Reviewed, UniProtKB/Swiss-Prot P38080 (AKL1_YEAST)

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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1108 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Ref.3
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
Gene Ontology (GO)
Biological process	actin cytoskeleton organization Inferred from mutant phenotype. Source: SGD protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro regulation of endocytosis Inferred from mutant phenotype. Source: SGD
Cellular component	cellular bud neck Inferred from direct assay. Source: SGD cytoplasm Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction. Source: IntAct 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
	P38800	1	EBI-9528,EBI-24597
HTS1	P07263	1	EBI-9528,EBI-18711
SKI8	Q02793	1	EBI-9528,EBI-17260
TRM9	P49957	1	EBI-9528,EBI-27735

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	9	ATP By similarity
Sites
	Active site	181	1	Proton acceptor By similarity
	Binding site	70	1	ATP By similarity
Amino acid modifications
	Modified residue	10	1	Phosphoserine Ref.8
	Modified residue	12	1	Phosphoserine Ref.8
	Modified residue	407	1	Phosphoserine Ref.8
	Modified residue	471	1	Phosphothreonine Ref.8
	Modified residue	496	1	Phosphoserine Ref.8
	Modified residue	501	1	Phosphoserine Ref.8
	Modified residue	504	1	Phosphoserine Ref.8 Ref.6
	Modified residue	511	1	Phosphoserine Ref.8
	Modified residue	518	1	Phosphoserine Ref.7
	Modified residue	521	1	Phosphoserine Ref.8 Ref.7 Ref.2
	Modified residue	533	1	Phosphoserine Ref.8
	Modified residue	538	1	Phosphothreonine Ref.8
	Modified residue	541	1	Phosphoserine Ref.8 Ref.5
	Modified residue	801	1	Phosphoserine Ref.8 Ref.5
	Modified residue	846	1	Phosphoserine Ref.8
	Modified residue	879	1	Phosphoserine Ref.7
	Modified residue	884	1	Phosphoserine Ref.7
	Modified residue	960	1	Phosphoserine Ref.7
	Modified residue	1048	1	Phosphoserine Ref.2 Ref.4
	Modified residue	1051	1	Phosphoserine Ref.2 Ref.4
	Modified residue	1072	1	Phosphoserine Ref.8 Ref.7 Ref.5
	Cross-link	1008		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.4
	Cross-link	1046		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P38080-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: AEC6CB0A707164E8	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

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. , 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: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"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: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521; SER-1048 AND SER-1051, MASS SPECTROMETRY.
[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: 14562106] [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: 12872131] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1048 AND SER-1051, UBIQUITINATION AT LYS-1008 AND LYS-1046, MASS SPECTROMETRY.
[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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541; SER-801 AND SER-1072, MASS SPECTROMETRY.
[6]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504, MASS SPECTROMETRY.
[7]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518; SER-521; SER-879; SER-884; SER-960 AND SER-1072, MASS SPECTROMETRY.
[8]	"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: 18407956] [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
EMBLGenBankDDBJ	Z35928 Genomic DNA. Translation: CAA85002.1.
PIR	S45917.
RefSeq	NP_009615.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1717N.
IntAct	P38080. 18 interactions.
Proteomic databases
PeptideAtlas	P38080.
Genome annotation databases
Ensembl	YBR059C. Saccharomyces cerevisiae. [Contig view]
GeneID	852351.
GenomeReviews	Gene locus YBR059C in contig Y13134_GR.
KEGG	sce:YBR059C.
NMPDR	fig|4932.3.peg.312.
Organism-specific databases
CYGD	YBR059c.
SGD	S000000263. AKL1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P38080.
OMA	P38080. LNEMRNE.
Enzyme and pathway databases
BRENDA	2.7.11.1. 250.
Gene expression databases
ArrayExpress	P38080.
GermOnline	YBR059C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	971101.

Entry information

Entry name

AKL1_YEAST

Accession

Primary (citable) accession number: P38080

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)