RSZ33_ARATH - dbPTM
RSZ33_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RSZ33_ARATH
UniProt AC Q8VYA5
Protein Name Serine/arginine-rich splicing factor RS2Z33
Gene Name RS2Z33
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 290
Subcellular Localization Nucleus speckle .
Protein Description Splicing factor involved in constitutive and/or alternative splicing. Regulates the splicing of its own pre-mRNA and the alternative splicing of RS30, RS31 and RS34. Associates the cyclin-dependent kinase G1 (CDKG1) with the spliceosome and recruits it to U1 snRNP to facilitate splicing..
Protein Sequence MPRYDDRYGNTRLYVGRLSSRTRTRDLERLFSRYGRVRDVDMKRDYAFVEFGDPRDADDARHYLDGRDFDGSRITVEFSRGAPRGSRDFDSRGPPPGAGRCFNCGVDGHWARDCTAGDWKNKCYRCGERGHIERNCKNSPKKLRRSGSYSRSPVRSRSPRRRRSPSRSLSRSRSYSRSRSPVRRRERSVEERSRSPKRMDDSLSPRARDRSPVLDDEGSPKIIDGSPPPSPKLQKEVGSDRDGGSPQDNGRNSVVSPVVGAGGDSSKEDRSPVDDDYEPNRTSPRGSESP
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
86PhosphorylationSRGAPRGSRDFDSRG
CCCCCCCCCCCCCCC		29.9225561503
91PhosphorylationRGSRDFDSRGPPPGA
CCCCCCCCCCCCCCC		38.8529654922
148PhosphorylationKKLRRSGSYSRSPVR
HHHHHCCCCCCCCCC		22.6025561503
149PhosphorylationKLRRSGSYSRSPVRS
HHHHCCCCCCCCCCC		16.1925561503
150PhosphorylationLRRSGSYSRSPVRSR
HHHCCCCCCCCCCCC		28.1625561503
152PhosphorylationRSGSYSRSPVRSRSP
HCCCCCCCCCCCCCC		23.0829654922
156PhosphorylationYSRSPVRSRSPRRRR
CCCCCCCCCCCCCCC		37.0329654922
158PhosphorylationRSPVRSRSPRRRRSP
CCCCCCCCCCCCCCC		24.8129654922
164PhosphorylationRSPRRRRSPSRSLSR
CCCCCCCCCCCCHHH		25.97-
166PhosphorylationPRRRRSPSRSLSRSR
CCCCCCCCCCHHHHH		35.43-
168PhosphorylationRRRSPSRSLSRSRSY
CCCCCCCCHHHHHHC		34.7329797451
180PhosphorylationRSYSRSRSPVRRRER
HHCCCCCCHHHHHHH		29.06-
188PhosphorylationPVRRRERSVEERSRS
HHHHHHHCHHHHHHC		29.1825561503
193PhosphorylationERSVEERSRSPKRMD
HHCHHHHHHCCCCCC		40.1529654922
199SulfoxidationRSRSPKRMDDSLSPR
HHHCCCCCCCCCCCC		9.3023289948
202PhosphorylationSPKRMDDSLSPRARD
CCCCCCCCCCCCHHC		26.8730291188
204PhosphorylationKRMDDSLSPRARDRS
CCCCCCCCCCHHCCC		19.1130291188
211PhosphorylationSPRARDRSPVLDDEG
CCCHHCCCCCCCCCC		24.5330291188
219PhosphorylationPVLDDEGSPKIIDGS
CCCCCCCCCCCCCCC		22.4430291188
226PhosphorylationSPKIIDGSPPPSPKL
CCCCCCCCCCCCHHH		30.4130291188
230PhosphorylationIDGSPPPSPKLQKEV
CCCCCCCCHHHHHHH		40.2030291188
239PhosphorylationKLQKEVGSDRDGGSP
HHHHHHCCCCCCCCC		34.3523776212
245PhosphorylationGSDRDGGSPQDNGRN
CCCCCCCCCCCCCCC		25.5623776212
253PhosphorylationPQDNGRNSVVSPVVG
CCCCCCCCCCCCCCC		23.6419880383
256PhosphorylationNGRNSVVSPVVGAGG
CCCCCCCCCCCCCCC		15.1530291188
265PhosphorylationVVGAGGDSSKEDRSP
CCCCCCCCCCCCCCC		46.7324601666
266PhosphorylationVGAGGDSSKEDRSPV
CCCCCCCCCCCCCCC		44.8223776212
271PhosphorylationDSSKEDRSPVDDDYE
CCCCCCCCCCCCCCC		41.4123776212
277PhosphorylationRSPVDDDYEPNRTSP
CCCCCCCCCCCCCCC		40.0423776212
282PhosphorylationDDYEPNRTSPRGSES
CCCCCCCCCCCCCCC		50.1223776212
283PhosphorylationDYEPNRTSPRGSESP
CCCCCCCCCCCCCCC		14.9023776212
287PhosphorylationNRTSPRGSESP----
CCCCCCCCCCC----		35.8619376835
289PhosphorylationTSPRGSESP------
CCCCCCCCC------		37.2919376835
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 RSZ33_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RSZ33_ARATH !!
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 RSZ33_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SR34_ARATHSR1physical
18674533
RSZ21_ARATHRSZP21physical
12176998
RSZ22_ARATHSRZ-22physical
12176998
SRC28_ARATHSCL28physical
12176998
SRC30_ARATHSCL30physical
12176998
SRC33_ARATHSR33physical
12176998
SL30A_ARATHSCL30Aphysical
12176998
SC35_ARATHSC35physical
12176998
SR34_ARATHSR1physical
12176998
SRS31_ARATHRSP31physical
12176998
SRC30_ARATHSCL30physical
21798944
AFC3_ARATHAME3physical
21798944
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RSZ33_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND MASSSPECTROMETRY.
"Phosphoproteomics reveals extensive in vivo phosphorylation ofArabidopsis proteins involved in RNA metabolism.";
de la Fuente van Bentem S., Anrather D., Roitinger E., Djamei A.,Hufnagl T., Barta A., Csaszar E., Dohnal I., Lecourieux D., Hirt H.;
Nucleic Acids Res. 34:3267-3278(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND MASSSPECTROMETRY.

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