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P53125

- ITC1_YEAST

UniProt

P53125 - ITC1_YEAST

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Protein

Imitation switch two complex protein 1

Gene
ITC1, YGL133W, G2842
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Functions as component of the ISW2 complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. THe ISW2 complex is involved in coordinating transcriptional repression and in inheritance of telomeric silencing. It is involved in repression of MAT a-specific genes, INO1, and early meiotic genes during mitotic growth dependent upon transcription factor UME6 and in a parallel pathway to the RPD3-SIN3 histone deacetylase complex. ITC1 is required for nucleosome-stimulated ATPase activity and chromatin-remodeling activity of the complex. Required for the repression of MATa a-specific genes.6 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. chromatin remodeling Source: SGD
  2. chromatin silencing at telomere Source: SGD
  3. negative regulation of transcription from RNA polymerase II promoter by pheromones Source: SGD
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-30628-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Imitation switch two complex protein 1
Gene namesi
Name:ITC1
Ordered Locus Names:YGL133W
ORF Names:G2842
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGL133w.
SGDiS000003101. ITC1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. CHRAC Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12641264Imitation switch two complex protein 1PRO_0000084270Add
BLAST

Proteomic databases

MaxQBiP53125.
PaxDbiP53125.
PeptideAtlasiP53125.

Expressioni

Gene expression databases

GenevestigatoriP53125.

Interactioni

Subunit structurei

Component of the ISW2 complex, which at least consists of ISW2, ITC1, DLS1 and DPB4. May form a stable subcomplex with ISW2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ISW2Q087733EBI-23967,EBI-31118

Protein-protein interaction databases

BioGridi33119. 140 interactions.
DIPiDIP-6737N.
IntActiP53125. 36 interactions.
MINTiMINT-469555.
STRINGi4932.YGL133W.

Structurei

3D structure databases

ProteinModelPortaliP53125.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 130108WACAdd
BLAST
Domaini423 – 48361DDTAdd
BLAST

Sequence similaritiesi

Contains 1 DDT domain.
Contains 1 WAC domain.

Phylogenomic databases

eggNOGiNOG302161.
GeneTreeiENSGT00530000066815.
HOGENOMiHOG000065973.
OMAiQIYRDRS.
OrthoDBiEOG7TTQHC.

Family and domain databases

InterProiIPR004022. DDT_dom.
IPR018500. DDT_dom_subgr.
IPR018501. DDT_dom_superfamily.
IPR028941. WHIM2_dom.
IPR013136. WSTF_Acf1_Cbp146.
[Graphical view]
PfamiPF02791. DDT. 1 hit.
PF10537. WAC_Acf1_DNA_bd. 1 hit.
PF15613. WHIM2. 1 hit.
[Graphical view]
SMARTiSM00571. DDT. 1 hit.
[Graphical view]
PROSITEiPS50827. DDT. 1 hit.
PS51136. WAC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53125-1 [UniParc]FASTAAdd to Basket

« Hide

MVLYKRKPIL LPDPKPLPLD LNVQVWHIEE TGEWFSSYEE FLERFDFYTR     50
HHFTCEITGT SCLTFFQALD SEETQFKYVE DRFPLKLREP VARFLHFNGI 100
RRLDALVEKV YARFKNDFFP GEVVYLRKQK DSSTTSSNSQ QSTPQPDDMV 150
EINSVGNPGL PQYQYQRRYV IKEKVQFNAT INPESREIVM PAHTKYMLIE 200
EAASSNKSFI VDQGQIYRDR STFTKHLIKC FFKITLQRAS SKMGAPWCVK 250
PEYLAMYGLT MEWPKDMLKY KEDEPVVARR SNSANVSSPE SEKNKRQSKS 300
SGKSNTSNDA SNKKETKKKR KPTEVNDSEN NSSEEDKKKG QNVTSETHSK 350
KRKKEANEEP NTENVESVPT PANAEPQAVT ITSIMDDLAL PYQHPPNIFP 400
NLTYYNEKLE CISLGSTKLS RPFDSFGKLL QAYQFLNTFG SKICLSHFSL 450
DQFITSLKCT DPYELKGEVV LVNIRTQTSK EQEIENNGLP MKNKAETTTE 500
EDSENPSDWQ RNSFIRDMIM KRNSDKVEYK IVHDDPASDD ILDNINHNGS 550
ALLIEVFTAL LRLFINEEGD WSCIVVENWI IDDKGVLMER KDERGEGEAK 600
QKRNAHGYFL QDKEKIDNLK DTLKENATEV QKESDAKNET NSESDSKSDS 650
DSEERDPKLE KCLNYRNVNW IERLTKRQFN NSYWLIILLG VLEDCRHLPM 700
YTEFIDSFIE KIIPKDISAT QLPKQLWRNF CRKLSFSDKV NALWILVDLV 750
SHFSPDIKAA VDDSMELCGQ IRSERFKVAR ELKTEAAVLS NLQGDLQAIQ 800
EKLNKTDENT PSADGADKKD DSESNSEPID LIIIEKKQKL IEEQDKKVQA 850
LQSDKNFLDN CLFENDLQRL KPLGLDRYGN RYFWLDHNGV PFPQYPAGMN 900
ETPKSNNSLS YHSGRLLIQG PKASSAKFFL NVSDEQLSNW QKIRNSEGIS 950
EATREVFGIS KTSSGSYNYV ENGIEVELLD SNDRVNPLIE LTPIQKKIMD 1000
ETPSRLLLSP DQWYCIDKLE DLSRIMDWLD NWGRKEHDLL RQIRPIMERI 1050
KSSLSLRDHA LSLTAFTKNE EKLLKELENN EFTENELNVD SMDVDDKNSG 1100
VKSEVDVQVD AEEKREAVID EKLEVIADEL MKLDDSSKTR NVLNRIQELE 1150
DQRDELLEQK KSIINSQRPG ARILARSERK RTKISRGNKV NKQIEILTDL 1200
VNYRHFKAME DVIAWKNVLA NSIWGSSLRK NASGNKRSGV IETVDDKLKD 1250
IVGQTSRTVT PAPN 1264
Length:1,264
Mass (Da):145,643
Last modified:October 1, 1996 - v1
Checksum:i45E4CF8835C7C746
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z72655 Genomic DNA. Translation: CAA96844.1.
BK006941 Genomic DNA. Translation: DAA07977.1.
PIRiS64146.
RefSeqiNP_011382.1. NM_001180998.1.

Genome annotation databases

EnsemblFungiiYGL133W; YGL133W; YGL133W.
GeneIDi852744.
KEGGisce:YGL133W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z72655 Genomic DNA. Translation: CAA96844.1 .
BK006941 Genomic DNA. Translation: DAA07977.1 .
PIRi S64146.
RefSeqi NP_011382.1. NM_001180998.1.

3D structure databases

ProteinModelPortali P53125.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33119. 140 interactions.
DIPi DIP-6737N.
IntActi P53125. 36 interactions.
MINTi MINT-469555.
STRINGi 4932.YGL133W.

Proteomic databases

MaxQBi P53125.
PaxDbi P53125.
PeptideAtlasi P53125.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL133W ; YGL133W ; YGL133W .
GeneIDi 852744.
KEGGi sce:YGL133W.

Organism-specific databases

CYGDi YGL133w.
SGDi S000003101. ITC1.

Phylogenomic databases

eggNOGi NOG302161.
GeneTreei ENSGT00530000066815.
HOGENOMi HOG000065973.
OMAi QIYRDRS.
OrthoDBi EOG7TTQHC.

Enzyme and pathway databases

BioCyci YEAST:G3O-30628-MONOMER.

Miscellaneous databases

NextBioi 972165.

Gene expression databases

Genevestigatori P53125.

Family and domain databases

InterProi IPR004022. DDT_dom.
IPR018500. DDT_dom_subgr.
IPR018501. DDT_dom_superfamily.
IPR028941. WHIM2_dom.
IPR013136. WSTF_Acf1_Cbp146.
[Graphical view ]
Pfami PF02791. DDT. 1 hit.
PF10537. WAC_Acf1_DNA_bd. 1 hit.
PF15613. WHIM2. 1 hit.
[Graphical view ]
SMARTi SM00571. DDT. 1 hit.
[Graphical view ]
PROSITEi PS50827. DDT. 1 hit.
PS51136. WAC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a 14.6 kb DNA fragment of Saccharomyces cerevisiae chromosome VII reveals SEC27, SSM1b, a putative S-adenosylmethionine-dependent enzyme and six new open reading frames."
    Escribano V., Eraso P., Portillo F., Mazon M.J.
    Yeast 12:887-892(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(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. "The Isw2 chromatin remodeling complex represses early meiotic genes upon recruitment by Ume6p."
    Goldmark J.P., Fazzio T.G., Estep P.W., Church G.M., Tsukiyama T.
    Cell 103:423-433(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE ISW2 COMPLEX.
  5. "The Saccharomyces cerevisiae Isw2p-Itc1p complex represses INO1 expression and maintains cell morphology."
    Sugiyama M., Nikawa J.
    J. Bacteriol. 183:4985-4993(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Interactions of Isw2 chromatin remodeling complex with nucleosomal arrays: analyses using recombinant yeast histones and immobilized templates."
    Gelbart M.E., Rechsteiner T., Richmond T.J., Tsukiyama T.
    Mol. Cell. Biol. 21:2098-2106(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE ISW2 COMPLEX, INTERACTION WITH ISW2, SUBCELLULAR LOCATION.
  7. "Widespread collaboration of Isw2 and Sin3-Rpd3 chromatin remodeling complexes in transcriptional repression."
    Fazzio T.G., Kooperberg C., Goldmark J.P., Neal C., Basom R., Delrow J., Tsukiyama T.
    Mol. Cell. Biol. 21:6450-6460(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE ISW2 COMPLEX.
  8. "Cell-type-dependent repression of yeast a-specific genes requires Itc1p, a subunit of the Isw2p-Itc1p chromatin remodelling complex."
    Ruiz C., Escribano V., Morgado E., Molina M., Mazon M.J.
    Microbiology 149:341-351(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Noncompetitive counteractions of DNA polymerase epsilon and ISW2/yCHRAC for epigenetic inheritance of telomere position effect in Saccharomyces cerevisiae."
    Iida T., Araki H.
    Mol. Cell. Biol. 24:217-227(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ISW2 COMPLEX, FUNCTION OF THE ISW2 COMPLEX.
  11. "Histone fold protein Dls1p is required for Isw2-dependent chromatin remodeling in vivo."
    McConnell A.D., Gelbart M.E., Tsukiyama T.
    Mol. Cell. Biol. 24:2605-2613(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ISW2 COMPLEX.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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].

Entry informationi

Entry nameiITC1_YEAST
AccessioniPrimary (citable) accession number: P53125
Secondary accession number(s): D6VU16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 114 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 2610 molecules/cell in log phase SD medium.

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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

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