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Protein

Chromodomain-helicase-DNA-binding protein 3

Gene

CHD3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri379 – 426PHD-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri456 – 503PHD-type 2PROSITE-ProRule annotationAdd BLAST48
Nucleotide bindingi761 – 768ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: ProtInc
  • DNA binding Source: ProtInc
  • helicase activity Source: UniProtKB
  • histone deacetylase activity Source: Reactome
  • poly(A) RNA binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • centrosome organization Source: UniProtKB
  • chromatin assembly or disassembly Source: Ensembl
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • spindle organization Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000170004-MONOMER.
ReactomeiR-HSA-3214815. HDACs deacetylate histones.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-73762. RNA Polymerase I Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromodomain-helicase-DNA-binding protein 3 (EC:3.6.4.12)
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:1918. CHD3.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • intermediate filament cytoskeleton Source: HPA
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • NuRD complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi1107.
OpenTargetsiENSG00000170004.
PharmGKBiPA26454.

Polymorphism and mutation databases

BioMutaiCHD3.
DMDMi88911273.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000802271 – 2000Chromodomain-helicase-DNA-binding protein 3Add BLAST2000

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei79PhosphoserineCombined sources1
Modified residuei324PhosphoserineCombined sources1
Modified residuei597PhosphoserineCombined sources1
Modified residuei713PhosphoserineCombined sources1
Cross-linki721Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki1308Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1367PhosphoserineCombined sources1
Modified residuei1601PhosphoserineCombined sources1
Modified residuei1605PhosphoserineCombined sources1
Modified residuei1646PhosphothreonineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ12873.
MaxQBiQ12873.
PaxDbiQ12873.
PeptideAtlasiQ12873.
PRIDEiQ12873.

PTM databases

iPTMnetiQ12873.
PhosphoSitePlusiQ12873.
SwissPalmiQ12873.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000170004.
CleanExiHS_CHD3.
ExpressionAtlasiQ12873. baseline and differential.
GenevisibleiQ12873. HS.

Organism-specific databases

HPAiHPA043368.

Interactioni

Subunit structurei

Central component of the nucleosome remodeling and histone deacetylase (NuRD) repressive complex. Interacts with TRIM28 and SERBP1. Interacts (via its C-terminal) with HABP4. Interacts with PCNT; the interaction regulates centrosome integrity.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BARD1Q997282EBI-523590,EBI-473181
DDX5P178444EBI-523590,EBI-351962
GIT1Q9Y2X72EBI-523590,EBI-466061
HTTP428583EBI-523590,EBI-466029
KDM1AO603414EBI-523590,EBI-710124
PRPF40AO754002EBI-523590,EBI-473291
SERBP1Q8NC515EBI-523590,EBI-523558
SUMO2P619563EBI-523590,EBI-473220

Protein-protein interaction databases

BioGridi107532. 151 interactors.
DIPiDIP-32496N.
IntActiQ12873. 110 interactors.
MINTiMINT-1185641.
STRINGi9606.ENSP00000369716.

Structurei

3D structure databases

ProteinModelPortaliQ12873.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini494 – 594Chromo 1PROSITE-ProRule annotationAdd BLAST101
Domaini631 – 673Chromo 2PROSITE-ProRule annotationAdd BLAST43
Domaini748 – 932Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST185
Domaini1064 – 1229Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1566 – 1966Required for interaction with PCNT1 PublicationAdd BLAST401

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi883 – 886DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi206 – 221Poly-AlaAdd BLAST16
Compositional biasi243 – 246Poly-Pro4
Compositional biasi355 – 358Poly-Lys4
Compositional biasi434 – 446Poly-GluAdd BLAST13
Compositional biasi697 – 703Poly-Lys7

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 2 chromo domains.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri379 – 426PHD-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri456 – 503PHD-type 2PROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0383. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000231124.
HOVERGENiHBG005326.
InParanoidiQ12873.
KOiK11642.
OMAiMNIPEYD.
OrthoDBiEOG091G00G4.
PhylomeDBiQ12873.
TreeFamiTF106448.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR028722. CHD3.
IPR012957. CHD_C2.
IPR012958. CHD_N.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR009462. DUF1086.
IPR009463. DUF1087.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR009071. HMG_box_dom.
IPR027417. P-loop_NTPase.
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.
[Graphical view]
PANTHERiPTHR10799:SF544. PTHR10799:SF544. 4 hits.
PfamiPF08074. 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_N. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM01146. DUF1086. 1 hit.
SM01147. DUF1087. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS00598. 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.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q12873-1) [UniParc]FASTAAdd 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
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
GO
Isoform 2 (identifier: Q12873-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,966
Mass (Da):222,861
Checksum:iF8D7B7C132B263A6
GO
Isoform 3 (identifier: Q12873-3) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:2,059
Mass (Da):233,037
Checksum:i3C71593E3C788027
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti121 – 126GEGDGG → PHFQQK in AAC50228 (PubMed:7560064).Curated6
Sequence conflicti309 – 312Missing in AAC50228 (PubMed:7560064).Curated4
Sequence conflicti653W → G in AAC50228 (PubMed:7560064).Curated1
Sequence conflicti1704K → N in AAC39923 (PubMed:9688266).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0487283A → V.Corresponds to variant rs931543dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0470971 – 32MKAAD…WGDRM → MASPLRDEEEEEEEMVVSEE EEEEEEEGDEEEEEEVEAAD EDDEEDDDEGVLGRGPGHDR GRDRHSPPGCHLFPPPPPPP PPLPPPPPPPP in isoform 3. CuratedAdd BLAST32
Alternative sequenceiVSP_0172311642 – 1675Missing in isoform 2. 2 PublicationsAdd BLAST34

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.
CCDSiCCDS32553.2. [Q12873-3]
CCDS32554.1. [Q12873-1]
CCDS32555.1. [Q12873-2]
RefSeqiNP_001005271.2. NM_001005271.2. [Q12873-3]
NP_001005273.1. NM_001005273.2. [Q12873-1]
NP_005843.2. NM_005852.3. [Q12873-2]
UniGeneiHs.25601.

Genome annotation databases

EnsembliENST00000330494; ENSP00000332628; ENSG00000170004. [Q12873-1]
ENST00000358181; ENSP00000350907; ENSG00000170004. [Q12873-2]
ENST00000380358; ENSP00000369716; ENSG00000170004. [Q12873-3]
GeneIDi1107.
KEGGihsa:1107.
UCSCiuc002gjd.3. human. [Q12873-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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.
CCDSiCCDS32553.2. [Q12873-3]
CCDS32554.1. [Q12873-1]
CCDS32555.1. [Q12873-2]
RefSeqiNP_001005271.2. NM_001005271.2. [Q12873-3]
NP_001005273.1. NM_001005273.2. [Q12873-1]
NP_005843.2. NM_005852.3. [Q12873-2]
UniGeneiHs.25601.

3D structure databases

ProteinModelPortaliQ12873.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107532. 151 interactors.
DIPiDIP-32496N.
IntActiQ12873. 110 interactors.
MINTiMINT-1185641.
STRINGi9606.ENSP00000369716.

PTM databases

iPTMnetiQ12873.
PhosphoSitePlusiQ12873.
SwissPalmiQ12873.

Polymorphism and mutation databases

BioMutaiCHD3.
DMDMi88911273.

Proteomic databases

EPDiQ12873.
MaxQBiQ12873.
PaxDbiQ12873.
PeptideAtlasiQ12873.
PRIDEiQ12873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330494; ENSP00000332628; ENSG00000170004. [Q12873-1]
ENST00000358181; ENSP00000350907; ENSG00000170004. [Q12873-2]
ENST00000380358; ENSP00000369716; ENSG00000170004. [Q12873-3]
GeneIDi1107.
KEGGihsa:1107.
UCSCiuc002gjd.3. human. [Q12873-1]

Organism-specific databases

CTDi1107.
DisGeNETi1107.
GeneCardsiCHD3.
H-InvDBHIX0013516.
HGNCiHGNC:1918. CHD3.
HPAiHPA043368.
MIMi602120. gene.
neXtProtiNX_Q12873.
OpenTargetsiENSG00000170004.
PharmGKBiPA26454.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0383. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000231124.
HOVERGENiHBG005326.
InParanoidiQ12873.
KOiK11642.
OMAiMNIPEYD.
OrthoDBiEOG091G00G4.
PhylomeDBiQ12873.
TreeFamiTF106448.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000170004-MONOMER.
ReactomeiR-HSA-3214815. HDACs deacetylate histones.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-73762. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSiCHD3. human.
GeneWikiiCHD3.
GenomeRNAii1107.
PROiQ12873.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000170004.
CleanExiHS_CHD3.
ExpressionAtlasiQ12873. baseline and differential.
GenevisibleiQ12873. HS.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR028722. CHD3.
IPR012957. CHD_C2.
IPR012958. CHD_N.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR009462. DUF1086.
IPR009463. DUF1087.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR009071. HMG_box_dom.
IPR027417. P-loop_NTPase.
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.
[Graphical view]
PANTHERiPTHR10799:SF544. PTHR10799:SF544. 4 hits.
PfamiPF08074. 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_N. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM01146. DUF1086. 1 hit.
SM01147. DUF1087. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS00598. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCHD3_HUMAN
AccessioniPrimary (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: November 30, 2016
This is version 181 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.