SRC33_ARATH - dbPTM
SRC33_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRC33_ARATH
UniProt AC Q9SEU4
Protein Name Serine/arginine-rich SC35-like splicing factor SCL33
Gene Name SCL33
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 287
Subcellular Localization Nucleus speckle . Nucleus, nucleoplasm . Cytoplasm . Colocalizes with spliceosome components. Follows a dynamic subcellular location during the cell cycle. Distributed throughout the cell on entry into mitosis, as the nuclear envelope breaks down. In
Protein Description Involved in intron recognition and spliceosome assembly. Binds to multiple 5'-GAAG-3' repeats found in its third intron, suggesting autoregulation of alternative splicing. [PubMed: 22913769 May be necessary for accurate splicing of the 3' region of introns.]
Protein Sequence MRGRSYTPSPPRGYGRRGRSPSPRGRYGGRSRDLPTSLLVRNLRHDCRQEDLRKSFEQFGPVKDIYLPRDYYTGDPRGFGFVQFMDPADAADAKHHMDGYLLLGRELTVVFAEENRKKPTEMRARERGGGRFRDRRRTPPRYYSRSRSPPPRRGRSRSRSGDYYSPPPRRHHPRSISPREERYDGRRSYSRSPASDGSRGRSLTPVRGKSRSLSPSPRRSISRSPRRSRSPSPKRNRSVSPRRSISRSPRRSRSPRRSRRSYTPEPARSRSQSPHGGQYDEDRSPSQ
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
5Phosphorylation---MRGRSYTPSPPR
---CCCCCCCCCCCC
23776212
6Phosphorylation--MRGRSYTPSPPRG
--CCCCCCCCCCCCC
23776212
7Phosphorylation-MRGRSYTPSPPRGY
-CCCCCCCCCCCCCC
23776212
9PhosphorylationRGRSYTPSPPRGYGR
CCCCCCCCCCCCCCC
23776212
14PhosphorylationTPSPPRGYGRRGRSP
CCCCCCCCCCCCCCC
23776212
20PhosphorylationGYGRRGRSPSPRGRY
CCCCCCCCCCCCCCC
23776212
22PhosphorylationGRRGRSPSPRGRYGG
CCCCCCCCCCCCCCC
23776212
31PhosphorylationRGRYGGRSRDLPTSL
CCCCCCCCCCCCHHH
25561503
144PhosphorylationRTPPRYYSRSRSPPP
CCCCCCCCCCCCCCC
29654922
146PhosphorylationPPRYYSRSRSPPPRR
CCCCCCCCCCCCCCC
29654922
148PhosphorylationRYYSRSRSPPPRRGR
CCCCCCCCCCCCCCC
29654922
156PhosphorylationPPPRRGRSRSRSGDY
CCCCCCCCCCCCCCC
25561503
158PhosphorylationPRRGRSRSRSGDYYS
CCCCCCCCCCCCCCC
23111157
160PhosphorylationRGRSRSRSGDYYSPP
CCCCCCCCCCCCCCC
30291188
163PhosphorylationSRSRSGDYYSPPPRR
CCCCCCCCCCCCCCC
23111157
164PhosphorylationRSRSGDYYSPPPRRH
CCCCCCCCCCCCCCC
23111157
165PhosphorylationSRSGDYYSPPPRRHH
CCCCCCCCCCCCCCC
30291188
175PhosphorylationPRRHHPRSISPREER
CCCCCCCCCCCCHHH
28011693
177PhosphorylationRHHPRSISPREERYD
CCCCCCCCCCHHHCC
28011693
188PhosphorylationERYDGRRSYSRSPAS
HHCCCCCCCCCCCCC
-
190PhosphorylationYDGRRSYSRSPASDG
CCCCCCCCCCCCCCC
-
202PhosphorylationSDGSRGRSLTPVRGK
CCCCCCCCCCCCCCC
19376835
204PhosphorylationGSRGRSLTPVRGKSR
CCCCCCCCCCCCCCC
19376835
238PhosphorylationPSPKRNRSVSPRRSI
CCCCCCCCCCCCHHC
-
248PhosphorylationPRRSISRSPRRSRSP
CCHHCCCCCCCCCCC
-
261PhosphorylationSPRRSRRSYTPEPAR
CCCCCCCCCCCCCCC
29654922
262PhosphorylationPRRSRRSYTPEPARS
CCCCCCCCCCCCCCC
19880383
263PhosphorylationRRSRRSYTPEPARSR
CCCCCCCCCCCCCCC
19880383
269PhosphorylationYTPEPARSRSQSPHG
CCCCCCCCCCCCCCC
29654922
271PhosphorylationPEPARSRSQSPHGGQ
CCCCCCCCCCCCCCC
-
284PhosphorylationGQYDEDRSPSQ----
CCCCCCCCCCC----
-
286PhosphorylationYDEDRSPSQ------
CCCCCCCCC------
-

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 SRC33_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRC33_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 SRC33_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRC28_ARATHSCL28physical
18674533
SRC30_ARATHSCL30physical
18674533
SL30A_ARATHSCL30Aphysical
18674533
SRC33_ARATHSR33physical
18674533
RU17_ARATHU1-70Kphysical
10593939
SRC33_ARATHSR33physical
10593939
SR45_ARATHSR45physical
10593939

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRC33_ARATH

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Related Literatures of Post-Translational Modification

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