5F9ZHX5_HUMAN	DNA helicase DNA helicase, EC 3.6.4.12	CHD3	1,357	Annotation score:
H7C2H0	H7C2H0_HUMAN	Chromodomain-helicase-DNA-binding p... Chromodomain-helicase-DNA-binding protein 3	CHD3	525	Annotation score:
H7C0J3	H7C0J3_HUMAN	Chromodomain-helicase-DNA-binding p... Chromodomain-helicase-DNA-binding protein 3	CHD3	383	Annotation score:
H7C3H7	H7C3H7_HUMAN	Chromodomain-helicase-DNA-binding p... Chromodomain-helicase-DNA-binding protein 3	CHD3	277	Annotation score:
A0A5F9ZHM2	A0A5F9ZHM2_HUMAN	Chromodomain-helicase-DNA-binding p... Chromodomain-helicase-DNA-binding protein 3	CHD3	188	Annotation score:
I3L229	I3L229_HUMAN	Chromodomain-helicase-DNA-binding p... Chromodomain-helicase-DNA-binding protein 3	CHD3	249	Annotation score:
I3L1I4	I3L1I4_HUMAN	Chromodomain-helicase-DNA-binding p... Chromodomain-helicase-DNA-binding protein 3	CHD3	110	Annotation score:
K7EPV1	K7EPV1_HUMAN	Chromodomain-helicase-DNA-binding p... Chromodomain-helicase-DNA-binding protein 3	CHD3	63	Annotation score:

Sequence cautionⁱ

The sequence AAB87383 differs from that shown. Differs from position 1967 onward for unknown reasons.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	121 – 126	GEGDGG → PHFQQK in AAC50228 (PubMed:7560064).Curated	6
Sequence conflictⁱ	309 – 312	Missing in AAC50228 (PubMed:7560064).Curated	4
Sequence conflictⁱ	653	W → G in AAC50228 (PubMed:7560064).Curated	1
Sequence conflictⁱ	1704	K → N in AAC39923 (PubMed:9688266).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_048728	3	A → V. Corresponds to variant dbSNP:rs931543Ensembl.	1
Natural variantⁱVAR_081506	457 – 2000	Missing in SNIBCPS. 1 PublicationAdd BLAST	1544
Natural variantⁱVAR_081507	886	H → R in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567855081EnsemblClinVar.	1
Natural variantⁱVAR_081508	915	L → F in SNIBCPS; increased function in chromatin remodeling. 1 PublicationCorresponds to variant dbSNP:rs1567855669EnsemblClinVar.	1
Natural variantⁱVAR_081509	921	E → K in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567855704EnsemblClinVar.	1
Natural variantⁱVAR_081510	961	G → E in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567856045EnsemblClinVar.	1
Natural variantⁱVAR_081511	985	R → Q in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567856331EnsemblClinVar.	1
Natural variantⁱVAR_081512	985	R → W in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1555611722EnsemblClinVar.	1
Natural variantⁱVAR_081513	1109	Missing in SNIBCPS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1567859975Ensembl.	1
Natural variantⁱVAR_081514	1120	D → H in SNIBCPS; the patient also carries a truncating variant in CIC; both variants may contribute to disease phenotype. 1 Publication	1
Natural variantⁱVAR_081515	1121	R → P in SNIBCPS; decreased function in chromatin remodeling; decreased ATPase activity. 1 PublicationCorresponds to variant dbSNP:rs1567860112EnsemblClinVar.	1
Natural variantⁱVAR_081516	1136	T → I in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567860640EnsemblClinVar.	1
Natural variantⁱVAR_081517	1158	W → R in SNIBCPS; highly decreased function in chromatin remodeling. 1 PublicationCorresponds to variant dbSNP:rs1567860891EnsemblClinVar.	1
Natural variantⁱVAR_081518	1159	N → K in SNIBCPS; highly decreased function in chromatin remodeling. 1 PublicationCorresponds to variant dbSNP:rs754919272EnsemblClinVar.	1
Natural variantⁱVAR_081519	1161	H → R in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567860919EnsemblClinVar.	1
Natural variantⁱVAR_081520	1169	R → W in SNIBCPS. 2 PublicationsCorresponds to variant dbSNP:rs1567861468EnsemblClinVar.	1
Natural variantⁱVAR_081521	1171	H → R in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567861489EnsemblClinVar.	1
Natural variantⁱVAR_081522	1172	R → Q in SNIBCPS; decreased function in chromatin remodeling; decreased ATPase activity. 1 PublicationCorresponds to variant dbSNP:rs1567861501EnsemblClinVar.	1
Natural variantⁱVAR_081523	1187	R → P in SNIBCPS; unknown pathological significance; does not affect function in chromatin remodeling; no effect on ATPase activity. 1 PublicationCorresponds to variant dbSNP:rs1567861571EnsemblClinVar.	1
Natural variantⁱVAR_081524	1236	L → P in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567861894EnsemblClinVar.	1
Natural variantⁱVAR_081525	1342	R → Q in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567863732EnsemblClinVar.	1
Natural variantⁱVAR_081526	1881	R → L in SNIBCPS. 1 PublicationCorresponds to variant dbSNP:rs1567877108EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_047097	1 – 32	MKAAD…WGDRM → MASPLRDEEEEEEEMVVSEE EEEEEEEGDEEEEEEVEAAD EDDEEDDDEGVLGRGPGHDR GRDRHSPPGCHLFPPPPPPP PPLPPPPPPPP in isoform 3. CuratedAdd BLAST		32
Alternative sequenceⁱVSP_017231	1642 – 1675	Missing in isoform 2. 2 PublicationsAdd BLAST		34

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U91543 mRNA Translation: AAC39923.1 AC104581 Genomic DNA No translation available. CH471108 Genomic DNA Translation: EAW90114.1 CH471108 Genomic DNA Translation: EAW90116.1 AF006515 mRNA Translation: AAB87383.1 Different termination. U08379 mRNA Translation: AAC50228.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS32553.2 [Q12873-3] CCDS32554.1 [Q12873-1] CCDS32555.1 [Q12873-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_001005271.2, NM_001005271.2 [Q12873-3] NP_001005273.1, NM_001005273.2 [Q12873-1] NP_005843.2, NM_005852.3 [Q12873-2]

Genome annotation databases

Ensemblⁱ	ENST00000330494.12; ENSP00000332628.7; ENSG00000170004.18 ENST00000358181.8; ENSP00000350907.4; ENSG00000170004.18 [Q12873-2] ENST00000380358.9; ENSP00000369716.4; ENSG00000170004.18 [Q12873-3]
GeneIDⁱ	1107
KEGGⁱ	hsa:1107
MANE-Selectⁱ	ENST00000330494.12; ENSP00000332628.7; NM_001005273.3; NP_001005273.1
UCSC genome browser More...UCSCⁱ	uc002gjd.3, human [Q12873-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q12873-3	CHD3 protein (Fragment)		HUMAN		661	UniRef100_Q12873-3

Protein	Similar proteins		Species	Score	Length	Source
Q12873	DNA helicase		TUPCH		2077	UniRef90_Q12873
DNA helicase		MOSMO		2062
DNA helicase		ZALCA		2061
DNA helicase		CAPHI		2061
Chromodomain helicase DNA binding protein 3		PONAB		2060
+371

Protein	Similar proteins		Species	Score	Length	Source
Q12873	DNA helicase		TUPCH		2077	UniRef50_Q12873
DNA helicase		MOSMO		2062
DNA helicase		ZALCA		2061
DNA helicase		CAPHI		2061
DNA helicase		PHOSS		2060
+1285

