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Q12873

- CHD3_HUMAN

UniProt

Q12873 - CHD3_HUMAN

Protein

Chromodomain-helicase-DNA-binding protein 3

Gene

CHD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (07 Feb 2006)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri379 – 42648PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri456 – 50348PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi761 – 7688ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent DNA helicase activity Source: ProtInc
    3. DNA binding Source: ProtInc
    4. helicase activity Source: UniProtKB
    5. poly(A) RNA binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. centrosome organization Source: UniProtKB
    2. chromatin assembly or disassembly Source: Ensembl
    3. chromatin modification Source: UniProtKB-KW
    4. DNA duplex unwinding Source: GOC
    5. regulation of transcription, DNA-templated Source: UniProtKB
    6. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    7. spindle organization Source: UniProtKB
    8. transcription, DNA-templated Source: UniProtKB-KW

    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

    ReactomeiREACT_953. 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
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:1918. CHD3.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
    Note: Associates with centrosomes in interphase and mitosis.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. intermediate filament cytoskeleton Source: HPA
    4. nucleolus Source: HPA
    5. nucleus Source: UniProtKB
    6. NuRD complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26454.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20002000Chromodomain-helicase-DNA-binding protein 3PRO_0000080227Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei324 – 3241Phosphoserine1 Publication
    Modified residuei713 – 7131Phosphoserine2 Publications
    Modified residuei1367 – 13671Phosphoserine1 Publication
    Modified residuei1601 – 16011Phosphoserine5 Publications
    Modified residuei1605 – 16051Phosphoserine4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ12873.
    PaxDbiQ12873.
    PRIDEiQ12873.

    PTM databases

    PhosphoSiteiQ12873.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ12873.
    BgeeiQ12873.
    CleanExiHS_CHD3.
    GenevestigatoriQ12873.

    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. 126 interactions.
    DIPiDIP-32496N.
    IntActiQ12873. 94 interactions.
    MINTiMINT-1185641.
    STRINGi9606.ENSP00000369716.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12873.
    SMRiQ12873. Positions 374-508, 627-683, 734-1231.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini494 – 594101Chromo 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini631 – 67343Chromo 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini748 – 932185Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1064 – 1229166Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1566 – 1966401Required for interaction with PCNTAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi883 – 8864DEAH box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi206 – 22116Poly-AlaAdd
    BLAST
    Compositional biasi243 – 2464Poly-Pro
    Compositional biasi355 – 3584Poly-Lys
    Compositional biasi434 – 44613Poly-GluAdd
    BLAST
    Compositional biasi697 – 7037Poly-Lys

    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)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri379 – 42648PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri456 – 50348PHD-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0553.
    HOGENOMiHOG000231124.
    HOVERGENiHBG005326.
    KOiK11642.
    OMAiEPEPGYR.
    OrthoDBiEOG7C8GG7.
    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.
    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]
    PANTHERiPTHR10799:SF544. PTHR10799:SF544. 1 hit.
    PfamiPF08074. 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]
    SMARTiSM00298. CHROMO. 2 hits.
    SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00249. PHD. 2 hits.
    SM00184. RING. 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. Align

