P32657 (CHD1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chromo domain-containing protein 1
EC=3.6.4.-

Alternative name(s):
ATP-dependent helicase CHD1

Gene names

Name:	CHD1
Ordered Locus Names:	YER164W
ORF Names:	SYGP-ORF4

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1468 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) complexes SAGA and SLIK. It recognizes H3K4me. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. Acts in opposition to the FACT complex in regulating polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the pol 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. Ref.3 Ref.4 Ref.8 Ref.9 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19 Ref.20 Ref.23
Subunit structure	Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Interacts with RTF1, SPT5 and with the FACT subunits POB3 and SPT16. Ref.5 Ref.6 Ref.8 Ref.13 Ref.18 Ref.27
Subcellular location	Nucleus Probable Ref.8.
Miscellaneous	Present with 1620 molecules/cell in log phase SD medium.
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.
Biophysicochemical properties	Kinetic parameters: KM=10.2 nM for ATP Ref.16

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Chromatin regulator Helicase Hydrolase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP-dependent chromatin remodeling Inferred from direct assay Ref.4. Source: SGD histone H2B conserved C-terminal lysine ubiquitination Inferred from mutant phenotype PubMed 22549955. Source: SGD negative regulation of DNA-dependent DNA replication Inferred from genetic interaction Ref.23. Source: SGD negative regulation of histone H3-K14 acetylation Inferred from mutant phenotype PubMed 19948887. Source: SGD negative regulation of histone H3-K9 acetylation Inferred from mutant phenotype PubMed 19948887. Source: SGD nucleosome mobilization Inferred from direct assay Ref.14. Source: SGD nucleosome positioning Inferred from direct assay Ref.16. Source: SGD regulation of transcription by chromatin organization Inferred from mutant phenotype Ref.15. Source: SGD regulation of transcriptional start site selection at RNA polymerase II promoter Inferred from genetic interaction PubMed 19948887. Source: SGD termination of RNA polymerase I transcription Inferred from genetic interaction Ref.20. Source: SGD termination of RNA polymerase II transcription Inferred from mutant phenotype PubMed 12504018. Source: SGD transcription elongation from RNA polymerase II promoter Inferred from genetic interaction Ref.8. Source: SGD
Cellular_component	SAGA complex Inferred from direct assay Ref.13. Source: SGD SLIK (SAGA-like) complex Inferred from direct assay Ref.13. Source: SGD mitochondrion Inferred from direct assay PubMed 14576278PubMed 16823961. Source: SGD nucleolar chromatin Inferred from direct assay Ref.20. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-dependent ATPase activity Inferred from direct assay Ref.4. Source: SGD chromatin DNA binding Inferred from direct assay Ref.8. Source: SGD helicase activity Inferred from electronic annotation. Source: UniProtKB-KW methylated histone residue binding Inferred from direct assay Ref.13. Source: SGD rDNA binding Inferred from direct assay Ref.20. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1468

1468

Chromo domain-containing protein 1

PRO_0000080237

Regions

Domain

195 – 257

63

Chromo 1

Domain

285 – 350

66

Chromo 2

Domain

388 – 562

175

Helicase ATP-binding

Domain

699 – 860

162

Helicase C-terminal

Nucleotide binding

401 – 408

8

ATP Potential

Motif

513 – 516

4

DEAH box

Amino acid modifications

Modified residue

36

1

Phosphoserine Ref.17 Ref.22 Ref.24

Modified residue

904

1

Phosphothreonine Ref.24

Modified residue

987

1

Phosphoserine Ref.7 Ref.22 Ref.24

Modified residue

989

1

Phosphoserine Ref.7 Ref.22 Ref.24

Modified residue

1272

1

Phosphoserine Ref.24

Modified residue

1300

1

Phosphoserine Ref.24

Modified residue

1302

1

Phosphothreonine Ref.22 Ref.24

Modified residue

1336

1

Phosphoserine Ref.22 Ref.24

Modified residue

1341

1

Phosphothreonine Ref.12

Modified residue

1358

1

Phosphoserine Ref.21

Modified residue

1364

1

Phosphoserine Ref.21

Modified residue

1372

1

Phosphoserine Ref.22 Ref.24

Cross-link

1144

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Experimental info

Mutagenesis

220

1

E → L or W: No interaction with methylated histone H3 'K-4'. Ref.13 Ref.27

Mutagenesis

222

1

H → Y: Confers interaction with methylated histone H3 'K-4'. Ref.13

Mutagenesis

314

1

L → Y: No effect on interaction with methylated histone H3 'K-4'. Ref.13

Mutagenesis

316

1

Y → E: Disrupts interaction with methylated histone H3 'K-4'; abrogates histone acetylation activity of SLIK. Ref.13

Secondary structure

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1468

Helix Strand Turn

Details...

Beta strand

179 – 187

9

Turn

190 – 192

3

Helix

193 – 196

4

Helix

204 – 210

7

Beta strand

211 – 217

7

Helix

222 – 224

3

Beta strand

226 – 228

3

Helix

230 – 233

4

Beta strand

234 – 237

4

Helix

239 – 249

11

Helix

251 – 258

8

Helix

264 – 283

20

Beta strand

286 – 297

12

Beta strand

299 – 301

3

Beta strand

303 – 311

9

Beta strand

320 – 323

4

Helix

324 – 330

7

Helix

332 – 338

7

Helix

1012 – 1025

14

Helix

1029 – 1031

3

Helix

1032 – 1037

6

Helix

1046 – 1091

46

Beta strand

1092 – 1094

3

Beta strand

1096 – 1098

3

Beta strand

1101 – 1103

3

Helix

1104 – 1112

9

Beta strand

1119 – 1122

4

Beta strand

1125 – 1129

5

Helix

1130 – 1150

21

Helix

1155 – 1157

3

Beta strand

1171 – 1173

3

Helix

1177 – 1190

14

Helix

1195 – 1200

6

Turn

1202 – 1204

3

Helix

1207 – 1209

3

Helix

1250 – 1264

15

Turn

1265 – 1268

4

Sequences

	Sequence		Length	Mass (Da)
	P32657 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 78BDB74C7FEC6BE5	FASTA	1,468	168,241
	10 20 30 40 50 60 MAAKDISTEV LQNPELYGLR RSHRAAAHQQ NYFNDSDDED DEDNIKQSRR KRMTTIEDDE 70 80 90 100 110 120 DEFEDEEGEE DSGEDEDEED FEEDDDYYGS PIKQNRSKPK SRTKSKSKSK PKSQSEKQST 130 140 150 160 170 180 VKIPTRFSNR QNKTVNYNID YSDDDLLESE DDYGSEEALS EENVHEASAN PQPEDFHGID 190 200 210 220 230 240 IVINHRLKTS LEEGKVLEKT VPDLNNCKEN YEFLIKWTDE SHLHNTWETY ESIGQVRGLK 250 260 270 280 290 300 RLDNYCKQFI IEDQQVRLDP YVTAEDIEIM DMERERRLDE FEEFHVPERI IDSQRASLED 310 320 330 340 350 360 GTSQLQYLVK WRRLNYDEAT WENATDIVKL APEQVKHFQN RENSKILPQY SSNYTSQRPR 370 380 390 400 410 420 FEKLSVQPPF IKGGELRDFQ LTGINWMAFL WSKGDNGILA DEMGLGKTVQ TVAFISWLIF 430 440 450 460 470 480 ARRQNGPHII VVPLSTMPAW LDTFEKWAPD LNCICYMGNQ KSRDTIREYE FYTNPRAKGK 490 500 510 520 530 540 KTMKFNVLLT TYEYILKDRA ELGSIKWQFM AVDEAHRLKN AESSLYESLN SFKVANRMLI 550 560 570 580 590 600 TGTPLQNNIK ELAALVNFLM PGRFTIDQEI DFENQDEEQE EYIHDLHRRI QPFILRRLKK 610 620 630 640 650 660 DVEKSLPSKT ERILRVELSD VQTEYYKNIL TKNYSALTAG AKGGHFSLLN IMNELKKASN 670 680 690 700 710 720 HPYLFDNAEE RVLQKFGDGK MTRENVLRGL IMSSGKMVLL DQLLTRLKKD GHRVLIFSQM 730 740 750 760 770 780 VRMLDILGDY LSIKGINFQR LDGTVPSAQR RISIDHFNSP DSNDFVFLLS TRAGGLGINL 790 800 810 820 830 840 MTADTVVIFD SDWNPQADLQ AMARAHRIGQ KNHVMVYRLV SKDTVEEEVL ERARKKMILE 850 860 870 880 890 900 YAIISLGVTD GNKYTKKNEP NAGELSAILK FGAGNMFTAT DNQKKLEDLN LDDVLNHAED 910 920 930 940 950 960 HVTTPDLGES HLGGEEFLKQ FEVTDYKADI DWDDIIPEEE LKKLQDEEQK RKDEEYVKEQ 970 980 990 1000 1010 1020 LEMMNRRDNA LKKIKNSVNG DGTAANSDSD DDSTSRSSRR RARANDMDSI GESEVRALYK 1030 1040 1050 1060 1070 1080 AILKFGNLKE ILDELIADGT LPVKSFEKYG ETYDEMMEAA KDCVHEEEKN RKEILEKLEK 1090 1100 1110 1120 1130 1140 HATAYRAKLK SGEIKAENQP KDNPLTRLSL KKREKKAVLF NFKGVKSLNA ESLLSRVEDL 1150 1160 1170 1180 1190 1200 KYLKNLINSN YKDDPLKFSL GNNTPKPVQN WSSNWTKEED EKLLIGVFKY GYGSWTQIRD 1210 1220 1230 1240 1250 1260 DPFLGITDKI FLNEVHNPVA KKSASSSDTT PTPSKKGKGI TGSSKKVPGA IHLGRRVDYL 1270 1280 1290 1300 1310 1320 LSFLRGGLNT KSPSADIGSK KLPTGPSKKR QRKPANHSKS MTPEITSSEP ANGPPSKRMK 1330 1340 1350 1360 1370 1380 ALPKGPAALI NNTRLSPNSP TPPLKSKVSR DNGTRQSSNP SSGSAHEKEY DSMDEEDCRH 1390 1400 1410 1420 1430 1440 TMSAIRTSLK RLRRGGKSLD RKEWAKILKT ELTTIGNHIE SQKGSSRKAS PEKYRKHLWS 1450 1460 YSANFWPADV KSTKLMAMYD KITESQKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Expanded lysine acetylation specificity of Gcn5 in native complexes." Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L. J. Biol. Chem. 274:5895-5900(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
[4]	"The chromo domain protein chd1p from budding yeast is an ATP-dependent chromatin-modifying factor." Tran H.G., Steger D.J., Iyer V.R., Johnson A.D. EMBO J. 19:2323-2331(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach." Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A., Shilatifard A., Buratowski S., Greenblatt J.F. Mol. Cell. Biol. 22:6979-6992(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH POB3 AND SPT16.
[6]	"The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway." Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L., Cook R.G., Workman J.L., Yates J.R. III, Grant P.A. Mol. Cell. Biol. 22:8774-8786(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
[7]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-987 AND SER-989, MASS SPECTROMETRY. Strain: 2124.
[8]	"Chromatin remodeling protein Chd1 interacts with transcription elongation factors and localizes to transcribed genes." Simic R., Lindstrom D.L., Tran H.G., Roinick K.L., Costa P.J., Johnson A.D., Hartzog G.A., Arndt K.M. EMBO J. 22:1846-1856(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RTF1 AND SPT5.
[9]	"Replication-independent assembly of nucleosome arrays in a novel yeast chromatin reconstitution system involves antisilencing factor Asf1p and chromodomain protein Chd1p." Robinson K.M., Schultz M.C. Mol. Cell. Biol. 23:7937-7946(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1144, MASS SPECTROMETRY. Strain: SUB592.
[12]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1341, MASS SPECTROMETRY. Strain: YAL6B.
[13]	"Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation." Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A. Nature 433:434-438(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE SAGA COMPLEX, IDENTIFICATION IN THE SLIK COMPLEX, FUNCTION IN SUBSTRATE RECOGNITION OF THE SLIK COMPLEX, INTERACTION WITH HISTONE H3, MUTAGENESIS OF GLU-220; HIS-222; LEU-314 AND TYR-316.
[14]	"Analysis of nucleosome repositioning by yeast ISWI and Chd1 chromatin remodeling complexes." Stockdale C., Flaus A., Ferreira H., Owen-Hughes T. J. Biol. Chem. 281:16279-16288(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"The ISWI and CHD1 chromatin remodelling activities influence ADH2 expression and chromatin organization." Xella B., Goding C., Agricola E., Di Mauro E., Caserta M. Mol. Microbiol. 59:1531-1541(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"Histone modifications influence the action of Snf2 family remodelling enzymes by different mechanisms." Ferreira H., Flaus A., Owen-Hughes T. J. Mol. Biol. 374:563-579(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[17]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY. Strain: ADR376.
[18]	"Rtf1 is a multifunctional component of the Paf1 complex that regulates gene expression by directing cotranscriptional histone modification." Warner M.H., Roinick K.L., Arndt K.M. Mol. Cell. Biol. 27:6103-6115(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RTF1.
[19]	"Chd1 and yFACT act in opposition in regulating transcription." Biswas D., Dutta-Biswas R., Stillman D.J. Mol. Cell. Biol. 27:6279-6287(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"RNA polymerase I in yeast transcribes dynamic nucleosomal rDNA." Jones H.S., Kawauchi J., Braglia P., Alen C.M., Kent N.A., Proudfoot N.J. Nat. Struct. Mol. Biol. 14:123-130(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH RDNA, FUNCTION.
[21]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358 AND SER-1364, MASS SPECTROMETRY.
[22]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-987; SER-989; THR-1302; SER-1336 AND SER-1372, MASS SPECTROMETRY.
[23]	"A role for Chd1 and Set2 in negatively regulating DNA replication in Saccharomyces cerevisiae." Biswas D., Takahata S., Xin H., Dutta-Biswas R., Yu Y., Formosa T., Stillman D.J. Genetics 178:649-659(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[24]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-904; SER-987; SER-989; SER-1272; SER-1300; THR-1302; SER-1336 AND SER-1372, MASS SPECTROMETRY.
[25]	"Molecular architecture of the S. cerevisiae SAGA complex." Wu P.Y., Ruhlmann C., Winston F., Schultz P. Mol. Cell 15:199-208(2004) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
[26]	"Structural polymorphism of chromodomains in Chd1." Okuda M., Horikoshi M., Nishimura Y. J. Mol. Biol. 365:1047-1062(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 172-252, DOMAIN.
[27]	"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: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 174-339, DOMAIN, INTERACTION WITH HISTONE H3K4ME3, MUTAGENESIS OF GLU-220.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U18917 Genomic DNA. Translation: AAB64691.1.
BK006939 Genomic DNA. Translation: DAA07826.1.

PIR

S30818.

RefSeq

NP_011091.1. NM_001179054.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DY7	NMR	-	A	172-252	[»]
2DY8	NMR	-	A	279-347	[»]
2H1E	X-ray	2.20	A/B	174-339	[»]
2XB0	X-ray	2.00	X	1009-1274	[»]
3MWY	X-ray	3.70	W	142-939	[»]
3TED	X-ray	2.00	A	1006-1274	[»]

ProteinModelPortal

P32657.

SMR

P32657. Positions 175-922, 1006-1266.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6362N.

IntAct

P32657. 37 interactions.

MINT

MINT-618890.

STRING

4932.YER164W.

Proteomic databases

PaxDb

P32657.

PeptideAtlas

P32657.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YER164W; YER164W; YER164W.

GeneID

856911.

KEGG

sce:YER164W.

Organism-specific databases

CYGD

YER164w.

SGD

S000000966. CHD1.

Phylogenomic databases

eggNOG

COG0553.

GeneTree

ENSGT00560000076896.

HOGENOM

HOG000207917.

KO

K11367.

OMA

IKWQFMA.

OrthoDB

EOG4TF3TB.

Enzyme and pathway databases

SABIO-RK

P32657.

Gene expression databases

Genevestigator

P32657.

GermOnline

YER164W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.10.10.60. 1 hit.

InterPro

IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR025260. DUF4208.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR009057. Homeodomain-like.
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.
SSF46689. Homeodomain_like. 1 hit.

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

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Other

EvolutionaryTrace

P32657.

NextBio

983353.

Entry information

Entry name

CHD1_YEAST

Accession

Primary (citable) accession number: P32657
Secondary accession number(s): D3DM72

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program