Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q14839 (CHD4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromodomain-helicase-DNA-binding protein 4

Short name=CHD-4
EC=3.6.4.12
Alternative name(s):
ATP-dependent helicase CHD4
Mi-2 autoantigen 218 kDa protein
Mi2-beta
Gene names
Name:CHD4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1912 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Ref.4 Ref.10

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.14 Ref.19

Subcellular location

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

Miscellaneous

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

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 2 chromo domains.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 2 PHD-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandATP-binding
DNA-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionChromatin regulator
Helicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP-dependent chromatin remodeling

Inferred from direct assay PubMed 16217013. Source: UniProt

DNA duplex unwinding

Traceable author statement PubMed 9326634. Source: GOC

regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 9326634. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNuRD complex

Inferred from direct assay Ref.14. Source: UniProtKB

centrosome

Inferred from direct assay Ref.10. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

nuclear chromatin

Inferred from direct assay PubMed 16217013. Source: UniProt

nucleoplasm

Inferred from direct assay PubMed 22720776. Source: UniProt

nucleus

Inferred from direct assay. Source: HPA

protein complex

Inferred from direct assay PubMed 16217013. Source: UniProt

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Traceable author statement PubMed 9326634. Source: ProtInc

DNA binding

Traceable author statement PubMed 9326634. Source: ProtInc

RNA polymerase II repressing transcription factor binding

Inferred from physical interaction PubMed 22926524. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.14Ref.4. Source: UniProtKB

zinc ion binding

Traceable author statement PubMed 7560064. Source: ProtInc

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14839-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14839-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1353-1353: R → RGVCGRPRPPPMGRSTRAVGPAHLPSLPP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19121912Chromodomain-helicase-DNA-binding protein 4
PRO_0000080228

Regions

Domain494 – 594101Chromo 1
Domain622 – 69776Chromo 2
Domain738 – 922185Helicase ATP-binding
Domain1054 – 1203150Helicase C-terminal
Zinc finger370 – 41748PHD-type 1
Zinc finger449 – 49648PHD-type 2
Nucleotide binding751 – 7588ATP Potential
Region1577 – 1912336Required for interaction with PCNT
Motif873 – 8764DEAH box
Compositional bias50 – 5910Poly-Lys
Compositional bias94 – 985Poly-Glu
Compositional bias114 – 1196Poly-Lys
Compositional bias134 – 1385Poly-Glu
Compositional bias139 – 1446Poly-Asp
Compositional bias227 – 2359Poly-Ala
Compositional bias248 – 2525Poly-Pro
Compositional bias350 – 3545Poly-Lys
Compositional bias1052 – 10554Poly-Leu
Compositional bias1294 – 13018Poly-Glu
Compositional bias1665 – 16684Poly-Glu

Amino acid modifications

Modified residue441Phosphoserine Ref.17 Ref.20
Modified residue3031Phosphoserine Ref.20
Modified residue3081Phosphoserine Ref.20
Modified residue3091Phosphoserine Ref.20
Modified residue3101Phosphoserine Ref.20
Modified residue3191Phosphoserine Ref.20
Modified residue4281Phosphoserine Ref.9 Ref.20
Modified residue5151Phosphoserine Ref.12 Ref.20
Modified residue5171Phosphothreonine Ref.20
Modified residue5291Phosphothreonine Ref.12
Modified residue5311Phosphoserine Ref.12
Modified residue13491Phosphoserine Ref.11
Modified residue15311Phosphoserine Ref.9 Ref.17
Modified residue15351Phosphoserine Ref.12 Ref.17 Ref.20
Modified residue15371Phosphoserine Ref.20
Modified residue15531Phosphothreonine Ref.15
Modified residue16021Phosphoserine Ref.20
Modified residue16431N6-acetyllysine Ref.16
Modified residue16531Phosphothreonine Ref.17
Modified residue16791Phosphothreonine Ref.17

Natural variations

Alternative sequence13531R → RGVCGRPRPPPMGRSTRAVG PAHLPSLPP in isoform 2.
VSP_011416
Natural variant1391E → D. Ref.1
Corresponds to variant rs1639122 [ dbSNP | Ensembl ].
VAR_031674
Natural variant16481S → L.
Corresponds to variant rs35512811 [ dbSNP | Ensembl ].
VAR_031675
Natural variant16551I → V.
Corresponds to variant rs16932768 [ dbSNP | Ensembl ].
VAR_031676

Experimental info

Sequence conflict34 – 363Missing in AAH38596. Ref.3

Secondary structure

.............................. 1912
Helix Strand Turn

Details...

