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P38080 (AKL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase AKL1

EC=2.7.11.1
Gene names
Name:AKL1
Ordered Locus Names:YBR059C
ORF Names:YBR0519
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1108 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Miscellaneous

Present with 3000 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-9528,EBI-9528

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 11081107Serine/threonine-protein kinase AKL1
PRO_0000085603

Regions

Domain35 – 319285Protein kinase
Nucleotide binding41 – 499ATP By similarity

Sites

Active site1811Proton acceptor By similarity
Binding site701ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.8
Modified residue101Phosphoserine Ref.7
Modified residue4071Phosphoserine Ref.6 Ref.7
Modified residue4711Phosphothreonine Ref.6
Modified residue5041Phosphoserine Ref.6 Ref.7
Modified residue5411Phosphoserine Ref.5 Ref.6 Ref.7
Modified residue5741Phosphoserine Ref.7
Modified residue8011Phosphoserine Ref.5 Ref.7
Modified residue8461Phosphoserine Ref.6 Ref.7
Modified residue9531Phosphoserine Ref.7
Modified residue9601Phosphoserine Ref.7
Modified residue10481Phosphoserine Ref.7
Modified residue10721Phosphoserine Ref.5
Cross-link1008Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.4
Cross-link1046Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.4

Sequences

Sequence LengthMass (Da)Tools
P38080 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: AEC6CB0A707164E8

FASTA1,108123,989
        10         20         30         40         50         60 
MSITNGTSRS VSAMGHPAVE RYTPGHIVCV GTHKVEVVNY LAEGGFAQIY VVKFLEYLNE 

        70         80         90        100        110        120 
FDNTASVPLK IGDVACLKRV LVQDENGLNE MRNEVEVMKK LKGAPNIVQY FDSNASRRRD 

       130        140        150        160        170        180 
GVQGFEVLLL MELCPNKSLL DYMNQRLSTK LTEAEIVKIM YDVALSISQM HYLPVSLIHR 

       190        200        210        220        230        240 
DIKIENVLVD AKNNFKLADF GSTSTCFPIV TTHQDIALLT QNIYVHTTPQ YRSPEMIDLY 

       250        260        270        280        290        300 
RCLPINEKSD IWALGVFLYK LLFFTTPFEM TGQFAILHSK YEFPVNKYSS KLINLIIIML 

       310        320        330        340        350        360 
AENPNLRPNI YQVLYHLCEI LNVEVPIEDK YAEGAYNFSK YTQFQNKLQN VQLQMYQLQQ 

       370        380        390        400        410        420 
KKIMQNNKLS DSEENLLNDM FLSSFEISSK LPMNASDGHA AVSRIPSQNV GQELEEEKES 

       430        440        450        460        470        480 
QSDQRKSTLS EDKSSRTTSN ANSSGTANNP QEINTIQSPG IEDKSIFENK TPGELYYPSV 

       490        500        510        520        530        540 
SELDTYLDKE LVKQSSDPTI SEQSPRLNTQ SLPQRQKSTS SYSSGGRSMK STSYGAATIG 

       550        560        570        580        590        600 
SDEALANEKT AGINKMKQHK SNNPFPKMNV AYHSTNELSN DASNFFLEEQ QQGQRYQQAQ 

       610        620        630        640        650        660 
NQTGTQGNTF PDESQYQSRV EQQQQQQDQP KGPANYSQRN FYTGRDRSNK PMQLGGTIAG 

       670        680        690        700        710        720 
DSGNRRVNFQ NISQNYATNS QSGYLPSQNS PAIPMVRPVI SMNQQQAQQI QAQQLQAQQM 

       730        740        750        760        770        780 
QAKQQMQAKQ QMQVQQQLQV QQQMQIQNAN NNGTYVSDRT NHTTEDMRNA QGGEPPILAG 

       790        800        810        820        830        840 
NSANEPMHSS SKNEALLIEL SPLKEDAGKQ SFQDTNEPQT GGIEDAGGSG TIKGSNNNRN 

       850        860        870        880        890        900 
GVLNLSLNEM DLSRDDTGAA VSSFSSSSSS ASIQQAKLSG RKGSSKRNNY STDELGDSMV 

       910        920        930        940        950        960 
SSESIDIDLD DARRGKTAER RPLHNERGHK DQARSSDASK SNQFKSKDFS SVSTRQPRQS 

       970        980        990       1000       1010       1020 
LDLNFQEVNL SSPTLTQEHR NKNDSPAPNS HHSYRVSPHA STAITENKRH STGHELSTRS 

      1030       1040       1050       1060       1070       1080 
NGKHETHRTG SKQRHDLERY RHSKDKDSNS SITISTSTPS EMRKSFARAR QSLDLERVRR 

      1090       1100 
EAMASSASSS GGSNGKRRSF FSVFRSEK 

« Hide

References

« Hide 'large scale' references
[1]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"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].
[4]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1008 AND LYS-1046.
Strain: SUB592.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541; SER-801 AND SER-1072, 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-407; THR-471; SER-504; SER-541 AND SER-846, 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-10; SER-407; SER-504; SER-541; SER-574; SER-801; SER-846; SER-953; SER-960 AND SER-1048, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z35928 Genomic DNA. Translation: CAA85002.1.
BK006936 Genomic DNA. Translation: DAA07179.1.
PIRS45917.
RefSeqNP_009615.1. NM_001178407.1.

3D structure databases

ProteinModelPortalP38080.
SMRP38080. Positions 25-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32763. 143 interactions.
DIPDIP-1717N.
IntActP38080. 26 interactions.
MINTMINT-409952.
STRING4932.YBR059C.

Proteomic databases

MaxQBP38080.
PaxDbP38080.
PeptideAtlasP38080.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR059C; YBR059C; YBR059C.
GeneID852351.
KEGGsce:YBR059C.

Organism-specific databases

CYGDYBR059c.
SGDS000000263. AKL1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00510000046552.
KOK08286.
OMAQNIYVHT.
OrthoDBEOG74BK1F.

Enzyme and pathway databases

BioCycYEAST:G3O-29030-MONOMER.

Gene expression databases

GenevestigatorP38080.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971101.

Entry information

Entry nameAKL1_YEAST
AccessionPrimary (citable) accession number: P38080
Secondary accession number(s): D6VQ59
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 14, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families