Q12873 (CHD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chromodomain-helicase-DNA-binding protein 3
Short name=CHD-3
EC=3.6.4.12

Alternative name(s):
ATP-dependent helicase CHD3
Mi-2 autoantigen 240 kDa protein
Mi2-alpha
Zinc finger helicase
Short name=hZFH

Gene names

Name:

CHD3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2000 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. Required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Ref.5 Ref.10
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	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. Ref.6 Ref.7 Ref.10
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › centrosome. Note: Associates with centrosomes in interphase and mitosis. Ref.10
Tissue specificity	Widely expressed. Ref.1
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.
Sequence caution	The sequence AAB87383.1 differs from that shown. Reason: Differs from position 1967 onward for unknown reasons.

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	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	centrosome organization Inferred from direct assay Ref.10. Source: UniProtKB chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc spindle organization Inferred from direct assay Ref.10. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	NuRD complex Inferred from direct assay. Source: BHF-UCL centrosome Inferred from direct assay Ref.10. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent DNA helicase activity Traceable author statement. Source: ProtInc DNA binding Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction Ref.5. Source: UniProtKB zinc ion binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BARD1	Q99728	2	EBI-523590,EBI-473181
DDX5	P17844	4	EBI-523590,EBI-351962
GIT1	Q9Y2X7	2	EBI-523590,EBI-466061
HTT	P42858	3	EBI-523590,EBI-466029
KDM1A	O60341	4	EBI-523590,EBI-710124
PRPF40A	O75400	2	EBI-523590,EBI-473291
SERBP1	Q8NC51	5	EBI-523590,EBI-523558

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q12873-1)

