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P25587 (LDB16_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Protein LDB16
Alternative name(s):
Low dye-binding protein 16
Gene names
Name:LDB16
Ordered Locus Names:YCL005W
ORF Names:YCL5W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in protein-linked oligosaccharide phosphorylation since the deletion reduces the negative charge of the cell surface. Ref.6

Subcellular location

Membrane; Multi-pass membrane protein. Lipid droplet Ref.4.

Miscellaneous

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

Ontologies

Keywords
   Cellular componentLipid droplet
Membrane
   DomainTransmembrane
Transmembrane helix
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lipid particle

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 256256Protein LDB16
PRO_0000202538

Regions

Transmembrane1 – 2121Helical; Potential
Transmembrane22 – 4221Helical; Potential
Topological domain43 – 7533Extracellular Potential
Transmembrane76 – 9621Helical; Potential
Topological domain97 – 256160Cytoplasmic Potential

Amino acid modifications

Modified residue1801Phosphothreonine Ref.10
Modified residue1841Phosphothreonine Ref.10
Modified residue2411Phosphoserine Ref.8 Ref.9 Ref.10

Sequences

Sequence LengthMass (Da)Tools
P25587 [UniParc].

Last modified May 16, 2003. Version 2.
Checksum: 49C8084FFCAF50E3

FASTA25629,024
        10         20         30         40         50         60 
MFVVDWSVQL CMGVISPLFR ALVQLPLSIF VWNGFQLVAL PINIPLRLFL GTSLSRLVAQ 

        70         80         90        100        110        120 
TSTLDFYVVL TLFQYFAVLC AFGSIIGLIF GFILGVFHSI CGVPSVYISL EWKRWFAPIR 

       130        140        150        160        170        180 
TVLERASTSI VNIMRGQTIA PIPMPKPNPT HISKPNMKKF HDEPGADDMT ITHDVNCYIT 

       190        200        210        220        230        240 
PCQTPTNEKI QHYNNDSFNT TTTDDEPTDI WDRSDTYQNS FVTNETLMSL SNRAKLRRNA 

       250 
SDADIVNIKI LRRNSR 

« Hide

References

« Hide 'large scale' references
[1]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Valles G., Volckaerts G.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"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.
[4]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"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].
[6]"A genome-wide screen for Saccharomyces cerevisiae nonessential genes involved in mannosyl phosphate transfer to mannoprotein-linked oligosaccharides."
Corbacho I., Olivero I., Hernandez L.M.
Fungal Genet. Biol. 42:773-790(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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 THR-180; THR-184 AND SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59720 Genomic DNA. Translation: CAC42965.1.
BK006937 Genomic DNA. Translation: DAA07475.1.
PIRS19390.
RefSeqNP_009922.2. NM_001178654.1.

3D structure databases

ProteinModelPortalP25587.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid30974. 7 interactions.
DIPDIP-5141N.
IntActP25587. 2 interactions.
MINTMINT-531438.
STRING4932.YCL005W.

Proteomic databases

PaxDbP25587.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL005W; YCL005W; YCL005W.
GeneID850351.
KEGGsce:YCL005W.

Organism-specific databases

CYGDYCL005w.
SGDS000000511. LDB16.

Phylogenomic databases

eggNOGNOG83696.
OrthoDBEOG7VX98H.

Enzyme and pathway databases

BioCycYEAST:G3O-29277-MONOMER.

Gene expression databases

GenevestigatorP25587.

Family and domain databases

ProtoNetSearch...

Other

NextBio965812.

Entry information

Entry nameLDB16_YEAST
AccessionPrimary (citable) accession number: P25587
Secondary accession number(s): D6VR06, Q8NIM5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 16, 2003
Last modified: May 14, 2014
This is version 86 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 III

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

Yeast

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