RUSD2_HUMAN - dbPTM
RUSD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RUSD2_HUMAN
UniProt AC Q8IZ73
Protein Name RNA pseudouridylate synthase domain-containing protein 2
Gene Name RPUSD2
Organism Homo sapiens (Human).
Sequence Length 545
Subcellular Localization
Protein Description
Protein Sequence MWLDRRGWLRVLGHWRYDLRRPSFTRTWSGDKGPMAETVSTQVGTEGGLRASHQQNGDAGGDAKVELSPGPPKPAGREVEPAPVGGEHPSAAAPGPGKHKKRRGATRERVVPPPKKRRTGVSFGDEHFAETSYYFEGGLRKVRPYYFDFRTYCKGRWVGHSLLHVFSTEFRAQPLAYYEAAVRAGRLQLNEKPVQDLNIVLKDNDFLRNTVHRHEPPVTAEPIRLLAENEDVVVVDKPSSIPVHPCGRFRHNTVIFILGKEHQLKELHPLHRLDRLTSGVLMFAKTAAVSERIHEQVRDRQLEKEYVCRVEGEFPTEEVTCKEPILVVSYKVGVCRVDPRGKPCETVFQRLSYNGQSSVVRCRPLTGRTHQIRVHLQFLGHPILNDPIYNSVAWGPSRGRGGYIPKTNEELLRDLVAEHQAKQSLDVLDLCEGDLSPGLTDSTAPSSELGKDDLEELAAAAQKMEEVAEAAPQELDTIALASEKAVETDVMNQETDPLCAECRLVRQDPLPQDLVMFLHALRYKGPGFEYFSPMPAWAQDDWQKD
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
29PhosphorylationPSFTRTWSGDKGPMA
CCCEEECCCCCCCCC		36.18-
52PhosphorylationTEGGLRASHQQNGDA
CCCCCCCCCCCCCCC		18.5223186163
68PhosphorylationGDAKVELSPGPPKPA
CCCEEEECCCCCCCC		17.8229255136
90PhosphorylationPVGGEHPSAAAPGPG
CCCCCCCCCCCCCCC		32.2325159151
119PhosphorylationPPPKKRRTGVSFGDE
CCCCCCCCCCCCCCC		46.0726074081
122PhosphorylationKKRRTGVSFGDEHFA
CCCCCCCCCCCCHHC		25.5126074081
131PhosphorylationGDEHFAETSYYFEGG
CCCHHCCEEEEECCC		20.7126074081
132PhosphorylationDEHFAETSYYFEGGL
CCHHCCEEEEECCCC		14.8926074081
133PhosphorylationEHFAETSYYFEGGLR
CHHCCEEEEECCCCC		21.4226074081
134PhosphorylationHFAETSYYFEGGLRK
HHCCEEEEECCCCCC		8.5726074081
192UbiquitinationGRLQLNEKPVQDLNI
CCCCCCCCCCCCCEE		49.79-
204UbiquitinationLNIVLKDNDFLRNTV
CEEEECCCHHHHHCC		40.1029967540
243UbiquitinationDKPSSIPVHPCGRFR
CCCCCCCCCCCCCCC		8.20-
243AcetylationDKPSSIPVHPCGRFR
CCCCCCCCCCCCCCC		8.20-
243UbiquitinationDKPSSIPVHPCGRFR
CCCCCCCCCCCCCCC		8.2029967540
265UbiquitinationLGKEHQLKELHPLHR
CCCHHHHHHHCCHHH		52.2229967540
290PhosphorylationFAKTAAVSERIHEQV
HHHHHHHHHHHHHHH		19.2124719451
304AcetylationVRDRQLEKEYVCRVE
HHHHHHHHEEEEEEE		64.0423749302
304UbiquitinationVRDRQLEKEYVCRVE
HHHHHHHHEEEEEEE		64.0429967540
345UbiquitinationDPRGKPCETVFQRLS
CCCCCCCCHHHHHHC		57.4424816145
361UbiquitinationNGQSSVVRCRPLTGR
CCCCCEEEEEECCCC		14.4729967540
403PhosphorylationPSRGRGGYIPKTNEE
CCCCCCCCCCCCCHH		19.5123403867
406UbiquitinationGRGGYIPKTNEELLR
CCCCCCCCCCHHHHH		55.1924816145
407PhosphorylationRGGYIPKTNEELLRD
CCCCCCCCCHHHHHH		42.3723403867
422UbiquitinationLVAEHQAKQSLDVLD
HHHHHHHHHCCCHHH		33.5729967540
436PhosphorylationDLCEGDLSPGLTDST
HHCCCCCCCCCCCCC		22.9728464451
440PhosphorylationGDLSPGLTDSTAPSS
CCCCCCCCCCCCCHH		33.5427251275
442PhosphorylationLSPGLTDSTAPSSEL
CCCCCCCCCCCHHHC		22.6427251275
443PhosphorylationSPGLTDSTAPSSELG
CCCCCCCCCCHHHCC		45.4527251275
446PhosphorylationLTDSTAPSSELGKDD
CCCCCCCHHHCCCCH		33.7027251275
447PhosphorylationTDSTAPSSELGKDDL
CCCCCCHHHCCCCHH		35.4627251275
477PhosphorylationAAPQELDTIALASEK
HCCHHHHHHHHHCCH		22.30-
491SulfoxidationKAVETDVMNQETDPL
HHHHCCCCCCCCCCC		4.8221406390
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 RUSD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RUSD2_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 RUSD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
AASD1_HUMANAARSD1physical
22863883
LZTL1_HUMANLZTFL1physical
22863883
MAOX_HUMANME1physical
22863883
SNF8_HUMANSNF8physical
22863883
TBCD_HUMANTBCDphysical
22863883
UGDH_HUMANUGDHphysical
22863883
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 RUSD2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-68, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory