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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: 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

    • ATP binding Source: UniProtKB-KW
    • chromatin DNA binding Source: SGD
    • DNA binding Source: SGD
    • DNA-dependent ATPase activity Source: SGD
    • helicase activity Source: UniProtKB-KW
    • methylated histone binding Source: SGD
    • nucleosome-dependent ATPase activity Source: SGD
    • rDNA binding Source: SGD

    GO - Biological processi

    • ATP-dependent chromatin remodeling Source: SGD
    • histone H2B conserved C-terminal lysine ubiquitination Source: SGD
    • negative regulation of DNA-dependent DNA replication Source: SGD
    • negative regulation of histone exchange Source: SGD
    • negative regulation of histone H3-K14 acetylation Source: SGD
    • negative regulation of histone H3-K9 acetylation Source: SGD
    • nucleosome mobilization Source: SGD
    • nucleosome organization Source: SGD
    • nucleosome positioning Source: SGD
    • regulation of chromatin organization Source: SGD
    • regulation of nucleosome density Source: SGD
    • regulation of transcriptional start site selection at RNA polymerase II promoter Source: SGD
    • termination of RNA polymerase II transcription Source: SGD
    • termination of RNA polymerase I transcription Source: SGD
    • 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 Componenti: Chromosome V

    Organism-specific databases

    CYGDiYER164w.
    EuPathDBiFungiDB:YER164W.
    SGDiS000000966. CHD1.

    Subcellular locationi

    GO - Cellular componenti

    • nuclear chromatin Source: SGD
    • nucleolar chromatin Source: SGD
    • SAGA complex Source: SGD
    • 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. 230 interactions.
    DIPiDIP-6362N.
    IntActiP32657. 39 interactions.
    MINTiMINT-618890.
    STRINGi4932.YER164W.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    OMAiMVHMLDI.
    OrthoDBiEOG7M98QM.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR000953. Chromo/shadow_dom.
    IPR023780. Chromo_domain.
    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:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U18917 Genomic DNA. Translation: AAB64691.1.
    BK006939 Genomic DNA. Translation: DAA07826.1.
    PIRiS30818.
    RefSeqiNP_011091.1. NM_001179054.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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...

    Protein-protein interaction databases

    BioGridi36917. 230 interactions.
    DIPiDIP-6362N.
    IntActiP32657. 39 interactions.
    MINTiMINT-618890.
    STRINGi4932.YER164W.

    Proteomic databases

    MaxQBiP32657.
    PaxDbiP32657.
    PeptideAtlasiP32657.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CYGDiYER164w.
    EuPathDBiFungiDB:YER164W.
    SGDiS000000966. CHD1.

    Phylogenomic databases

    eggNOGiCOG0553.
    GeneTreeiENSGT00760000119067.
    HOGENOMiHOG000207917.
    InParanoidiP32657.
    KOiK11367.
    OMAiMVHMLDI.
    OrthoDBiEOG7M98QM.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiP32657.
    NextBioi983353.
    PROiP32657.

    Gene expression databases

    GenevestigatoriP32657.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR000953. Chromo/shadow_dom.
    IPR023780. Chromo_domain.
    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]
    ProtoNetiSearch...

    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: April 29, 2015
    This is version 156 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.