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Protein

La protein homolog

Gene

LHP1

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

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

  • nucleotide binding Source: InterPro
  • RNA binding Source: SGD
  • tRNA binding Source: SGD

GO - Biological processi

  • tRNA processing Source: SGD
Complete GO annotation...

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 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDL051w.
EuPathDBiFungiDB:YDL051W.
SGDiS000002209. LHP1.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: SGD
  • nucleoplasm Source: SGD
  • nucleus Source: SGD
  • ribonucleoprotein complex Source: InterPro
Complete GO annotation...

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 residuei104 – 1041Omega-N-methylarginine1 Publication
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.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP33399.
PaxDbiP33399.
PeptideAtlasiP33399.

Interactioni

Subunit structurei

Interacts with SXM1.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi32008. 99 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.
GeneTreeiENSGT00790000123043.
InParanoidiP33399.
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

        10         20         30         40         50
MSEKPQQEEQ EKPQSRRNSF AVIEFTPEVL DRCLKQVEFY FSEFNFPYDR
60 70 80 90 100
FLRTTAEKND GWVPISTIAT FNRMKKYRPV DKVIEALRSS EILEVSADGE
110 120 130 140 150
NVKRRVPLDL TAARNARIEQ NQRTLAVMNF PHEDVEASQI PELQENLEAF
160 170 180 190 200
FKKLGEINQV RLRRDHRNKK FNGTVLVEFK TIPECEAFLK SYSNDDESNE
210 220 230 240 250
ILSYEGKKLS VLTKKQFDLQ REASKSKNFS GRSRSFNGHK KKNLPKFPKN
260 270
KKKNGKEESK EDSSAIADDD EEHKE
Length:275
Mass (Da):32,104
Last modified:October 1, 1994 - v2
Checksum:i43CDB2E6C740978D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi32008. 99 interactions.
DIPiDIP-6444N.
IntActiP33399. 19 interactions.
MINTiMINT-652314.
STRINGi4932.YDL051W.

Proteomic databases

MaxQBiP33399.
PaxDbiP33399.
PeptideAtlasiP33399.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYDL051w.
EuPathDBiFungiDB:YDL051W.
SGDiS000002209. LHP1.

Phylogenomic databases

eggNOGiCOG5193.
GeneTreeiENSGT00790000123043.
InParanoidiP33399.
KOiK11090.
OMAiWVELKTI.
OrthoDBiEOG7GXPPZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29469-MONOMER.

Miscellaneous databases

NextBioi968869.
PROiP33399.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
  32. "Analysis of the proteome of Saccharomyces cerevisiae for methylarginine."
    Low J.K., Hart-Smith G., Erce M.A., Wilkins M.R.
    J. Proteome Res. 12:3884-3899(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-104.

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: June 24, 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

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

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.