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P33399

- LHP1_YEAST

UniProt

P33399 - LHP1_YEAST

Protein

La protein homolog

Gene

LHP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Molecular chaperone that binds nascent RNA polymerase III transcripts, stabilizing these RNAs against exonucleases. Required for the 3' endonucleolytic cleavage that matures tRNA precursors and for efficient folding of certain pre-tRNAs. Cooperaes with GCD14 in the maturation of a subset of RNA polymerase III transcripts. Functions also in the assembly of certain RNA polymerase II-transcribed RNAs into RNPs. Binds and stabilizes newly synthesized U6 snRNA as well as precursors of U3 snRNA from degradation. Facilitates efficient Sm protein binding, thus assisting formation of the U4/U6 snRNP. Required fot Ty3 normal transposition frequency.16 Publications

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. protein binding Source: IntAct
    3. RNA binding Source: SGD
    4. tRNA binding Source: SGD

    GO - Biological processi

    1. tRNA processing Source: SGD

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29469-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    La protein homolog
    Alternative name(s):
    La autoantigen homolog
    La ribonucleoprotein
    Gene namesi
    Name:LHP1
    Synonyms:LAH1, YLA1
    Ordered Locus Names:YDL051W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDL051w.
    SGDiS000002209. LHP1.

    Subcellular locationi

    Nucleus 3 Publications
    Note: Imported into nucleus by the nuclear transport factor SXM1.

    GO - Cellular componenti

    1. nucleolus Source: SGD
    2. nucleoplasm Source: SGD
    3. nucleus Source: SGD
    4. ribonucleoprotein complex Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151S → A: Prevents phosphorylation; when associated with A-19 and A-235. 1 Publication
    Mutagenesisi19 – 191S → A: Prevents phosphorylation; when associated with A-15 and A-235. 1 Publication
    Mutagenesisi235 – 2351S → A: Prevents phosphorylation; when associated with A-15 and A-19. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 275274La protein homologPRO_0000207608Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei15 – 151Phosphoserine3 Publications
    Modified residuei19 – 191Phosphoserine6 Publications
    Modified residuei230 – 2301Phosphoserine1 Publication
    Modified residuei233 – 2331Phosphoserine1 Publication
    Modified residuei235 – 2351Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylation is not required for the roles tRNA and snRNP biogenesis.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP33399.
    PaxDbiP33399.
    PeptideAtlasiP33399.

    Expressioni

    Gene expression databases

    GenevestigatoriP33399.

    Interactioni

    Subunit structurei

    Interacts with SXM1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRP40P332032EBI-10046,EBI-701

    Protein-protein interaction databases

    BioGridi32008. 95 interactions.
    DIPiDIP-6444N.
    IntActiP33399. 19 interactions.
    MINTiMINT-652314.
    STRINGi4932.YDL051W.

    Structurei

    3D structure databases

    ProteinModelPortaliP33399.
    SMRiP33399. Positions 26-202.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 11290HTH La-type RNA-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini123 – 21694RRMPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi240 – 25617Nuclear localization signalSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 HTH La-type RNA-binding domain.PROSITE-ProRule annotation
    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5193.
    GeneTreeiENSGT00750000117664.
    KOiK11090.
    OMAiWVELKTI.
    OrthoDBiEOG7GXPPZ.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.30.70.330. 1 hit.
    InterProiIPR002344. Lupus_La.
    IPR006630. Lupus_La_RNA-bd.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF05383. La. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view]
    PRINTSiPR00302. LUPUSLA.
    SMARTiSM00715. LA. 1 hit.
    SM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50961. HTH_LA. 1 hit.
    PS50102. RRM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P33399-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEKPQQEEQ EKPQSRRNSF AVIEFTPEVL DRCLKQVEFY FSEFNFPYDR    50
    FLRTTAEKND GWVPISTIAT FNRMKKYRPV DKVIEALRSS EILEVSADGE 100
    NVKRRVPLDL TAARNARIEQ NQRTLAVMNF PHEDVEASQI PELQENLEAF 150
    FKKLGEINQV RLRRDHRNKK FNGTVLVEFK TIPECEAFLK SYSNDDESNE 200
    ILSYEGKKLS VLTKKQFDLQ REASKSKNFS GRSRSFNGHK KKNLPKFPKN 250
    KKKNGKEESK EDSSAIADDD EEHKE 275
    Length:275
    Mass (Da):32,104
    Last modified:October 1, 1994 - v2
    Checksum:i43CDB2E6C740978D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33023 Genomic DNA. Translation: AAA21777.1.
    Z74099 Genomic DNA. Translation: CAA98612.1.
    AY558373 Genomic DNA. Translation: AAS56699.1.
    L13282 Unassigned DNA. Translation: AAA16515.1.
    X80801 Genomic DNA. Translation: CAA56782.1.
    BK006938 Genomic DNA. Translation: DAA11805.1.
    PIRiB48600.
    RefSeqiNP_010232.1. NM_001180110.1.

