TRUA_HUMAN - dbPTM
TRUA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRUA_HUMAN
UniProt AC Q9Y606
Protein Name tRNA pseudouridine synthase A
Gene Name PUS1
Organism Homo sapiens (Human).
Sequence Length 427
Subcellular Localization Isoform 1: Mitochondrion .
Isoform 2: Nucleus .
Protein Description Converts specific uridines to PSI in a number of tRNA substrates. Acts on positions 27/28 in the anticodon stem and also positions 34 and 36 in the anticodon of an intron containing tRNA. Involved in regulation of nuclear receptor activity through pseudouridylation of SRA1 RNA..
Protein Sequence MGLQLRALLGAFGRWTLRLGPRPSCSPRMAGNAEPPPAGAACPQDRRSCSGRAGGDRVWEDGEHPAKKLKSGGDEERREKPPKRKIVLLMAYSGKGYHGMQRNVGSSQFKTIEDDLVSALVRSGCIPENHGEDMRKMSFQRCARTDKGVSAAGQVVSLKVWLIDDILEKINSHLPSHIRILGLKRVTGGFNSKNRCDARTYCYLLPTFAFAHKDRDVQDETYRLSAETLQQVNRLLACYKGTHNFHNFTSQKGPQDPSACRYILEMYCEEPFVREGLEFAVIRVKGQSFMMHQIRKMVGLVVAIVKGYAPESVLERSWGTEKVDVPKAPGLGLVLERVHFEKYNQRFGNDGLHEPLDWAQEEGKVAAFKEEHIYPTIIGTERDERSMAQWLSTLPIHNFSATALTAGGTGAKVPSPLEGSEGDGDTD
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
26PhosphorylationLGPRPSCSPRMAGNA
CCCCCCCCCCCCCCC
21.6328555341
67AcetylationEDGEHPAKKLKSGGD
CCCCCCHHHCCCCCC
64.1925953088
110UbiquitinationNVGSSQFKTIEDDLV
CCCCHHCCCHHHHHH
40.74-
138PhosphorylationGEDMRKMSFQRCART
CHHHHHHHHHHHHCC
22.6624719451
145PhosphorylationSFQRCARTDKGVSAA
HHHHHHCCCCCCCCC
24.4429759185
147AcetylationQRCARTDKGVSAAGQ
HHHHCCCCCCCCCCC
61.6725953088
147MalonylationQRCARTDKGVSAAGQ
HHHHCCCCCCCCCCC
61.6726320211
150PhosphorylationARTDKGVSAAGQVVS
HCCCCCCCCCCCEEE
22.52-
176PhosphorylationKINSHLPSHIRILGL
HHHHCCCCCEEEECC
37.60-
187PhosphorylationILGLKRVTGGFNSKN
EECCCCCCCCCCCCC
35.3025599653
201PhosphorylationNRCDARTYCYLLPTF
CCCCHHHHHHHHHHH
3.5822210691
207PhosphorylationTYCYLLPTFAFAHKD
HHHHHHHHHHHHCCC
27.8022210691
221PhosphorylationDRDVQDETYRLSAET
CCCCCCCHHCCCHHH
23.4120068231
222PhosphorylationRDVQDETYRLSAETL
CCCCCCHHCCCHHHH
13.9122210691
239PhosphorylationVNRLLACYKGTHNFH
HHHHHHHHCCCCCCC
13.5722817900
249PhosphorylationTHNFHNFTSQKGPQD
CCCCCCCCCCCCCCC
35.2528857561
250PhosphorylationHNFHNFTSQKGPQDP
CCCCCCCCCCCCCCH
26.2520873877
342AcetylationLERVHFEKYNQRFGN
EEEEEHHHHHHHCCC
48.8626822725
364UbiquitinationDWAQEEGKVAAFKEE
HHHHHHCCEEEEEHH
31.79-
369UbiquitinationEGKVAAFKEEHIYPT
HCCEEEEEHHHCCCE
58.42-
3692-HydroxyisobutyrylationEGKVAAFKEEHIYPT
HCCEEEEEHHHCCCE
58.42-
380PhosphorylationIYPTIIGTERDERSM
CCCEECCCCCCHHHH
19.8924719451
392PhosphorylationRSMAQWLSTLPIHNF
HHHHHHHHCCCCCCC
25.5719664995
415PhosphorylationGTGAKVPSPLEGSEG
CCCCCCCCCCCCCCC
45.1430266825
420PhosphorylationVPSPLEGSEGDGDTD
CCCCCCCCCCCCCCC
29.0923927012
426PhosphorylationGSEGDGDTD------
CCCCCCCCC------
49.4925159151

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 TRUA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRUA_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 TRUA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARP3_HUMANACTR3physical
22863883
GDE_HUMANAGLphysical
22863883
ARPC2_HUMANARPC2physical
22863883
BCAT1_HUMANBCAT1physical
22863883
SYFA_HUMANFARSAphysical
22863883
IDE_HUMANIDEphysical
22863883
NCBP1_HUMANNCBP1physical
22863883
NRDC_HUMANNRD1physical
22863883
NSUN2_HUMANNSUN2physical
22863883
PFD1_HUMANPFDN1physical
22863883
PFD5_HUMANPFDN5physical
22863883
RFA1_HUMANRPA1physical
22863883
SP100_HUMANSP100physical
22863883
VPS29_HUMANVPS29physical
22863883

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
600462Myopathy with lactic acidosis and sideroblastic anemia 1 (MLASA1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRUA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415; SER-420 ANDTHR-426, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND THR-426, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND THR-426, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-426, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-426, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, AND MASSSPECTROMETRY.

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