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P32801 (ELM1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 138. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase ELM1

EC=2.7.11.1
Gene names
Name:ELM1
Ordered Locus Names:YKL048C
ORF Names:YKL261
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length640 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processCell cycle
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxial 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

cytokinesis checkpoint

Traceable author statement PubMed 10725226. Source: SGD

glucose metabolic process

Inferred from mutant phenotype PubMed 15340085. Source: SGD

positive regulation of protein autophosphorylation

Inferred from direct assay PubMed 16861226. Source: SGD

protein autophosphorylation

Inferred from direct assay PubMed 16861226. Source: SGD

protein phosphorylation

Inferred from direct assay PubMed 12847291PubMed 16201971PubMed 9180279. 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

   Cellular_componentcellular bud neck contractile ring

Traceable author statement PubMed 10652251. Source: SGD

   Molecular_functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 640640Serine/threonine-protein kinase ELM1
PRO_0000085951

Regions

Domain88 – 420333Protein kinase
Nucleotide binding94 – 1029ATP By similarity

Sites

Active site2591Proton acceptor By similarity
Binding site1171ATP By similarity

Amino acid modifications

Modified residue1521Phosphoserine Ref.7
Modified residue5161Phosphoserine Ref.8
Modified residue5191Phosphoserine Ref.7 Ref.8

Experimental info

Mutagenesis2001T → G: Allows selective inhibition in vivo. Ref.5
Sequence conflict3901E → Y in AAA02892. Ref.1
Sequence conflict484 – 4852TV → SD in AAA02892. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P32801 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 33C3A7E188DF12C4

FASTA64072,150
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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]"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.
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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-516 AND SER-519, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRS37869.
RefSeqNP_012876.1. NM_001179614.1.

3D structure databases

ProteinModelPortalP32801.
SMRP32801. Positions 80-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34085. 392 interactions.
DIPDIP-2731N.
IntActP32801. 5 interactions.
MINTMINT-691352.
STRING4932.YKL048C.

Proteomic databases

MaxQBP32801.
PaxDbP32801.
PeptideAtlasP32801.
PRIDEP32801.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL048C; YKL048C; YKL048C.
GeneID853818.
KEGGsce:YKL048C.

Organism-specific databases

CYGDYKL048c.
SGDS000001531. ELM1.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000066096.
KOK00924.
OMAELPFFGE.
OrthoDBEOG7TQVBC.

Enzyme and pathway databases

BioCycYEAST:G3O-31849-MONOMER.
BRENDA2.7.10.2. 984.

Gene expression databases

GenevestigatorP32801.

Family and domain databases

InterProIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR24347. PTHR24347. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio974996.
PROP32801.

Entry information

Entry nameELM1_YEAST
AccessionPrimary (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: June 11, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families