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: Q12873-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1642-1675: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2000	2000	Chromodomain-helicase-DNA-binding protein 3		PRO_0000080227
Regions
	Domain	494 – 594	101	Chromo 1
	Domain	631 – 673	43	Chromo 2
	Domain	748 – 932	185	Helicase ATP-binding
	Domain	1064 – 1229	166	Helicase C-terminal
	Zinc finger	379 – 426	48	PHD-type 1
	Zinc finger	456 – 503	48	PHD-type 2
	Nucleotide binding	761 – 768	8	ATP Potential
	Region	1566 – 1966	401	Required for interaction with PCNT
	Motif	883 – 886	4	DEAH box
	Compositional bias	206 – 221	16	Poly-Ala
	Compositional bias	243 – 246	4	Poly-Pro
	Compositional bias	355 – 358	4	Poly-Lys
	Compositional bias	434 – 446	13	Poly-Glu
	Compositional bias	697 – 703	7	Poly-Lys
Amino acid modifications
	Modified residue	43	1	Phosphoserine Ref.11
	Modified residue	324	1	Phosphoserine Ref.9
	Modified residue	713	1	Phosphoserine Ref.8 Ref.9 Ref.12 Ref.13 Ref.14 Ref.15
	Modified residue	1361	1	Phosphoserine Ref.13
	Modified residue	1364	1	Phosphoserine Ref.13
	Modified residue	1367	1	Phosphoserine Ref.13
	Modified residue	1549	1	Phosphoserine Ref.14
	Modified residue	1601	1	Phosphoserine Ref.8 Ref.9 Ref.12 Ref.13 Ref.14 Ref.15
	Modified residue	1605	1	Phosphoserine Ref.9 Ref.13 Ref.14 Ref.15
Natural variations
	Alternative sequence	1642 – 1675	34	Missing in isoform 2.		VSP_017231
	Natural variant	3	1	A → V. Corresponds to variant rs931543 [ dbSNP | Ensembl ].		VAR_048728
Experimental info
	Sequence conflict	121 – 126	6	GEGDGG → PHFQQK in AAC50228. Ref.4
	Sequence conflict	309 – 312	4	Missing in AAC50228. Ref.4
	Sequence conflict	653	1	W → G in AAC50228. Ref.4
	Sequence conflict	1704	1	K → N in AAC39923. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 7, 2006. Version 3. Checksum: 4494F56E5D0E7083	FASTA	2,000	226,592
	10 20 30 40 50 60 MKAADTVILW ARSKNDQLRI SFPPGLCWGD RMPDKDDIRL LPSALGVKKR KRGPKKQKEN 70 80 90 100 110 120 KPGKPRKRKK RDSEEEFGSE RDEYREKSES GGSEYGTGPG RKRRRKHREK KEKKTKRRKK 130 140 150 160 170 180 GEGDGGQKQV EQKSSATLLL TWGLEDVEHV FSEEDYHTLT NYKAFSQFMR PLIAKKNPKI 190 200 210 220 230 240 PMSKMMTILG AKWREFSANN PFKGSAAAVA AAAAAAAAAV AEQVSAAVSS ATPIAPSGPP 250 260 270 280 290 300 ALPPPPAADI QPPPIRRAKT KEGKGPGHKR RSKSPRVPDG RKKLRGKKMA PLKIKLGLLG 310 320 330 340 350 360 GKRKKGGSYV FQSDEGPEPE AEESDLDSGS VHSASGRPDG PVRTKKLKRG RPGRKKKKVL 370 380 390 400 410 420 GCPAVAGEEE VDGYETDHQD YCEVCQQGGE IILCDTCPRA YHLVCLDPEL DRAPEGKWSC 430 440 450 460 470 480 PHCEKEGVQW EAKEEEEEYE EEGEEEGEKE EEDDHMEYCR VCKDGGELLC CDACISSYHI 490 500 510 520 530 540 HCLNPPLPDI PNGEWLCPRC TCPVLKGRVQ KILHWRWGEP PVAVPAPQQA DGNPDVPPPR 550 560 570 580 590 600 PLQGRSEREF FVKWVGLSYW HCSWAKELQL EIFHLVMYRN YQRKNDMDEP PPLDYGSGED 610 620 630 640 650 660 DGKSDKRKVK DPHYAEMEEK YYRFGIKPEW MTVHRIINHS VDKKGNYHYL VKWRDLPYDQ 670 680 690 700 710 720 STWEEDEMNI PEYEEHKQSY WRHRELIMGE DPAQPRKYKK KKKELQGDGP PSSPTNDPTV 730 740 750 760 770 780 KYETQPRFIT ATGGTLHMYQ LEGLNWLRFS WAQGTDTILA DEMGLGKTIQ TIVFLYSLYK 790 800 