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UniProtKB/Swiss-Prot entry P38080


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AKL1_YEAST
Primary accession number P38080
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1994
Sequence was last modified on October 1, 1994 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 75)
Name and origin of the protein
Protein name Serine/threonine-protein kinase AKL1
Synonym EC 2.7.11.1
Gene name
Name: AKL1
OrderedLocusNames: YBR059C
ORFNames: YBR0519
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521; SER-1048 AND SER-1051, AND MASS SPECTROMETRY.
DOI=10.1038/nbt0302-301; PubMed=11875433 [NCBI, ExPASy, EBI, Israel, Japan]
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M.;
"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae.";
Nat. Biotechnol. 20:301-305(2002).
[3]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1048 AND SER-1051, UBIQUITINATION AT LYS-1008 AND LYS-1046, AND MASS SPECTROMETRY.
DOI=10.1038/nbt849; PubMed=12872131 [NCBI, ExPASy, EBI, Israel, Japan]
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.;
"A proteomics approach to understanding protein ubiquitination.";
Nat. Biotechnol. 21:921-926(2003).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541; SER-801 AND SER-1072, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518; SER-521; SER-879; SER-884; SER-960 AND SER-1072, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-12; SER-407; THR-471; SER-496; SER-501; SER-504; SER-511; SER-521; SER-533; THR-538; SER-541; SER-801; SER-846 AND SER-1072, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z35928; CAA85002.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S45917; S45917.
RefSeq NP_009615.1; -.
3D structure databases
ModBase P38080.
Protein-protein interaction databases
DIP DIP:1717N; -.
IntAct P38080; -.
Organism-specific databases
CYGD YBR059c; -.
SGD S000000263; AKL1.
Yeast-GFP YBR059C.
Gene expression databases
ArrayExpress P38080; -.
GermOnline YBR059C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005935; Cellular component: cellular bud neck (inferred from direct assay from SGD).
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0030036; Biological process: actin cytoskeleton organization (inferred from mutant phenotype from SGD).
GO:0030100; Biological process: regulation of endocytosis (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P38080.
Proteomic databases
PeptideAtlas P38080; -.
Genome annotation databases
Ensembl YBR059C; Saccharomyces cerevisiae. [Contig view]
GeneID 852351; -.
GenomeReviews Y13134_GR; YBR059C.
KEGG sce:YBR059C; -.
NMPDR fig|4932.3.peg.312; -.
Phylogenomic databases
HOGENOM P38080; -.
Other
LinkHub P38080; -.
ProtoNet P38080.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1108  1108     Serine/threonine-protein kinase AKL1. PRO_0000085603
DOMAIN   35    319  285     Protein kinase. 
NP_BIND   41     49  9     ATP (By similarity). 
ACT_SITE   181    181        Proton acceptor (By similarity). 
BINDING   70     70        ATP (By similarity). 
MOD_RES   10     10        Phosphoserine. 
MOD_RES   12     12        Phosphoserine. 
MOD_RES   407    407        Phosphoserine. 
MOD_RES   471    471        Phosphothreonine. 
MOD_RES   496    496        Phosphoserine. 
MOD_RES   501    501        Phosphoserine. 
MOD_RES   504    504        Phosphoserine. 
MOD_RES   511    511        Phosphoserine. 
MOD_RES   518    518        Phosphoserine. 
MOD_RES   521    521        Phosphoserine. 
MOD_RES   533    533        Phosphoserine. 
MOD_RES   538    538        Phosphothreonine. 
MOD_RES   541    541        Phosphoserine. 
MOD_RES   801    801        Phosphoserine. 
MOD_RES   846    846        Phosphoserine. 
MOD_RES   879    879        Phosphoserine. 
MOD_RES   884    884        Phosphoserine. 
MOD_RES   960    960        Phosphoserine. 
MOD_RES   1048   1048        Phosphoserine. 
MOD_RES   1051   1051        Phosphoserine. 
MOD_RES   1072   1072        Phosphoserine. 
CROSSLNK   1008   1008        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   1046   1046        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
Sequence information
Length: 1108 AA [This is the length of the unprocessed precursor] Molecular weight: 123989 Da [This is the MW of the unprocessed precursor] CRC64: AEC6CB0A707164E8 [This is a checksum on the sequence]
        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 

P38080 in FASTA format

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