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P32657

- CHD1_YEAST

UniProt

P32657 - CHD1_YEAST

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Protein

Chromo domain-containing protein 1

Gene

CHD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.11 Publications

Kineticsi

  1. KM=10.2 nM for ATP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi401 – 4088ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. chromatin DNA binding Source: SGD
  3. DNA binding Source: SGD
  4. DNA-dependent ATPase activity Source: SGD
  5. helicase activity Source: UniProtKB-KW
  6. methylated histone binding Source: SGD
  7. nucleosome-dependent ATPase activity Source: SGD
  8. rDNA binding Source: SGD

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. ATP-dependent chromatin remodeling Source: SGD
  3. histone H2B conserved C-terminal lysine ubiquitination Source: SGD
  4. negative regulation of DNA-dependent DNA replication Source: SGD
  5. negative regulation of histone exchange Source: SGD
  6. negative regulation of histone H3-K14 acetylation Source: SGD
  7. negative regulation of histone H3-K9 acetylation Source: SGD
  8. nucleosome mobilization Source: SGD
  9. nucleosome positioning Source: SGD
  10. regulation of chromatin organization Source: SGD
  11. regulation of transcriptional start site selection at RNA polymerase II promoter Source: SGD
  12. regulation of transcription by chromatin organization Source: SGD
  13. termination of RNA polymerase II transcription Source: SGD
  14. termination of RNA polymerase I transcription Source: SGD
  15. transcription elongation from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30325-MONOMER.
SABIO-RKP32657.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromo domain-containing protein 1 (EC:3.6.4.-)
Alternative name(s):
ATP-dependent helicase CHD1
Gene namesi
Name:CHD1
Ordered Locus Names:YER164W
ORF Names:SYGP-ORF4
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome V

Organism-specific databases

CYGDiYER164w.
SGDiS000000966. CHD1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nuclear chromatin Source: SGD
  2. nucleolar chromatin Source: SGD
  3. SAGA complex Source: SGD
  4. SLIK (SAGA-like) complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi220 – 2201E → L or W: No interaction with methylated histone H3 'K-4'. 2 Publications
Mutagenesisi222 – 2221H → Y: Confers interaction with methylated histone H3 'K-4'. 1 Publication
Mutagenesisi314 – 3141L → Y: No effect on interaction with methylated histone H3 'K-4'. 1 Publication
Mutagenesisi316 – 3161Y → E: Disrupts interaction with methylated histone H3 'K-4'; abrogates histone acetylation activity of SLIK. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14681468Chromo domain-containing protein 1PRO_0000080237Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361Phosphoserine3 Publications
Modified residuei72 – 721Phosphoserine1 Publication
Modified residuei987 – 9871Phosphoserine2 Publications
Modified residuei989 – 9891Phosphoserine2 Publications
Cross-linki1144 – 1144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei1336 – 13361Phosphoserine2 Publications
Modified residuei1364 – 13641Phosphoserine1 Publication
Modified residuei1372 – 13721Phosphoserine1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP32657.
PaxDbiP32657.
PeptideAtlasiP32657.

Expressioni

Gene expression databases

GenevestigatoriP32657.

Interactioni

Subunit structurei

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 SPT16.6 Publications

Protein-protein interaction databases

BioGridi36917. 227 interactions.
DIPiDIP-6362N.
IntActiP32657. 38 interactions.
MINTiMINT-618890.
STRINGi4932.YER164W.

Structurei

Secondary structure

1
1468
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi179 – 1879
Turni190 – 1923
Helixi193 – 1964
Helixi204 – 2107
Beta strandi211 – 2177
Helixi222 – 2243
Beta strandi226 – 2283
Helixi230 – 2334
Beta strandi234 – 2374
Helixi239 – 24911
Helixi251 – 2588
Helixi264 – 28320
Beta strandi286 – 29712
Beta strandi299 – 3013
Beta strandi303 – 3119
Beta strandi320 – 3234
Helixi324 – 3307
Helixi332 – 3387
Helixi1012 – 102514
Helixi1029 – 10313
Helixi1032 – 10376
Helixi1046 – 109146
Beta strandi1092 – 10943
Beta strandi1096 – 10983
Beta strandi1101 – 11033
Helixi1104 – 11129
Beta strandi1119 – 11224
Beta strandi1125 – 11295
Helixi1130 – 115021
Helixi1155 – 11573
Beta strandi1171 – 11733
Helixi1177 – 119014
Helixi1195 – 12006
Turni1202 – 12043
Helixi1207 – 12093
Helixi1250 – 126415
Turni1265 – 12684

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DY7NMR-A172-252[»]
2DY8NMR-A279-347[»]
2H1EX-ray2.20A/B174-339[»]
2XB0X-ray2.00X1009-1274[»]
3MWYX-ray3.70W142-939[»]
3TEDX-ray2.00A1006-1274[»]
ProteinModelPortaliP32657.
SMRiP32657. Positions 175-922, 1006-1266.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32657.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini195 – 25763Chromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini285 – 35066Chromo 2PROSITE-ProRule annotationAdd
BLAST
Domaini388 – 562175Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini699 – 860162Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi513 – 5164DEAH box

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 2 chromo domains.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000207917.
InParanoidiP32657.
KOiK11367.
OMAiYTDVKLD.
OrthoDBiEOG7M98QM.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR025260. DUF4208.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR009057. Homeodomain-like.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamiPF00385. Chromo. 2 hits.
PF13907. DUF4208. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 2 hits.
PROSITEiPS00598. CHROMO_1. 2 hits.
PS50013. CHROMO_2. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32657-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAKDISTEV LQNPELYGLR RSHRAAAHQQ NYFNDSDDED DEDNIKQSRR
60 70 80 90 100
KRMTTIEDDE DEFEDEEGEE DSGEDEDEED FEEDDDYYGS PIKQNRSKPK
110 120 130 140 150
SRTKSKSKSK PKSQSEKQST VKIPTRFSNR QNKTVNYNID YSDDDLLESE
160 170 180 190 200
DDYGSEEALS EENVHEASAN PQPEDFHGID IVINHRLKTS LEEGKVLEKT
210 220 230 240 250
VPDLNNCKEN YEFLIKWTDE SHLHNTWETY ESIGQVRGLK RLDNYCKQFI
260 270 280 290 300
IEDQQVRLDP YVTAEDIEIM DMERERRLDE FEEFHVPERI IDSQRASLED
310 320 330 340 350
GTSQLQYLVK WRRLNYDEAT WENATDIVKL APEQVKHFQN RENSKILPQY
360 370 380 390 400
SSNYTSQRPR FEKLSVQPPF IKGGELRDFQ LTGINWMAFL WSKGDNGILA
410 420 430 440 450
DEMGLGKTVQ TVAFISWLIF ARRQNGPHII VVPLSTMPAW LDTFEKWAPD
460 470 480 490 500
LNCICYMGNQ KSRDTIREYE FYTNPRAKGK KTMKFNVLLT TYEYILKDRA
510 520 530 540 550
ELGSIKWQFM AVDEAHRLKN AESSLYESLN SFKVANRMLI TGTPLQNNIK
560 570 580 590 600
ELAALVNFLM PGRFTIDQEI DFENQDEEQE EYIHDLHRRI QPFILRRLKK
610 620 630 640 650
DVEKSLPSKT ERILRVELSD VQTEYYKNIL TKNYSALTAG AKGGHFSLLN
660 670 680 690 700
IMNELKKASN HPYLFDNAEE RVLQKFGDGK MTRENVLRGL IMSSGKMVLL
710 720 730 740 750
DQLLTRLKKD GHRVLIFSQM VRMLDILGDY LSIKGINFQR LDGTVPSAQR
760 770 780 790 800
RISIDHFNSP DSNDFVFLLS TRAGGLGINL MTADTVVIFD SDWNPQADLQ
810 820 830 840 850
AMARAHRIGQ KNHVMVYRLV SKDTVEEEVL ERARKKMILE YAIISLGVTD
860 870 880 890 900
GNKYTKKNEP NAGELSAILK FGAGNMFTAT DNQKKLEDLN LDDVLNHAED
910 920 930 940 950
HVTTPDLGES HLGGEEFLKQ FEVTDYKADI DWDDIIPEEE LKKLQDEEQK
960 970 980 990 1000
RKDEEYVKEQ LEMMNRRDNA LKKIKNSVNG DGTAANSDSD DDSTSRSSRR
1010 1020 1030 1040 1050
RARANDMDSI GESEVRALYK AILKFGNLKE ILDELIADGT LPVKSFEKYG
1060 1070 1080 1090 1100
ETYDEMMEAA KDCVHEEEKN RKEILEKLEK HATAYRAKLK SGEIKAENQP
1110 1120 1130 1140 1150
KDNPLTRLSL KKREKKAVLF NFKGVKSLNA ESLLSRVEDL KYLKNLINSN
1160 1170 1180 1190 1200
YKDDPLKFSL GNNTPKPVQN WSSNWTKEED EKLLIGVFKY GYGSWTQIRD
1210 1220 1230 1240 1250
DPFLGITDKI FLNEVHNPVA KKSASSSDTT PTPSKKGKGI TGSSKKVPGA
1260 1270 1280 1290 1300
IHLGRRVDYL LSFLRGGLNT KSPSADIGSK KLPTGPSKKR QRKPANHSKS
1310 1320 1330 1340 1350
MTPEITSSEP ANGPPSKRMK ALPKGPAALI NNTRLSPNSP TPPLKSKVSR
1360 1370 1380 1390 1400
DNGTRQSSNP SSGSAHEKEY DSMDEEDCRH TMSAIRTSLK RLRRGGKSLD
1410 1420 1430 1440 1450
RKEWAKILKT ELTTIGNHIE SQKGSSRKAS PEKYRKHLWS YSANFWPADV
1460
KSTKLMAMYD KITESQKK
Length:1,468
Mass (Da):168,241
Last modified:October 1, 1993 - v1
Checksum:i78BDB74C7FEC6BE5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U18917 Genomic DNA. Translation: AAB64691.1.
BK006939 Genomic DNA. Translation: DAA07826.1.
PIRiS30818.
RefSeqiNP_011091.1. NM_001179054.1.

