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P43612

- SA155_YEAST

UniProt

P43612 - SA155_YEAST

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Protein

SIT4-associating protein SAP155

Gene

SAP155

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

Functioni

Positive regulator of protein phosphatase SIT4. Involved in directing expression of TOR-repressed genes and in dephosphorylation of NPR1 in response to nutrient starvation. Negatively modulates K+ efflux of the cell by the Na+-K+/H+ antiporter NHA1.2 Publications

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Enzyme and pathway databases

BioCyciYEAST:G3O-30487-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
SIT4-associating protein SAP155
Gene namesi
Name:SAP155
Ordered Locus Names:YFR040W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VI

Organism-specific databases

CYGDiYFR040w.
SGDiS000001936. SAP155.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10021002SIT4-associating protein SAP155PRO_0000097561Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581Phosphoserine1 Publication
Modified residuei255 – 2551Phosphoserine1 Publication
Modified residuei613 – 6131Phosphothreonine1 Publication
Modified residuei618 – 6181Phosphothreonine1 Publication

Post-translational modificationi

Hyperphosphorylated in the absence of SIT4.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP43612.
PaxDbiP43612.
PeptideAtlasiP43612.

Expressioni

Gene expression databases

GenevestigatoriP43612.

Interactioni

Subunit structurei

Associates with the SIT4 protein phosphatase catalytic subunit in a cell-cycle-dependent manner.

Binary interactionsi

WithEntry#Exp.IntActNotes
SIT4P206048EBI-16370,EBI-13707

Protein-protein interaction databases

BioGridi31198. 151 interactions.
DIPiDIP-5852N.
IntActiP43612. 32 interactions.
MINTiMINT-632146.
STRINGi4932.YFR040W.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi938 – 99760Asn-richAdd
BLAST

Sequence similaritiesi

Belongs to the SAPS family.Curated

Phylogenomic databases

eggNOGiNOG301298.
GeneTreeiENSGT00390000009899.
HOGENOMiHOG000142084.
InParanoidiP43612.
KOiK15457.
OMAiNNFWHNV.
OrthoDBiEOG7647CP.

Family and domain databases

InterProiIPR007587. SAPS.
[Graphical view]
PANTHERiPTHR12634. PTHR12634. 1 hit.
PfamiPF04499. SAPS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P43612-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSFWPFGQNL NHSNINKILD EYFHVLHELE RINPSVGKAI PAIFNNVQER
60 70 80 90 100
GTSDSLDSIP EEYSHGDEVK TARGDQKSRF EKDDQQERYE KEEEERSMNS
110 120 130 140 150
SESSTTSFSS GSTSKTDLDE EDISNATAPM MVTTKNLDNS FIERMLVETE
160 170 180 190 200
LLNELSRQNK TLLDFICFGF FFDKKTNKKV NNMEYLVDQL MECISKIKTA
210 220 230 240 250
TTVDLNNLID YQEQQQLDDS SQEDVYVESD TEQEEEKEDD NNSNNKKRRK
260 270 280 290 300
RGSSSFGNDD INNNDDDDDA NEDDESAYLT KATIISEIFS LDIWLISESL
310 320 330 340 350
VKNQSYLNKI WSIINQPNFN SENSPLVPIF LKINQNLLLT RQDQYLNFIR
360 370 380 390 400
TERSFVDDML KHVDISLLMD FFLKIISTDK IESPTGIIEL VYDQNLISKC
410 420 430 440 450
LSFLNNKESP ADIQACVGDF LKALIAISAN APLDDISIGP NSLTRQLASP
460 470 480 490 500
ESIAKLVDIM INQRGAALNT TVSIVIELIR KNNSDYDQVN LLTTTIKTHP
510 520 530 540 550
PSNRDPIYLG YLLRKFSNHL SDFFQIILDI ENDANIPLHE NQLHEKFKPL
560 570 580 590 600
GFERFKVVEL IAELLHCSNM GLMNSKRAER IARRRDKVRS QLSHHLQDAL
610 620 630 640 650
NDLSIEEKEQ LKTKHSPTRD TDHDLKNNNG KIDNDNNDND DESDYGDEID
660 670 680 690 700
ESFEIPYINM KQNIKLRTDP TVGDLFKIKL YDTRIVSKIM ELFLTHPWNN
710 720 730 740 750
FWHNVIFDII QQIFNGRMDF SYNSFLVLSL FNLKSSYQFM TDIVISDEKG
760 770 780 790 800
TDVSRFSPVI RDPNFDFKIT TDFILRGYQD SYKFYELRKM NLGYMGHIVL
810 820 830 840 850
IAEEVVKFSK LYKVELISPD IQVILQTEEW QYYSEEVLNE TRMMYSKILG
860 870 880 890 900
GGSYIDDGNG NIIPQLPDNT TVLTPNGDAS NNNEILDSDT GSSNGTSGGG
910 920 930 940 950
QLINVESLEE QLSLSTESDL HNKLREMLIN RAQEDVDNKN TENGVFILGP
960 970 980 990 1000
PEDKNSNSNI NNTNHNSNNS NNNDNNDNND NDNDNTRNYN EDADNDNDYD

HE
Length:1,002
Mass (Da):115,002
Last modified:September 21, 2011 - v4
Checksum:i50CDC17130333022
GO

Sequence cautioni

The sequence BAA09279.1 differs from that shown. Reason: Frameshift at position 74. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti663 – 6631N → T(PubMed:8686379)Curated
Sequence conflicti663 – 6631N → T in BAA09279. (PubMed:7670463)Curated
Sequence conflicti668 – 6681T → G in CAC42243. (PubMed:11779790)Curated
Sequence conflicti674 – 69017DLFKI…VSKIM → TYSKSNYMIRDCFQNN AA sequence (PubMed:8649382)CuratedAdd
BLAST
Sequence conflicti815 – 82410ELISPDIQVI → DYISRYSSN in AAC49303. (PubMed:8649382)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50560 Genomic DNA. Translation: AAC49303.1.
AJ318331 Genomic DNA. Translation: CAC42243.1.
D50617 Genomic DNA. Translation: BAA09279.1. Frameshift.
BK006940 Genomic DNA. Translation: DAA12483.2.
RefSeqiNP_116698.3. NM_001180005.2.

Genome annotation databases

EnsemblFungiiYFR040W; YFR040W; YFR040W.
GeneIDi850601.
KEGGisce:YFR040W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50560 Genomic DNA. Translation: AAC49303.1 .
AJ318331 Genomic DNA. Translation: CAC42243.1 .
D50617 Genomic DNA. Translation: BAA09279.1 . Frameshift.
BK006940 Genomic DNA. Translation: DAA12483.2 .
RefSeqi NP_116698.3. NM_001180005.2.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31198. 151 interactions.
DIPi DIP-5852N.
IntActi P43612. 32 interactions.
MINTi MINT-632146.
STRINGi 4932.YFR040W.

Proteomic databases

MaxQBi P43612.
PaxDbi P43612.
PeptideAtlasi P43612.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YFR040W ; YFR040W ; YFR040W .
GeneIDi 850601.
KEGGi sce:YFR040W.

Organism-specific databases

CYGDi YFR040w.
SGDi S000001936. SAP155.

Phylogenomic databases

eggNOGi NOG301298.
GeneTreei ENSGT00390000009899.
HOGENOMi HOG000142084.
InParanoidi P43612.
KOi K15457.
OMAi NNFWHNV.
OrthoDBi EOG7647CP.

Enzyme and pathway databases

BioCyci YEAST:G3O-30487-MONOMER.

Miscellaneous databases

NextBioi 966469.

Gene expression databases

Genevestigatori P43612.

Family and domain databases

InterProi IPR007587. SAPS.
[Graphical view ]
PANTHERi PTHR12634. PTHR12634. 1 hit.
Pfami PF04499. SAPS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The SAPs, a new family of proteins, associate and function positively with the SIT4 phosphatase."
    Luke M.M., della Seta F., di Como C.J., Sugimoto H., Kobayashi R., Arndt K.T.
    Mol. Cell. Biol. 16:2744-2755(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH SIT4, PHOSPHORYLATION.
  2. "Sit4p protein phosphatase is required for sensitivity of Saccharomyces cerevisiae to Kluyveromyces lactis zymocin."
    Jablonowski D., Butler A.R., Fichtner L., Gardiner D., Schaffrath R., Stark M.J.R.
    Genetics 159:1479-1489(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION OF FRAMESHIFT.
  3. "Analysis of a 36.2 kb DNA sequence including the right telomere of chromosome VI from Saccharomyces cerevisiae."
    Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.
    Yeast 12:149-167(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 663.
    Strain: ATCC 204508 / S288c.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "TOR controls transcriptional and translational programs via Sap-Sit4 protein phosphatase signaling effectors."
    Rohde J.R., Campbell S., Zurita-Martinez S.A., Cutler N.S., Ashe M., Cardenas M.E.
    Mol. Cell. Biol. 24:8332-8341(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Ability of Sit4p to promote K+ efflux via Nha1p is modulated by Sap155p and Sap185p."
    Manlandro C.M.A., Haydon D.H., Rosenwald A.G.
    Eukaryot. Cell 4:1041-1049(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "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 THR-613 AND THR-618, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, 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-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSA155_YEAST
AccessioniPrimary (citable) accession number: P43612
Secondary accession number(s): D6VTS3, Q96VG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: September 21, 2011
Last modified: October 29, 2014
This is version 127 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5960 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

External Data

Dasty 3