    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

    MKAADTVILW ARSKNDQLRI SFPPGLCWGD RMPDKDDIRL LPSALGVKKR     50
    KRGPKKQKEN KPGKPRKRKK RDSEEEFGSE RDEYREKSES GGSEYGTGPG 100
    RKRRRKHREK KEKKTKRRKK GEGDGGQKQV EQKSSATLLL TWGLEDVEHV 150
    FSEEDYHTLT NYKAFSQFMR PLIAKKNPKI PMSKMMTILG AKWREFSANN 200
    PFKGSAAAVA AAAAAAAAAV AEQVSAAVSS ATPIAPSGPP ALPPPPAADI 250
    QPPPIRRAKT KEGKGPGHKR RSKSPRVPDG RKKLRGKKMA PLKIKLGLLG 300
    GKRKKGGSYV FQSDEGPEPE AEESDLDSGS VHSASGRPDG PVRTKKLKRG 350
    RPGRKKKKVL GCPAVAGEEE VDGYETDHQD YCEVCQQGGE IILCDTCPRA 400
    YHLVCLDPEL DRAPEGKWSC PHCEKEGVQW EAKEEEEEYE EEGEEEGEKE 450
    EEDDHMEYCR VCKDGGELLC CDACISSYHI HCLNPPLPDI PNGEWLCPRC 500
    TCPVLKGRVQ KILHWRWGEP PVAVPAPQQA DGNPDVPPPR PLQGRSEREF 550
    FVKWVGLSYW HCSWAKELQL EIFHLVMYRN YQRKNDMDEP PPLDYGSGED 600
    DGKSDKRKVK DPHYAEMEEK YYRFGIKPEW MTVHRIINHS VDKKGNYHYL 650
    VKWRDLPYDQ STWEEDEMNI PEYEEHKQSY WRHRELIMGE DPAQPRKYKK 700
    KKKELQGDGP PSSPTNDPTV KYETQPRFIT ATGGTLHMYQ LEGLNWLRFS 750
    WAQGTDTILA DEMGLGKTIQ TIVFLYSLYK EGHTKGPFLV SAPLSTIINW 800
    EREFQMWAPK FYVVTYTGDK DSRAIIRENE FSFEDNAIKG GKKAFKMKRE 850
    AQVKFHVLLT SYELITIDQA ALGSIRWACL VVDEAHRLKN NQSKFFRVLN 900
    GYKIDHKLLL TGTPLQNNLE ELFHLLNFLT PERFNNLEGF LEEFADISKE 950
    DQIKKLHDLL GPHMLRRLKA DVFKNMPAKT ELIVRVELSP MQKKYYKYIL 1000
    TRNFEALNSR GGGNQVSLLN IMMDLKKCCN HPYLFPVAAM ESPKLPSGAY 1050
    EGGALIKSSG KLMLLQKMLR KLKEQGHRVL IFSQMTKMLD LLEDFLDYEG 1100
    YKYERIDGGI TGALRQEAID RFNAPGAQQF CFLLSTRAGG LGINLATADT 1150
    VIIFDSDWNP HNDIQAFSRA HRIGQANKVM IYRFVTRASV EERITQVAKR 1200
    KMMLTHLVVR PGLGSKAGSM SKQELDDILK FGTEELFKDE NEGENKEEDS 1250
    SVIHYDNEAI ARLLDRNQDA TEDTDVQNMN EYLSSFKVAQ YVVREEDKIE 1300
    EIEREIIKQE ENVDPDYWEK LLRHHYEQQQ EDLARNLGKG KRVRKQVNYN 1350
    DAAQEDQDNQ SEYSVGSEEE DEDFDERPEG RRQSKRQLRN EKDKPLPPLL 1400
    ARVGGNIEVL GFNTRQRKAF LNAVMRWGMP PQDAFTTQWL VRDLRGKTEK 1450
    EFKAYVSLFM RHLCEPGADG SETFADGVPR EGLSRQQVLT RIGVMSLVKK 1500
    KVQEFEHING RWSMPELMPD PSADSKRSSR ASSPTKTSPT TPEASATNSP 1550
    CTSKPATPAP SEKGEGIRTP LEKEEAENQE EKPEKNSRIG EKMETEADAP 1600
    SPAPSLGERL EPRKIPLEDE VPGVPGEMEP EPGYRGDREK SATESTPGER 1650
    GEEKPLDGQE HRERPEGETG DLGKREDVKG DRELRPGPRD EPRSNGRREE 1700
    KTEKPRFMFN IADGGFTELH TLWQNEERAA ISSGKLNEIW HRRHDYWLLA 1750
    GIVLHGYARW QDIQNDAQFA IINEPFKTEA NKGNFLEMKN KFLARRFKLL 1800
    EQALVIEEQL RRAAYLNLSQ EPAHPAMALH ARFAEAECLA ESHQHLSKES 1850
    LAGNKPANAV LHKVLNQLEE LLSDMKADVT RLPATLSRIP PIAARLQMSE 1900
    RSILSRLASK GTEPHPTPAY PPGPYATPPG YGAAFSAAPV GALAAAGANY 1950
    SQMPAGSFIT AATNGPPVLV KKEKEMVGAL VSDGLDRKEP RAGEVICIDD 2000
    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 AAB87383.1 differs from that shown. Reason: Differs from position 1967 onward for unknown reasons.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti121 – 1266GEGDGG → PHFQQK in AAC50228. (PubMed:7560064)Curated
    Sequence conflicti309 – 3124Missing in AAC50228. (PubMed:7560064)Curated
    Sequence conflicti653 – 6531W → G in AAC50228. (PubMed:7560064)Curated
    Sequence conflicti1704 – 17041K → N in AAC39923. (PubMed:9688266)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31A → V.
    Corresponds to variant rs931543 [ dbSNP | Ensembl ].
    VAR_048728

