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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 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. 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
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_228222. HDACs deacetylate histones.
REACT_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
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 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

BgeeiQ12873.
CleanExiHS_CHD3.
ExpressionAtlasiQ12873. baseline and differential.
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. 129 interactions.
DIPiDIP-32496N.
IntActiQ12873. 96 interactions.
MINTiMINT-1185641.
STRINGi9606.ENSP00000369716.

Structurei

3D structure databases

ProteinModelPortaliQ12873.
SMRiQ12873. Positions 374-508, 627-683, 758-1209.
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.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000231124.
HOVERGENiHBG005326.
InParanoidiQ12873.
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

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

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:
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.
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:
EMBLi
GenBanki
DDBJi
Links Updated
U91543 mRNA. Translation: AAC39923.1 .
AC104581 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90114.1 .
CH471108 Genomic DNA. Translation: EAW90116.1 .
AF006515 mRNA. Translation: AAB87383.1 . Different termination.
U08379 mRNA. Translation: AAC50228.1 .
CCDSi CCDS32553.2. [Q12873-3 ]
CCDS32554.1. [Q12873-1 ]
CCDS32555.1. [Q12873-2 ]
RefSeqi NP_001005271.2. NM_001005271.2. [Q12873-3 ]
NP_001005273.1. NM_001005273.2. [Q12873-1 ]
NP_005843.2. NM_005852.3. [Q12873-2 ]
UniGenei Hs.25601.

3D structure databases

ProteinModelPortali Q12873.
SMRi Q12873. Positions 374-508, 627-683, 758-1209.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107532. 129 interactions.
DIPi DIP-32496N.
IntActi Q12873. 96 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.
GeneTreei ENSGT00760000119067.
HOGENOMi HOG000231124.
HOVERGENi HBG005326.
InParanoidi Q12873.
KOi K11642.
OMAi EPEPGYR.
OrthoDBi EOG7C8GG7.
PhylomeDBi Q12873.
TreeFami TF106448.

Enzyme and pathway databases

Reactomei REACT_228222. HDACs deacetylate histones.
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

Bgeei Q12873.
CleanExi HS_CHD3.
ExpressionAtlasi Q12873. baseline and differential.
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: November 26, 2014
This is version 159 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