Q14839 (CHD4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1912 AA.
Sequence status	Complete.
Protein existence	Evidence 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.9
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 By similarity. Interacts with ZGPAT; the interaction is direct. Interacts with PCNT. Ref.5 Ref.6 Ref.7 Ref.9 Ref.12
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › centrosome. Note: Associates with centrosomes in interphase. Ref.9
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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	ATP-binding DNA-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Chromatin regulator Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription from RNA polymerase II promoter Traceable author statement PubMed 9326634. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	NuRD complex Inferred from direct assay Ref.12. Source: UniProtKB centrosome Inferred from direct assay Ref.9. Source: UniProtKB cytoplasm Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	ATP 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 zinc ion binding Traceable author statement PubMed 7560064. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MYC	P01106	2	EBI-372916,EBI-447544

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1912

1912

Chromodomain-helicase-DNA-binding protein 4

PRO_0000080228

Regions

Domain

494 – 594

101

Chromo 1

Domain

622 – 697

76

Chromo 2

Domain

738 – 922

185

Helicase ATP-binding

Domain

1054 – 1203

150

Helicase C-terminal

Zinc finger

370 – 417

48

PHD-type 1

Zinc finger

449 – 496

48

PHD-type 2

Nucleotide binding

751 – 758

8

ATP Potential

Region

1577 – 1912

336

Required for interaction with PCNT

Motif

873 – 876

4

DEAH box

Compositional bias

50 – 59

10

Poly-Lys

Compositional bias

94 – 98

5

Poly-Glu

Compositional bias

114 – 119

6

Poly-Lys

Compositional bias

134 – 138

5

Poly-Glu

Compositional bias

139 – 144

6

Poly-Asp

Compositional bias

227 – 235

9

Poly-Ala

Compositional bias

248 – 252

5

Poly-Pro

Compositional bias

350 – 354

5

Poly-Lys

Compositional bias

1052 – 1055

4

Poly-Leu

Compositional bias

1294 – 1301

8

Poly-Glu

Compositional bias

1665 – 1668

4

Poly-Glu

Amino acid modifications

Modified residue

44

1

Phosphoserine Ref.15 Ref.17

Modified residue

303

1

Phosphoserine Ref.17

Modified residue

308

1

Phosphoserine Ref.17

Modified residue

309

1

Phosphoserine Ref.17

Modified residue

310

1

Phosphoserine Ref.17

Modified residue

319

1

Phosphoserine Ref.17

Modified residue

428

1

Phosphoserine Ref.8 Ref.17

Modified residue

515

1

Phosphoserine Ref.11 Ref.17

Modified residue

517

1

Phosphothreonine Ref.17

Modified residue

529

1

Phosphothreonine Ref.11

Modified residue

531

1

Phosphoserine Ref.11

Modified residue

1308

1

Phosphoserine By similarity

Modified residue

1349

1

Phosphoserine Ref.10

Modified residue

1531

1

Phosphoserine Ref.8 Ref.15

Modified residue

1535

1

Phosphoserine Ref.11 Ref.15 Ref.17

Modified residue

1537

1

Phosphoserine Ref.17

Modified residue

1540

1

Phosphothreonine By similarity

Modified residue

1545

1

Phosphothreonine By similarity

Modified residue

1549

1

Phosphothreonine By similarity

Modified residue

1553

1

Phosphothreonine Ref.13

Modified residue

1602

1

Phosphoserine Ref.17

Modified residue

1643

1

N6-acetyllysine Ref.14

Modified residue

1653

1

Phosphothreonine Ref.15

Modified residue

1679

1

Phosphothreonine Ref.15

Natural variations

Alternative sequence

1353

1

R → RGVCGRPRPPPMGRSTRAVG PAHLPSLPP in isoform 2.

VSP_011416

Natural variant

139

1

E → D. Ref.1
Corresponds to variant rs1639122 [ dbSNP | Ensembl ].

VAR_031674

Natural variant

1648

1

S → L.
Corresponds to variant rs35512811 [ dbSNP | Ensembl ].

VAR_031675

Natural variant

1655

1

I → V.
Corresponds to variant rs16932768 [ dbSNP | Ensembl ].

VAR_031676

Experimental info

Sequence conflict

34 – 36

3

Missing in AAH38596. Ref.3

Secondary structure

1

.

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.

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.

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.

.

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.

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.

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1912

Helix Strand Turn

Details...

