Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein kinase ELM1

Gene

ELM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 SWE1.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei117 – 1171ATPPROSITE-ProRule annotation
Active sitei259 – 2591Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi94 – 1029ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • budding cell bud growth Source: SGD
  • cell morphogenesis Source: SGD
  • glucose metabolic process Source: SGD
  • mitotic cytokinesis Source: SGD
  • positive regulation of protein autophosphorylation Source: SGD
  • protein autophosphorylation Source: SGD
  • protein phosphorylation Source: SGD
  • pseudohyphal growth Source: SGD
  • response to drug Source: SGD
  • septin ring assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31849-MONOMER.
BRENDAi2.7.10.2. 984.
ReactomeiREACT_280487. CREB phosphorylation through the activation of CaMKK.
REACT_301208. AMPK inhibits chREBP transcriptional activation activity.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase ELM1 (EC:2.7.11.1)
Gene namesi
Name:ELM1
Ordered Locus Names:YKL048C
ORF Names:YKL261
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XI

Organism-specific databases

CYGDiYKL048c.
EuPathDBiFungiDB:YKL048C.
SGDiS000001531. ELM1.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi200 – 2001T → G: Allows selective inhibition in vivo. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 640640Serine/threonine-protein kinase ELM1PRO_0000085951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei152 – 1521Phosphoserine1 Publication
Modified residuei516 – 5161Phosphoserine1 Publication
Modified residuei519 – 5191Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32801.
PaxDbiP32801.
PeptideAtlasiP32801.
PRIDEiP32801.

Expressioni

Gene expression databases

GenevestigatoriP32801.

Interactioni

Protein-protein interaction databases

BioGridi34085. 393 interactions.
DIPiDIP-2731N.
IntActiP32801. 5 interactions.
MINTiMINT-691352.
STRINGi4932.YKL048C.

Structurei

3D structure databases

ProteinModelPortaliP32801.
SMRiP32801. Positions 80-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 420333Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000066096.
InParanoidiP32801.
OMAiELPFFGE.
OrthoDBiEOG7TQVBC.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32801-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPRQLIPTL IPEWAPLSQQ SCIREDELDS PPITPTSQTS SFGSSFSQQK
60 70 80 90 100
PTYSTIIGEN IHTILDEIRP YVKKITVSDQ DKKTINQYTL GVSAGSGQFG
110 120 130 140 150
YVRKAYSSTL GKVVAVKIIP KKPWNAQQYS VNQVMRQIQL WKSKGKITTN
160 170 180 190 200
MSGNEAMRLM NIEKCRWEIF AASRLRNNVH IVRLIECLDS PFSESIWIVT
210 220 230 240 250
NWCSLGELQW KRDDDEDILP QWKKIVISNC SVSTFAKKIL EDMTKGLEYL
260 270 280 290 300
HSQGCIHRDI KPSNILLDEE EKVAKLSDFG SCIFTPQSLP FSDANFEDCF
310 320 330 340 350
QRELNKIVGT PAFIAPELCH LGNSKRDFVT DGFKLDIWSL GVTLYCLLYN
360 370 380 390 400
ELPFFGENEF ETYHKIIEVS LSSKINGNTL NDLVIKRLLE KDVTLRISIQ
410 420 430 440 450
DLVKVLSRDQ PIDSRNHSQI SSSSVNPVRN EGPVRRFFGR LLTKKGKKKT
460 470 480 490 500
SGKGKDKVLV SATSKVTPSI HIDEEPDKEC FSTTVLRSSP DSSDYCSSLG
510 520 530 540 550
EEAIQVTDFL DTFCRSNESL PNLTVNNDKQ NSDMKTDRSE SSSHSSLKIP
560 570 580 590 600
TPIKAMIRLK SSPKENGNRT HINCSQDKPS SPLMDRTVGK RTVNNSGARK
610 620 630 640
LAHSSNILNF KAYINSEDSD IRETVEDVKT YLNFADNGQI
Length:640
Mass (Da):72,150
Last modified:June 1, 1994 - v2
Checksum:i33C3A7E188DF12C4
GO

Sequence cautioni

The sequence AAA02892.1 differs from that shown. Reason: Frameshift at position 539. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti390 – 3901E → Y in AAA02892 (PubMed:8395007).Curated
Sequence conflicti484 – 4852TV → SD in AAA02892 (PubMed:8395007).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS37869.
RefSeqiNP_012876.1. NM_001179614.1.

Genome annotation databases

EnsemblFungiiYKL048C; YKL048C; YKL048C.
GeneIDi853818.
KEGGisce:YKL048C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS37869.
RefSeqiNP_012876.1. NM_001179614.1.

3D structure databases

ProteinModelPortaliP32801.
SMRiP32801. Positions 80-439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34085. 393 interactions.
DIPiDIP-2731N.
IntActiP32801. 5 interactions.
MINTiMINT-691352.
STRINGi4932.YKL048C.

Proteomic databases

MaxQBiP32801.
PaxDbiP32801.
PeptideAtlasiP32801.
PRIDEiP32801.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL048C; YKL048C; YKL048C.
GeneIDi853818.
KEGGisce:YKL048C.

Organism-specific databases

CYGDiYKL048c.
EuPathDBiFungiDB:YKL048C.
SGDiS000001531. ELM1.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000066096.
InParanoidiP32801.
OMAiELPFFGE.
OrthoDBiEOG7TQVBC.

Enzyme and pathway databases

BioCyciYEAST:G3O-31849-MONOMER.
BRENDAi2.7.10.2. 984.
ReactomeiREACT_280487. CREB phosphorylation through the activation of CaMKK.
REACT_301208. AMPK inhibits chREBP transcriptional activation activity.

Miscellaneous databases

NextBioi974996.
PROiP32801.

Gene expression databases

GenevestigatoriP32801.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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].

Entry informationi

Entry nameiELM1_YEAST
AccessioniPrimary (citable) accession number: P32801
Secondary accession number(s): D6VXN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: June 1, 1994
Last modified: May 27, 2015
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 149 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.