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Q06147 (LCB5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. 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:
Sphingoid long chain base kinase 5

Short name=LCB kinase 5
EC=2.7.1.91
Alternative name(s):
Sphinganine kinase 5
Gene names
Name:LCB5
Ordered Locus Names:YLR260W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length687 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of the sphingoid long chain bases dihydrosphingosine (DHS or sphinganine) and phytosphingosine (PHS) to form dihydrosphingosine 1-phosphate (DHS-1P) and phytosphingosine 1-phosphate (PHS-1P) respectively. Redundant to LCB4, is only responsible for few percent of the total activity. Involved in the biosynthesis of sphingolipids and ceramides. Involved in heat-induced transient cell cycle arrest. Accumulation of phosphorylated sphingoid long chain bases (LCBPs) stimulates calcium influx and activates calcineurin signaling. Involved in heat-stress resistance. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7

Catalytic activity

ATP + sphinganine = ADP + sphinganine 1-phosphate.

ATP + phytosphingosine = ADP + phytosphingosine 1-phosphate.

Subcellular location

Golgi apparatus membrane; Peripheral membrane protein Ref.7.

Miscellaneous

Present with 1760 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 DAGKc domain.

Biophysicochemical properties

Kinetic parameters:

KM=2 µM for dihydrosphingosine Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 687687Sphingoid long chain base kinase 5
PRO_0000255957

Regions

Domain266 – 405140DAGKc
Nucleotide binding276 – 2783ATP By similarity
Nucleotide binding366 – 3683ATP By similarity
Nucleotide binding652 – 6543ATP By similarity
Region333 – 3364Substrate binding By similarity

Sites

Active site3351Proton donor/acceptor By similarity
Binding site3081ATP By similarity
Binding site3401ATP By similarity
Binding site4341ATP By similarity
Binding site4401ATP By similarity

Amino acid modifications

Lipidation911S-palmitoyl cysteine By similarity
Lipidation941S-palmitoyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q06147 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 205C32F3570042FA

FASTA68777,566
        10         20         30         40         50         60 
MTLKPSKRRK GRSRHSRKKQ ITSAILTEEG IMIKAKPSSP YTYANRMADK RSRSSIDNIS 

        70         80         90        100        110        120 
RTSFQSNISR TSFQSNSDNN SIFETASLIS CVTCLSDTDT IDRSETSTTD TSKDDLSANP 

       130        140        150        160        170        180 
KLHYPSVNGQ LPANTVIPYG RILDARYIEK EPLHYYDANS SPSSPLSSSM SNISEKCDLD 

       190        200        210        220        230        240 
ELESSQKKER KGNSLSRGSN SSSSLLTSRS PFTKLVEVIF ARPRRHDVVP KRVSLYIDYK 

       250        260        270        280        290        300 
PHSSSHLKEE DDLVEEILKR SYKNTRRNKS IFVIINPFGG KGKAKKLFMT KAKPLLLASR 

       310        320        330        340        350        360 
CSIEVVYTKY PGHAIEIARE MDIDKYDTIA CASGDGIPHE VINGLYQRPD HVKAFNNIAI 

       370        380        390        400        410        420 
TEIPCGSGNA MSVSCHWTNN PSYSTLCLIK SIETRIDLMC CSQPSYAREH PKLSFLSQTY 

       430        440        450        460        470        480 
GLIAETDINT EFIRWMGPAR FELGVAFNII QKKKYPCEIY VKYAAKSKNE LKNHYLEHKN 

       490        500        510        520        530        540 
KGSLEFQHIT MNKDNEDCDN YNYENEYETE NEDEDEDADA DDEDSHLISR DLADSSADQI 

       550        560        570        580        590        600 
KEEDFKIKYP LDEGIPSDWE RLDPNISNNL GIFYTGKMPY VAADTKFFPA ALPSDGTMDM 

       610        620        630        640        650        660 
VITDARTSLT RMAPILLGLD KGSHVLQPEV LHSKILAYKI IPKLGNGLFS VDGEKFPLEP 

       670        680 
LQVEIMPRLC KTLLRNGRYV DTDFDSM 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [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]"The LCB4 (YOR171c) and LCB5 (YLR260w) genes of Saccharomyces encode sphingoid long chain base kinases."
Nagiec M.M., Skrzypek M.S., Nagiec E.E., Lester R.L., Dickson R.C.
J. Biol. Chem. 273:19437-19442(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]"Accumulation of phosphorylated sphingoid long chain bases results in cell growth inhibition in Saccharomyces cerevisiae."
Kim S., Fyrst H., Saba J.D.
Genetics 156:1519-1529(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Role for de novo sphingoid base biosynthesis in the heat-induced transient cell cycle arrest of Saccharomyces cerevisiae."
Jenkins G.M., Hannun Y.A.
J. Biol. Chem. 276:8574-8581(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Calcium influx and signaling in yeast stimulated by intracellular sphingosine 1-phosphate accumulation."
Birchwood C.J., Saba J.D., Dickson R.C., Cunningham K.W.
J. Biol. Chem. 276:11712-11718(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Lcb4p is a key regulator of ceramide synthesis from exogenous long chain sphingoid base in Saccharomyces cerevisiae."
Funato K., Lombardi R., Vallee B., Riezman H.
J. Biol. Chem. 278:7325-7334(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"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].
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U17244 Genomic DNA. Translation: AAB67377.1.
BK006945 Genomic DNA. Translation: DAA09573.1.
PIRS51398.
RefSeqNP_013361.1. NM_001182147.1.

3D structure databases

ProteinModelPortalQ06147.
SMRQ06147. Positions 265-674.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31528. 134 interactions.
IntActQ06147. 1 interaction.
MINTMINT-2784711.
STRING4932.YLR260W.

Proteomic databases

PaxDbQ06147.
PeptideAtlasQ06147.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR260W; YLR260W; YLR260W.
GeneID850964.
KEGGsce:YLR260W.

Organism-specific databases

CYGDYLR260w.
SGDS000004250. LCB5.

Phylogenomic databases

eggNOGCOG1597.
GeneTreeENSGT00690000101761.
HOGENOMHOG000207396.
KOK04718.
OMAISRTSFQ.
OrthoDBEOG7KH9TK.

Enzyme and pathway databases

BioCycMetaCyc:YLR260W-MONOMER.
YEAST:YLR260W-MONOMER.

Gene expression databases

GenevestigatorQ06147.

Family and domain databases

InterProIPR016064. ATP-NAD_kinase_PpnK-typ.
IPR001206. Diacylglycerol_kinase_cat_dom.
[Graphical view]
PfamPF00781. DAGK_cat. 1 hit.
[Graphical view]
SMARTSM00046. DAGKc. 1 hit.
[Graphical view]
SUPFAMSSF111331. SSF111331. 2 hits.
PROSITEPS50146. DAGK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio967451.

Entry information

Entry nameLCB5_YEAST
AccessionPrimary (citable) accession number: Q06147
Secondary accession number(s): D6VYQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families