TRUB1_HUMAN - dbPTM
TRUB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRUB1_HUMAN
UniProt AC Q8WWH5
Protein Name Probable tRNA pseudouridine synthase 1 {ECO:0000305}
Gene Name TRUB1 {ECO:0000303|PubMed:12736709, ECO:0000312|HGNC:HGNC:16060}
Organism Homo sapiens (Human).
Sequence Length 349
Subcellular Localization Nucleus . Cytoplasm, cytosol . Catalyzes pseudouridylation of mRNAs in the nucleus.
Protein Description Pseudouridine synthase that catalyzes pseudouridylation of mRNAs. [PubMed: 28073919 Mediates pseudouridylation of mRNAs with the consensus sequence 5'-GUUCNANNC-3', harboring a stem-loop structure]
Protein Sequence MAASEAAVVSSPSLKTDTSPVLETAGTVAAMAATPSARAAAAVVAAAARTGSEARVSKAALATKLLSLSGVFAVHKPKGPTSAELLNRLKEKLLAEAGMPSPEWTKRKKQTLKIGHGGTLDSAARGVLVVGIGSGTKMLTSMLSGSKRYTAIGELGKATDTLDSTGRVTEEKPYDKITQEDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKRGEVVEAKPARPVTVYSISLQKFQPPFFTLDVECGGGFYIRSLVSDIGKELSSCANVLELTRTKQGPFTLEEHALPEDKWTIDDIAQSLEHCSSLFPAELALKKSKPESNEQVLSCEYITLNEPKREDDVIKTC
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
2Acetylation------MAASEAAVV
------CCCCCCEEE		21.5022223895
4Phosphorylation----MAASEAAVVSS
----CCCCCCEEECC		20.4521955146
10PhosphorylationASEAAVVSSPSLKTD
CCCCEEECCCCCCCC		29.9029255136
11PhosphorylationSEAAVVSSPSLKTDT
CCCEEECCCCCCCCC		13.6029255136
13PhosphorylationAAVVSSPSLKTDTSP
CEEECCCCCCCCCCC		44.4329255136
16PhosphorylationVSSPSLKTDTSPVLE
ECCCCCCCCCCCCHH		50.2130278072
18PhosphorylationSPSLKTDTSPVLETA
CCCCCCCCCCCHHHH		39.9130278072
19PhosphorylationPSLKTDTSPVLETAG
CCCCCCCCCCHHHHH		18.8030278072
24PhosphorylationDTSPVLETAGTVAAM
CCCCCHHHHHHHHHH		26.6530278072
27PhosphorylationPVLETAGTVAAMAAT
CCHHHHHHHHHHHCC		12.4221955146
34PhosphorylationTVAAMAATPSARAAA
HHHHHHCCHHHHHHH		14.2925159151
36PhosphorylationAAMAATPSARAAAAV
HHHHCCHHHHHHHHH		26.4922199227
50PhosphorylationVVAAAARTGSEARVS
HHHHHHHCCCHHHHH		40.0928555341
58UbiquitinationGSEARVSKAALATKL
CCHHHHHHHHHHHHH		34.5227667366
88MethylationTSAELLNRLKEKLLA
CHHHHHHHHHHHHHH		47.29115919045
90UbiquitinationAELLNRLKEKLLAEA
HHHHHHHHHHHHHHC		49.9529967540
101PhosphorylationLAEAGMPSPEWTKRK
HHHCCCCCHHHHHHH		26.9321815630
105PhosphorylationGMPSPEWTKRKKQTL
CCCCHHHHHHHCCEE		21.2222199227
106UbiquitinationMPSPEWTKRKKQTLK
CCCHHHHHHHCCEEE		64.3929967540
119PhosphorylationLKIGHGGTLDSAARG
EEECCCCCCCCCCCC		31.8023312004
122PhosphorylationGHGGTLDSAARGVLV
CCCCCCCCCCCCEEE		27.2623312004
134PhosphorylationVLVVGIGSGTKMLTS
EEEEEECCCHHHHHH		41.17-
136PhosphorylationVVGIGSGTKMLTSML
EEEECCCHHHHHHHH		18.2525627689
144O-linked_GlycosylationKMLTSMLSGSKRYTA
HHHHHHHCCCCCEEE		32.1730379171
146O-linked_GlycosylationLTSMLSGSKRYTAIG
