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Q12873 (CHD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromodomain-helicase-DNA-binding protein 3

Short name=CHD-3
EC=3.6.4.12
Alternative name(s):
ATP-dependent helicase CHD3
Mi-2 autoantigen 240 kDa protein
Mi2-alpha
Zinc finger helicase
Short name=hZFH
Gene names
Name:CHD3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2000 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.10

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. Ref.7 Ref.8 Ref.10

Subcellular location

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Associates with centrosomes in interphase and mitosis. Ref.10

Tissue specificity

Widely expressed. Ref.1

Miscellaneous

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

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 2 chromo domains.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 2 PHD-type zinc fingers.

Sequence caution

The sequence AAB87383.1 differs from that shown. Reason: Differs from position 1967 onward for unknown reasons.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandATP-binding
DNA-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionChromatin regulator
Helicase
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcentrosome organization

Inferred from direct assay Ref.10. Source: UniProtKB

chromatin assembly or disassembly

Inferred from electronic annotation. Source: Ensembl

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.4. Source: ProtInc

spindle organization

Inferred from direct assay Ref.10. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNuRD complex

Inferred from direct assay PubMed 17827154. Source: BHF-UCL

centrosome

Inferred from direct assay Ref.10. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

intermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Traceable author statement Ref.4. Source: ProtInc

DNA binding

Traceable author statement Ref.4. Source: ProtInc

zinc ion binding

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12873-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q12873-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1642-1675: Missing.
Isoform 3 (identifier: Q12873-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20002000Chromodomain-helicase-DNA-binding protein 3
PRO_0000080227

Regions

Domain494 – 594101Chromo 1
Domain631 – 67343Chromo 2
Domain748 – 932185Helicase ATP-binding
Domain1064 – 1229166Helicase C-terminal
Zinc finger379 – 42648PHD-type 1
Zinc finger456 – 50348PHD-type 2
Nucleotide binding761 – 7688ATP Potential
Region1566 – 1966401Required for interaction with PCNT
Motif883 – 8864DEAH box
Compositional bias206 – 22116Poly-Ala
Compositional bias243 – 2464Poly-Pro
Compositional bias355 – 3584Poly-Lys
Compositional bias434 – 44613Poly-Glu
Compositional bias697 – 7037Poly-Lys

Amino acid modifications

Modified residue3241Phosphoserine Ref.9
Modified residue7131Phosphoserine Ref.12 Ref.14
Modified residue13671Phosphoserine Ref.12
Modified residue16011Phosphoserine Ref.9 Ref.11 Ref.12 Ref.14 Ref.15
Modified residue16051Phosphoserine Ref.9 Ref.12 Ref.14 Ref.15

Natural variations

Alternative sequence1 – 3232MKAAD…WGDRM → MASPLRDEEEEEEEMVVSEE EEEEEEEGDEEEEEEVEAAD EDDEEDDDEGVLGRGPGHDR GRDRHSPPGCHLFPPPPPPP PPLPPPPPPPP in isoform 3.
VSP_047097
Alternative sequence1642 – 167534Missing in isoform 2.
VSP_017231
Natural variant31A → V.
Corresponds to variant rs931543 [ dbSNP | Ensembl ].
VAR_048728

Experimental info

Sequence conflict121 – 1266GEGDGG → PHFQQK in AAC50228. Ref.5
Sequence conflict309 – 3124Missing in AAC50228. Ref.5
Sequence conflict6531W → G in AAC50228. Ref.5
Sequence conflict17041K → N in AAC39923. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 7, 2006. Version 3.
Checksum: 4494F56E5D0E7083

FASTA2,000226,592
        10         20         30         40         50         60 
MKAADTVILW ARSKNDQLRI SFPPGLCWGD RMPDKDDIRL LPSALGVKKR KRGPKKQKEN 

        70         80         90        100        110        120 
KPGKPRKRKK RDSEEEFGSE RDEYREKSES GGSEYGTGPG RKRRRKHREK KEKKTKRRKK 

       130        140        150        160        170        180 
GEGDGGQKQV EQKSSATLLL TWGLEDVEHV FSEEDYHTLT NYKAFSQFMR PLIAKKNPKI 

       190        200        210        220        230        240 
PMSKMMTILG AKWREFSANN PFKGSAAAVA AAAAAAAAAV AEQVSAAVSS ATPIAPSGPP 

       250        260        270        280        290        300 
ALPPPPAADI QPPPIRRAKT KEGKGPGHKR RSKSPRVPDG RKKLRGKKMA PLKIKLGLLG 

       310        320        330        340        350        360 
GKRKKGGSYV FQSDEGPEPE AEESDLDSGS VHSASGRPDG PVRTKKLKRG RPGRKKKKVL 

       370        380        390        400        410        420 
GCPAVAGEEE VDGYETDHQD YCEVCQQGGE IILCDTCPRA YHLVCLDPEL DRAPEGKWSC 

       430        440        450        460        470        480 
PHCEKEGVQW EAKEEEEEYE EEGEEEGEKE EEDDHMEYCR VCKDGGELLC CDACISSYHI 