Sequences

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

Last modified November 2, 2010. Version 2.
Checksum: 765ED8485B7BBB85

FASTA1,912218,005
        10         20         30         40         50         60 
MASGLGSPSP CSAGSEEEDM DALLNNSLPP PHPENEEDPE EDLSETETPK LKKKKKPKKP 

        70         80         90        100        110        120 
RDPKIPKSKR QKKERMLLCR QLGDSSGEGP EFVEEEEEVA LRSDSEGSDY TPGKKKKKKL 

       130        140        150        160        170        180 
GPKKEKKSKS KRKEEEEEED DDDDSKEPKS SAQLLEDWGM EDIDHVFSEE DYRTLTNYKA 

       190        200        210        220        230        240 
FSQFVRPLIA AKNPKIAVSK MMMVLGAKWR EFSTNNPFKG SSGASVAAAA AAAVAVVESM 

       250        260        270        280        290        300 
VTATEVAPPP PPVEVPIRKA KTKEGKGPNA RRKPKGSPRV PDAKKPKPKK VAPLKIKLGG 

       310        320        330        340        350        360 
FGSKRKRSSS EDDDLDVESD FDDASINSYS VSDGSTSRSS RSRKKLRTTK KKKKGEEEVT 

       370        380        390        400        410        420 
AVDGYETDHQ DYCEVCQQGG EIILCDTCPR AYHMVCLDPD MEKAPEGKWS CPHCEKEGIQ 

       430        440        450        460        470        480 
WEAKEDNSEG EEILEEVGGD LEEEDDHHME FCRVCKDGGE LLCCDTCPSS YHIHCLNPPL 

       490        500        510        520        530        540 
PEIPNGEWLC PRCTCPALKG KVQKILIWKW GQPPSPTPVP RPPDADPNTP SPKPLEGRPE 

       550        560        570        580        590        600 
RQFFVKWQGM SYWHCSWVSE LQLELHCQVM FRNYQRKNDM DEPPSGDFGG DEEKSRKRKN 

       610        620        630        640        650        660 
KDPKFAEMEE RFYRYGIKPE WMMIHRILNH SVDKKGHVHY LIKWRDLPYD QASWESEDVE 

       670        680        690        700        710        720 
IQDYDLFKQS YWNHRELMRG EEGRPGKKLK KVKLRKLERP PETPTVDPTV KYERQPEYLD 

       730        740        750        760        770        780 
ATGGTLHPYQ MEGLNWLRFS WAQGTDTILA DEMGLGKTVQ TAVFLYSLYK EGHSKGPFLV 

       790        800        810        820        830        840 
SAPLSTIINW EREFEMWAPD MYVVTYVGDK DSRAIIRENE FSFEDNAIRG GKKASRMKKE 

       850        860        870        880        890        900 
ASVKFHVLLT SYELITIDMA ILGSIDWACL IVDEAHRLKN NQSKFFRVLN GYSLQHKLLL 

       910        920        930        940        950        960 
TGTPLQNNLE ELFHLLNFLT PERFHNLEGF LEEFADIAKE DQIKKLHDML GPHMLRRLKA 

       970        980        990       1000       1010       1020 
DVFKNMPSKT ELIVRVELSP MQKKYYKYIL TRNFEALNAR GGGNQVSLLN VVMDLKKCCN 

      1030       1040       1050       1060       1070       1080 
HPYLFPVAAM EAPKMPNGMY DGSALIRASG KLLLLQKMLK NLKEGGHRVL IFSQMTKMLD 

      1090       1100       1110       1120       1130       1140 
LLEDFLEHEG YKYERIDGGI TGNMRQEAID RFNAPGAQQF CFLLSTRAGG LGINLATADT 

      1150       1160       1170       1180       1190       1200 
VIIYDSDWNP HNDIQAFSRA HRIGQNKKVM IYRFVTRASV EERITQVAKK KMMLTHLVVR 

      1210       1220       1230       1240       1250       1260 
PGLGSKTGSM SKQELDDILK FGTEELFKDE ATDGGGDNKE GEDSSVIHYD DKAIERLLDR 

      1270       1280       1290       1300       1310       1320 
NQDETEDTEL QGMNEYLSSF KVAQYVVREE EMGEEEEVER EIIKQEESVD PDYWEKLLRH 

      1330       1340       1350       1360       1370       1380 
HYEQQQEDLA RNLGKGKRIR KQVNYNDGSQ EDRDWQDDQS DNQSDYSVAS EEGDEDFDER 

      1390       1400       1410       1420       1430       1440 
SEAPRRPSRK GLRNDKDKPL PPLLARVGGN IEVLGFNARQ RKAFLNAIMR YGMPPQDAFT 

      1450       1460       1470       1480       1490       1500 
TQWLVRDLRG KSEKEFKAYV SLFMRHLCEP GADGAETFAD GVPREGLSRQ HVLTRIGVMS 

