P32801 (ELM1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase ELM1
EC=2.7.11.1

Gene names

Name:	ELM1
Ordered Locus Names:	YKL048C
ORF Names:	YKL261

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	640 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Important role in G1 events required for bud emergence and septin organization. Coordinates cell growth and cell division at G2/M, essential for efficient cytokinesis and for regulation of SWE1. Ref.1 Ref.5
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Miscellaneous	Present with 149 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.
Sequence caution	The sequence AAA02892.1 differs from that shown. Reason: Frameshift at position 539.

Ontologies

Keywords
Biological process	Cell cycle
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axial cellular bud site selection Traceable author statement PubMed 10652251. Source: SGD budding cell bud growth Inferred from mutant phenotype PubMed 10234786. Source: SGD cell morphogenesis Inferred from mutant phenotype PubMed 16607009PubMed 9427410. Source: SGD glucose metabolic process Inferred from mutant phenotype PubMed 15340085. Source: SGD positive regulation of protein autophosphorylation Inferred from mutant phenotype PubMed 16861226. Source: SGD protein autophosphorylation Inferred from direct assay PubMed 16861226. Source: SGD pseudohyphal growth Inferred from mutant phenotype PubMed 9891070. Source: SGD response to drug Inferred from mutant phenotype PubMed 16751665. Source: SGD response to osmotic stress Traceable author statement PubMed 10652251. Source: SGD septin checkpoint Traceable author statement PubMed 10725226. Source: SGD
Cellular_component	cellular bud neck contractile ring Traceable author statement PubMed 10652251. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay PubMed 12847291PubMed 16201971PubMed 9180279. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 640	640	Serine/threonine-protein kinase ELM1		PRO_0000085951
Regions
	Domain	88 – 420	333	Protein kinase
	Nucleotide binding	94 – 102	9	ATP By similarity
Sites
	Active site	259	1	Proton acceptor By similarity
	Binding site	117	1	ATP By similarity
Amino acid modifications
	Modified residue	152	1	Phosphoserine Ref.7
	Modified residue	519	1	Phosphoserine Ref.7
Experimental info
	Mutagenesis	200	1	T → G: Allows selective inhibition in vivo. Ref.5
	Sequence conflict	390	1	E → Y in AAA02892. Ref.1
	Sequence conflict	484 – 485	2	TV → SD in AAA02892. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P32801 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: 33C3A7E188DF12C4	FASTA	640	72,150
	10 20 30 40 50 60 MSPRQLIPTL IPEWAPLSQQ SCIREDELDS PPITPTSQTS SFGSSFSQQK PTYSTIIGEN 70 80 90 100 110 120 IHTILDEIRP YVKKITVSDQ DKKTINQYTL GVSAGSGQFG YVRKAYSSTL GKVVAVKIIP 130 140 150 160 170 180 KKPWNAQQYS VNQVMRQIQL WKSKGKITTN MSGNEAMRLM NIEKCRWEIF AASRLRNNVH 190 200 210 220 230 240 IVRLIECLDS PFSESIWIVT NWCSLGELQW KRDDDEDILP QWKKIVISNC SVSTFAKKIL 250 260 270 280 290 300 EDMTKGLEYL HSQGCIHRDI KPSNILLDEE EKVAKLSDFG SCIFTPQSLP FSDANFEDCF 310 320 330 340 350 360 QRELNKIVGT PAFIAPELCH LGNSKRDFVT DGFKLDIWSL GVTLYCLLYN ELPFFGENEF 370 380 390 400 410 420 ETYHKIIEVS LSSKINGNTL NDLVIKRLLE KDVTLRISIQ DLVKVLSRDQ PIDSRNHSQI 430 440 450 460 470 480 SSSSVNPVRN EGPVRRFFGR LLTKKGKKKT SGKGKDKVLV SATSKVTPSI HIDEEPDKEC 490 500 510 520 530 540 FSTTVLRSSP DSSDYCSSLG EEAIQVTDFL DTFCRSNESL PNLTVNNDKQ NSDMKTDRSE 550 560 570 580 590 600 SSSHSSLKIP TPIKAMIRLK SSPKENGNRT HINCSQDKPS SPLMDRTVGK RTVNNSGARK 610 620 630 640 LAHSSNILNF KAYINSEDSD IRETVEDVKT YLNFADNGQI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulation of dimorphism in Saccharomyces cerevisiae: involvement of the novel protein kinase homolog Elm1p and protein phosphatase 2A." Blacketer M.J., Koehler C.M., Coats S.G., Myers A.M., Madaule P. Mol. Cell. Biol. 13:5567-5581(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, FUNCTION.
[2]	"The sequence of a 17.5 kb DNA fragment on the left arm of yeast chromosome XI identifies the protein kinase gene ELM1, the DNA primase gene PRI2, a new gene encoding a putative histone and seven new open reading frames." Purnelle B., Tettelin H., van Dyck L., Skala J., Goffeau A. Yeast 9:1379-1384(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Specific inhibition of Elm1 kinase activity reveals functions required for early G1 events." Sreenivasan A., Bishop A.C., Shokat K.M., Kellogg D.R. Mol. Cell. Biol. 23:6327-6337(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF THR-200.
[6]	"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].
[7]	"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-152 AND SER-519, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M81258 Unassigned DNA. Translation: AAA02892.1. Frameshift. X71621 Genomic DNA. No translation available. Z28048 Genomic DNA. Translation: CAA81883.1. BK006944 Genomic DNA. Translation: DAA09109.1.
PIR	S37869.
RefSeq	NP_012876.1. NM_001179614.1.
3D structure databases
ProteinModelPortal	P32801.
SMR	P32801. Positions 80-448.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2731N.
IntAct	P32801. 6 interactions.
MINT	MINT-691352.
STRING	4932.YKL048C.
Proteomic databases
PaxDb	P32801.
PeptideAtlas	P32801.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKL048C; YKL048C; YKL048C.
GeneID	853818.
KEGG	sce:YKL048C.
Organism-specific databases
CYGD	YKL048c.
SGD	S000001531. ELM1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00700000106221.
HOGENOM	HOG000066096.
KO	K00924.
OMA	ELPFFGE.
OrthoDB	EOG4T7CCH.
Enzyme and pathway databases
BRENDA	2.7.10.2. 984.
Gene expression databases
Genevestigator	P32801.
GermOnline	YKL048C. 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	974996.

Entry information

Entry name

ELM1_YEAST

Accession

Primary (citable) accession number: P32801
Secondary accession number(s): D6VXN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program