PUS1_SCHPO - dbPTM
PUS1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUS1_SCHPO
UniProt AC O94396
Protein Name tRNA pseudouridine synthase 1
Gene Name pus1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 534
Subcellular Localization Nucleus .
Protein Description Formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of transfer RNAs; at positions 34 and 36 of intron-containing precursor tRNA(Ile) and at position 35 in the intron-containing tRNA(Tyr). [PubMed: 11095668 Catalyzes pseudouridylation at position 44 in U2 snRNA (By similarity Also catalyzes pseudouridylation of mRNAs (By similarity]
Protein Sequence MGRGGKRTWYNGDRREAKRNRPNSIYNGEGRPENLVVGEKKPKRKVACLVGYCGSGYHGMQLNPPSKTIEGDLFDAFVKAGAVSSYNADDPKKVALARAARTDKGVHAAGNVISLKLIMEDEKLIEKVNEHLPPSIRLWDVIRTINSFNPRTYCESRIYEYMVPTYAFVPPKPSSILGNCIMKNSPMPAEPINKENINQLSRSLFYEEGKEFWDDYDIAAKEILSLYEQDPEGFVNPYSKRGAAALANSENNKGSEAGVSAKTNPDMDSDSSAIVNEFLKPDSVEDESAGSKIDPSYRLERALKHIEVLKLKNYRISADRLSVIRETLNQYVGVHNFHNFTVGQAFHQKNSNRVIRSFTASDPFMIGDTEWISCKVHGQSFMLHQIRKMIALAILVVRTGCPVERIQDAFKKTKINIPKGPGFGLLLESPFFKGYNEHKAPENNRDPIDFTKYEQKITAFKHAHIYDKIFLEEARKQVFHCFLSFIDSYNEEDFSYLSDIGITEKTQEVSSKLPDVLSSDEEEDSAENKDDLEG
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
24PhosphorylationAKRNRPNSIYNGEGR
HHHCCCCCCCCCCCC		29.1825720772
249PhosphorylationGAAALANSENNKGSE
HHHHHHCCCCCCCCC		35.7721712547
255PhosphorylationNSENNKGSEAGVSAK
CCCCCCCCCCCCCCC		26.3621712547
263PhosphorylationEAGVSAKTNPDMDSD
CCCCCCCCCCCCCCC		52.2621712547
269PhosphorylationKTNPDMDSDSSAIVN
CCCCCCCCCCHHHHH		32.5225720772
271PhosphorylationNPDMDSDSSAIVNEF
CCCCCCCCHHHHHHH		26.1424763107
272PhosphorylationPDMDSDSSAIVNEFL
CCCCCCCHHHHHHHH		27.3124763107
283PhosphorylationNEFLKPDSVEDESAG
HHHHCCCCCCCCCCC		35.6127738172
518PhosphorylationSKLPDVLSSDEEEDS
HCCCCCCCCCCHHHH		35.2828889911
519PhosphorylationKLPDVLSSDEEEDSA
CCCCCCCCCCHHHHH		44.9028889911
525PhosphorylationSSDEEEDSAENKDDL
CCCCHHHHHHCCHHC		40.5428889911
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 PUS1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PUS1_SCHPO !!
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 PUS1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DCR1_SCHPOdcr1genetic
18818364
RPN1_SCHPOmts4physical
16149916
UBI4P_SCHPOubi4physical
23038266
SFT1_SCHPOsft1genetic
22681890
FEP1_SCHPOfep1genetic
22681890
BST1_SCHPObst1genetic
22681890
TRMB_SCHPOtrm8genetic
22681890
CG121_SCHPOcgi121genetic
22681890
DAD1_SCHPOdad1genetic
22681890
MET10_SCHPOSPCC584.01cgenetic
22681890
RICTR_SCHPOste20genetic
22681890
GIT3_SCHPOgit3genetic
22681890
COM1_SCHPOctp1genetic
22681890
YOR2_SCHPOrng9genetic
22681890
RM01_SCHPOSPAC1610.02cgenetic
22681890
ATP11_SCHPOatp11genetic
22681890
SEC14_SCHPOspo20genetic
22681890
YKN4_SCHPOmca1genetic
22681890
RCD1_SCHPOrcd1genetic
22681890
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PUS1_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518; SER-519 ANDSER-525, AND MASS SPECTROMETRY.

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