810 820 830 840 EGHTKGPFLV SAPLSTIINW EREFQMWAPK FYVVTYTGDK DSRAIIRENE FSFEDNAIKG 850 860 870 880 890 900 GKKAFKMKRE AQVKFHVLLT SYELITIDQA ALGSIRWACL VVDEAHRLKN NQSKFFRVLN 910 920 930 940 950 960 GYKIDHKLLL TGTPLQNNLE ELFHLLNFLT PERFNNLEGF LEEFADISKE DQIKKLHDLL 970 980 990 1000 1010 1020 GPHMLRRLKA DVFKNMPAKT ELIVRVELSP MQKKYYKYIL TRNFEALNSR GGGNQVSLLN 1030 1040 1050 1060 1070 1080 IMMDLKKCCN HPYLFPVAAM ESPKLPSGAY EGGALIKSSG KLMLLQKMLR KLKEQGHRVL 1090 1100 1110 1120 1130 1140 IFSQMTKMLD LLEDFLDYEG YKYERIDGGI TGALRQEAID RFNAPGAQQF CFLLSTRAGG 1150 1160 1170 1180 1190 1200 LGINLATADT VIIFDSDWNP HNDIQAFSRA HRIGQANKVM IYRFVTRASV EERITQVAKR 1210 1220 1230 1240 1250 1260 KMMLTHLVVR PGLGSKAGSM SKQELDDILK FGTEELFKDE NEGENKEEDS SVIHYDNEAI 1270 1280 1290 1300 1310 1320 ARLLDRNQDA TEDTDVQNMN EYLSSFKVAQ YVVREEDKIE EIEREIIKQE ENVDPDYWEK 1330 1340 1350 1360 1370 1380 LLRHHYEQQQ EDLARNLGKG KRVRKQVNYN DAAQEDQDNQ SEYSVGSEEE DEDFDERPEG 1390 1400 1410 1420 1430 1440 RRQSKRQLRN EKDKPLPPLL ARVGGNIEVL GFNTRQRKAF LNAVMRWGMP PQDAFTTQWL 1450 1460 1470 1480 1490 1500 VRDLRGKTEK EFKAYVSLFM RHLCEPGADG SETFADGVPR EGLSRQQVLT RIGVMSLVKK 1510 1520 1530 1540 1550 1560 KVQEFEHING RWSMPELMPD PSADSKRSSR ASSPTKTSPT TPEASATNSP CTSKPATPAP 1570 1580 1590 1600 1610 1620 SEKGEGIRTP LEKEEAENQE EKPEKNSRIG EKMETEADAP SPAPSLGERL EPRKIPLEDE 1630 1640 1650 1660 1670 1680 VPGVPGEMEP EPGYRGDREK SATESTPGER GEEKPLDGQE HRERPEGETG DLGKREDVKG 1690 1700 1710 1720 1730 1740 DRELRPGPRD EPRSNGRREE KTEKPRFMFN IADGGFTELH TLWQNEERAA ISSGKLNEIW 1750 1760 1770 1780 1790 1800 HRRHDYWLLA GIVLHGYARW QDIQNDAQFA IINEPFKTEA NKGNFLEMKN KFLARRFKLL 1810 1820 1830 1840 1850 1860 EQALVIEEQL RRAAYLNLSQ EPAHPAMALH ARFAEAECLA ESHQHLSKES LAGNKPANAV 1870 1880 1890 1900 1910 1920 LHKVLNQLEE LLSDMKADVT RLPATLSRIP PIAARLQMSE RSILSRLASK GTEPHPTPAY 1930 1940 1950 1960 1970 1980 PPGPYATPPG YGAAFSAAPV GALAAAGANY SQMPAGSFIT AATNGPPVLV KKEKEMVGAL 1990 2000 VSDGLDRKEP RAGEVICIDD
	Isoform 2 [UniParc]. Checksum: F8D7B7C132B263A6	FASTA	1,966	222,861
	10 20 30 40 50 60 MKAADTVILW ARSKNDQLRI SFPPGLCWGD RMPDKDDIRL LPSALGVKKR KRGPKKQKEN 70 80 90 100 110 120 KPGKPRKRKK RDSEEEFGSE RDEYREKSES GGSEYGTGPG RKRRRKHREK KEKKTKRRKK 130 140 150 160 170 180 GEGDGGQKQV EQKSSATLLL TWGLEDVEHV FSEEDYHTLT NYKAFSQFMR PLIAKKNPKI 190 200 210 220 230 240 PMSKMMTILG AKWREFSANN PFKGSAAAVA AAAAAAAAAV AEQVSAAVSS ATPIAPSGPP 250 260 270 280 290 300 ALPPPPAADI QPPPIRRAKT KEGKGPGHKR RSKSPRVPDG RKKLRGKKMA PLKIKLGLLG 310 320 330 340 350 360 GKRKKGGSYV FQSDEGPEPE AEESDLDSGS VHSASGRPDG PVRTKKLKRG RPGRKKKKVL 370 380 390 400 410 420 GCPAVAGEEE VDGYETDHQD YCEVCQQGGE IILCDTCPRA YHLVCLDPEL DRAPEGKWSC 430 440 450 460 470 480 PHCEKEGVQW EAKEEEEEYE EEGEEEGEKE EEDDHMEYCR VCKDGGELLC CDACISSYHI 490 500 510 520 530 540 HCLNPPLPDI PNGEWLCPRC TCPVLKGRVQ KILHWRWGEP PVAVPAPQQA DGNPDVPPPR 550 560 570 580 590 600 PLQGRSEREF FVKWVGLSYW HCSWAKELQL EIFHLVMYRN YQRKNDMDEP PPLDYGSGED 610 620 630 640 650 660 DGKSDKRKVK DPHYAEMEEK YYRFGIKPEW MTVHRIINHS VDKKGNYHYL VKWRDLPYDQ 670 680 690 700 710 720 STWEEDEMNI PEYEEHKQSY WRHRELIMGE DPAQPRKYKK KKKELQGDGP PSSPTNDPTV 730 740 750 760 770 780 KYETQPRFIT ATGGTLHMYQ LEGLNWLRFS WAQGTDTILA DEMGLGKTIQ TIVFLYSLYK 790 800 810 820 830 840 EGHTKGPFLV SAPLSTIINW EREFQMWAPK FYVVTYTGDK DSRAIIRENE FSFEDNAIKG 850 860 870 880 890 900 GKKAFKMKRE AQVKFHVLLT SYELITIDQA ALGSIRWACL VVDEAHRLKN NQSKFFRVLN 910 920 930 940 950 960 GYKIDHKLLL TGTPLQNNLE ELFHLLNFLT PERFNNLEGF LEEFADISKE DQIKKLHDLL 970 980 990 1000 1010 1020 GPHMLRRLKA DVFKNMPAKT ELIVRVELSP MQKKYYKYIL TRNFEALNSR GGGNQVSLLN 1030 1040 1050 1060 1070 1080 IMMDLKKCCN HPYLFPVAAM ESPKLPSGAY EGGALIKSSG KLMLLQKMLR KLKEQGHRVL 1090 1100 1110 1120 1130 1140 IFSQMTKMLD LLEDFLDYEG YKYERIDGGI TGALRQEAID RFNAPGAQQF CFLLSTRAGG 1150 1160 1170 1180 1190 1200 LGINLATADT VIIFDSDWNP HNDIQAFSRA HRIGQANKVM IYRFVTRASV EERITQVAKR 1210 1220 1230 1240 1250 1260 KMMLTHLVVR PGLGSKAGSM SKQELDDILK FGTEELFKDE NEGENKEEDS SVIHYDNEAI 1270 1280 1290 1300 1310 1320 ARLLDRNQDA TEDTDVQNMN EYLSSFKVAQ YVVREEDKIE EIEREIIKQE ENVDPDYWEK 1330 1340 1350 1360 1370 1380 LLRHHYEQQQ EDLARNLGKG KRVRKQVNYN DAAQEDQDNQ SEYSVGSEEE DEDFDERPEG 1390 1400 1410 1420 1430 1440 RRQSKRQLRN EKDKPLPPLL ARVGGNIEVL GFNTRQRKAF LNAVMRWGMP PQDAFTTQWL 1450 1460 1470 1480 1490 1500 VRDLRGKTEK EFKAYVSLFM RHLCEPGADG SETFADGVPR EGLSRQQVLT RIGVMSLVKK 1510 1520 1530 1540 1550 1560 KVQEFEHING RWSMPELMPD PSADSKRSSR ASSPTKTSPT TPEASATNSP CTSKPATPAP 1570 1580 1590 1600 1610 1620 SEKGEGIRTP LEKEEAENQE EKPEKNSRIG EKMETEADAP SPAPSLGERL EPRKIPLEDE 1630 1640 1650 1660 1670 1680 VPGVPGEMEP EPGYRGDREK SEDVKGDREL RPGPRDEPRS NGRREEKTEK PRFMFNIADG 1690 1700 1710 1720 1730 1740 GFTELHTLWQ NEERAAISSG KLNEIWHRRH DYWLLAGIVL HGYARWQDIQ NDAQFAIINE 1750 1760 1770 1780 1790 1800 PFKTEANKGN FLEMKNKFLA RRFKLLEQAL VIEEQLRRAA YLNLSQEPAH PAMALHARFA 1810 1820 1830 1840 1850 1860 EAECLAESHQ HLSKESLAGN KPANAVLHKV LNQLEELLSD MKADVTRLPA TLSRIPPIAA 1870 1880 1890 1900 1910 1920 RLQMSERSIL SRLASKGTEP HPTPAYPPGP YATPPGYGAA FSAAPVGALA AAGANYSQMP 1930 1940 1950 1960 AGSFITAATN GPPVLVKKEK EMVGALVSDG LDRKEPRAGE VICIDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9688266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
[2]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Characterization of the CHD family of proteins." Woodage T., Basrai M.A., Baxevanis A.D., Hieter P., Collins F.S. Proc. Natl. Acad. Sci. U.S.A. 94:11472-11477(1997) [PubMed: 9326634] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1966 (ISOFORM 2). Tissue: Fetus.
[4]	"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: 7560064] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 121-654. Tissue: Thymus.
[5]	"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: 9804427] [Abstract] Cited for: IDENTIFICATION AS A COMPONENT OF THE NURD COMPLEX, FUNCTION.
[6]	"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: 11230151] [Abstract] Cited for: INTERACTION WITH TRIM28.
[7]	"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: 12505151] [Abstract] Cited for: INTERACTION WITH HABP4 AND SERBP1.