       490        500        510        520        530        540 
HCLNPPLPDI PNGEWLCPRC TCPVLKGRVQ KILHWRWGEP PVAVPAPQQA DGNPDVPPPR 

       550        560        570        580        590        600 
PLQGRSEREF FVKWVGLSYW HCSWAKELQL EIFHLVMYRN YQRKNDMDEP PPLDYGSGED 

       610        620        630        640        650        660 
DGKSDKRKVK DPHYAEMEEK YYRFGIKPEW MTVHRIINHS VDKKGNYHYL VKWRDLPYDQ 

       670        680        690        700        710        720 
STWEEDEMNI PEYEEHKQSY WRHRELIMGE DPAQPRKYKK KKKELQGDGP PSSPTNDPTV 

       730        740        750        760        770        780 
KYETQPRFIT ATGGTLHMYQ LEGLNWLRFS WAQGTDTILA DEMGLGKTIQ TIVFLYSLYK 

       790        800        810        820        830        840 
EGHTKGPFLV SAPLSTIINW EREFQMWAPK FYVVTYTGDK DSRAIIRENE FSFEDNAIKG 

       850        860        870        880        890        900 
GKKAFKMKRE AQVKFHVLLT SYELITIDQA ALGSIRWACL VVDEAHRLKN NQSKFFRVLN 

       910        920        930        940        950        960 
GYKIDHKLLL TGTPLQNNLE ELFHLLNFLT PERFNNLEGF LEEFADISKE DQIKKLHDLL 

       970        980        990       1000       1010       1020 
GPHMLRRLKA DVFKNMPAKT ELIVRVELSP MQKKYYKYIL TRNFEALNSR GGGNQVSLLN 

      1030       1040       1050       1060       1070       1080 
IMMDLKKCCN HPYLFPVAAM ESPKLPSGAY EGGALIKSSG KLMLLQKMLR KLKEQGHRVL 

      1090       1100       1110       1120       1130       1140 
IFSQMTKMLD LLEDFLDYEG YKYERIDGGI TGALRQEAID RFNAPGAQQF CFLLSTRAGG 

      1150       1160       1170       1180       1190       1200 
LGINLATADT VIIFDSDWNP HNDIQAFSRA HRIGQANKVM IYRFVTRASV EERITQVAKR 

      1210       1220       1230       1240       1250       1260 
KMMLTHLVVR PGLGSKAGSM SKQELDDILK FGTEELFKDE NEGENKEEDS SVIHYDNEAI 

      1270       1280       1290       1300       1310       1320 
ARLLDRNQDA TEDTDVQNMN EYLSSFKVAQ YVVREEDKIE EIEREIIKQE ENVDPDYWEK 

      1330       1340       1350       1360       1370       1380 
LLRHHYEQQQ EDLARNLGKG KRVRKQVNYN DAAQEDQDNQ SEYSVGSEEE DEDFDERPEG 

      1390       1400       1410       1420       1430       1440 
RRQSKRQLRN EKDKPLPPLL ARVGGNIEVL GFNTRQRKAF LNAVMRWGMP PQDAFTTQWL 

      1450       1460       1470       1480       1490       1500 
VRDLRGKTEK EFKAYVSLFM RHLCEPGADG SETFADGVPR EGLSRQQVLT RIGVMSLVKK 

      1510       1520       1530       1540       1550       1560 
KVQEFEHING RWSMPELMPD PSADSKRSSR ASSPTKTSPT TPEASATNSP CTSKPATPAP 

      1570       1580       1590       1600       1610       1620 
SEKGEGIRTP LEKEEAENQE EKPEKNSRIG EKMETEADAP SPAPSLGERL EPRKIPLEDE 

      1630       1640       1650       1660       1670       1680 
VPGVPGEMEP EPGYRGDREK SATESTPGER GEEKPLDGQE HRERPEGETG DLGKREDVKG 

      1690       1700       1710       1720       1730       1740 
DRELRPGPRD EPRSNGRREE KTEKPRFMFN IADGGFTELH TLWQNEERAA ISSGKLNEIW 

      1750       1760       1770       1780       1790       1800 
HRRHDYWLLA GIVLHGYARW QDIQNDAQFA IINEPFKTEA NKGNFLEMKN KFLARRFKLL 

      1810       1820       1830       1840       1850       1860 
EQALVIEEQL RRAAYLNLSQ EPAHPAMALH ARFAEAECLA ESHQHLSKES LAGNKPANAV 

      1870       1880       1890       1900       1910       1920 
LHKVLNQLEE LLSDMKADVT RLPATLSRIP PIAARLQMSE RSILSRLASK GTEPHPTPAY 

      1930       1940       1950       1960       1970       1980 
PPGPYATPPG YGAAFSAAPV GALAAAGANY SQMPAGSFIT AATNGPPVLV KKEKEMVGAL 

      1990       2000 
VSDGLDRKEP RAGEVICIDD 

« Hide

Isoform 2 [UniParc].