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U91543 mRNA Translation: AAC39923.1 AC104581 Genomic DNA No translation available. CH471108 Genomic DNA Translation: EAW90114.1 CH471108 Genomic DNA Translation: EAW90116.1 AF006515 mRNA Translation: AAB87383.1 Different termination. U08379 mRNA Translation: AAC50228.1
CCDSⁱ	CCDS32553.2 [Q12873-3] CCDS32554.1 [Q12873-1] CCDS32555.1 [Q12873-2]
RefSeqⁱ	NP_001005271.2, NM_001005271.2 [Q12873-3] NP_001005273.1, NM_001005273.2 [Q12873-1] NP_005843.2, NM_005852.3 [Q12873-2]

3D structure databases

AlphaFoldDBⁱ	Q12873
SMRⁱ	Q12873
ModBaseⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	107532, 715 interactors
ComplexPortalⁱ	CPX-880, MBD2/NuRD nucleosome remodeling and deacetylase complex CPX-922, MBD3/NuRD nucleosome remodeling and deacetylase complex
CORUMⁱ	Q12873
DIPⁱ	DIP-32496N
ELMⁱ	Q12873
IntActⁱ	Q12873, 157 interactors
MINTⁱ	Q12873
STRINGⁱ	9606.ENSP00000369716

Protein family/group databases

MoonDBⁱ	Q12873, Predicted

MoonDBⁱ

Q12873, Predicted

PTM databases

GlyGenⁱ	Q12873, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	Q12873
MetOSiteⁱ	Q12873
PhosphoSitePlusⁱ	Q12873
SwissPalmⁱ	Q12873

Genetic variation databases

BioMutaⁱ	CHD3
DMDMⁱ	88911273

Proteomic databases

EPDⁱ	Q12873
jPOSTⁱ	Q12873
MassIVEⁱ	Q12873
MaxQBⁱ	Q12873
PaxDbⁱ	Q12873
PeptideAtlasⁱ	Q12873
PRIDEⁱ	Q12873
ProteomicsDBⁱ	20268 58995 [Q12873-1] 58996 [Q12873-2]

Protocols and materials databases

ABCDⁱ	Q12873, 1 sequenced antibody
Antibodypediaⁱ	12273, 304 antibodies from 38 providers
The DNASU plasmid repository More...DNASUⁱ	1107

Genome annotation databases

Ensemblⁱ	ENST00000330494.12; ENSP00000332628.7; ENSG00000170004.18 ENST00000358181.8; ENSP00000350907.4; ENSG00000170004.18 [Q12873-2] ENST00000380358.9; ENSP00000369716.4; ENSG00000170004.18 [Q12873-3]
GeneIDⁱ	1107
KEGGⁱ	hsa:1107
MANE-Selectⁱ	ENST00000330494.12; ENSP00000332628.7; NM_001005273.3; NP_001005273.1
UCSCⁱ	uc002gjd.3, human [Q12873-1]

Organism-specific databases

CTDⁱ	1107
DisGeNETⁱ	1107
GeneCardsⁱ	CHD3
HGNCⁱ	HGNC:1918, CHD3
HPAⁱ	ENSG00000170004, Low tissue specificity
MalaCardsⁱ	CHD3
MIMⁱ	602120, gene 618205, phenotype
neXtProtⁱ	NX_Q12873
OpenTargetsⁱ	ENSG00000170004
PharmGKBⁱ	PA26454
VEuPathDBⁱ	HostDB:ENSG00000170004
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0383, Eukaryota
GeneTreeⁱ	ENSGT00940000158001
HOGENOMⁱ	CLU_000315_22_2_1
InParanoidⁱ	Q12873
OMAⁱ	MIRKPVE
OrthoDBⁱ	54215at2759
PhylomeDBⁱ	Q12873
TreeFamⁱ	TF106448

Enzyme and pathway databases

PathwayCommonsⁱ	Q12873
Reactomeⁱ	R-HSA-3214815, HDACs deacetylate histones R-HSA-427389, ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression R-HSA-4551638, SUMOylation of chromatin organization proteins R-HSA-6804758, Regulation of TP53 Activity through Acetylation R-HSA-73762, RNA Polymerase I Transcription Initiation R-HSA-8943724, Regulation of PTEN gene transcription R-HSA-9679191, Potential therapeutics for SARS
SignaLinkⁱ	Q12873
SIGNORⁱ	Q12873

Miscellaneous databases

BioGRID-ORCSⁱ	1107, 14 hits in 1097 CRISPR screens
ChiTaRSⁱ	CHD3, human
GeneWikiⁱ	CHD3
GenomeRNAiⁱ	1107
Pharosⁱ	Q12873, Tbio
Protein Ontology More...PROⁱ	PR:Q12873
RNActⁱ	Q12873, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000170004, Expressed in cortical plate and 228 other tissues
ExpressionAtlasⁱ	Q12873, baseline and differential
Genevisibleⁱ	Q12873, HS

Family and domain databases

Gene3Dⁱ	1.10.30.10, 1 hit 3.30.40.10, 2 hits 3.40.50.10810, 1 hit 3.40.50.300, 1 hit
InterProⁱ	View protein in InterPro IPR012957, CHD_C2 IPR009462, CHD_II_SANT-like IPR012958, CHD_N IPR016197, Chromo-like_dom_sf IPR000953, Chromo/chromo_shadow_dom IPR023780, Chromo_domain IPR023779, Chromodomain_CS IPR002464, DNA/RNA_helicase_DEAH_CS IPR009463, DUF1087 IPR014001, Helicase_ATP-bd IPR001650, Helicase_C IPR036910, HMG_box_dom_sf IPR027417, P-loop_NTPase IPR038718, SNF2-like_sf IPR000330, SNF2_N IPR019786, Zinc_finger_PHD-type_CS IPR011011, Znf_FYVE_PHD IPR001965, Znf_PHD IPR019787, Znf_PHD-finger IPR013083, Znf_RING/FYVE/PHD
Pfamⁱ	View protein in Pfam PF08074, CHDCT2, 1 hit PF08073, CHDNT, 1 hit PF00385, Chromo, 1 hit PF06461, DUF1086, 1 hit PF06465, DUF1087, 1 hit PF00271, Helicase_C, 1 hit PF00628, PHD, 2 hits PF00176, SNF2-rel_dom, 1 hit
SMARTⁱ	View protein in SMART SM00298, CHROMO, 2 hits SM00487, DEXDc, 1 hit SM01146, DUF1086, 1 hit SM01147, DUF1087, 1 hit SM00490, HELICc, 1 hit SM00249, PHD, 2 hits
SUPFAMⁱ	SSF47095, SSF47095, 1 hit SSF52540, SSF52540, 2 hits SSF54160, SSF54160, 2 hits SSF57903, SSF57903, 1 hit
PROSITEⁱ	View protein in PROSITE PS00598, CHROMO_1, 1 hit PS50013, CHROMO_2, 2 hits PS00690, DEAH_ATP_HELICASE, 1 hit PS51192, HELICASE_ATP_BIND_1, 1 hit PS51194, HELICASE_CTER, 1 hit PS01359, ZF_PHD_1, 2 hits PS50016, ZF_PHD_2, 2 hits
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CHD3_HUMAN
Accessionⁱ	Q12873Primary (citable) accession number: Q12873 Secondary accession number(s): D3DTQ9, E9PG89, Q9Y4I0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
	Last sequence update:	February 7, 2006
	Last modified:	May 25, 2022
	This is version 222 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

Reference proteome

Documents

Human chromosome 17
Human chromosome 17: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
SIMILARITY comments
Index of protein domains and families

UniProtKB

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Help

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Supporting data

UniProtKB - Q12873 (CHD3_HUMAN)

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Chromodomain-helicase-DNA-binding protein 3

CHD3

Select a section on the left to see content.

<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

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

Protein family/group 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

Cytoskeleton

Cytoskeleton

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

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Genetic variation 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

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

Q12873

Protein-protein interaction databases

Miscellaneous 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

3D structure 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

Domains and Repeats

Region

Motif

Compositional bias

<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

Zinc finger

Keywords - Domaini

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

Natural variant

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

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Genetic variation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