      1510       1520       1530       1540       1550       1560 
LIRKKVQEFE HVNGRWSMPE LAEVEENKKM SQPGSPSPKT PTPSTPGDTQ PNTPAPVPPA 

      1570       1580       1590       1600       1610       1620 
EDGIKIEENS LKEEESIEGE KEVKSTAPET AIECTQAPAP ASEDEKVVVE PPEGEEKVEK 

      1630       1640       1650       1660       1670       1680 
AEVKERTEEP METEPKGAAD VEKVEEKSAI DLTPIVVEDK EEKKEEEEKK EVMLQNGETP 

      1690       1700       1710       1720       1730       1740 
KDLNDEKQKK NIKQRFMFNI ADGGFTELHS LWQNEERAAT VTKKTYEIWH RRHDYWLLAG 

      1750       1760       1770       1780       1790       1800 
IINHGYARWQ DIQNDPRYAI LNEPFKGEMN RGNFLEIKNK FLARRFKLLE QALVIEEQLR 

      1810       1820       1830       1840       1850       1860 
RAAYLNMSED PSHPSMALNT RFAEVECLAE SHQHLSKESM AGNKPANAVL HKVLKQLEEL 

      1870       1880       1890       1900       1910 
LSDMKADVTR LPATIARIPP VAVRLQMSER NILSRLANRA PEPTPQQVAQ QQ 

« Hide

Isoform 2 [UniParc].

Checksum: C4D5E61DFE83B27B
Show »

FASTA1,940220,848

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]"Engineering a protein scaffold from a PHD finger."
Kwan A.H.Y., Gell D.A., Verger A., Crossley M., Matthews J.M., Mackay J.P.
Structure 11:803-813(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X86691 mRNA. Translation: CAA60384.1.
AC006064 Genomic DNA. No translation available.
BC038596 mRNA. Translation: AAH38596.1.
CCDSCCDS8552.1. [Q14839-1]
RefSeqNP_001264.2. NM_001273.2. [Q14839-1]
XP_006719021.1. XM_006718958.1. [Q14839-2]
UniGeneHs.162233.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MM2NMR-A446-501[»]
1MM3NMR-A446-476[»]
A490-501[»]
2EE1NMR-A618-674[»]
2L5UNMR-A365-420[»]
2L75NMR-A446-501[»]
ProteinModelPortalQ14839.
SMRQ14839. Positions 365-420, 446-501, 618-674.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107533. 82 interactions.
DIPDIP-31183N.
IntActQ14839. 24 interactions.
MINTMINT-349766.
STRING9606.ENSP00000349508.

PTM databases

PhosphoSiteQ14839.

Polymorphism databases

DMDM311033360.

Proteomic databases

MaxQBQ14839.
PaxDbQ14839.
PRIDEQ14839.

Protocols and materials databases

DNASU1108.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309577; ENSP00000312419; ENSG00000111642. [Q14839-2]
ENST00000357008; ENSP00000349508; ENSG00000111642. [Q14839-1]
ENST00000544484; ENSP00000440392; ENSG00000111642.
GeneID1108.
KEGGhsa:1108.
UCSCuc001qpo.3. human. [Q14839-1]
uc001qpp.3. human. [Q14839-2]

Organism-specific databases

CTD1108.
GeneCardsGC12M006679.
H-InvDBHIX0201859.
HGNCHGNC:1919. CHD4.
HPAHPA012008.
MIM603277. gene.
neXtProtNX_Q14839.
PharmGKBPA26455.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOGENOMHOG000231124.
HOVERGENHBG005326.
KOK11643.
OMAMLLCRQL.
OrthoDBEOG7C8GG7.
PhylomeDBQ14839.
TreeFamTF106448.

Gene expression databases

ArrayExpressQ14839.
BgeeQ14839.
CleanExHS_CHD4.
GenevestigatorQ14839.

Family and domain databases

Gene3D3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProIPR028725. 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]
PANTHERPTHR10799:SF554. PTHR10799:SF554. 1 hit.
PfamPF08074. CHDCT2. 1 hit.
PF08073. CHDNT. 1 hit.
PF00385. Chromo. 2 hits.
PF06461. DUF1086. 1 hit.
PF06465. DUF1087. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00628. PHD. 2 hits.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEPS00598. 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]
ProtoNetSearch...

Other

ChiTaRSCHD4. human.
EvolutionaryTraceQ14839.
GeneWikiCHD4.
GenomeRNAi1108.
NextBio4598.
PMAP-CutDBQ14839.
PROQ14839.
SOURCESearch...

Entry information

Entry nameCHD4_HUMAN
AccessionPrimary (citable) accession number: Q14839
Secondary accession number(s): Q8IXZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM