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Protein

Serine/threonine-protein kinase PSK2

Gene

PSK2

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

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 SRO9.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei870 – 8701ATPPROSITE-ProRule annotation
Active sitei975 – 9751Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi847 – 8559ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • negative regulation of cytoplasmic translation Source: SGD
  • negative regulation of glycogen biosynthetic process Source: SGD
  • protein phosphorylation Source: SGD
  • regulation of (1->6)-beta-D-glucan biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33459-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PSK2 (EC:2.7.11.1)
Alternative name(s):
PAS kinase 2
Gene namesi
Name:PSK2
Ordered Locus Names:YOL045W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL045W.
SGDiS000005405. PSK2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11011101Serine/threonine-protein kinase PSK2PRO_0000086156Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei118 – 1181PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ08217.
PeptideAtlasiQ08217.
TopDownProteomicsiQ08217.

PTM databases

iPTMnetiQ08217.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
UGP1P328613EBI-9839,EBI-19987

Protein-protein interaction databases

BioGridi34357. 125 interactions.
DIPiDIP-6430N.
IntActiQ08217. 4 interactions.
MINTiMINT-692966.

Structurei

3D structure databases

ProteinModelPortaliQ08217.
SMRiQ08217. Positions 769-1100.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini841 – 1099259Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00760000119045.
InParanoidiQ08217.
KOiK08286.
OMAiCLMFGVS.
OrthoDBiEOG7G4QPK.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000014. PAS.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00091. PAS. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08217-1 [UniParc]FASTAAdd to basket

« Hide

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

I
Length:1,101
Mass (Da):124,373
Last modified:November 1, 1996 - v1
Checksum:i3FC9CF3EF99B7937
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74788 Genomic DNA. Translation: CAA99051.1.
Z74786 Genomic DNA. Translation: CAA99047.1.
BK006948 Genomic DNA. Translation: DAA10737.1.
PIRiS66730.
RefSeqiNP_014597.1. NM_001183299.1.

Genome annotation databases

EnsemblFungiiYOL045W; YOL045W; YOL045W.
GeneIDi854111.
KEGGisce:YOL045W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74788 Genomic DNA. Translation: CAA99051.1.
Z74786 Genomic DNA. Translation: CAA99047.1.
BK006948 Genomic DNA. Translation: DAA10737.1.
PIRiS66730.
RefSeqiNP_014597.1. NM_001183299.1.

3D structure databases

ProteinModelPortaliQ08217.
SMRiQ08217. Positions 769-1100.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34357. 125 interactions.
DIPiDIP-6430N.
IntActiQ08217. 4 interactions.
MINTiMINT-692966.

PTM databases

iPTMnetiQ08217.

Proteomic databases

MaxQBiQ08217.
PeptideAtlasiQ08217.
TopDownProteomicsiQ08217.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL045W; YOL045W; YOL045W.
GeneIDi854111.
KEGGisce:YOL045W.

Organism-specific databases

EuPathDBiFungiDB:YOL045W.
SGDiS000005405. PSK2.

Phylogenomic databases

GeneTreeiENSGT00760000119045.
InParanoidiQ08217.
KOiK08286.
OMAiCLMFGVS.
OrthoDBiEOG7G4QPK.

Enzyme and pathway databases

BioCyciYEAST:G3O-33459-MONOMER.

Miscellaneous databases

NextBioi975801.
PROiQ08217.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000014. PAS.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00091. PAS. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. 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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "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 THR-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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 THR-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSK2_YEAST
AccessioniPrimary (citable) accession number: Q08217
Secondary accession number(s): D6W221
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 142 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 2220 molecules/cell in log phase SD medium.1 Publication

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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

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 one 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.