P43612 (SA155_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SIT4-associating protein SAP155

Gene names

Name:	SAP155
Ordered Locus Names:	YFR040W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1002 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.9
Subunit structure	Associates with the SIT4 protein phosphatase catalytic subunit in a cell-cycle-dependent manner.
Subcellular location	Cytoplasm Ref.6.
Post-translational modification	Hyperphosphorylated in the absence of SIT4. Ref.1
Miscellaneous	Present with 5960 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the SAPS family.
Sequence caution	The sequence BAA09279.1 differs from that shown. Reason: Frameshift at position 74.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Cytoplasm
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from mutant phenotype Ref.1. Source: SGD
Cellular_component	cytoplasm Inferred from physical interaction Ref.1. Source: SGD
Molecular_function	protein serine/threonine phosphatase activity Inferred from physical interaction Ref.1. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SIT4	P20604	14	EBI-16370,EBI-13707
TIP41	Q12199	3	EBI-16370,EBI-38123

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1002	1002	SIT4-associating protein SAP155		PRO_0000097561
Regions
	Compositional bias	938 – 997	60	Asn-rich
Amino acid modifications
	Modified residue	55	1	Phosphoserine Ref.12
	Modified residue	58	1	Phosphoserine Ref.11 Ref.12
	Modified residue	613	1	Phosphothreonine Ref.10
	Modified residue	616	1	Phosphoserine Ref.10
	Modified residue	618	1	Phosphothreonine Ref.10
Experimental info
	Sequence conflict	663	1	N → T Ref.3
	Sequence conflict	663	1	N → T in BAA09279. Ref.4
	Sequence conflict	668	1	T → G in CAC42243. Ref.2
	Sequence conflict	674 – 690	17	DLFKI…VSKIM → TYSKSNYMIRDCFQNN AA sequence Ref.1
	Sequence conflict	815 – 824	10	ELISPDIQVI → DYISRYSSN in AAC49303. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P43612 [UniParc]. Last modified September 21, 2011. Version 4. Checksum: 50CDC17130333022	FASTA	1,002	115,002
	10 20 30 40 50 60 MSFWPFGQNL NHSNINKILD EYFHVLHELE RINPSVGKAI PAIFNNVQER GTSDSLDSIP 70 80 90 100 110 120 EEYSHGDEVK TARGDQKSRF EKDDQQERYE KEEEERSMNS SESSTTSFSS GSTSKTDLDE 130 140 150 160 170 180 EDISNATAPM MVTTKNLDNS FIERMLVETE LLNELSRQNK TLLDFICFGF FFDKKTNKKV 190 200 210 220 230 240 NNMEYLVDQL MECISKIKTA TTVDLNNLID YQEQQQLDDS SQEDVYVESD TEQEEEKEDD 250 260 270 280 290 300 NNSNNKKRRK RGSSSFGNDD INNNDDDDDA NEDDESAYLT KATIISEIFS LDIWLISESL 310 320 330 340 350 360 VKNQSYLNKI WSIINQPNFN SENSPLVPIF LKINQNLLLT RQDQYLNFIR TERSFVDDML 370 380 390 400 410 420 KHVDISLLMD FFLKIISTDK IESPTGIIEL VYDQNLISKC LSFLNNKESP ADIQACVGDF 430 440 450 460 470 480 LKALIAISAN APLDDISIGP NSLTRQLASP ESIAKLVDIM INQRGAALNT TVSIVIELIR 490 500 510 520 530 540 KNNSDYDQVN LLTTTIKTHP PSNRDPIYLG YLLRKFSNHL SDFFQIILDI ENDANIPLHE 550 560 570 580 590 600 NQLHEKFKPL GFERFKVVEL IAELLHCSNM GLMNSKRAER IARRRDKVRS QLSHHLQDAL 610 620 630 640 650 660 NDLSIEEKEQ LKTKHSPTRD TDHDLKNNNG KIDNDNNDND DESDYGDEID ESFEIPYINM 670 680 690 700 710 720 KQNIKLRTDP TVGDLFKIKL YDTRIVSKIM ELFLTHPWNN FWHNVIFDII QQIFNGRMDF 730 740 750 760 770 780 SYNSFLVLSL FNLKSSYQFM TDIVISDEKG TDVSRFSPVI RDPNFDFKIT TDFILRGYQD 790 800 810 820 830 840 SYKFYELRKM NLGYMGHIVL IAEEVVKFSK LYKVELISPD IQVILQTEEW QYYSEEVLNE 850 860 870 880 890 900 TRMMYSKILG GGSYIDDGNG NIIPQLPDNT TVLTPNGDAS NNNEILDSDT GSSNGTSGGG 910 920 930 940 950 960 QLINVESLEE QLSLSTESDL HNKLREMLIN RAQEDVDNKN TENGVFILGP PEDKNSNSNI 970 980 990 1000 NNTNHNSNNS NNNDNNDNND NDNDNTRNYN EDADNDNDYD HE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T. Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 663. Strain: ATCC 204508 / S288c.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] 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; SER-616 AND THR-618, MASS SPECTROMETRY.
[11]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, MASS SPECTROMETRY.
[12]	"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-55 AND SER-58, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
RefSeq	NP_116698.3. NM_001180005.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5852N.
IntAct	P43612. 30 interactions.
MINT	MINT-632146.
STRING	4932.YFR040W.
Proteomic databases
PaxDb	P43612.
PeptideAtlas	P43612.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YFR040W; YFR040W; YFR040W.
GeneID	850601.
KEGG	sce:YFR040W.
Organism-specific databases
CYGD	YFR040w.
SGD	S000001936. SAP155.
Phylogenomic databases
eggNOG	NOG301298.
GeneTree	ENSGT00390000009899.
HOGENOM	HOG000142084.
KO	K15457.
OMA	YSKILGG.
OrthoDB	EOG47WRX1.
Gene expression databases
Genevestigator	P43612.
GermOnline	YFR040W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR007587. SAPS. [Graphical view]
PANTHER	PTHR12634. PTHR12634. 1 hit.
Pfam	PF04499. SAPS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	966469.

Entry information

Entry name

SA155_YEAST

Accession

Primary (citable) accession number: P43612
Secondary accession number(s): D6VTS3, Q96VG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	September 21, 2011
Last modified:	May 1, 2013
This is version 115 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program