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Q14839

- CHD4_HUMAN

UniProt

Q14839 - CHD4_HUMAN

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Protein
Chromodomain-helicase-DNA-binding protein 4
Gene
CHD4
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.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri370 – 41748PHD-type 1
Add
BLAST
Zinc fingeri449 – 49648PHD-type 2
Add
BLAST
Nucleotide bindingi751 – 7588ATP 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. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  5. protein binding Source: UniProtKB
  6. zinc ion binding Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. ATP-dependent chromatin remodeling Source: UniProt
  2. DNA duplex unwinding Source: GOC
  3. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  4. spindle assembly Source: InterPro
  5. 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 4 (EC:3.6.4.12)
Short name:
CHD-4
Alternative name(s):
ATP-dependent helicase CHD4
Mi-2 autoantigen 218 kDa protein
Mi2-beta
Gene namesi
Name:CHD4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:1919. CHD4.

Subcellular locationi

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

GO - Cellular componenti

  1. NuRD complex Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. nuclear chromatin Source: UniProt
  5. nucleoplasm Source: UniProt
  6. nucleus Source: HPA
  7. protein complex Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26455.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19121912Chromodomain-helicase-DNA-binding protein 4
PRO_0000080228Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441Phosphoserine2 Publications
Modified residuei303 – 3031Phosphoserine1 Publication
Modified residuei308 – 3081Phosphoserine1 Publication
Modified residuei309 – 3091Phosphoserine1 Publication
Modified residuei310 – 3101Phosphoserine1 Publication
Modified residuei319 – 3191Phosphoserine1 Publication
Modified residuei428 – 4281Phosphoserine2 Publications
Modified residuei515 – 5151Phosphoserine2 Publications
Modified residuei517 – 5171Phosphothreonine1 Publication
Modified residuei529 – 5291Phosphothreonine1 Publication
Modified residuei531 – 5311Phosphoserine1 Publication
Modified residuei1349 – 13491Phosphoserine1 Publication
Modified residuei1531 – 15311Phosphoserine2 Publications
Modified residuei1535 – 15351Phosphoserine3 Publications
Modified residuei1537 – 15371Phosphoserine1 Publication
Modified residuei1553 – 15531Phosphothreonine1 Publication
Modified residuei1602 – 16021Phosphoserine1 Publication
Modified residuei1643 – 16431N6-acetyllysine1 Publication
Modified residuei1653 – 16531Phosphothreonine1 Publication
Modified residuei1679 – 16791Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ14839.
PaxDbiQ14839.
PRIDEiQ14839.

PTM databases

PhosphoSiteiQ14839.

Miscellaneous databases

PMAP-CutDBQ14839.

Expressioni

Gene expression databases

ArrayExpressiQ14839.
BgeeiQ14839.
CleanExiHS_CHD4.
GenevestigatoriQ14839.

Organism-specific databases

HPAiHPA012008.

Interactioni

Subunit structurei

Central component of the nucleosome remodeling and histone deacetylase (NuRD) repressor complex. Interacts directly with IKFZ1 in the NuRD complex. Interacts with TRIM27. Part of a complex containing ATR and HDAC2. Interacts with KLF1; the interaction depends on sumoylation of KLF1, and leads to its transcriptional repression. Interacts with ZGPAT; the interaction is direct. Interacts with BCL6, BRD4 and PCNT.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HDAC1Q135476EBI-372916,EBI-301834
MYCP011062EBI-372916,EBI-447544

Protein-protein interaction databases

BioGridi107533. 83 interactions.
DIPiDIP-31183N.
IntActiQ14839. 24 interactions.
MINTiMINT-349766.
STRINGi9606.ENSP00000349508.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni374 – 3763
Beta strandi386 – 3894
Helixi394 – 3974
Helixi414 – 4174
Beta strandi450 – 4523
Turni453 – 4553
Beta strandi459 – 4635
Beta strandi465 – 4673
Beta strandi473 – 4786
Turni491 – 4966
Beta strandi629 – 6324
Beta strandi638 – 6425
Turni649 – 6513
Beta strandi653 – 6564
Helixi664 – 67310

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MM2NMR-A446-501[»]
1MM3NMR-A446-476[»]
A490-501[»]
2EE1NMR-A618-674[»]
2L5UNMR-A365-420[»]
2L75NMR-A446-501[»]
ProteinModelPortaliQ14839.
SMRiQ14839. Positions 365-420, 446-501, 618-674.

Miscellaneous databases

EvolutionaryTraceiQ14839.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini494 – 594101Chromo 1
Add
BLAST
Domaini622 – 69776Chromo 2
Add
BLAST
Domaini738 – 922185Helicase ATP-binding
Add
BLAST
Domaini1054 – 1203150Helicase C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1577 – 1912336Required for interaction with PCNT
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi873 – 8764DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi50 – 5910Poly-Lys
Compositional biasi94 – 985Poly-Glu
Compositional biasi114 – 1196Poly-Lys
Compositional biasi134 – 1385Poly-Glu
Compositional biasi139 – 1446Poly-Asp
Compositional biasi227 – 2359Poly-Ala
Compositional biasi248 – 2525Poly-Pro
Compositional biasi350 – 3545Poly-Lys
Compositional biasi1052 – 10554Poly-Leu
Compositional biasi1294 – 13018Poly-Glu
Compositional biasi1665 – 16684Poly-Glu

Sequence similaritiesi

Contains 2 chromo domains.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0553.
HOGENOMiHOG000231124.
HOVERGENiHBG005326.
KOiK11643.
OMAiMLLCRQL.
OrthoDBiEOG7C8GG7.
PhylomeDBiQ14839.
TreeFamiTF106448.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR028725. CHD4.
IPR012957. CHD_C2.
IPR012958. CHD_N.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR009462. DUF1086.
IPR009463. DUF1087.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
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:SF554. PTHR10799:SF554. 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]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS00598. CHROMO_1. 2 hits.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14839-1) [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

MASGLGSPSP CSAGSEEEDM DALLNNSLPP PHPENEEDPE EDLSETETPK     50
LKKKKKPKKP RDPKIPKSKR QKKERMLLCR QLGDSSGEGP EFVEEEEEVA 100
LRSDSEGSDY TPGKKKKKKL GPKKEKKSKS KRKEEEEEED DDDDSKEPKS 150
SAQLLEDWGM EDIDHVFSEE DYRTLTNYKA FSQFVRPLIA AKNPKIAVSK 200
MMMVLGAKWR EFSTNNPFKG SSGASVAAAA AAAVAVVESM VTATEVAPPP 250
PPVEVPIRKA KTKEGKGPNA RRKPKGSPRV PDAKKPKPKK VAPLKIKLGG 300
FGSKRKRSSS EDDDLDVESD FDDASINSYS VSDGSTSRSS RSRKKLRTTK 350
KKKKGEEEVT AVDGYETDHQ DYCEVCQQGG EIILCDTCPR AYHMVCLDPD 400
MEKAPEGKWS CPHCEKEGIQ WEAKEDNSEG EEILEEVGGD LEEEDDHHME 450
FCRVCKDGGE LLCCDTCPSS YHIHCLNPPL PEIPNGEWLC PRCTCPALKG 500
KVQKILIWKW GQPPSPTPVP RPPDADPNTP SPKPLEGRPE RQFFVKWQGM 550
SYWHCSWVSE LQLELHCQVM FRNYQRKNDM DEPPSGDFGG DEEKSRKRKN 600
KDPKFAEMEE RFYRYGIKPE WMMIHRILNH SVDKKGHVHY LIKWRDLPYD 650
QASWESEDVE IQDYDLFKQS YWNHRELMRG EEGRPGKKLK KVKLRKLERP 700
PETPTVDPTV KYERQPEYLD ATGGTLHPYQ MEGLNWLRFS WAQGTDTILA 750
DEMGLGKTVQ TAVFLYSLYK EGHSKGPFLV SAPLSTIINW EREFEMWAPD 800
MYVVTYVGDK DSRAIIRENE FSFEDNAIRG GKKASRMKKE ASVKFHVLLT 850
SYELITIDMA ILGSIDWACL IVDEAHRLKN NQSKFFRVLN GYSLQHKLLL 900
TGTPLQNNLE ELFHLLNFLT PERFHNLEGF LEEFADIAKE DQIKKLHDML 950
GPHMLRRLKA DVFKNMPSKT ELIVRVELSP MQKKYYKYIL TRNFEALNAR 1000
GGGNQVSLLN VVMDLKKCCN HPYLFPVAAM EAPKMPNGMY DGSALIRASG 1050
KLLLLQKMLK NLKEGGHRVL IFSQMTKMLD LLEDFLEHEG YKYERIDGGI 1100
TGNMRQEAID RFNAPGAQQF CFLLSTRAGG LGINLATADT VIIYDSDWNP 1150
HNDIQAFSRA HRIGQNKKVM IYRFVTRASV EERITQVAKK KMMLTHLVVR 1200
PGLGSKTGSM SKQELDDILK FGTEELFKDE ATDGGGDNKE GEDSSVIHYD 1250
DKAIERLLDR NQDETEDTEL QGMNEYLSSF KVAQYVVREE EMGEEEEVER 1300
EIIKQEESVD PDYWEKLLRH HYEQQQEDLA RNLGKGKRIR KQVNYNDGSQ 1350
EDRDWQDDQS DNQSDYSVAS EEGDEDFDER SEAPRRPSRK GLRNDKDKPL 1400
PPLLARVGGN IEVLGFNARQ RKAFLNAIMR YGMPPQDAFT TQWLVRDLRG 1450
KSEKEFKAYV SLFMRHLCEP GADGAETFAD GVPREGLSRQ HVLTRIGVMS 1500
LIRKKVQEFE HVNGRWSMPE LAEVEENKKM SQPGSPSPKT PTPSTPGDTQ 1550
PNTPAPVPPA EDGIKIEENS LKEEESIEGE KEVKSTAPET AIECTQAPAP 1600
ASEDEKVVVE PPEGEEKVEK AEVKERTEEP METEPKGAAD VEKVEEKSAI 1650
DLTPIVVEDK EEKKEEEEKK EVMLQNGETP KDLNDEKQKK NIKQRFMFNI 1700
ADGGFTELHS LWQNEERAAT VTKKTYEIWH RRHDYWLLAG IINHGYARWQ 1750
DIQNDPRYAI LNEPFKGEMN RGNFLEIKNK FLARRFKLLE QALVIEEQLR 1800
RAAYLNMSED PSHPSMALNT RFAEVECLAE SHQHLSKESM AGNKPANAVL 1850
HKVLKQLEEL LSDMKADVTR LPATIARIPP VAVRLQMSER NILSRLANRA 1900
PEPTPQQVAQ QQ 1912
Length:1,912
Mass (Da):218,005
Last modified:November 2, 2010 - v2
Checksum:i765ED8485B7BBB85
GO
Isoform 2 (identifier: Q14839-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1353-1353: R → RGVCGRPRPPPMGRSTRAVGPAHLPSLPP

