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Q12873

- CHD3_HUMAN

UniProt

Q12873 - CHD3_HUMAN

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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

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 1
Add
BLAST
Zinc fingeri456 – 50348PHD-type 2
Add
BLAST
Nucleotide bindingi761 – 7688ATP Reviewed prediction

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
Complete GO annotation...

GO - Biological processi

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

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

GO - Cellular componenti

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

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 3
PRO_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. 95 interactions.
MINTiMINT-1185641.
STRINGi9606.ENSP00000369716.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini494 – 594101Chromo 1
Add
BLAST
Domaini631 – 67343Chromo 2
Add
BLAST
Domaini748 – 932185Helicase ATP-binding
Add
BLAST
Domaini1064 – 1229166Helicase C-terminal
Add
BLAST

Region

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

Motif

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

Compositional bias

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

Sequence similaritiesi

Contains 2 chromo domains.

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.

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.
VSP_047097Add
BLAST
Alternative sequencei1642 – 167534Missing in isoform 2.
VSP_017231Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1266GEGDGG → PHFQQK in AAC50228. 1 Publication
Sequence conflicti309 – 3124Missing in AAC50228. 1 Publication
Sequence conflicti653 – 6531W → G in AAC50228. 1 Publication
Sequence conflicti1704 – 17041K → N in AAC39923. 1 Publication

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...

Protein-protein interaction databases

BioGridi 107532. 126 interactions.
DIPi DIP-32496N.
IntActi Q12873. 95 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 156 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

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