SC35_ARATH - dbPTM
SC35_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SC35_ARATH
UniProt AC Q9FMG4
Protein Name Serine/arginine-rich splicing factor SC35
Gene Name SC35
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 303
Subcellular Localization Nucleus speckle .
Protein Description Probably involved in intron recognition and spliceosome assembly, but not involved in alternative splicing regulation of the SCL33 intron..
Protein Sequence MSHFGRSGPPDISDTYSLLVLNITFRTTADDLYPLFAKYGKVVDVFIPRDRRTGDSRGFAFVRYKYKDEAHKAVERLDGRVVDGREITVQFAKYGPNAEKISKGRVVEPPPKSRRSRSRSPRRSRSPRRSRSPPRRRSPRRSRSPRRRSRDDYREKDYRKRSRSRSYDRRERHEEKDRDHRRRTRSRSASPDEKRRVRGRYDNESRSHSRSLSASPARRSPRSSSPQKTSPAREVSPDKRSNERSPSPRRSLSPRSPALQKASPSKEMSPERRSNERSPSPGSPAPLRKVDAASRSQSPYAAE
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
7Phosphorylation-MSHFGRSGPPDISD
-CCCCCCCCCCCHHH
-
130PhosphorylationRSRSPRRSRSPPRRR
CCCCCCCCCCCCCCC
23776212
132PhosphorylationRSPRRSRSPPRRRSP
CCCCCCCCCCCCCCC
23776212
186PhosphorylationDHRRRTRSRSASPDE
HHHHHHHHCCCCHHH
25561503
188PhosphorylationRRRTRSRSASPDEKR
HHHHHHCCCCHHHHH
25561503
190PhosphorylationRTRSRSASPDEKRRV
HHHHCCCCHHHHHCH
25561503
211PhosphorylationESRSHSRSLSASPAR
CCCCCCCCCCCCCCC
23776212
213PhosphorylationRSHSRSLSASPARRS
CCCCCCCCCCCCCCC
23776212
215PhosphorylationHSRSLSASPARRSPR
CCCCCCCCCCCCCCC
23776212
220PhosphorylationSASPARRSPRSSSPQ
CCCCCCCCCCCCCCC
27288362
223PhosphorylationPARRSPRSSSPQKTS
CCCCCCCCCCCCCCC
23776212
224PhosphorylationARRSPRSSSPQKTSP
CCCCCCCCCCCCCCC
23776212
225PhosphorylationRRSPRSSSPQKTSPA
CCCCCCCCCCCCCCC
23776212
229PhosphorylationRSSSPQKTSPAREVS
CCCCCCCCCCCCCCC
23776212
230PhosphorylationSSSPQKTSPAREVSP
CCCCCCCCCCCCCCC
23776212
236PhosphorylationTSPAREVSPDKRSNE
CCCCCCCCCCCCCCC
25561503
241PhosphorylationEVSPDKRSNERSPSP
CCCCCCCCCCCCCCC
25561503
245PhosphorylationDKRSNERSPSPRRSL
CCCCCCCCCCCCCCC
25561503
247PhosphorylationRSNERSPSPRRSLSP
CCCCCCCCCCCCCCC
25561503
251PhosphorylationRSPSPRRSLSPRSPA
CCCCCCCCCCCCCHH
23776212
253PhosphorylationPSPRRSLSPRSPALQ
CCCCCCCCCCCHHHH
23776212
256PhosphorylationRRSLSPRSPALQKAS
CCCCCCCCHHHHHCC
23776212
263PhosphorylationSPALQKASPSKEMSP
CHHHHHCCCCCCCCH
23776212
265PhosphorylationALQKASPSKEMSPER
HHHHCCCCCCCCHHH
23776212
269PhosphorylationASPSKEMSPERRSNE
CCCCCCCCHHHHCCC
23776212
274PhosphorylationEMSPERRSNERSPSP
CCCHHHHCCCCCCCC
19880383
278PhosphorylationERRSNERSPSPGSPA
HHHCCCCCCCCCCCC
23111157
280PhosphorylationRSNERSPSPGSPAPL
HCCCCCCCCCCCCCH
23111157
283PhosphorylationERSPSPGSPAPLRKV
CCCCCCCCCCCHHHC
23111157
294PhosphorylationLRKVDAASRSQSPYA
HHHCCHHHHCCCCCC
23776212
296PhosphorylationKVDAASRSQSPYAAE
HCCHHHHCCCCCCCC
23776212
298PhosphorylationDAASRSQSPYAAE--
CHHHHCCCCCCCC--
23776212
300PhosphorylationASRSQSPYAAE----
HHHCCCCCCCC----
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 SC35_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SC35_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 SC35_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRC30_ARATHSCL30physical
18674533
SL30A_ARATHSCL30Aphysical
18674533
SRC33_ARATHSR33physical
18674533
SC35_ARATHSC35physical
18674533

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SC35_ARATH

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Related Literatures of Post-Translational Modification

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