Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P32657

- CHD1_YEAST

UniProt

P32657 - CHD1_YEAST

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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.
    GeneTreeiENSGT00560000076896.
    HOGENOMiHOG000207917.
    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

    MAAKDISTEV LQNPELYGLR RSHRAAAHQQ NYFNDSDDED DEDNIKQSRR     50
    KRMTTIEDDE DEFEDEEGEE DSGEDEDEED FEEDDDYYGS PIKQNRSKPK 100
    SRTKSKSKSK PKSQSEKQST VKIPTRFSNR QNKTVNYNID YSDDDLLESE 150
    DDYGSEEALS EENVHEASAN PQPEDFHGID IVINHRLKTS LEEGKVLEKT 200
    VPDLNNCKEN YEFLIKWTDE SHLHNTWETY ESIGQVRGLK RLDNYCKQFI 250
    IEDQQVRLDP YVTAEDIEIM DMERERRLDE FEEFHVPERI IDSQRASLED 300
    GTSQLQYLVK WRRLNYDEAT WENATDIVKL APEQVKHFQN RENSKILPQY 350
    SSNYTSQRPR FEKLSVQPPF IKGGELRDFQ LTGINWMAFL WSKGDNGILA 400
    DEMGLGKTVQ TVAFISWLIF ARRQNGPHII VVPLSTMPAW LDTFEKWAPD 450
    LNCICYMGNQ KSRDTIREYE FYTNPRAKGK KTMKFNVLLT TYEYILKDRA 500
    ELGSIKWQFM AVDEAHRLKN AESSLYESLN SFKVANRMLI TGTPLQNNIK 550
    ELAALVNFLM PGRFTIDQEI DFENQDEEQE EYIHDLHRRI QPFILRRLKK 600
    DVEKSLPSKT ERILRVELSD VQTEYYKNIL TKNYSALTAG AKGGHFSLLN 650
    IMNELKKASN HPYLFDNAEE RVLQKFGDGK MTRENVLRGL IMSSGKMVLL 700
    DQLLTRLKKD GHRVLIFSQM VRMLDILGDY LSIKGINFQR LDGTVPSAQR 750
    RISIDHFNSP DSNDFVFLLS TRAGGLGINL MTADTVVIFD SDWNPQADLQ 800
    AMARAHRIGQ KNHVMVYRLV SKDTVEEEVL ERARKKMILE YAIISLGVTD 850
    GNKYTKKNEP NAGELSAILK FGAGNMFTAT DNQKKLEDLN LDDVLNHAED 900
    HVTTPDLGES HLGGEEFLKQ FEVTDYKADI DWDDIIPEEE LKKLQDEEQK 950
    RKDEEYVKEQ LEMMNRRDNA LKKIKNSVNG DGTAANSDSD DDSTSRSSRR 1000
    RARANDMDSI GESEVRALYK AILKFGNLKE ILDELIADGT LPVKSFEKYG 1050
    ETYDEMMEAA KDCVHEEEKN RKEILEKLEK HATAYRAKLK SGEIKAENQP 1100
    KDNPLTRLSL KKREKKAVLF NFKGVKSLNA ESLLSRVEDL KYLKNLINSN 1150
    YKDDPLKFSL GNNTPKPVQN WSSNWTKEED EKLLIGVFKY GYGSWTQIRD 1200
    DPFLGITDKI FLNEVHNPVA KKSASSSDTT PTPSKKGKGI TGSSKKVPGA 1250
    IHLGRRVDYL LSFLRGGLNT KSPSADIGSK KLPTGPSKKR QRKPANHSKS 1300
    MTPEITSSEP ANGPPSKRMK ALPKGPAALI NNTRLSPNSP TPPLKSKVSR 1350
    DNGTRQSSNP SSGSAHEKEY DSMDEEDCRH TMSAIRTSLK RLRRGGKSLD 1400
    RKEWAKILKT ELTTIGNHIE SQKGSSRKAS PEKYRKHLWS YSANFWPADV 1450
    KSTKLMAMYD KITESQKK 1468
    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 ENSGT00560000076896.
    HOGENOMi HOG000207917.
    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

    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 1, 2014
    This is version 149 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