[8]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713 AND SER-1601, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-713; SER-1601 AND SER-1605, MASS SPECTROMETRY. 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: 17626165] [Abstract] Cited for: INTERACTION WITH PCNT, SUBCELLULAR LOCATION, FUNCTION.
[11]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713 AND SER-1601, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-1361; SER-1364; SER-1367; SER-1601 AND SER-1605, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-1549; SER-1601 AND SER-1605, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-1601 AND SER-1605, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U91543 mRNA. Translation: AAC39923.1. CH471108 Genomic DNA. Translation: EAW90114.1. CH471108 Genomic DNA. Translation: EAW90116.1. AF006515 mRNA. Translation: AAB87383.1. Different termination. U08379 mRNA. Translation: AAC50228.1.
IPI	IPI00373870. IPI00411592.
RefSeq	NP_001005271.2. NM_001005271.2. NP_001005273.1. NM_001005273.2. NP_005843.2. NM_005852.3.
UniGene	Hs.25601.
3D structure databases
ProteinModelPortal	Q12873.
SMR	Q12873. Positions 374-1287.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-32496N.
IntAct	Q12873. 77 interactions.
MINT	MINT-1185641.
STRING	Q12873.
PTM databases
PhosphoSite	Q12873.
Polymorphism databases
DMDM	88911273.
Proteomic databases
PRIDE	Q12873.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000330494; ENSP00000332628; ENSG00000170004.
GeneID	1107.
KEGG	hsa:1107.
UCSC	uc002gjd.2. human. uc002gjf.2. human.
Organism-specific databases
CTD	1107.
GeneCards	GC17P007732.
H-InvDB	HIX0013516.
HGNC	HGNC:1918. CHD3.
MIM	602120. gene.
neXtProt	NX_Q12873.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07827.
HOVERGEN	HBG005326.
PhylomeDB	Q12873.
Enzyme and pathway databases
Pathway_Interaction_DB	hdac_classi_pathway. Signaling events mediated by HDAC Class I.
Gene expression databases
ArrayExpress	Q12873.
Bgee	Q12873.
CleanEx	HS_CHD3.
Genevestigator	Q12873.
GermOnline	ENSG00000170004. Homo sapiens.
Family and domain databases
InterPro	IPR012957. CHD_C2. IPR012958. CHD_N. IPR023780. Chromo_domain. IPR000953. Chromo_domain/shadow. IPR016197. Chromodomain-like. IPR023779. Chromodomain_CS. IPR014001. DEAD-like_helicase. IPR002464. DNA/RNA_helicase_DEAH_CS. IPR009462. DUF1086. IPR009463. DUF1087. IPR001650. Helicase_C. IPR000910. HMG_HMG1/HMG2. 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]
Gene3D	G3DSA:1.10.30.10. HMG-box. 1 hit. G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 2 hits.
KO	K11642.
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. 1 hit. SSF57903. FYVE_PHD_ZnF. 2 hits.
PROSITE	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]
ProtoNet	Search...
Other
NextBio	4590.
SOURCE	Search...

Entry information

Entry name

CHD3_HUMAN

Accession

Primary (citable) accession number: Q12873
Secondary accession number(s): D3DTQ9, Q9Y4I0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	February 7, 2006
Last modified:	January 25, 2012
This is version 129 of the entry and version 3 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.