O14646 (CHD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chromodomain-helicase-DNA-binding protein 1
Short name=CHD-1
EC=3.6.4.12

Alternative name(s):
ATP-dependent helicase CHD1

Gene names

Name:

CHD1

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	1710 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Is also associated with histone deacetylase (HDAC) activity By similarity. Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3. Required for maintaining open chromatin and pluripotency in embryonic stem cells. Ref.8
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Component of the SAGA complex By similarity. Interacts with BCLAF1, NCoR, SRP20 and SAFB By similarity. Specifically interacts with methylated H3K4me2 and H3K4me3. Interacts with the FACT complex, the PAF complex and the U2 snRNP. Interacts directly with PAF1, SFA3A1, SFA3A2, SFA3A3, SNF2 and SSRP1. Ref.4 Ref.7 Ref.8 Ref.15
Subcellular location	Nucleus. Cytoplasm By similarity. Note: Is released into the cytoplasm when cells enter mitosis and is reincorporated into chromatin during telophase-cytokinesis By similarity.
Domain	The 2 chromodomains are involved in the binding to the histone H3 methyllysine at position 4 (H3K4me3). Ref.7
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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Chromatin regulator Helicase Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin remodeling Inferred from electronic annotation. Source: Compara regulation of transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent DNA helicase activity Traceable author statement Ref.1. Source: ProtInc DNA binding Inferred from electronic annotation. Source: UniProtKB-KW methylated histone residue binding Inferred from direct assay PubMed 21029866. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NS1	B2BUF1	3	EBI-1560858,EBI-4291940	From a different organism.

Alternative products

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

Isoform 1 (identifier: O14646-1)

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: O14646-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1684-1684: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1710

1710

Chromodomain-helicase-DNA-binding protein 1

PRO_0000080224

Regions

Domain

272 – 364

93

Chromo 1

Domain

389 – 452

64

Chromo 2

Domain

493 – 663

171

Helicase ATP-binding

Domain

792 – 943

152

Helicase C-terminal

Repeat

1628 – 1632

5

1

Repeat

1634 – 1638

5

2

Repeat

1640 – 1644

5

3

Nucleotide binding

506 – 513

8

ATP Potential

Region

1628 – 1644

17

3 X 5 AA repeats of H-S-D-H-R

Motif

614 – 617

4

DEAH box

Compositional bias

1 – 70

70

Ser-rich

Compositional bias

117 – 137

21

Ser-rich

Amino acid modifications

Modified residue

5

1

Phosphoserine By similarity

Modified residue

215

1

Phosphoserine Ref.14

Modified residue

216

1

Phosphoserine Ref.14

Modified residue

237

1

Phosphothreonine Ref.10

Modified residue

241

1

Phosphoserine Ref.10

Modified residue

250

1

Phosphothreonine Ref.12

Modified residue

252

1

Phosphoserine Ref.12

Modified residue

1025

1

Phosphoserine Ref.12

Modified residue

1040

1

Phosphoserine Ref.9 Ref.10 Ref.12

Modified residue

1081

1

Phosphoserine Ref.9

Modified residue

1096

1

Phosphoserine Ref.10 Ref.14

Modified residue

1098

1

Phosphoserine Ref.10 Ref.14

Modified residue

1100

1

Phosphoserine Ref.10 Ref.14

Modified residue

1102

1

Phosphoserine Ref.14

Modified residue

1353

1

Phosphoserine Ref.14

Modified residue

1355

1

Phosphoserine Ref.14

Modified residue

1356

1

Phosphoserine Ref.14

Modified residue

1360

1

Phosphoserine Ref.14

Modified residue

1363

1

Phosphoserine Ref.14

Modified residue

1371

1

Phosphoserine Ref.14

Modified residue

1677

1

Phosphoserine Ref.9 Ref.10 Ref.12

Natural variations

Alternative sequence

1684

1

Missing in isoform 2.

VSP_038432

Natural variant

264

1

P → T.
Corresponds to variant rs10062803 [ dbSNP | Ensembl ].

