Serine/threonine-protein kinase AKL1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38080 (AKL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 118. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase AKL1
EC=2.7.11.1

Gene names

Name:	AKL1
Ordered Locus Names:	YBR059C
ORF Names:	YBR0519

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	1108 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from mutant phenotype PubMed 12956961. Source: SGD regulation of endocytosis Inferred from mutant phenotype PubMed 12956961. Source: SGD
Cellular_component	cellular bud neck Inferred from direct assay PubMed 14562095. Source: SGD cytoplasm Inferred from direct assay PubMed 14562095. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase activity Inferred from direct assay PubMed 16319894. Source: SGD protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-9528,EBI-9528

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1108

1108

Serine/threonine-protein kinase AKL1

PRO_0000085603

Regions

Domain

35 – 319

285

Protein kinase

Nucleotide binding

41 – 49

ATP By similarity

Sites

Active site

181

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.9

Modified residue

Phosphoserine Ref.9

Modified residue

407

Phosphoserine Ref.9

Modified residue

471

Phosphothreonine Ref.9

Modified residue

496

Phosphoserine Ref.9

Modified residue

501

Phosphoserine Ref.9

Modified residue

504

Phosphoserine Ref.7 Ref.9

Modified residue

511

Phosphoserine Ref.9

Modified residue

518

Phosphoserine Ref.8

Modified residue

521

Phosphoserine Ref.3 Ref.8 Ref.9

Modified residue

533

Phosphoserine Ref.9

Modified residue

538

Phosphothreonine Ref.9

Modified residue

541

Phosphoserine Ref.6 Ref.9

Modified residue

801

Phosphoserine Ref.6 Ref.9

Modified residue

846

Phosphoserine Ref.9

Modified residue

879

Phosphoserine Ref.8

Modified residue

884

Phosphoserine Ref.8

Modified residue

960

Phosphoserine Ref.8

Modified residue

1048

Phosphoserine Ref.3 Ref.5

Modified residue

1051

Phosphoserine Ref.3 Ref.5

Modified residue

1072

Phosphoserine Ref.6 Ref.8 Ref.9

Cross-link

1008

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Cross-link

1046

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P38080 [UniParc].

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

FASTA

1,108

123,989

        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' referencesShow '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. 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521; SER-1048 AND SER-1051, MASS SPECTROMETRY. Strain: 2124.
[4]	"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].
[5]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1048 AND SER-1051, UBIQUITINATION AT LYS-1008 AND LYS-1046, MASS SPECTROMETRY. Strain: SUB592.
[6]	"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, MASS SPECTROMETRY. Strain: ADR376.
[7]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." 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. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504, MASS SPECTROMETRY.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518; SER-521; SER-879; SER-884; SER-960 AND SER-1072, MASS SPECTROMETRY.
[9]	"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-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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z35928 Genomic DNA. Translation: CAA85002.1. BK006936 Genomic DNA. Translation: DAA07179.1.
PIR	S45917.
RefSeq	NP_009615.1. NM_001178407.1.
3D structure databases
ProteinModelPortal	P38080.
SMR	P38080. Positions 25-365.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1717N.
IntAct	P38080. 27 interactions.
MINT	MINT-409952.
STRING	4932.YBR059C.
Proteomic databases
PaxDb	P38080.
PeptideAtlas	P38080.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBR059C; YBR059C; YBR059C.
GeneID	852351.
KEGG	sce:YBR059C.
Organism-specific databases
CYGD	YBR059c.
SGD	S000000263. AKL1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00510000046552.
KO	K08286.
OMA	QNIYVHT.
OrthoDB	EOG4NCQNG.
Gene expression databases
Genevestigator	P38080.
GermOnline	YBR059C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	971101.

Entry information

Entry name

AKL1_YEAST

Accession

Primary (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 1, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome II

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents