Q08217 (PSK2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase PSK2
EC=2.7.11.1

Alternative name(s):
PAS kinase 2

Gene names

Name:	PSK2
Ordered Locus Names:	YOL045W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1101 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine-protein kinase involved in the control of sugar metabolism and translation. Phosphorylates UGP1, which is required for normal glycogen and beta-(1,6)-glucan synthesis. This phosphorylation shifts glucose partitioning toward cell wall glucan synthesis at the expense of glycogen synthesis. Phosphorylates also the glycogen synthase GSY2 and the translation factors CAF20, TIF11 and SRO9. Ref.4 Ref.7
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Cytoplasm Ref.5.
Miscellaneous	Present with 2220 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Translation regulation
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of glycogen biosynthetic process Inferred from mutant phenotype Ref.4. Source: SGD regulation of (1->6)-beta-D-glucan biosynthetic process Inferred from genetic interaction Ref.7. Source: SGD regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from mutant phenotype Ref.4. Source: SGD signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
UGP1	P32861	3	EBI-9839,EBI-19987

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1101	1101	Serine/threonine-protein kinase PSK2		PRO_0000086156
Regions
	Domain	841 – 1099	259	Protein kinase
	Nucleotide binding	847 – 855	9	ATP By similarity
Sites
	Active site	975	1	Proton acceptor By similarity
	Binding site	870	1	ATP By similarity
Amino acid modifications
	Modified residue	118	1	Phosphothreonine Ref.9
	Modified residue	155	1	Phosphothreonine Ref.9
	Modified residue	156	1	Phosphoserine Ref.9
	Modified residue	434	1	Phosphoserine Ref.8
	Modified residue	680	1	Phosphoserine Ref.9
	Modified residue	692	1	Phosphoserine Ref.9
	Modified residue	717	1	Phosphoserine Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Q08217 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3FC9CF3EF99B7937	FASTA	1,101	124,373
	10 20 30 40 50 60 MTYPVSAAAP ADISYSKNTP LVGLSKPPCL YQHASSSVDS FSSTFSDDDR SDLVAVPNES 70 80 90 100 110 120 PHAFSYNPIS PNSLGVRLTI LRRSLEIMVN SPDILHELKK KAPVIAYPPS LRHTRNLTET 130 140 150 160 170 180 ATLSASRDPL NGSLISPLVS NMPSPASRPV IQRATSLMVL PDNDTASKLN PAKSELENLL 190 200 210 220 230 240 FLLNLALENN SFERASDLHM LSLLNIKKIN FDSDIQKSET LKKVLLDSLA EPFFENYKKF 250 260 270 280 290 300 PHKDLGSKSQ YNEYEEKHDD IVSLADIKPQ QDYSRILHPF TSAKNSGPEA IFTCSQQYPW 310 320 330 340 350 360 NFKAANDLAC LTFGISKNVI KALTLLDLIH TDSRNFVLEK IMNAEDDNQE IVFTGETIPI 370 380 390 400 410 420 VQPNSTSNNN VPNLIWASLW AKRKNGLLVC VFEKTPCDYI DVMLNLRDFS VDSIIDTTHF 430 440 450 460 470 480 LENFDKKKQQ ESTSPMTEKK TVKFANEIHD IGSVSHSLSK LIDDVRFGKV FSADDDLLPL 490 500 510 520 530 540 SIRVANHVNE ERYFTLNCLS ENIPCAVTTS VLENEIKLKI HSLPYQAGLF IVDSHTLSLL 550 560 570 580 590 600 SFNKSVAKNM FGLRLHELAG SSVTKLVPSL ADMISYINKT YPMLNITLPE NKGLVLTEHF 610 620 630 640 650 660 FRKIEAEMHH DKDSFYTSIG LDGCHKDGNL IKVDVQLRVL NTNAVLLWIT HSRDVVIENY 670 680 690 700 710 720 TTVPSQLPML KENEIDVVGS RGSSSASSKK SSEKIPVNTL KAMADLSISS AETISNSDDE 730 740 750 760 770 780 VDLNQVNEKL RETSCGKVRG IESNDNNNYD DDMTMVDDPE LKHKIELTKM YTQDKSKFVK 790 800 810 820 830 840 DDNFKVDEKF IMRIIEPING EEIKKETNEL DKRNSTLKAT YLTTPEANIG SQKRIKKFSD 850 860 870 880 890 900 FTILQVMGEG AYGKVNLCIH NREHYIVVIK MIFKERILVD TWVRDRKLGT IPSEIQIMAT 910 920 930 940 950 960 LNKNSQENIL KLLDFFEDDD YYYIETPVHG ETGSIDLFDV IEFKKDMVEH EAKLVFKQVV 970 980 990 1000 1010 1020 ASIKHLHDQG IVHRDIKDEN VIVDSHGFVK LIDFGSAAYI KSGPFDVFVG TMDYAAPEVL 1030 1040 1050 1060 1070 1080 GGSSYKGKPQ DIWALGVLLY TIIYKENPYY NIDEILEGEL RFDKSEHVSE ECISLIKRIL 1090 1100 TREVDKRPTI DEIYEDKWLK I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"PAS kinase: an evolutionarily conserved PAS domain-regulated serine/threonine kinase." Rutter J., Michnoff C.H., Harper S.M., Gardner K.H., McKnight S.L. Proc. Natl. Acad. Sci. U.S.A. 98:8991-8996(2001) [PubMed: 11459942] [Abstract] Cited for: DOMAIN.
[4]	"Coordinate regulation of sugar flux and translation by PAS kinase." Rutter J., Probst B.L., McKnight S.L. Cell 111:17-28(2002) [PubMed: 12372297] [Abstract] Cited for: FUNCTION.
[5]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Regulation of glucose partitioning by PAS kinase and Ugp1 phosphorylation." Smith T.L., Rutter J. Mol. Cell 26:491-499(2007) [PubMed: 17531808] [Abstract] Cited for: FUNCTION.
[8]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, MASS SPECTROMETRY.
[9]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118; THR-155; SER-156; SER-680; SER-692 AND SER-717, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z74788 Genomic DNA. Translation: CAA99051.1. Z74786 Genomic DNA. Translation: CAA99047.1. BK006948 Genomic DNA. Translation: DAA10737.1.
PIR	S66730.
RefSeq	NP_014597.1. NM_001183299.1.
3D structure databases
ProteinModelPortal	Q08217.
SMR	Q08217. Positions 287-397, 839-1100.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6430N.
IntAct	Q08217. 6 interactions.
MINT	MINT-692966.
STRING	Q08217.
Proteomic databases
PeptideAtlas	Q08217.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOL045W; YOL045W; YOL045W.
GeneID	854111.
KEGG	sce:YOL045W.
NMPDR	fig|4932.3.peg.5689.
Organism-specific databases
CYGD	YOL045w.
SGD	S000005405. PSK2.
Phylogenomic databases
eggNOG	fuNOG04340.
GeneTree	EFGT00070000008712.
HOGENOM	HBG396821.
OMA	TVKFANE.
OrthoDB	EOG4SBJ62.
Gene expression databases
ArrayExpress	Q08217.
Genevestigator	Q08217.
GermOnline	YOL045W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000014. PAS. IPR000719. Prot_kinase_cat_dom. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K08286.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00091. PAS. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	975801.

Entry information

Entry name

PSK2_YEAST

Accession

Primary (citable) accession number: Q08217
Secondary accession number(s): D6W221

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program