Note: No experimental confirmation available.

Show »
Length:1,940
Mass (Da):220,848
Checksum:iC4D5E61DFE83B27B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti139 – 1391E → D.1 Publication
Corresponds to variant rs1639122 [ dbSNP | Ensembl ].
VAR_031674
Natural varianti1648 – 16481S → L.
Corresponds to variant rs35512811 [ dbSNP | Ensembl ].
VAR_031675
Natural varianti1655 – 16551I → V.
Corresponds to variant rs16932768 [ dbSNP | Ensembl ].
VAR_031676

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1353 – 13531R → RGVCGRPRPPPMGRSTRAVG PAHLPSLPP in isoform 2.
VSP_011416

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 363Missing in AAH38596. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X86691 mRNA. Translation: CAA60384.1.
AC006064 Genomic DNA. No translation available.
BC038596 mRNA. Translation: AAH38596.1.
CCDSiCCDS8552.1. [Q14839-1]
RefSeqiNP_001264.2. NM_001273.2. [Q14839-1]
XP_006719021.1. XM_006718958.1. [Q14839-2]
UniGeneiHs.162233.

Genome annotation databases

EnsembliENST00000309577; ENSP00000312419; ENSG00000111642. [Q14839-2]
ENST00000357008; ENSP00000349508; ENSG00000111642. [Q14839-1]
ENST00000544484; ENSP00000440392; ENSG00000111642.
GeneIDi1108.
KEGGihsa:1108.
UCSCiuc001qpo.3. human. [Q14839-1]
uc001qpp.3. human. [Q14839-2]

Polymorphism databases

DMDMi311033360.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X86691 mRNA. Translation: CAA60384.1 .
AC006064 Genomic DNA. No translation available.
BC038596 mRNA. Translation: AAH38596.1 .
CCDSi CCDS8552.1. [Q14839-1 ]
RefSeqi NP_001264.2. NM_001273.2. [Q14839-1 ]
XP_006719021.1. XM_006718958.1. [Q14839-2 ]
UniGenei Hs.162233.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MM2 NMR - A 446-501 [» ]
1MM3 NMR - A 446-476 [» ]
A 490-501 [» ]
2EE1 NMR - A 618-674 [» ]
2L5U NMR - A 365-420 [» ]
2L75 NMR - A 446-501 [» ]
ProteinModelPortali Q14839.
SMRi Q14839. Positions 365-420, 446-501, 618-674.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107533. 83 interactions.
DIPi DIP-31183N.
IntActi Q14839. 24 interactions.
MINTi MINT-349766.
STRINGi 9606.ENSP00000349508.