    Genome annotation databases

    EnsemblFungiiYDL051W; YDL051W; YDL051W.
    GeneIDi851509.
    KEGGisce:YDL051W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33023 Genomic DNA. Translation: AAA21777.1 .
    Z74099 Genomic DNA. Translation: CAA98612.1 .
    AY558373 Genomic DNA. Translation: AAS56699.1 .
    L13282 Unassigned DNA. Translation: AAA16515.1 .
    X80801 Genomic DNA. Translation: CAA56782.1 .
    BK006938 Genomic DNA. Translation: DAA11805.1 .
    PIRi B48600.
    RefSeqi NP_010232.1. NM_001180110.1.

    3D structure databases

    ProteinModelPortali P33399.
    SMRi P33399. Positions 26-202.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32008. 95 interactions.
    DIPi DIP-6444N.
    IntActi P33399. 19 interactions.
    MINTi MINT-652314.
    STRINGi 4932.YDL051W.

    Proteomic databases

    MaxQBi P33399.
    PaxDbi P33399.
    PeptideAtlasi P33399.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL051W ; YDL051W ; YDL051W .
    GeneIDi 851509.
    KEGGi sce:YDL051W.

    Organism-specific databases

    CYGDi YDL051w.
    SGDi S000002209. LHP1.

    Phylogenomic databases

    eggNOGi COG5193.
    GeneTreei ENSGT00750000117664.
    KOi K11090.
    OMAi WVELKTI.
    OrthoDBi EOG7GXPPZ.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29469-MONOMER.

    Miscellaneous databases

    NextBioi 968869.

