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Protein

SIT4-associating protein SAP190

Gene

SAP190

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

Positive regulator of protein phosphatase SIT4. Involved in the general amino acid control (GAAC) response regulated by TOR. Involved in the dephosphorylation of the elongator complex subunit IKI3.2 Publications

GO - Biological processi

  1. dephosphorylation Source: SGD
  2. G1/S transition of mitotic cell cycle Source: SGD
  3. TOR signaling Source: SGD
  4. tRNA wobble uridine modification Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Enzyme and pathway databases

BioCyciYEAST:G3O-32004-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
SIT4-associating protein SAP190
Gene namesi
Name:SAP190
Ordered Locus Names:YKR028W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

SGDiS000001736. SAP190.

Subcellular locationi

Cytoplasm Curated

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 – 10331033SIT4-associating protein SAP190PRO_0000046107Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei774 – 7741Phosphoserine3 Publications
Modified residuei857 – 8571Phosphoserine2 Publications
Modified residuei862 – 8621Phosphoserine1 Publication
Modified residuei892 – 8921Phosphoserine1 Publication
Modified residuei990 – 9901Phosphothreonine1 Publication
Modified residuei991 – 9911Phosphoserine1 Publication

Post-translational modificationi

Hyperphosphorylated in the absence of SIT4.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP36123.
PaxDbiP36123.
PeptideAtlasiP36123.
PRIDEiP36123.

Expressioni

Gene expression databases

GenevestigatoriP36123.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
SIT4P206044EBI-16392,EBI-13707

Protein-protein interaction databases

BioGridi34161. 104 interactions.
DIPiDIP-4850N.
IntActiP36123. 9 interactions.
MINTiMINT-518659.
STRINGi4932.YKR028W.

Family & Domainsi

Sequence similaritiesi

Belongs to the SAPS family.Curated

Phylogenomic databases

eggNOGiNOG303042.
GeneTreeiENSGT00390000009899.
HOGENOMiHOG000248046.
InParanoidiP36123.
KOiK15458.
OrthoDBiEOG7647CP.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P36123-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGSFWKFGQ DYSIESPVSK ILNSAFIKIN KDQDDDVPTG TCEENIADDE
60 70 80 90 100
DNSSHDYAAS EDNVVNENEE KEEENTLPTT ESEYENYRPN LDVLDDLLDD
110 120 130 140 150
DELYTELMCS NFKLLIFLKY PDVLSKLIEY VTNEKILDEE TDSAKKPEII
160 170 180 190 200
EGVNDHPILI ERDRKDKKED AEEGGDSEET TNDSDHDSGD ERSVDSEETS
210 220 230 240 250
ITLPPESEEQ VETRRARIAA EILSADVWPI SAAIMQNKDL LGRLWSILDH
260 270 280 290 300
PAPLPIPAST YFMKINERLL DMDITGMLEF ILSRDSLVAR FLTHVDNPSL
310 320 330 340 350
MDFLLKVIST DKPDSPTGVI KILKSQELIP KLLDHLNPEY GISTQSAAGD
360 370 380 390 400
FIKAFVTLST NSSNELASGI GPNELTRQLV SEEMIEKLIK IMLKGGTSLS
410 420 430 440 450
NGVGIIIELI RKNNSDYDFI QLVYTTLESH PPTDRDPIHL IHLVKLFAKH
460 470 480 490 500
MPDFADMLDK TKLPLMEMPF GNIEPLGFER FKICELIAEL LHCSNMTLLN
510 520 530 540 550
EPNGEMIAQE RDIERAKELE TSTEKENITA IVDNKSSYYD KDCVEKDITE
560 570 580 590 600
NLGALQINNQ GSEEDELNDT GVSSVKLDVK SDAKVVEGLE NDASGVELYD
610 620 630 640 650
ETLSDTESVR ECLREKPLVG DRLKIALEDT KILISILDMF TEFPWNNFLH
660 670 680 690 700
NVIFDIAQQI FNGPLKTGYN RFLLKDYLVD AYLTKKIVDA DKACQDYEKK
710 720 730 740 750
TGLRYGYMGH LTLVAEEISK FKEYIDEMKL TFCNTAVSDR LEEPFWKEYS
760 770 780 790 800
ETILADTREK YNTVLGDFGN DQESDDDVIR NSDSEDIIGD TEGNENYGNG
810 820 830 840 850
ENDELLSNGH DSGNMDLYYN FNNNENEENE EDYAEYSDVD NKNYYNNVET
860 870 880 890 900
NDDDYDSDDG KSKSAESEFT DKISEHRDGN SLYNEDNDEN GSDKWTSGTS
910 920 930 940 950
LFPPDHFPSR SQPSDPKLQD QNIFHHQFDF EGVGDDDDYM DPNDDGQSYA
960 970 980 990 1000
RPGNPLYTTP KTPPRPKTIL FNSLSALDNN GEDEEVALGT SVDDRMDNEI
1010 1020 1030
SSDEEDSEDE DEENDMGNEE GYSLYRSRSK EAF
Length:1,033
Mass (Da):117,098
Last modified:October 1, 1996 - v2
Checksum:i33E5575B58B73B1A
GO

Sequence cautioni

The sequence CAA82100.1 differs from that shown. Reason: Frameshift at position 1009. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50561 Genomic DNA. Translation: AAC49304.1.
Z28253 Genomic DNA. Translation: CAA82100.1. Frameshift.
BK006944 Genomic DNA. Translation: DAA09183.2.
PIRiS38100.
RefSeqiNP_012953.2. NM_001179818.2.

Genome annotation databases

EnsemblFungiiYKR028W; YKR028W; YKR028W.
GeneIDi853899.
KEGGisce:YKR028W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50561 Genomic DNA. Translation: AAC49304.1.
Z28253 Genomic DNA. Translation: CAA82100.1. Frameshift.
BK006944 Genomic DNA. Translation: DAA09183.2.
PIRiS38100.
RefSeqiNP_012953.2. NM_001179818.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34161. 104 interactions.
DIPiDIP-4850N.
IntActiP36123. 9 interactions.
MINTiMINT-518659.
STRINGi4932.YKR028W.

Proteomic databases

MaxQBiP36123.
PaxDbiP36123.
PeptideAtlasiP36123.
PRIDEiP36123.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKR028W; YKR028W; YKR028W.
GeneIDi853899.
KEGGisce:YKR028W.

Organism-specific databases

SGDiS000001736. SAP190.

Phylogenomic databases

eggNOGiNOG303042.
GeneTreeiENSGT00390000009899.
HOGENOMiHOG000248046.
InParanoidiP36123.
KOiK15458.
OrthoDBiEOG7647CP.

Enzyme and pathway databases

BioCyciYEAST:G3O-32004-MONOMER.

Miscellaneous databases

NextBioi975221.

Gene expression databases

GenevestigatoriP36123.

Family and domain databases

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

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], IDENTIFICATION OF FRAMESHIFT, INTERACTION WITH SIT4, PHOSPHORYLATION.
    Strain: S288c / GRF88.
  2. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 1009.
    Strain: ATCC 204508 / S288c.
  4. "The yeast elongator histone acetylase requires Sit4-dependent dephosphorylation for toxin-target capacity."
    Jablonowski D., Fichtner L., Stark M.J.R., Schaffrath R.
    Mol. Biol. Cell 15:1459-1469(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "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.
  6. "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-774 AND SER-857, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "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-774, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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-774; SER-857; SER-862; SER-892; THR-990 AND SER-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSA190_YEAST
AccessioniPrimary (citable) accession number: P36123
Secondary accession number(s): D6VX93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: 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.