LHP1_YEAST - dbPTM
LHP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LHP1_YEAST
UniProt AC P33399
Protein Name La protein homolog
Gene Name LHP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 275
Subcellular Localization Nucleus . Imported into nucleus by the nuclear transport factor SXM1.
Protein Description 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..
Protein Sequence MSEKPQQEEQEKPQSRRNSFAVIEFTPEVLDRCLKQVEFYFSEFNFPYDRFLRTTAEKNDGWVPISTIATFNRMKKYRPVDKVIEALRSSEILEVSADGENVKRRVPLDLTAARNARIEQNQRTLAVMNFPHEDVEASQIPELQENLEAFFKKLGEINQVRLRRDHRNKKFNGTVLVEFKTIPECEAFLKSYSNDDESNEILSYEGKKLSVLTKKQFDLQREASKSKNFSGRSRSFNGHKKKNLPKFPKNKKKNGKEESKEDSSAIADDDEEHKE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSEKPQQEE
------CCCCHHHHH
55.0922369663
2Acetylation------MSEKPQQEE
------CCCCHHHHH
55.0922814378
15PhosphorylationEEQEKPQSRRNSFAV
HHHHCCCHHHHCEEE
41.5622369663
19PhosphorylationKPQSRRNSFAVIEFT
CCCHHHHCEEEEEEC
16.8722369663
26PhosphorylationSFAVIEFTPEVLDRC
CEEEEEECHHHHHHH
13.0220377248
58AcetylationFLRTTAEKNDGWVPI
HHHHHCHHCCCEEEH
58.8524489116
76AcetylationATFNRMKKYRPVDKV
HCHHCCHHCCCHHHH
36.8325381059
82AcetylationKKYRPVDKVIEALRS
HHCCCHHHHHHHHHC
45.4024489116
103UbiquitinationSADGENVKRRVPLDL
CCCCCCCCCCCCCCH
46.1722817900
104MethylationADGENVKRRVPLDLT
CCCCCCCCCCCCCHH
40.3123865587
153UbiquitinationNLEAFFKKLGEINQV
HHHHHHHHHHHHHHE
57.4723749301
191PhosphorylationECEAFLKSYSNDDES
HHHHHHHHCCCCCCC
35.6230377154
193PhosphorylationEAFLKSYSNDDESNE
HHHHHHCCCCCCCCC
40.6530377154
198PhosphorylationSYSNDDESNEILSYE
HCCCCCCCCCEEEEC
46.9227017623
203PhosphorylationDESNEILSYEGKKLS
CCCCCEEEECCCEEE
27.1430377154
207AcetylationEILSYEGKKLSVLTK
CEEEECCCEEEEEEH
38.3024489116
207SuccinylationEILSYEGKKLSVLTK
CEEEECCCEEEEEEH
38.3023954790
215AcetylationKLSVLTKKQFDLQRE
EEEEEEHHHHHHHHH
51.4624489116
225AcetylationDLQREASKSKNFSGR
HHHHHHHCCCCCCCC
72.9325381059
227AcetylationQREASKSKNFSGRSR
HHHHHCCCCCCCCCC
66.7925381059
230PhosphorylationASKSKNFSGRSRSFN
HHCCCCCCCCCCCCC
42.5617287358
233PhosphorylationSKNFSGRSRSFNGHK
CCCCCCCCCCCCCCC
35.4817287358
235PhosphorylationNFSGRSRSFNGHKKK
CCCCCCCCCCCCCCC
25.0619823750
240AcetylationSRSFNGHKKKNLPKF
CCCCCCCCCCCCCCC
67.8325381059
246AcetylationHKKKNLPKFPKNKKK
CCCCCCCCCCCCCCC
76.9624489116
259PhosphorylationKKNGKEESKEDSSAI
CCCCCCCCHHHHHCC
42.3029136822
263PhosphorylationKEESKEDSSAIADDD
CCCCHHHHHCCCCCC
23.8225521595
264PhosphorylationEESKEDSSAIADDDE
CCCHHHHHCCCCCCH
35.7025521595

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of LHP1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LHP1_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LHP1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LHP1_YEASTLHP1physical
14759368
SRP68_YEASTSRP68physical
14759368
