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Protein

Activatory protein CHA4

Gene

CHA4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Activates the CHA1 gene for L-serine dehydratase. Binds to the DNA sequence 5'-GVGGARAYRTRATTCCRC-3'.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi44 – 7027Zn(2)-C6 fungal-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cellular amino acid catabolic process Source: SGD
  • positive regulation of transcription, DNA-templated Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-32248-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Activatory protein CHA4
Gene namesi
Name:CHA4
Synonyms:SIL2, SIL3
Ordered Locus Names:YLR098C
ORF Names:L8004.8
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR098c.
EuPathDBiFungiDB:YLR098C.
SGDiS000004088. CHA4.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 648648Activatory protein CHA4PRO_0000114942Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei164 – 1641Phosphoserine2 Publications
Modified residuei166 – 1661Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP43634.
PaxDbiP43634.

Interactioni

Protein-protein interaction databases

BioGridi31371. 77 interactions.
DIPiDIP-1798N.
IntActiP43634. 10 interactions.
MINTiMINT-397314.
STRINGi4932.YLR098C.

Structurei

3D structure databases

ProteinModelPortaliP43634.
SMRiP43634. Positions 42-73.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi32 – 354Poly-Asn
Compositional biasi48 – 525Poly-Arg
Compositional biasi105 – 1095Poly-Ser
Compositional biasi195 – 1984Poly-Gln
Compositional biasi302 – 3065Poly-Ser

Sequence similaritiesi

Contains 1 Zn(2)-C6 fungal-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG75868.
GeneTreeiENSGT00530000067248.
HOGENOMiHOG000074724.
InParanoidiP43634.
OMAiMAWYLSG.
OrthoDBiEOG7Q5HPH.

Family and domain databases

Gene3Di4.10.240.10. 1 hit.
InterProiIPR007219. Transcription_factor_dom_fun.
IPR001138. Zn2-C6_fun-type_DNA-bd.
[Graphical view]
PfamiPF04082. Fungal_trans. 1 hit.
PF00172. Zn_clus. 1 hit.
[Graphical view]
SMARTiSM00906. Fungal_trans. 1 hit.
SM00066. GAL4. 1 hit.
[Graphical view]
SUPFAMiSSF57701. SSF57701. 1 hit.
PROSITEiPS00463. ZN2_CY6_FUNGAL_1. 1 hit.
PS50048. ZN2_CY6_FUNGAL_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P43634-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMLEPSPPPL TTTVTPSLPS SLKKSVTDND QNNNNVPRKR KLACQNCRRR
60 70 80 90 100
RRKCNMEKPC SNCIKFRTEC VFTQQDLRNK RYSTTYVEAL QSQIRSLKEQ
110 120 130 140 150
LQILSSSSST IASNALSSLK NNSDHGDAPN EKILKYGETA QSALPSSESN
160 170 180 190 200
DENESDAFTK KMPSESPPPV GTNSIYPSNS LSIIKKKTDG STRYQQQQVS
210 220 230 240 250
LKNLSRSPLI LRSLSLFFKW LYPGHYLFIH RETFLSAFFG DTNTKSYYCS
260 270 280 290 300
EELVFAIAAL GSLISYKSET ELFQQSEVFY QRAKTIVLKK IFQLEDSSLA
310 320 330 340 350
ESSSSSKLAI IQTLLCLAFY DIGSGENPMA WYLSGLAFRI AHEIGLHLNP
360 370 380 390 400
EAWSNVYEDE LSIMDFEVRS RIYWGCYIAD HLIAILFGRS TSLRLSNSTV
410 420 430 440 450
PETDELPEIE TGIEEYIYDP KVILSTANPL KKLIVLSRIT EIFASKIFSP
460 470 480 490 500
NETLLQRSEY LAKFNLEVYN WRRDLPPELQ WTKRSLMEMT DFNPTIAYVW
510 520 530 540 550
FHYYIVLISY NKPFIYEIKQ SRELVEGYVD ELYYLLKVWK NKFKTFEKAT
560 570 580 590 600
IYMIYSAILA IQCMKSNLIK KDRKQDFLNF LSAPTLNYEL ARKFIENSED
610 620 630 640
ALHNSETMDL LGTLSHGNDF ALEYNFDFTL LNEIDMLIGG NTNDGLSK
Length:648
Mass (Da):74,393
Last modified:November 1, 1995 - v1
Checksum:iCF3381B4C0356F82
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49975 Genomic DNA. Translation: CAA90276.1.
U53876 Genomic DNA. Translation: AAB67542.1.
Z73270 Genomic DNA. Translation: CAA97662.1.
BK006945 Genomic DNA. Translation: DAA09414.1.
PIRiS59723.
RefSeqiNP_013199.1. NM_001181985.1.

Genome annotation databases

EnsemblFungiiYLR098C; YLR098C; YLR098C.
GeneIDi850787.
KEGGisce:YLR098C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49975 Genomic DNA. Translation: CAA90276.1.
U53876 Genomic DNA. Translation: AAB67542.1.
Z73270 Genomic DNA. Translation: CAA97662.1.
BK006945 Genomic DNA. Translation: DAA09414.1.
PIRiS59723.
RefSeqiNP_013199.1. NM_001181985.1.

3D structure databases

ProteinModelPortaliP43634.
SMRiP43634. Positions 42-73.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31371. 77 interactions.
DIPiDIP-1798N.
IntActiP43634. 10 interactions.
MINTiMINT-397314.
STRINGi4932.YLR098C.

Proteomic databases

MaxQBiP43634.
PaxDbiP43634.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR098C; YLR098C; YLR098C.
GeneIDi850787.
KEGGisce:YLR098C.

Organism-specific databases

CYGDiYLR098c.
EuPathDBiFungiDB:YLR098C.
SGDiS000004088. CHA4.

Phylogenomic databases

eggNOGiNOG75868.
GeneTreeiENSGT00530000067248.
HOGENOMiHOG000074724.
InParanoidiP43634.
OMAiMAWYLSG.
OrthoDBiEOG7Q5HPH.

Enzyme and pathway databases

BioCyciYEAST:G3O-32248-MONOMER.

Miscellaneous databases

NextBioi966987.
PROiP43634.

Family and domain databases

Gene3Di4.10.240.10. 1 hit.
InterProiIPR007219. Transcription_factor_dom_fun.
IPR001138. Zn2-C6_fun-type_DNA-bd.
[Graphical view]
PfamiPF04082. Fungal_trans. 1 hit.
PF00172. Zn_clus. 1 hit.
[Graphical view]
SMARTiSM00906. Fungal_trans. 1 hit.
SM00066. GAL4. 1 hit.
[Graphical view]
SUPFAMiSSF57701. SSF57701. 1 hit.
PROSITEiPS00463. ZN2_CY6_FUNGAL_1. 1 hit.
PS50048. ZN2_CY6_FUNGAL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cha4p of Saccharomyces cerevisiae activates transcription via serine/threonine response elements."
    Holmberg S., Schjerling P.
    Genetics 144:467-478(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "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-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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-164 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCHA4_YEAST
AccessioniPrimary (citable) accession number: P43634
Secondary accession number(s): D6VY98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 24, 2015
This is version 122 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 396 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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