Checksum: F8D7B7C132B263A6
Show »

FASTA1,966222,861
Isoform 3 [UniParc].

Checksum: 3C71593E3C788027
Show »

FASTA2,059233,037

References

« Hide 'large scale' references
[1]"Identification of a human 17p-located cDNA encoding a protein of the Snf2-like helicase family."
Aubry F., Mattei M.-G., Galibert F.
Eur. J. Biochem. 254:558-564(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
[2]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Characterization of the CHD family of proteins."
Woodage T., Basrai M.A., Baxevanis A.D., Hieter P., Collins F.S.
Proc. Natl. Acad. Sci. U.S.A. 94:11472-11477(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1966 (ISOFORM 2).
Tissue: Fetus.
[5]"Molecular analysis of a major antigenic region of the 240 kD protein of Mi-2 autoantigen."
Ge Q., Nilasena D.S., O'Brien C.A., Frank M.B., Targoff I.N.
J. Clin. Invest. 96:1730-1737(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 121-654.
Tissue: Thymus.
[6]"Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex."
Tong J.K., Hassig C.A., Schnitzler G.R., Kingston R.E., Schreiber S.L.
Nature 395:917-921(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A COMPONENT OF THE NURD COMPLEX, FUNCTION.
[7]"Targeting histone deacetylase complexes via KRAB-zinc finger proteins: the PHD and bromodomains of KAP-1 form a cooperative unit that recruits a novel isoform of the Mi-2alpha subunit of NuRD."
Schultz D.C., Friedman J.R., Rauscher F.J. III
Genes Dev. 15:428-443(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM28.
[8]"Characterization of a new family of proteins that interact with the C-terminal region of the chromatin-remodeling factor CHD-3."
Lemos T.A., Passos D.O., Nery F.C., Kobarg J.
FEBS Lett. 533:14-20(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HABP4 AND SERBP1.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-1601 AND SER-1605, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Chromatin remodeling proteins interact with pericentrin to regulate centrosome integrity."
Sillibourne J.E., Delaval B., Redick S., Sinha M., Doxsey S.J.
Mol. Biol. Cell 18:3667-3680(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PCNT, SUBCELLULAR LOCATION, FUNCTION.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1601, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-1367; SER-1601 AND SER-1605, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-1601 AND SER-1605, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1601 AND SER-1605, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001005271.2. NM_001005271.2.
NP_001005273.1. NM_001005273.2.
NP_005843.2. NM_005852.3.
UniGeneHs.25601.

3D structure databases

ProteinModelPortalQ12873.
SMRQ12873. Positions 350-1287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107532. 123 interactions.
DIPDIP-32496N.
IntActQ12873. 95 interactions.
MINTMINT-1185641.
STRING9606.ENSP00000369716.

PTM databases

PhosphoSiteQ12873.

Polymorphism databases

DMDM88911273.

Proteomic databases

PaxDbQ12873.
PRIDEQ12873.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330494; ENSP00000332628; ENSG00000170004. [Q12873-1]
ENST00000358181; ENSP00000350907; ENSG00000170004. [Q12873-2]
ENST00000380358; ENSP00000369716; ENSG00000170004. [Q12873-3]
GeneID1107.
KEGGhsa:1107.
UCSCuc002gje.2. human. [Q12873-1]
uc002gjf.2. human. [Q12873-2]

Organism-specific databases

CTD1107.
GeneCardsGC17P007788.
H-InvDBHIX0013516.
HGNCHGNC:1918. CHD3.
HPAHPA043368.
MIM602120. gene.
neXtProtNX_Q12873.
PharmGKBPA26454.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOGENOMHOG000231124.
HOVERGENHBG005326.
KOK11642.
OMAEPEPGYR.
OrthoDBEOG7C8GG7.
PhylomeDBQ12873.
TreeFamTF106448.

Gene expression databases

ArrayExpressQ12873.
BgeeQ12873.
CleanExHS_CHD3.
GenevestigatorQ12873.

Family and domain databases

Gene3D1.10.30.10. 1 hit.
3.30.40.10. 2 hits.
InterProIPR028722. CHD3.
IPR012957. CHD_C2.
IPR012958. CHD_N.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
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.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERPTHR10799:SF464. PTHR10799:SF464. 1 hit.
PfamPF08074. CHDCT2. 1 hit.
PF08073. CHDNT. 1 hit.
PF00385. Chromo. 2 hits.
PF06461. DUF1086. 1 hit.
PF06465. DUF1087. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00628. PHD. 2 hits.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMSSF47095. SSF47095. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEPS00598. 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]
ProtoNetSearch...

Other

ChiTaRSCHD3. human.
GeneWikiCHD3.
GenomeRNAi1107.
NextBio4590.
PROQ12873.
SOURCESearch...

Entry information

Entry nameCHD3_HUMAN
AccessionPrimary (citable) accession number: Q12873
Secondary accession number(s): D3DTQ9, E9PG89, Q9Y4I0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 7, 2006
Last modified: March 19, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM