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Protein

Protein SIC1

Gene

SIC1

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

Substrate and inhibitor of the cyclin-dependent protein kinase CDC28. Its activity could be important for faithful segregation of chromosomes to daughter cells. It acts in response to a signal from a post-start checkpoint.1 Publication

GO - Molecular functioni

  1. cyclin-dependent protein serine/threonine kinase inhibitor activity Source: SGD

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: SGD
  2. negative regulation of macroautophagy Source: SGD
  3. negative regulation of protein serine/threonine kinase activity Source: GOC
  4. regulation of cyclin-dependent protein serine/threonine kinase activity Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-32230-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SIC1
Alternative name(s):
CDK inhibitor p40
Gene namesi
Name:SIC1
Synonyms:SDB25
Ordered Locus Names:YLR079W
ORF Names:L9449.8
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

CYGDiYLR079w.
SGDiS000004069. SIC1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi173 – 1731T → A: Impairs the ability to arrest the cell cycle. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Protein SIC1PRO_0000097751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphothreonine; by PHO851 Publication
Modified residuei33 – 331Phosphothreonine1 Publication
Modified residuei76 – 761Phosphoserine1 Publication
Modified residuei173 – 1731Phosphothreonine2 Publications
Modified residuei198 – 1981Phosphoserine2 Publications
Modified residuei201 – 2011Phosphoserine2 Publications
Modified residuei268 – 2681Lysine derivative
Modified residuei272 – 2721Lysine derivative
Modified residuei274 – 2741Lysine derivative

Post-translational modificationi

Phosphorylated by cyclin-dependent kinases CDC28 and PHO85 in association with G1-cyclins, promoting degradation of SIC1 and exit form G1.5 Publications
May contain a covalently attached chromophore.
The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38634.
PaxDbiP38634.
PRIDEiP38634.

Expressioni

Gene expression databases

GenevestigatoriP38634.

Interactioni

Subunit structurei

Interacts with HOG1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC14Q006842EBI-17127,EBI-4192
HOG1P324854EBI-17127,EBI-8437

Protein-protein interaction databases

BioGridi31352. 316 interactions.
DIPiDIP-6817N.
IntActiP38634. 20 interactions.
MINTiMINT-648606.
STRINGi4932.YLR079W.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V7DX-ray2.31E67-85[»]
DisProtiDP00631.
ProteinModelPortaliP38634.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi124 – 13512Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi200 – 2067Asp/Glu-rich (acidic)

Phylogenomic databases

eggNOGiNOG42466.
HOGENOMiHOG000141931.
InParanoidiP38634.
KOiK03085.
OMAiVITFEMA.
OrthoDBiEOG79GTHN.

Sequencei

Sequence statusi: Complete.

P38634-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTPSTPPRSR GTRYLAQPSG NTSSSALMQG QKTPQKPSQN LVPVTPSTTK
60 70 80 90 100
SFKNAPLLAP PNSNMGMTSP FNGLTSPQRS PFPKSSVKRT LFQFESHDNG
110 120 130 140 150
TVREEQEPLG RVNRILFPTQ QNVDIDAAEE EEEGEVLLPP SRPTSARQLH
160 170 180 190 200
LSLERDEFDQ THRKKIIKDV PGTPSDKVIT FELAKNWNNN SPKNDARSQE
210 220 230 240 250
SEDEEDIIIN PVRVGKNPFA SDELVTQEIR NERKRAMLRE NPDIEDVITY
260 270 280
VNKKGEVVEK RRLTDEEKRR FKPKALFQSR DQEH
Length:284
Mass (Da):32,223
Last modified:October 1, 1994 - v1
Checksum:i7913636340678F78
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1671I → T in CAA55118. (PubMed:7958845)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01300 Genomic DNA. Translation: AAA20052.1.
X78309 Genomic DNA. Translation: CAA55118.1.
Z73251 Genomic DNA. Translation: CAA97638.1.
U53880 Genomic DNA. Translation: AAB67583.1.
BK006945 Genomic DNA. Translation: DAA09395.1.
PIRiS47921.
RefSeqiNP_013180.1. NM_001181966.1.

Genome annotation databases

EnsemblFungiiYLR079W; YLR079W; YLR079W.
GeneIDi850768.
KEGGisce:YLR079W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01300 Genomic DNA. Translation: AAA20052.1.
X78309 Genomic DNA. Translation: CAA55118.1.
Z73251 Genomic DNA. Translation: CAA97638.1.
U53880 Genomic DNA. Translation: AAB67583.1.
BK006945 Genomic DNA. Translation: DAA09395.1.
PIRiS47921.
RefSeqiNP_013180.1. NM_001181966.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V7DX-ray2.31E67-85[»]
DisProtiDP00631.
ProteinModelPortaliP38634.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31352. 316 interactions.
DIPiDIP-6817N.
IntActiP38634. 20 interactions.
MINTiMINT-648606.
STRINGi4932.YLR079W.

Proteomic databases

MaxQBiP38634.
PaxDbiP38634.
PRIDEiP38634.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR079W; YLR079W; YLR079W.
GeneIDi850768.
KEGGisce:YLR079W.

Organism-specific databases

CYGDiYLR079w.
SGDiS000004069. SIC1.

Phylogenomic databases

eggNOGiNOG42466.
HOGENOMiHOG000141931.
InParanoidiP38634.
KOiK03085.
OMAiVITFEMA.
OrthoDBiEOG79GTHN.

Enzyme and pathway databases

BioCyciYEAST:G3O-32230-MONOMER.

Miscellaneous databases

NextBioi966930.

Gene expression databases

GenevestigatoriP38634.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An inhibitor of yeast cyclin-dependent protein kinase plays an important role in ensuring the genomic integrity of daughter cells."
    Nugroho T.T., Mendenhall M.D.
    Mol. Cell. Biol. 14:3320-3328(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 182-188; 238-250 AND 260-283.
    Strain: ATCC 204508 / S288c.
  2. "P40SDB25, a putative CDK inhibitor, has a role in the M/G1 transition in Saccharomyces cerevisiae."
    Donovan J.D., Toyn J.H., Johnson A.L., Johnston L.H.
    Genes Dev. 8:1640-1653(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Phosphorylation of Sic1, a cyclin-dependent kinase (Cdk) inhibitor, by Cdk including Pho85 kinase is required for its prompt degradation."
    Nishizawa M., Kawasumi M., Fujino M., Toh-e A.
    Mol. Biol. Cell 9:2393-2405(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-5; THR-33 AND SER-76.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Hog1 mediates cell-cycle arrest in G1 phase by the dual targeting of Sic1."
    Escote X., Zapater M., Clotet J., Posas F.
    Nat. Cell Biol. 6:997-1002(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-173, MUTAGENESIS OF THR-173, INTERACTION WITH HOG1.
  9. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  10. "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 THR-173 AND SER-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  11. "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].
  12. "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-198 AND SER-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSIC1_YEAST
AccessioniPrimary (citable) accession number: P38634
Secondary accession number(s): D6VY79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: February 4, 2015
This is version 128 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 768 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.