dbPTM

RSZ32_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RSZ32_ARATH
UniProt AC	Q9FYB7
Protein Name	Serine/arginine-rich splicing factor RS2Z32
Gene Name	RS2Z32
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	284
Subcellular Localization	Nucleus.
Protein Description	Probably involved in intron recognition and spliceosome assembly..
Protein Sequence	MPRYDDRYGNTRLYVGRLSSRTRTRDLERLFSRYGRVRDVDMKRDYAFVEFSDPRDADDARYYLDGRDFDGSRITVEASRGAPRGSRDNGSRGPPPGSGRCFNCGVDGHWARDCTAGDWKNKCYRCGERGHIERNCKNSPSPKKARQGGSYSRSPVKSRSPRRRRSPSRSRSYSRGRSYSRSRSPVRREKSVEDRSRSPKAMERSVSPKGRDQSLSPDRKVIDASPKRGSDYDGSPKENGNGRNSASPIVGGGESPVGLNGQDRSPIDDEAELSRPSPKGSESP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
52	Phosphorylation	DYAFVEFSDPRDADD CEEEEEECCCCCCCC	32.95	19880383
91	Phosphorylation	RGSRDNGSRGPPPGS CCCCCCCCCCCCCCC	40.08	25561503
98	Phosphorylation	SRGPPPGSGRCFNCG CCCCCCCCCCCCCCC	28.92	25561503
139	Phosphorylation	IERNCKNSPSPKKAR HHHCCCCCCCCHHHC	16.55	23776212
141	Phosphorylation	RNCKNSPSPKKARQG HCCCCCCCCHHHCCC	49.53	23776212
150	Phosphorylation	KKARQGGSYSRSPVK HHHCCCCCCCCCCCC	27.10	30407730
151	Phosphorylation	KARQGGSYSRSPVKS HHCCCCCCCCCCCCC	16.04	30407730
152	Phosphorylation	ARQGGSYSRSPVKSR HCCCCCCCCCCCCCC	28.16	27531888
154	Phosphorylation	QGGSYSRSPVKSRSP CCCCCCCCCCCCCCC	28.27	27531888
158	Phosphorylation	YSRSPVKSRSPRRRR CCCCCCCCCCCCCCC	37.92	19376835
160	Phosphorylation	RSPVKSRSPRRRRSP CCCCCCCCCCCCCCC	29.83	19376835
166	Phosphorylation	RSPRRRRSPSRSRSY CCCCCCCCCCCCCHH	25.97	-
168	Phosphorylation	PRRRRSPSRSRSYSR CCCCCCCCCCCHHHC	44.10	-
172	Phosphorylation	RSPSRSRSYSRGRSY CCCCCCCHHHCCCCC	28.80	29797451
184	Phosphorylation	RSYSRSRSPVRREKS CCCCCCCCCCCCCCC	29.06	18463617
191	Phosphorylation	SPVRREKSVEDRSRS CCCCCCCCHHHHHCC	26.45	25561503
196	Phosphorylation	EKSVEDRSRSPKAME CCCHHHHHCCHHHHH	49.81	25561503
205	Phosphorylation	SPKAMERSVSPKGRD CHHHHHHCCCCCCCC	17.40	27531888
207	Phosphorylation	KAMERSVSPKGRDQS HHHHHCCCCCCCCCC	23.34	27531888
214	Phosphorylation	SPKGRDQSLSPDRKV CCCCCCCCCCCCCCE	34.79	19880383
216	Phosphorylation	KGRDQSLSPDRKVID CCCCCCCCCCCCEEE	29.96	19880383
225	Phosphorylation	DRKVIDASPKRGSDY CCCEEECCCCCCCCC	27.49	19880383
230	Phosphorylation	DASPKRGSDYDGSPK ECCCCCCCCCCCCCC	36.71	23776212
232	Phosphorylation	SPKRGSDYDGSPKEN CCCCCCCCCCCCCCC	24.73	23776212
235	Phosphorylation	RGSDYDGSPKENGNG CCCCCCCCCCCCCCC	29.87	23776212
245	Phosphorylation	ENGNGRNSASPIVGG CCCCCCCCCCCCCCC	28.85	19880383
247	Phosphorylation	GNGRNSASPIVGGGE CCCCCCCCCCCCCCC	18.25	27531888
255	Phosphorylation	PIVGGGESPVGLNGQ CCCCCCCCCCCCCCC	28.32	30291188
265	Phosphorylation	GLNGQDRSPIDDEAE CCCCCCCCCCCCCHH	34.20	23776212
274	Phosphorylation	IDDEAELSRPSPKGS CCCCHHHCCCCCCCC	33.38	23776212
277	Phosphorylation	EAELSRPSPKGSESP CHHHCCCCCCCCCCC	37.83	23776212
281	Phosphorylation	SRPSPKGSESP---- CCCCCCCCCCC----	40.81	23776212
283	Phosphorylation	PSPKGSESP------ CCCCCCCCC------	37.29	23776212

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 RSZ32_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RSZ32_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 RSZ32_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RSZ32_ARATH !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RSZ32_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158; SER-160; SER-214;SER-216; SER-225; SER-230 AND SER-235, AND MASS SPECTROMETRY.	19376835 [Abstract]
"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-265, AND MASSSPECTROMETRY.	19245862 [Abstract]
"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-225, AND MASSSPECTROMETRY.	16807317 [Abstract]