Genome annotation databases

EnsemblFungiiYER164W; YER164W; YER164W.
GeneIDi856911.
KEGGisce:YER164W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U18917 Genomic DNA. Translation: AAB64691.1 .
BK006939 Genomic DNA. Translation: DAA07826.1 .
PIRi S30818.
RefSeqi NP_011091.1. NM_001179054.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P32657.
SMRi P32657. Positions 175-922, 1006-1266.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36917. 227 interactions.
DIPi DIP-6362N.
IntActi P32657. 38 interactions.
MINTi MINT-618890.
STRINGi 4932.YER164W.

Proteomic databases

MaxQBi P32657.
PaxDbi P32657.
PeptideAtlasi P32657.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YER164W ; YER164W ; YER164W .
GeneIDi 856911.
KEGGi sce:YER164W.

Organism-specific databases

CYGDi YER164w.
SGDi S000000966. CHD1.

Phylogenomic databases

eggNOGi COG0553.
GeneTreei ENSGT00760000119067.
HOGENOMi HOG000207917.
InParanoidi P32657.
KOi K11367.
OMAi YTDVKLD.
OrthoDBi EOG7M98QM.

Enzyme and pathway databases

BioCyci YEAST:G3O-30325-MONOMER.
SABIO-RK P32657.

Miscellaneous databases

EvolutionaryTracei P32657.
NextBioi 983353.
PROi P32657.

Gene expression databases

Genevestigatori P32657.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
3.40.50.300. 2 hits.
InterProi 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.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view ]
Pfami PF00385. Chromo. 2 hits.
PF13907. DUF4208. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view ]
SMARTi SM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 2 hits.
PROSITEi PS00598. CHROMO_1. 2 hits.
PS50013. CHROMO_2. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. 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. "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.
  8. "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.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1144.
    Strain: SUB592.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  16. "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.
  17. "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.
  18. Cited for: ASSOCIATION WITH RDNA, FUNCTION.
  19. "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-1364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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.
  21. "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; SER-987; SER-989; SER-1336 AND SER-1372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-72; SER-987; SER-989 AND SER-1336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "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.
  25. "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.
  26. "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.

Entry informationi

Entry nameiCHD1_YEAST
AccessioniPrimary (citable) accession number: P32657
Secondary accession number(s): D3DM72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 29, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1620 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3