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Protein

Serine/threonine-protein kinase PKH1

Gene

PKH1

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

Activates YPK1 by phosphorylating of a threonine residue.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei154 – 1541ATPBy similarity
Binding sitei210 – 2101ATPBy similarity
Active sitei249 – 2491Proton acceptorPROSITE-ProRule annotation
Binding sitei253 – 2531ATP; via carbonyl oxygenBy similarity
Binding sitei267 – 2671ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi135 – 1373ATPBy similarity
Nucleotide bindingi204 – 2063ATPBy similarity

GO - Molecular functioni

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

GO - Biological processi

  • cytoplasmic mRNA processing body assembly Source: SGD
  • endocytosis Source: SGD
  • late endosome to vacuole transport via multivesicular body sorting pathway Source: SGD
  • MAPK cascade involved in cell wall organization or biogenesis Source: SGD
  • peptidyl-serine phosphorylation Source: SGD
  • protein phosphorylation Source: SGD
  • regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30014-MONOMER.
ReactomeiR-SCE-114604. GPVI-mediated activation cascade.
R-SCE-1257604. PIP3 activates AKT signaling.
R-SCE-165158. Activation of AKT2.
R-SCE-202424. Downstream TCR signaling.
R-SCE-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-SCE-389357. CD28 dependent PI3K/Akt signaling.
R-SCE-389513. CTLA4 inhibitory signaling.
R-SCE-392451. G beta:gamma signalling through PI3Kgamma.
R-SCE-444257. RSK activation.
R-SCE-5218920. VEGFR2 mediated vascular permeability.
R-SCE-5218921. VEGFR2 mediated cell proliferation.
R-SCE-5625740. RHO GTPases activate PKNs.
R-SCE-6804757. Regulation of TP53 Degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PKH1 (EC:2.7.11.1)
Alternative name(s):
3-phosphoinositide-dependent protein kinase 1
Gene namesi
Name:PKH1
Ordered Locus Names:YDR490C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR490C.
SGDiS000002898. PKH1.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: SGD
  • cytosol Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 766766Serine/threonine-protein kinase PKH1PRO_0000086552Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei294 – 2941PhosphoserineCombined sources
Modified residuei296 – 2961PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03407.

PTM databases

iPTMnetiQ03407.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP82P028292EBI-32467,EBI-8659

Protein-protein interaction databases

BioGridi32542. 91 interactions.
DIPiDIP-1518N.
IntActiQ03407. 10 interactions.
MINTiMINT-395391.

Structurei

3D structure databases

ProteinModelPortaliQ03407.
SMRiQ03407. Positions 65-411.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini125 – 391267Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni156 – 20146PIF-pocketBy similarityAdd
BLAST

Domaini

The PIF-pocket is a small lobe in the catalytic domain required by the enzyme for the binding to the hydrophobic motif of its substrates. It is an allosteric regulatory site that can accommodate small compounds acting as allosteric inhibitors.By similarity

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074819.
InParanoidiQ03407.
KOiK06276.
OrthoDBiEOG76MKKG.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03407-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNRSLTEAD HALLSKPLVP TSAEHTQTQE YPRPFVDGSN SQSGSELQAS
60 70 80 90 100
PQGQFGEKAL TSTNRFIPLA NDDPGMQHEM GLDPSMRRRR EEWAERGAAK
110 120 130 140 150
IVKDVVDPAT GELTKHVVKM GIKDFKFGEQ LGDGSYSSVV LATARDSGKK
160 170 180 190 200
YAVKVLSKEY LIRQKKVKYV TVEKLALQKL NGTKGIFKLF FTFQDEASLY
210 220 230 240 250
FLLEYAPHGD FLGLIKKYGS LNETCARYYA SQIIDAVDSL HNIGIIHRDI
260 270 280 290 300
KPENILLDKN MKVKLTDFGT AKILPEEPSN TADGKPYFDL YAKSKSFVGT
310 320 330 340 350
AEYVSPELLN DNYTDSRCDI WAFGCILYQM LAGKPPFKAA NEYLTFQKVM
360 370 380 390 400
KIQYAFTAGF PQIVKDLVKK LLVRDPNDRL TIKQIKAHLF FHEVNFEDGS
410 420 430 440 450
VWDDNPPEIQ PYKINAEAMK PLQKVSESDT TVKMANLQLA GNGHADTPLQ
460 470 480 490 500
APAATSQEHS VISMTAATAA FNKDYTSQPK LGSKSSTSVR SASNNTDREV
510 520 530 540 550
IQKKVSKNRA SVSSPSISTT SRGKDNRSRS SDAFWSRYLQ NMDERVLLMK
560 570 580 590 600
EVALSTRNLE DSPVGLENVA LDYKNPLDIE PPTDSAGKFY KKMFLITNLG
610 620 630 640 650
RALVFVKRRS LSMWEEQEFE LQFELELNDV EKIRFISDQV LEIDGSRTIF
660 670 680 690 700
IGCKERAVLM KLWKLIHNGM TAKPKVVSPK SDHKMFDKFI LQKRQNTKKK
710 720 730 740 750
NQAPPVPQSN RLINGLPDRC ILKTPEEGAL HTKRPTSLQT RSSSNYSKLL
760
ARSTQMRKNM TRTDEK
Length:766
Mass (Da):86,253
Last modified:November 1, 1996 - v1
Checksum:i7FFD32E8BE8BC367
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33050 Genomic DNA. Translation: AAB64917.1.
BK006938 Genomic DNA. Translation: DAA12323.1.
PIRiS69657.
RefSeqiNP_010778.3. NM_001180798.3.

Genome annotation databases

EnsemblFungiiYDR490C; YDR490C; YDR490C.
GeneIDi852101.
KEGGisce:YDR490C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33050 Genomic DNA. Translation: AAB64917.1.
BK006938 Genomic DNA. Translation: DAA12323.1.
PIRiS69657.
RefSeqiNP_010778.3. NM_001180798.3.

3D structure databases

ProteinModelPortaliQ03407.
SMRiQ03407. Positions 65-411.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32542. 91 interactions.
DIPiDIP-1518N.
IntActiQ03407. 10 interactions.
MINTiMINT-395391.

PTM databases

iPTMnetiQ03407.

Proteomic databases

MaxQBiQ03407.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR490C; YDR490C; YDR490C.
GeneIDi852101.
KEGGisce:YDR490C.

Organism-specific databases

EuPathDBiFungiDB:YDR490C.
SGDiS000002898. PKH1.

Phylogenomic databases

GeneTreeiENSGT00550000074819.
InParanoidiQ03407.
KOiK06276.
OrthoDBiEOG76MKKG.

Enzyme and pathway databases

BioCyciYEAST:G3O-30014-MONOMER.
ReactomeiR-SCE-114604. GPVI-mediated activation cascade.
R-SCE-1257604. PIP3 activates AKT signaling.
R-SCE-165158. Activation of AKT2.
R-SCE-202424. Downstream TCR signaling.
R-SCE-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-SCE-389357. CD28 dependent PI3K/Akt signaling.
R-SCE-389513. CTLA4 inhibitory signaling.
R-SCE-392451. G beta:gamma signalling through PI3Kgamma.
R-SCE-444257. RSK activation.
R-SCE-5218920. VEGFR2 mediated vascular permeability.
R-SCE-5218921. VEGFR2 mediated cell proliferation.
R-SCE-5625740. RHO GTPases activate PKNs.
R-SCE-6804757. Regulation of TP53 Degradation.

Miscellaneous databases

PROiQ03407.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. 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 IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(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. "Functional counterparts of mammalian protein kinases PDK1 and SGK in budding yeast."
    Casamayor A., Torrance P.D., Kobayashi T., Thorner J., Alessi D.R.
    Curr. Biol. 9:186-197(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  5. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "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-296, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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-294 AND SER-296, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPKH1_YEAST
AccessioniPrimary (citable) accession number: Q03407
Secondary accession number(s): D6VTB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: November 1, 1996
Last modified: June 8, 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

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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.