PTM databases

PhosphoSitei Q14839.

Polymorphism databases

DMDMi 311033360.

Proteomic databases

MaxQBi Q14839.
PaxDbi Q14839.
PRIDEi Q14839.

Protocols and materials databases

DNASUi 1108.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309577 ; ENSP00000312419 ; ENSG00000111642 . [Q14839-2 ]
ENST00000357008 ; ENSP00000349508 ; ENSG00000111642 . [Q14839-1 ]
ENST00000544484 ; ENSP00000440392 ; ENSG00000111642 .
GeneIDi 1108.
KEGGi hsa:1108.
UCSCi uc001qpo.3. human. [Q14839-1 ]
uc001qpp.3. human. [Q14839-2 ]

Organism-specific databases

CTDi 1108.
GeneCardsi GC12M006679.
H-InvDB HIX0201859.
HGNCi HGNC:1919. CHD4.
HPAi HPA012008.
MIMi 603277. gene.
neXtProti NX_Q14839.
PharmGKBi PA26455.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0553.
HOGENOMi HOG000231124.
HOVERGENi HBG005326.
KOi K11643.
OMAi MLLCRQL.
OrthoDBi EOG7C8GG7.
PhylomeDBi Q14839.
TreeFami TF106448.

Enzyme and pathway databases

Reactomei REACT_953. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

ChiTaRSi CHD4. human.
EvolutionaryTracei Q14839.
GeneWikii CHD4.
GenomeRNAii 1108.
NextBioi 4598.
PMAP-CutDB Q14839.
PROi Q14839.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14839.
Bgeei Q14839.
CleanExi HS_CHD4.
Genevestigatori Q14839.

Family and domain databases

Gene3Di 3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProi IPR028725. CHD4.
IPR012957. CHD_C2.
IPR012958. CHD_N.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR009462. DUF1086.
IPR009463. DUF1087.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
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:SF554. PTHR10799:SF554. 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 SSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEi PS00598. CHROMO_1. 2 hits.
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. "The major dermatomyositis specific Mi-2 autoantigen is a presumed helicase involved in transcriptional activation."
    Seelig H.P., Moosbrugger I., Ehrfeld H., Fink T., Renz M., Genth E.
    Arthritis Rheum. 38:1389-1399(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-139.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Skin.
  4. "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.
  5. "Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4."
    Schmidt D.R., Schreiber S.L.
    Biochemistry 38:14711-14717(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX CONTAINING ATR AND HDAC2, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Ikaros DNA-binding proteins direct formation of chromatin remodeling complexes in lymphocytes."
    Kim J., Sif S., Jones B., Jackson A., Koipally J., Heller E., Winandy S., Viel A., Sawyer A., Ikeda T., Kingston R., Georgopoulos K.
    Immunity 10:345-355(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IKZF1 IN THE NURD COMPLEX.
  7. "Mi-2 beta associates with BRG1 and RET finger protein at the distinct regions with transcriptional activating and repressing abilities."
    Shimono Y., Murakami H., Kawai K., Wade P.A., Shimokata K., Takahashi M.
    J. Biol. Chem. 278:51638-51645(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM27.
  8. "MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation."
    Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R., Boss J.M., Wade P.A.
    Cell 119:75-86(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL6, IDENTIFICATION IN THE NURD COMPLEX.
  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-428 AND SER-1531, 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515; THR-529; SER-531 AND SER-1535, 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. "ZIP: a novel transcription repressor, represses EGFR oncogene and suppresses breast carcinogenesis."
    Li R., Zhang H., Yu W., Chen Y., Gui B., Liang J., Wang Y., Sun L., Yang X., Zhang Y., Shi L., Li Y., Shang Y.
    EMBO J. 28:2763-2776(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZGPAT.
  15. "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 THR-1553, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1643, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-44; SER-1531; SER-1535; THR-1653 AND THR-1679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3."
    Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W., Howley P.M.
    Mol. Cell. Biol. 31:2641-2652(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRD4.
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-303; SER-308; SER-309; SER-310; SER-319; SER-428; SER-515; THR-517; SER-1535; SER-1537 AND SER-1602, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: STRUCTURE BY NMR OF 446-501.
  22. "Solution structures of the chromo domain of human chromodomain helicase-DNA-binding protein 4."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 618-674.

Entry informationi

Entry nameiCHD4_HUMAN
AccessioniPrimary (citable) accession number: Q14839
Secondary accession number(s): Q8IXZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 2, 2010
Last modified: September 3, 2014
This is version 163 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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