Turn

374 – 376

3

Beta strand

386 – 389

4

Helix

394 – 397

4

Helix

414 – 417

4

Beta strand

450 – 452

3

Turn

453 – 455

3

Beta strand

459 – 463

5

Beta strand

465 – 467

3

Beta strand

473 – 478

6

Turn

491 – 496

6

Beta strand

629 – 632

4

Beta strand

638 – 642

5

Turn

649 – 651

3

Beta strand

653 – 656

4

Helix

664 – 673

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 2, 2010. Version 2. Checksum: 765ED8485B7BBB85	FASTA	1,912	218,005
	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
	Isoform 2 [UniParc]. Checksum: C4D5E61DFE83B27B	FASTA	1,940	220,848
	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 EDRGVCGRPR PPPMGRSTRA VGPAHLPSLP 1390 1400 1410 1420 1430 1440 PDWQDDQSDN QSDYSVASEE GDEDFDERSE APRRPSRKGL RNDKDKPLPP LLARVGGNIE 1450 1460 1470 1480 1490 1500 VLGFNARQRK AFLNAIMRYG MPPQDAFTTQ WLVRDLRGKS EKEFKAYVSL FMRHLCEPGA 1510 1520 1530 1540 1550 1560 DGAETFADGV PREGLSRQHV LTRIGVMSLI RKKVQEFEHV NGRWSMPELA EVEENKKMSQ 1570 1580 1590 1600 1610 1620 PGSPSPKTPT PSTPGDTQPN TPAPVPPAED GIKIEENSLK EEESIEGEKE VKSTAPETAI 1630 1640 1650 1660 1670 1680 ECTQAPAPAS EDEKVVVEPP EGEEKVEKAE VKERTEEPME TEPKGAADVE KVEEKSAIDL 1690 1700 1710 1720 1730 1740 TPIVVEDKEE KKEEEEKKEV MLQNGETPKD LNDEKQKKNI KQRFMFNIAD GGFTELHSLW 1750 1760 1770 1780 1790 1800 QNEERAATVT KKTYEIWHRR HDYWLLAGII NHGYARWQDI QNDPRYAILN EPFKGEMNRG 1810 1820 1830 1840 1850 1860 NFLEIKNKFL ARRFKLLEQA LVIEEQLRRA AYLNMSEDPS HPSMALNTRF AEVECLAESH 1870 1880 1890 1900 1910 1920 QHLSKESMAG NKPANAVLHK VLKQLEELLS DMKADVTRLP ATIARIPPVA VRLQMSERNI 1930 1940 LSRLANRAPE PTPQQVAQQQ

References

	« Hide 'large scale' referencesShow '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. , 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, 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]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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.
[10]	"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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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.
[13]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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, MASS SPECTROMETRY.
[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-44; SER-1531; SER-1535; THR-1653 AND THR-1679, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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].
[17]	"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, MASS SPECTROMETRY.
[18]	"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.
[19]	"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.

IPI

IPI00000846.
IPI00455210.

RefSeq

NP_001264.2. NM_001273.2.

UniGene

Hs.162233.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MM2	NMR	-	A	446-501	[»]
1MM3	NMR	-	A	446-501	[»]
2EE1	NMR	-	A	618-674	[»]
2L5U	NMR	-	A	365-420	[»]
2L75	NMR	-	A	446-501	[»]

ProteinModelPortal

Q14839.

SMR

Q14839. Positions 365-420, 446-501, 618-674.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31183N.

IntAct

Q14839. 20 interactions.

MINT

MINT-349766.

STRING

9606.ENSP00000349508.

PTM databases

PhosphoSite

Q14839.

Polymorphism databases

DMDM

311033360.

Proteomic databases

PaxDb

Q14839.

PRIDE

Q14839.

Protocols and materials databases

DNASU

1108.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000309577; ENSP00000312419; ENSG00000111642.
ENST00000357008; ENSP00000349508; ENSG00000111642.
ENST00000544484; ENSP00000440392; ENSG00000111642.

GeneID

1108.

KEGG

hsa:1108.

UCSC

uc001qpo.3. human.
uc001qpp.3. human.

Organism-specific databases

CTD

1108.

GeneCards

GC12M006679.

H-InvDB

HIX0201859.

HGNC

HGNC:1919. CHD4.

HPA

HPA012008.

MIM

603277. gene.

neXtProt

NX_Q14839.

PharmGKB

PA26455.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0553.

HOGENOM

HOG000231124.

HOVERGEN

HBG005326.

KO

K11643.

OMA

ERMLLCR.

OrthoDB

EOG4WH8JX.

Enzyme and pathway databases

Pathway_Interaction_DB

hdac_classi_pathway. Signaling events mediated by HDAC Class I.

Gene expression databases

ArrayExpress

Q14839.

Bgee

Q14839.

CleanEx

HS_CHD4.

Genevestigator

Q14839.

GermOnline

ENSG00000111642. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 2 hits.

InterPro

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.
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]

Pfam

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]

SMART

SM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]

SUPFAM

SSF54160. Chromodomain-like. 2 hits.
SSF57903. FYVE_PHD_ZnF. 2 hits.

PROSITE

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]

ProtoNet

Search...

Other

ChiTaRS

CHD4. human.

EvolutionaryTrace

Q14839.

GenomeRNAi

1108.

NextBio

4598.

PMAP-CutDB

Q14839.

SOURCE

Search...

Entry information

Entry name

CHD4_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 150 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.