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3232MKAAD…WGDRM → MASPLRDEEEEEEEMVVSEE EEEEEEEGDEEEEEEVEAAD EDDEEDDDEGVLGRGPGHDR GRDRHSPPGCHLFPPPPPPP PPLPPPPPPPP in isoform 3. CuratedVSP_047097Add
    BLAST
    Alternative sequencei1642 – 167534Missing in isoform 2. 2 PublicationsVSP_017231Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    UCSCiuc002gje.2. human. [Q12873-1]
    uc002gjf.2. human. [Q12873-2]

    Polymorphism databases

    DMDMi88911273.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 ]
    UniGenei Hs.25601.

    3D structure databases

    ProteinModelPortali Q12873.
    SMRi Q12873. Positions 374-508, 627-683, 734-1231.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107532. 126 interactions.
    DIPi DIP-32496N.
    IntActi Q12873. 94 interactions.
    MINTi MINT-1185641.
    STRINGi 9606.ENSP00000369716.

    PTM databases

    PhosphoSitei Q12873.

    Polymorphism databases

    DMDMi 88911273.

    Proteomic databases

    MaxQBi Q12873.
    PaxDbi Q12873.
    PRIDEi Q12873.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330494 ; ENSP00000332628 ; ENSG00000170004 . [Q12873-1 ]
    ENST00000358181 ; ENSP00000350907 ; ENSG00000170004 . [Q12873-2 ]
    ENST00000380358 ; ENSP00000369716 ; ENSG00000170004 . [Q12873-3 ]
    GeneIDi 1107.
    KEGGi hsa:1107.
    UCSCi uc002gje.2. human. [Q12873-1 ]
    uc002gjf.2. human. [Q12873-2 ]

    Organism-specific databases

    CTDi 1107.
    GeneCardsi GC17P007788.
    H-InvDB HIX0013516.
    HGNCi HGNC:1918. CHD3.
    HPAi HPA043368.
    MIMi 602120. gene.
    neXtProti NX_Q12873.
    PharmGKBi PA26454.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0553.
    HOGENOMi HOG000231124.
    HOVERGENi HBG005326.
    KOi K11642.
    OMAi EPEPGYR.
    OrthoDBi EOG7C8GG7.
    PhylomeDBi Q12873.
    TreeFami TF106448.

    Enzyme and pathway databases

    Reactomei REACT_953. RNA Polymerase I Transcription Initiation.

    Miscellaneous databases

    ChiTaRSi CHD3. human.
    GeneWikii CHD3.
    GenomeRNAii 1107.
    NextBioi 4590.
    PROi Q12873.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12873.
    Bgeei Q12873.
    CleanExi HS_CHD3.
    Genevestigatori Q12873.

    Family and domain databases

    Gene3Di 1.10.30.10. 1 hit.
    3.30.40.10. 2 hits.
    3.40.50.300. 2 hits.
    InterProi IPR028722. 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 ]
    PANTHERi PTHR10799:SF544. PTHR10799:SF544. 1 hit.
    Pfami PF08074. 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 ]
    SMARTi SM00298. CHROMO. 2 hits.
    SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00249. PHD. 2 hits.
    SM00184. RING. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47095. SSF47095. 1 hit.
    SSF52540. SSF52540. 2 hits.
    SSF54160. SSF54160. 3 hits.
    SSF57903. SSF57903. 1 hit.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    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: October 1, 2014
    This is version 157 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

    External Data

    Dasty 3