SRP72_YEASTSRP72physical
14759368
LSM5_YEASTLSM5genetic
11333229
LSM6_YEASTLSM6genetic
11333229
LSM7_YEASTLSM7genetic
11333229
LSM8_YEASTLSM8genetic
9857199
SRP68_YEASTSRP68physical
16554755
TRM1_YEASTTRM1genetic
16581807
REXO1_YEASTRNH70genetic
18456844
LOC1_YEASTLOC1genetic
19061648
ERF3_YEASTSUP35genetic
19061648
POP8_YEASTPOP8genetic
19061648
POP7_YEASTPOP7genetic
19061648
ARC1_YEASTARC1genetic
19061648
XPOT_YEASTLOS1genetic
19061648
EFTU_YEASTTUF1genetic
19061648
PFD5_YEASTGIM5genetic
19061648
LSM7_YEASTLSM7genetic
19061648
BRR1_YEASTBRR1genetic
19061648
SSBP1_YEASTSBP1genetic
19061648
PAT1_YEASTPAT1genetic
19061648
CAF16_YEASTCAF16genetic
19061648
ELP1_YEASTIKI3genetic
19061648
MRT4_YEASTMRT4genetic
19061648
NOP12_YEASTNOP12genetic
19061648
CSI1_YEASTCSI1genetic
19061648
MED1_YEASTMED1genetic
19061648
LSM1_YEASTLSM1genetic
19596813
RPA14_YEASTRPA14genetic
20093466
UME6_YEASTUME6genetic
20093466
LSM6_YEASTLSM6genetic
20093466
VMA21_YEASTVMA21genetic
20093466
THIK_YEASTPOT1genetic
20093466
XPOT_YEASTLOS1genetic
20093466
ROM2_YEASTROM2genetic
20093466
MSC1_YEASTMSC1genetic
20093466
LSM7_YEASTLSM7genetic
20093466
NST1_YEASTNST1genetic
20093466
MSN1_YEASTMSN1genetic
20093466
MSB4_YEASTMSB4genetic
20093466
MEK1_YEASTMEK1genetic
20093466
BRR1_YEASTBRR1genetic
20093466
PUS3_YEASTDEG1genetic
16581807
LSM8_YEASTLSM8genetic
21212361
VMA21_YEASTVMA21genetic
27708008
LSM2_YEASTLSM2genetic
27708008
POP7_YEASTPOP7genetic
27708008
SYF1_YEASTSYF1genetic
27708008
TFC4_YEASTTFC4genetic
27708008
BCD1_YEASTBCD1genetic
27708008
RPC9_YEASTRPC17genetic
27708008
CDC11_YEASTCDC11genetic
27708008
PRP24_YEASTPRP24genetic
27708008
TRM6_YEASTGCD10genetic
27708008
RPC6_YEASTRPC34genetic
27708008
GPN2_YEASTGPN2genetic
27708008
PRP4_YEASTPRP4genetic
27708008
ELO2_YEASTELO2genetic
27708008
UME6_YEASTUME6genetic
27708008
LSM6_YEASTLSM6genetic
27708008
BUD27_YEASTBUD27genetic
27708008
THIK_YEASTPOT1genetic
27708008
XPOT_YEASTLOS1genetic
27708008
ROM2_YEASTROM2genetic
27708008
NST1_YEASTNST1genetic
27708008
LSM7_YEASTLSM7genetic
27708008
MSN1_YEASTMSN1genetic
27708008
BRR1_YEASTBRR1genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LHP1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-19, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-19; SER-230;SER-233 AND SER-235, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.
"Phosphorylation of the Saccharomyces cerevisiae La protein does notappear to be required for its functions in tRNA maturation and nascentRNA 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).
Cited for: PHOSPHORYLATION AT SER-15; SER-19 AND SER-235, MASS SPECTROMETRY,FUNCTION, AND MUTAGENESIS OF SER-15; SER-19 AND SER-235.

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