Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein kinase SCH9

Gene

SCH9

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

Protein kinase that is part of growth control pathway which is at least partially redundant with the cAMP pathway. Regulates both BCY1 phosphorylation and MPK1 activity (PubMed:20702584). Regulates ribosome biogenesis, translation initiation, and entry into stationary phase in a TORC1-dependent manner (PubMed:17560372).2 Publications

Miscellaneous

Present with 3850 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by cAMP.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei441ATP1
Active sitei538Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi418 – 426ATP9

GO - Molecular functioni

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

GO - Biological processi

  • age-dependent response to oxidative stress involved in chronological cell aging Source: SGD
  • intracellular signal transduction Source: GO_Central
  • peptidyl-serine phosphorylation Source: GO_Central
  • positive regulation of ribosomal protein gene transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of transcription from RNA polymerase III promoter Source: SGD
  • positive regulation of transcription from RNA polymerase I promoter Source: SGD
  • protein phosphorylation Source: SGD
  • regulation of protein localization Source: SGD
  • regulation of response to osmotic stress Source: SGD
  • regulation of sphingolipid biosynthetic process Source: SGD
  • regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: SGD
  • replicative cell aging Source: SGD

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, cAMP, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31231-MONOMER.
BRENDAi2.7.11.1. 984.
ReactomeiR-SCE-114604. GPVI-mediated activation cascade.
R-SCE-1257604. PIP3 activates AKT signaling.
R-SCE-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-SCE-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-SCE-165158. Activation of AKT2.
R-SCE-166208. mTORC1-mediated signalling.
R-SCE-198323. AKT phosphorylates targets in the cytosol.
R-SCE-198693. AKT phosphorylates targets in the nucleus.
R-SCE-198753. ERK/MAPK targets.
R-SCE-199418. Negative regulation of the PI3K/AKT network.
R-SCE-203615. eNOS activation.
R-SCE-211163. AKT-mediated inactivation of FOXO1A.
R-SCE-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-SCE-375165. NCAM signaling for neurite out-growth.
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-450385. Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
R-SCE-5218920. VEGFR2 mediated vascular permeability.
R-SCE-6804757. Regulation of TP53 Degradation.
R-SCE-6804758. Regulation of TP53 Activity through Acetylation.
R-SCE-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-SCE-881907. Gastrin-CREB signalling pathway via PKC and MAPK.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase SCH9 (EC:2.7.11.1)
Gene namesi
Name:SCH9
Synonyms:KOM1
Ordered Locus Names:YHR205W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR205W.
SGDiS000001248. SCH9.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000866381 – 824Serine/threonine-protein kinase SCH9Add BLAST824

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei570Phosphothreonine; by PKH1 or PKH21 Publication1
Modified residuei711Phosphoserine; by TORC11 Publication1
Modified residuei723Phosphothreonine; by TORC1Combined sources1 Publication1
Modified residuei726Phosphoserine; by TORC1Combined sources1 Publication1
Modified residuei737Phosphothreonine; by TORC11 Publication1
Modified residuei758Phosphoserine; by TORC11 Publication1
Modified residuei765Phosphoserine; by TORC11 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP11792.
PRIDEiP11792.

PTM databases

iPTMnetiP11792.

Interactioni

Protein-protein interaction databases

BioGridi36639. 652 interactors.
ELMiP11792.
IntActiP11792. 10 interactors.
MINTiMINT-607351.
STRINGi4932.YHR205W.

Structurei

3D structure databases

ProteinModelPortaliP11792.
SMRiP11792.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini185 – 361C2Add BLAST177
Domaini412 – 671Protein kinaseAdd BLAST260
Domaini672 – 748AGC-kinase C-terminalAdd BLAST77

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi227 – 267Asn-richAdd BLAST41

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00890000139324.
HOGENOMiHOG000233033.
InParanoidiP11792.
KOiK19800.
OMAiVLIFEMC.
OrthoDBiEOG092C0HH3.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiView protein in InterPro
IPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR035892. C2_domain_sf.
IPR011009. Kinase-like_dom_sf.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF00168. C2. 2 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
SMARTiView protein in SMART
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.

Sequencei

Sequence statusi: Complete.

P11792-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMNFFTSKSS NQDTGFSSQH QHPNGQNNGN NNSSTAGNDN GYPCKLVSSG
60 70 80 90 100
PCASSNNGAL FTNFTLQTAT PTTAISQDLY AMGTTGITSE NALFQMKSMN
110 120 130 140 150
NGISSVNNNN SNTPTIITTS QEETNAGNVH GDTGGNSLQN SEDDNFSSSS
160 170 180 190 200
TTKCLLSSTS SLSINQREAA AAAYGPDTDI PRGKLEVTII EARDLVTRSK
210 220 230 240 250
DSQPYVVCTF ESSEFISNGP ESLGAINNNN NNNNNNQHNQ NQHINNNNEN
260 270 280 290 300
TNPDAASQHH NNNSGWNGSQ LPSIKEHLKK KPLYTHRSSS QLDQLNSCSS
310 320 330 340 350
VTDPSKRSSN SSSGSSNGPK NDSSHPIWHH KTTFDVLGSH SELDISVYDA
360 370 380 390 400
AHDHMFLGQV RLYPMIHNLA HASQHQWHSL KPRVIDEVVS GDILIKWTYK
410 420 430 440 450
QTKKRHYGPQ DFEVLRLLGK GTFGQVYQVK KKDTQRIYAM KVLSKKVIVK
460 470 480 490 500
KNEIAHTIGE RNILVTTASK SSPFIVGLKF SFQTPTDLYL VTDYMSGGEL
510 520 530 540 550
FWHLQKEGRF SEDRAKFYIA ELVLALEHLH DNDIVYRDLK PENILLDANG
560 570 580 590 600
NIALCDFGLS KADLKDRTNT FCGTTEYLAP ELLLDETGYT KMVDFWSLGV
610 620 630 640 650
LIFEMCCGWS PFFAENNQKM YQKIAFGKVK FPRDVLSQEG RSFVKGLLNR
660 670 680 690 700
NPKHRLGAID DGRELRAHPF FADIDWEALK QKKIPPPFKP HLVSETDTSN
710 720 730 740 750
FDPEFTTAST SYMNKHQPMM TATPLSPAMQ AKFAGFTFVD ESAIDEHVNN
760 770 780 790 800
NRKFLQNSYF MEPGSFIPGN PNLPPDEDVI DDDGDEDIND GFNQEKNMNN
810 820
SHSQMDFDGD QHMDDEFVSG RFEI
Length:824
Mass (Da):91,812
Last modified:September 5, 2006 - v3
Checksum:iBA84BE0F27143AB5
GO

Sequence cautioni

The sequence AAB69735 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti366I → S in CAA31073 (PubMed:3290050).Curated1
Sequence conflicti751N → K in CAA31073 (PubMed:3290050).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12560 Genomic DNA. Translation: CAA31073.1.
X57629 Genomic DNA. Translation: CAA40853.1.
U00029 Genomic DNA. Translation: AAB69735.1. Different initiation.
BK006934 Genomic DNA. Translation: DAA06898.1.
PIRiS48986.
RefSeqiNP_012075.1. NM_001179336.1.

Genome annotation databases

EnsemblFungiiYHR205W; YHR205W; YHR205W.
GeneIDi856612.
KEGGisce:YHR205W.

Similar proteinsi

Entry informationi

Entry nameiSCH9_YEAST
AccessioniPrimary (citable) accession number: P11792
Secondary accession number(s): D3DLF4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: September 5, 2006
Last modified: November 22, 2017
This is version 183 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-2 is the initiator.Curated

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