HHHHHCCCCCEEEEE		15.5830379171
146PhosphorylationLTSMLSGSKRYTAIG
HHHHHCCCCCEEEEE		15.5824260401
147AcetylationTSMLSGSKRYTAIGE
HHHHCCCCCEEEEEH		53.6125953088
147UbiquitinationTSMLSGSKRYTAIGE
HHHHCCCCCEEEEEH		53.6129967540
149PhosphorylationMLSGSKRYTAIGELG
HHCCCCCEEEEEHHH		12.3128152594
150PhosphorylationLSGSKRYTAIGELGK
HCCCCCEEEEEHHHH		18.8128152594
157UbiquitinationTAIGELGKATDTLDS
EEEEHHHHHCCCCCC		61.8224816145
172UbiquitinationTGRVTEEKPYDKITQ
CCCCCCCCCCCCCCH		42.5229967540
174PhosphorylationRVTEEKPYDKITQED
CCCCCCCCCCCCHHH		40.72-
176UbiquitinationTEEKPYDKITQEDIE
CCCCCCCCCCHHHHH		41.6429967540
200PhosphorylationIMQVPPLYSALKKDG
CCCCCCHHHHHHHCC		9.5528796482
201PhosphorylationMQVPPLYSALKKDGQ
CCCCCHHHHHHHCCC		34.5023401153
204AcetylationPPLYSALKKDGQRLS
CCHHHHHHHCCCCHH		48.847410097
204UbiquitinationPPLYSALKKDGQRLS
CCHHHHHHHCCCCHH		48.8429967540
205AcetylationPLYSALKKDGQRLST
CHHHHHHHCCCCHHH		68.867410107
205UbiquitinationPLYSALKKDGQRLST
CHHHHHHHCCCCHHH		68.86-
211PhosphorylationKKDGQRLSTLMKRGE
HHCCCCHHHHHHCCC		22.9925159151
212PhosphorylationKDGQRLSTLMKRGEV
HCCCCHHHHHHCCCE		35.1525627689
223AcetylationRGEVVEAKPARPVTV
CCCEEECCCCCCEEE		26.2126051181
223UbiquitinationRGEVVEAKPARPVTV
CCCEEECCCCCCEEE		26.2129967540
234PhosphorylationPVTVYSISLQKFQPP
CEEEEEEEECCCCCC		20.8624719451
257PhosphorylationGGGFYIRSLVSDIGK
CCCHHHHHHHHHHHH		24.4620860994
260PhosphorylationFYIRSLVSDIGKELS
HHHHHHHHHHHHHHH		28.8920860994
264UbiquitinationSLVSDIGKELSSCAN
HHHHHHHHHHHHHHH		56.68-
267PhosphorylationSDIGKELSSCANVLE
HHHHHHHHHHHHHHH		25.1821406692
268PhosphorylationDIGKELSSCANVLEL
HHHHHHHHHHHHHHH		29.8521406692
276PhosphorylationCANVLELTRTKQGPF
HHHHHHHHCCCCCCC		27.2421406692
279UbiquitinationVLELTRTKQGPFTLE
HHHHHCCCCCCCCCC		50.3929967540
294UbiquitinationEHALPEDKWTIDDIA
CCCCCCCCCCHHHHH		44.5729967540
319UbiquitinationPAELALKKSKPESNE
HHHHHHHCCCCCCCC		65.6429967540
321UbiquitinationELALKKSKPESNEQV
HHHHHCCCCCCCCCE		62.7829967540
330PhosphorylationESNEQVLSCEYITLN
CCCCCEEEEEEEECC		13.1729978859
333PhosphorylationEQVLSCEYITLNEPK
CCEEEEEEEECCCCC		11.9728796482
335PhosphorylationVLSCEYITLNEPKRE
EEEEEEEECCCCCCC		23.7228796482
340SumoylationYITLNEPKREDDVIK
EEECCCCCCCCCCCC		63.34-
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 TRUB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRUB1_HUMAN !!
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 TRUB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
FMT_HUMANMTFMTphysical
28514442
UBP11_HUMANUSP11physical
28514442
TCAL1_HUMANTCEAL1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRUB1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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