    Gene expression databases

    Genevestigatori P33399.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.30.70.330. 1 hit.
    InterProi IPR002344. Lupus_La.
    IPR006630. Lupus_La_RNA-bd.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF05383. La. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00302. LUPUSLA.
    SMARTi SM00715. LA. 1 hit.
    SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50961. HTH_LA. 1 hit.
    PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "La proteins from Drosophila melanogaster and Saccharomyces cerevisiae: a yeast homolog of the La autoantigen is dispensable for growth."
      Yoo C.J., Wolin S.L.
      Mol. Cell. Biol. 14:5412-5424(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
      Strain: YPH501.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "A yeast RNA binding protein that resembles the human autoantigen La."
      Lin-Marq N., Clarkson S.G.
      J. Mol. Biol. 245:81-85(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-275, CHARACTERIZATION.
    6. "A suppressor gene that enables Saccharomyces cerevisiae to grow without making sphingolipids encodes a protein that resembles an Escherichia coli fatty acyltransferase."
      Nagiec M.M., Wells G.B., Lester R.L., Dickson R.C.
      J. Biol. Chem. 268:22156-22163(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 1-252.
    7. "The yeast La protein is required for the 3' endonucleolytic cleavage that matures tRNA precursors."
      Yoo C.J., Wolin S.L.
      Cell 89:393-402(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "A nuclear import pathway for a protein involved in tRNA maturation."
      Rosenblum J.S., Pemberton L.F., Blobel G.
      J. Cell Biol. 139:1655-1661(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SXM1, FUNCTION, SUBCELLULAR LOCATION.
    9. "A role for the yeast La protein in U6 snRNP assembly: evidence that the La protein is a molecular chaperone for RNA polymerase III transcripts."
      Pannone B.K., Xue D., Wolin S.L.
      EMBO J. 17:7442-7453(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, U6 RNA-BINDING.
    10. "The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA."
      Anderson J., Phan L., Cuesta R., Carlson B.A., Pak M., Asano K., Bjoerk G.R., Tamame M., Hinnebusch A.G.
      Genes Dev. 12:3650-3662(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Nuclear import and the evolution of a multifunctional RNA-binding protein."
      Rosenblum J.S., Pemberton L.F., Bonifaci N., Blobel G.
      J. Cell Biol. 143:887-899(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SXM1, SUBCELLULAR LOCATION.
    12. "Assembly of 5S ribosomal RNA is required at a specific step of the pre-rRNA processing pathway."
      Dechampesme A.M., Koroleva O., Leger-Silvestre I., Gas N., Camier S.
      J. Cell Biol. 145:1369-1380(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    13. "Two yeast La motif-containing proteins are RNA-binding proteins that associate with polyribosomes."
      Sobel S.G., Wolin S.L.
      Mol. Biol. Cell 10:3849-3862(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "GCD14p, a repressor of GCN4 translation, cooperates with Gcd10p and Lhp1p in the maturation of initiator methionyl-tRNA in Saccharomyces cerevisiae."
      Calvo O., Cuesta R., Anderson J., Gutierrez N., Garcia-Barrio M.T., Hinnebusch A.G., Tamame M.
      Mol. Cell. Biol. 19:4167-4181(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "U snRNP assembly in yeast involves the La protein."
      Xue D., Rubinson D.A., Pannone B.K., Yoo C.J., Wolin S.L.
      EMBO J. 19:1650-1660(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    16. "Precursors to the U3 small nucleolar RNA lack small nucleolar RNP proteins but are stabilized by La binding."
      Kufel J., Allmang C., Chanfreau G., Petfalski E., Lafontaine D.L., Tollervey D.
      Mol. Cell. Biol. 20:5415-5424(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    17. "Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast La protein."
      Pannone B.K., Kim S.D., Noe D.A., Wolin S.L.
      Genetics 158:187-196(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Phosphorylation of the Saccharomyces cerevisiae La protein does not appear to be required for its functions in tRNA maturation and nascent RNA stabilization."
      Long K.S., Cedervall T., Walch-Solimena C., Noe D.A., Huddleston M.J., Annan R.S., Wolin S.L.
      RNA 7:1589-1602(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-15; SER-19 AND SER-235, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, MUTAGENESIS OF SER-15; SER-19 AND SER-235.
    19. "Lsm proteins are required for normal processing of pre-tRNAs and their efficient association with La-homologous protein Lhp1p."
      Kufel J., Allmang C., Verdone L., Beggs J.D., Tollervey D.
      Mol. Cell. Biol. 22:5248-5256(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    20. "A La protein requirement for efficient pre-tRNA folding."
      Chakshusmathi G., Kim S.D., Rubinson D.A., Wolin S.L.
      EMBO J. 22:6562-6572(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Ty3 requires yeast La homologous protein for wild-type frequencies of transposition."
      Aye M., Sandmeyer S.B.
      Mol. Microbiol. 49:501-515(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "A complex pathway for 3' processing of the yeast U3 snoRNA."
      Kufel J., Allmang C., Verdone L., Beggs J., Tollervey D.
      Nucleic Acids Res. 31:6788-6797(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Identification of Lhp1p-associated RNAs by microarray analysis in Saccharomyces cerevisiae reveals association with coding and noncoding RNAs."
      Inada M., Guthrie C.
      Proc. Natl. Acad. Sci. U.S.A. 101:434-439(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING.
    24. "Host factors that affect Ty3 retrotransposition in Saccharomyces cerevisiae."
      Aye M., Irwin B., Beliakova-Bethell N., Chen E., Garrus J., Sandmeyer S.
      Genetics 168:1159-1176(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
      Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
      Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    26. "The La protein functions redundantly with tRNA modification enzymes to ensure tRNA structural stability."
      Copela L.A., Chakshusmathi G., Sherrer R.L., Wolin S.L.
      RNA 12:644-654(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    27. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    28. "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-15; SER-19; SER-230; SER-233 AND SER-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "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-15 AND SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "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-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLHP1_YEAST
    AccessioniPrimary (citable) accession number: P33399
    Secondary accession number(s): D6VRU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

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

    External Data

    Dasty 3