VAR_055652

Experimental info

Sequence conflict

392

1

E → G in AAB87381. Ref.1

Secondary structure

1

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1710

Helix Strand Turn

Details...

Beta strand

273 – 283

11

Helix

290 – 292

3

Helix

294 – 300

7

Turn

303 – 306

4

Beta strand

315 – 322

8

Helix

327 – 329

3

Beta strand

331 – 333

3

Helix

335 – 340

6

Helix

347 – 354

8

Helix

1128 – 1138

11

Helix

1144 – 1146

3

Helix

1148 – 1154

7

Helix

1162 – 1180

19

Beta strand

1201 – 1204

4

Beta strand

1207 – 1210

4

Helix

1211 – 1227

17

Helix

1232 – 1236

5

Beta strand

1249 – 1251

3

Helix

1255 – 1268

14

Helix

1273 – 1278

6

Beta strand

1280 – 1283

4

Turn

1285 – 1287

3

Helix

1299 – 1324

26

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 24, 2009. Version 2. Checksum: D888AAA46FDA31B1	FASTA	1,710	196,688
	10 20 30 40 50 60 MNGHSDEESV RNSSGESSQS DDDSGSASGS GSGSSSGSSS DGSSSQSGSS DSDSGSESGS 70 80 90 100 110 120 QSESESDTSR ENKVQAKPPK VDGAEFWKSS PSILAVQRSA ILKKQQQQQQ QQQHQASSNS 130 140 150 160 170 180 GSEEDSSSSE DSDDSSSEVK RKKHKDEDWQ MSGSGSPSQS GSDSESEEER EKSSCDETES 190 200 210 220 230 240 DYEPKNKVKS RKPQNRSKSK NGKKILGQKK RQIDSSEEDD DEEDYDNDKR SSRRQATVNV 250 260 270 280 290 300 SYKEDEEMKT DSDDLLEVCG EDVPQPEEEE FETIERFMDC RIGRKGATGA TTTIYAVEAD 310 320 330 340 350 360 GDPNAGFEKN KEPGEIQYLI KWKGWSHIHN TWETEETLKQ QNVRGMKKLD NYKKKDQETK 370 380 390 400 410 420 RWLKNASPED VEYYNCQQEL TDDLHKQYQI VERIIAHSNQ KSAAGYPDYY CKWQGLPYSE 430 440 450 460 470 480 CSWEDGALIS KKFQACIDEY FSRNQSKTTP FKDCKVLKQR PRFVALKKQP SYIGGHEGLE 490 500 510 520 530 540 LRDYQLNGLN WLAHSWCKGN SCILADEMGL GKTIQTISFL NYLFHEHQLY GPFLLVVPLS 550 560 570 580 590 600 TLTSWQREIQ TWASQMNAVV YLGDINSRNM IRTHEWTHHQ TKRLKFNILL TTYEILLKDK 610 620 630 640 650 660 AFLGGLNWAF IGVDEAHRLK NDDSLLYKTL IDFKSNHRLL ITGTPLQNSL KELWSLLHFI 670 680 690 700 710 720 MPEKFSSWED FEEEHGKGRE YGYASLHKEL EPFLLRRVKK DVEKSLPAKV EQILRMEMSA 730 740 750 760 770 780 LQKQYYKWIL TRNYKALSKG SKGSTSGFLN IMMELKKCCN HCYLIKPPDN NEFYNKQEAL 790 800 810 820 830 840 QHLIRSSGKL ILLDKLLIRL RERGNRVLIF SQMVRMLDIL AEYLKYRQFP FQRLDGSIKG 850 860 870 880 890 900 ELRKQALDHF NAEGSEDFCF LLSTRAGGLG INLASADTVV IFDSDWNPQN DLQAQARAHR 910 920 930 940 950 960 IGQKKQVNIY RLVTKGSVEE DILERAKKKM VLDHLVIQRM DTTGKTVLHT GSAPSSSTPF 970 980 990 1000 1010 1020 NKEELSAILK FGAEELFKEP EGEEQEPQEM DIDEILKRAE THENEPGPLT VGDELLSQFK 1030 1040 1050 1060 1070 1080 VANFSNMDED DIELEPERNS KNWEEIIPED QRRRLEEEER QKELEEIYML PRMRNCAKQI 1090 1100 1110 1120 1130 1140 SFNGSEGRRS RSRRYSGSDS DSISEGKRPK KRGRPRTIPR ENIKGFSDAE IRRFIKSYKK 1150 1160 1170 1180 1190 1200 FGGPLERLDA IARDAELVDK SETDLRRLGE LVHNGCIKAL KDSSSGTERT GGRLGKVKGP 1210 1220 1230 1240 1250 1260 TFRISGVQVN AKLVISHEEE LIPLHKSIPS DPEERKQYTI PCHTKAAHFD IDWGKEDDSN 1270 1280 1290 1300 1310 1320 LLIGIYEYGY GSWEMIKMDP DLSLTHKILP DDPDKKPQAK QLQTRADYLI KLLSRDLAKK 1330 1340 1350 1360 1370 1380 EALSGAGSSK RRKARAKKNK AMKSIKVKEE IKSDSSPLPS EKSDEDDDKL SESKSDGRER 1390 1400 1410 1420 1430 1440 SKKSSVSDAP VHITASGEPV PISEESEELD QKTFSICKER MRPVKAALKQ LDRPEKGLSE 1450 1460 1470 1480 1490 1500 REQLEHTRQC LIKIGDHITE CLKEYTNPEQ IKQWRKNLWI FVSKFTEFDA RKLHKLYKHA 1510 1520 1530 1540 1550 1560 IKKRQESQQN SDQNSNLNPH VIRNPDVERL KENTNHDDSS RDSYSSDRHL TQYHDHHKDR 1570 1580 1590 1600 1610 1620 HQGDSYKKSD SRKRPYSSFS NGKDHRDWDH YKQDSRYYSD REKHRKLDDH RSRDHRSNLE 1630 1640 1650 1660 1670 1680 GSLKDRSHSD HRSHSDHRLH SDHRSSSEYT HHKSSRDYRY HSDWQMDHRA SSSGPRSPLD 1690 1700 1710 QRSPYGSRSP FEHSVEHKST PEHTWSSRKT
	Isoform 2 [UniParc]. Checksum: 8B2C96C7597E55B4	FASTA	1,709	196,590
	10 20 30 40 50 60 MNGHSDEESV RNSSGESSQS DDDSGSASGS GSGSSSGSSS DGSSSQSGSS DSDSGSESGS 70 80 90 100 110 120 QSESESDTSR ENKVQAKPPK VDGAEFWKSS PSILAVQRSA ILKKQQQQQQ QQQHQASSNS 130 140 150 160 170 180 GSEEDSSSSE DSDDSSSEVK RKKHKDEDWQ MSGSGSPSQS GSDSESEEER EKSSCDETES 190 200 210 220 230 240 DYEPKNKVKS RKPQNRSKSK NGKKILGQKK RQIDSSEEDD DEEDYDNDKR SSRRQATVNV 250 260 270 280 290 300 SYKEDEEMKT DSDDLLEVCG EDVPQPEEEE FETIERFMDC RIGRKGATGA TTTIYAVEAD 310 320 330 340 350 360 GDPNAGFEKN KEPGEIQYLI KWKGWSHIHN TWETEETLKQ QNVRGMKKLD NYKKKDQETK 370 380 390 400 410 420 RWLKNASPED VEYYNCQQEL TDDLHKQYQI VERIIAHSNQ KSAAGYPDYY CKWQGLPYSE 430 440 450 460 470 480 CSWEDGALIS KKFQACIDEY FSRNQSKTTP FKDCKVLKQR PRFVALKKQP SYIGGHEGLE 490 500 510 520 530 540 LRDYQLNGLN WLAHSWCKGN SCILADEMGL GKTIQTISFL NYLFHEHQLY GPFLLVVPLS 550 560 570 580 590 600 TLTSWQREIQ TWASQMNAVV YLGDINSRNM IRTHEWTHHQ TKRLKFNILL TTYEILLKDK 610 620 630 640 650 660 AFLGGLNWAF IGVDEAHRLK NDDSLLYKTL IDFKSNHRLL ITGTPLQNSL KELWSLLHFI 670 680 690 700 710 720 MPEKFSSWED FEEEHGKGRE YGYASLHKEL EPFLLRRVKK DVEKSLPAKV EQILRMEMSA 730 740 750 760 770 780 LQKQYYKWIL TRNYKALSKG SKGSTSGFLN IMMELKKCCN HCYLIKPPDN NEFYNKQEAL 790 800 810 820 830 840 QHLIRSSGKL ILLDKLLIRL RERGNRVLIF SQMVRMLDIL AEYLKYRQFP FQRLDGSIKG 850 860 870 880 890 900 ELRKQALDHF NAEGSEDFCF LLSTRAGGLG INLASADTVV IFDSDWNPQN DLQAQARAHR 910 920 930 940 950 960 IGQKKQVNIY RLVTKGSVEE DILERAKKKM VLDHLVIQRM DTTGKTVLHT GSAPSSSTPF 970 980 990 1000 1010 1020 NKEELSAILK FGAEELFKEP EGEEQEPQEM DIDEILKRAE THENEPGPLT VGDELLSQFK 1030 1040 1050 1060 1070 1080 VANFSNMDED DIELEPERNS KNWEEIIPED QRRRLEEEER QKELEEIYML PRMRNCAKQI 1090 1100 1110 1120 1130 1140 SFNGSEGRRS RSRRYSGSDS DSISEGKRPK KRGRPRTIPR ENIKGFSDAE IRRFIKSYKK 1150 1160 1170 1180 1190 1200 FGGPLERLDA IARDAELVDK SETDLRRLGE LVHNGCIKAL KDSSSGTERT GGRLGKVKGP 1210 1220 1230 1240 1250 1260 TFRISGVQVN AKLVISHEEE LIPLHKSIPS DPEERKQYTI PCHTKAAHFD IDWGKEDDSN 1270 1280 1290 1300 1310 1320 LLIGIYEYGY GSWEMIKMDP DLSLTHKILP DDPDKKPQAK QLQTRADYLI KLLSRDLAKK 1330 1340 1350 1360 1370 1380 EALSGAGSSK RRKARAKKNK AMKSIKVKEE IKSDSSPLPS EKSDEDDDKL SESKSDGRER 1390 1400 1410 1420 1430 1440 SKKSSVSDAP VHITASGEPV PISEESEELD QKTFSICKER MRPVKAALKQ LDRPEKGLSE 1450 1460 1470 1480 1490 1500 REQLEHTRQC LIKIGDHITE CLKEYTNPEQ IKQWRKNLWI FVSKFTEFDA RKLHKLYKHA 1510 1520 1530 1540 1550 1560 IKKRQESQQN SDQNSNLNPH VIRNPDVERL KENTNHDDSS RDSYSSDRHL TQYHDHHKDR 1570 1580 1590 1600 1610 1620 HQGDSYKKSD SRKRPYSSFS NGKDHRDWDH YKQDSRYYSD REKHRKLDDH RSRDHRSNLE 1630 1640 1650 1660 1670 1680 GSLKDRSHSD HRSHSDHRLH SDHRSSSEYT HHKSSRDYRY HSDWQMDHRA SSSGPRSPLD 1690 1700 QRSYGSRSPF EHSVEHKSTP EHTWSSRKT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [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: Cerebellum.
[4]	"Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains." Sims R.J. III, Chen C.-F., Santos-Rosa H., Kouzarides T., Patel S.S., Reinberg D. J. Biol. Chem. 280:41789-41792(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH H3K4ME2 AND H3K4ME3.
[5]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[6]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[7]	"Molecular implications of evolutionary differences in CHD double chromodomains." Flanagan J.F., Blus B.J., Kim D., Clines K.L., Rastinejad F., Khorasanizadeh S. J. Mol. Biol. 369:334-342(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN, INTERACTION WITH HISTONE H3K4ME3.
[8]	"Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing." Sims R.J. III, Millhouse S., Chen C.-F., Lewis B.A., Erdjument-Bromage H., Tempst P., Manley J.L., Reinberg D. Mol. Cell 28:665-676(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH H3K4ME3; PAF1; SFA3A1; SFA3A2; SFA3A3; SNF2 AND SSRP1.
[9]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1040; SER-1081 AND SER-1677, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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 THR-237; SER-241; SER-1040; SER-1096; SER-1098; SER-1100 AND SER-1677, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[12]	"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 THR-250; SER-252; SER-1025; SER-1040 AND SER-1677, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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].
[14]	"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-215; SER-216; SER-1096; SER-1098; SER-1100; SER-1102; SER-1353; SER-1355; SER-1356; SER-1360; SER-1363 AND SER-1371, MASS SPECTROMETRY.
[15]	"Double chromodomains cooperate to recognize the methylated histone H3 tail." Flanagan J.F., Mi L.-Z., Chruszcz M., Cymborowski M., Clines K.L., Kim Y., Minor W., Rastinejad F., Khorasanizadeh S. Nature 438:1181-1185(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 268-443, INTERACTION WITH HISTONE H3K4ME3.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF006513 mRNA. Translation: AAB87381.1.
AC022121 Genomic DNA. No translation available.
BC117134 mRNA. Translation: AAI17135.1.

IPI

IPI00297851.
IPI00954192.

RefSeq

NP_001261.2. NM_001270.2.

UniGene

Hs.643465.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B2T	X-ray	2.45	A/B	268-443	[»]
			C	268-373	[»]
2B2U	X-ray	2.95	A/B	268-443	[»]
			C	268-373	[»]
2B2V	X-ray	2.65	A/B	268-443	[»]
			C	268-373	[»]
2B2W	X-ray	2.40	A/B	268-443	[»]
			C	268-373	[»]
2B2Y	X-ray	2.35	A/B	268-443	[»]
			C	268-373	[»]
4B4C	X-ray	1.62	A	1119-1327	[»]

ProteinModelPortal

O14646.

SMR

O14646. Positions 269-1020, 1124-1327.

ModBase

Search...

Protein-protein interaction databases

IntAct

O14646. 1 interaction.

STRING

9606.ENSP00000284049.

PTM databases

PhosphoSite

O14646.

Proteomic databases

PaxDb

O14646.

PRIDE

O14646.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000284049; ENSP00000284049; ENSG00000153922.

GeneID

1105.

KEGG

hsa:1105.

UCSC

uc003knf.3. human.

Organism-specific databases

CTD

1105.

GeneCards

GC05M098219.

H-InvDB

HIX0005061.

HGNC

HGNC:1915. CHD1.

HPA

HPA022236.

MIM

602118. gene.

neXtProt

NX_O14646.

PharmGKB

PA26451.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0553.

HOGENOM

HOG000207917.

HOVERGEN

HBG005325.

InParanoid

O14646.

KO

K11367.

OMA

AETHENE.

OrthoDB

EOG4PG601.

PhylomeDB

O14646.

Gene expression databases

ArrayExpress

O14646.

Bgee

O14646.

CleanEx

HS_CHD1.

Genevestigator

O14646.

GermOnline

ENSG00000153922. Homo sapiens.

Family and domain databases

InterPro

IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR025260. DUF4208.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR000330. SNF2_N.
[Graphical view]

Pfam

PF00385. Chromo. 2 hits.
PF13907. DUF4208. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]

SMART

SM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

SUPFAM

SSF54160. Chromodomain-like. 2 hits.

PROSITE

PS00598. CHROMO_1. 2 hits.
PS50013. CHROMO_2. 2 hits.
PS00690. DEAH_ATP_HELICASE. False negative.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00445. Epirubicin.

EvolutionaryTrace

O14646.

GenomeRNAi

1105.

NextBio

4580.

SOURCE

Search...

Entry information

Entry name

CHD1_HUMAN

Accession

Primary (citable) accession number: O14646
Secondary accession number(s): Q17RZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 24, 2009
Last modified:	April 3, 2013
This is version 122 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.