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P33399 (LHP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
La protein homolog
Alternative name(s):
La autoantigen homolog
La ribonucleoprotein
Gene names
Name:LHP1
Synonyms:LAH1, YLA1
Ordered Locus Names:YDL051W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.26

Subunit structure

Interacts with SXM1. Ref.8 Ref.11

Subcellular location

Nucleus. Note: Imported into nucleus by the nuclear transport factor SXM1. Ref.8 Ref.11 Ref.13

Post-translational modification

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

Sequence similarities

Contains 1 HTH La-type RNA-binding domain.

Contains 1 RRM (RNA recognition motif) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRP40P332032EBI-10046,EBI-701

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.31
Chain2 – 275274La protein homolog
PRO_0000207608

Regions

Domain23 – 11290HTH La-type RNA-binding
Domain123 – 21694RRM
Motif240 – 25617Nuclear localization signal Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.31
Modified residue151Phosphoserine Ref.18 Ref.28 Ref.29
Modified residue191Phosphoserine Ref.18 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30
Modified residue2301Phosphoserine Ref.28
Modified residue2331Phosphoserine Ref.28
Modified residue2351Phosphoserine Ref.18 Ref.28

Experimental info

Mutagenesis151S → A: Prevents phosphorylation; when associated with A-19 and A-235. Ref.18
Mutagenesis191S → A: Prevents phosphorylation; when associated with A-15 and A-235. Ref.18
Mutagenesis2351S → A: Prevents phosphorylation; when associated with A-15 and A-19. Ref.18

Sequences

Sequence LengthMass (Da)Tools
P33399 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 43CDB2E6C740978D

FASTA27532,104
        10         20         30         40         50         60 
MSEKPQQEEQ EKPQSRRNSF AVIEFTPEVL DRCLKQVEFY FSEFNFPYDR FLRTTAEKND 

        70         80         90        100        110        120 
GWVPISTIAT FNRMKKYRPV DKVIEALRSS EILEVSADGE NVKRRVPLDL TAARNARIEQ 

       130        140        150        160        170        180 
NQRTLAVMNF PHEDVEASQI PELQENLEAF FKKLGEINQV RLRRDHRNKK FNGTVLVEFK 

       190        200        210        220        230        240 
TIPECEAFLK SYSNDDESNE ILSYEGKKLS VLTKKQFDLQ REASKSKNFS GRSRSFNGHK 

       250        260        270 
KKNLPKFPKN KKKNGKEESK EDSSAIADDD EEHKE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB48600.
RefSeqNP_010232.1. NM_001180110.1.

3D structure databases

ProteinModelPortalP33399.
SMRP33399. Positions 26-202.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32008. 95 interactions.
DIPDIP-6444N.
IntActP33399. 19 interactions.
MINTMINT-652314.
STRING4932.YDL051W.

Proteomic databases

MaxQBP33399.
PaxDbP33399.
PeptideAtlasP33399.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL051W; YDL051W; YDL051W.
GeneID851509.
KEGGsce:YDL051W.

Organism-specific databases

CYGDYDL051w.
SGDS000002209. LHP1.

Phylogenomic databases

eggNOGCOG5193.
GeneTreeENSGT00750000117664.
KOK11090.
OMAWVELKTI.
OrthoDBEOG7GXPPZ.

Enzyme and pathway databases

BioCycYEAST:G3O-29469-MONOMER.

Gene expression databases

GenevestigatorP33399.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
3.30.70.330. 1 hit.
InterProIPR002344. Lupus_La.
IPR006630. Lupus_La_RNA-bd.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF05383. La. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PRINTSPR00302. LUPUSLA.
SMARTSM00715. LA. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50961. HTH_LA. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968869.

Entry information

Entry nameLHP1_YEAST
AccessionPrimary (citable) accession number: P33399
Secondary accession number(s): D6VRU5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 1, 1994
Last modified: July 9, 2014
This is version 136 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 IV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families