RBS1A_ARATH - dbPTM
RBS1A_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBS1A_ARATH
UniProt AC P10795
Protein Name Ribulose bisphosphate carboxylase small chain 1A, chloroplastic
Gene Name RBCS-1A
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 180
Subcellular Localization Plastid, chloroplast membrane
Peripheral membrane protein . Plastid, chloroplast stroma .
Protein Description RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site (By similarity)..
Protein Sequence MASSMLSSATMVASPAQATMVAPFNGLKSSAAFPATRKANNDITSITSNGGRVNCMQVWPPIGKKKFETLSYLPDLTDSELAKEVDYLIRNKWIPCVEFELEHGFVYREHGNSPGYYDGRYWTMWKLPLFGCTDSAQVLKEVEECKKEYPNAFIRIIGFDNTRQVQCISFIAYKPPSFTG
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
69PhosphorylationIGKKKFETLSYLPDL
CCCCEEEEECCCCCC
24.9222092075
71PhosphorylationKKKFETLSYLPDLTD
CCEEEEECCCCCCCH
31.8523776212
72PhosphorylationKKFETLSYLPDLTDS
CEEEEECCCCCCCHH
25.9323776212
77PhosphorylationLSYLPDLTDSELAKE
ECCCCCCCHHHHHHH
44.8830291188
79PhosphorylationYLPDLTDSELAKEVD
CCCCCCHHHHHHHHH
29.3130291188
87PhosphorylationELAKEVDYLIRNKWI
HHHHHHHHHHHCCCC
14.8129654922
113PhosphorylationVYREHGNSPGYYDGR
EEEECCCCCCCCCCC
25.0523776212
116PhosphorylationEHGNSPGYYDGRYWT
ECCCCCCCCCCCCEE
11.1923776212
117PhosphorylationHGNSPGYYDGRYWTM
CCCCCCCCCCCCEEE
20.1723776212
126AcetylationGRYWTMWKLPLFGCT
CCCEEEEEEEECCCC
29.4221311031
133PhosphorylationKLPLFGCTDSAQVLK
EEEECCCCCHHHHHH
33.1130291188
135PhosphorylationPLFGCTDSAQVLKEV
EECCCCCHHHHHHHH
11.4930291188
162PhosphorylationRIIGFDNTRQVQCIS
EEEECCCCCEEEEEE
25.0730291188
177PhosphorylationFIAYKPPSFTG----
EEEECCCCCCC----
43.9219376835
179PhosphorylationAYKPPSFTG------
EECCCCCCC------
46.4429654922

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 RBS1A_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBS1A_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 RBS1A_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MD37C_ARATHHSP70physical
20028838
SUMO3_ARATHSUMO3physical
20855607
SUMO1_ARATHSUMO1physical
20855607

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBS1A_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-79; SER-113 AND SER-177,AND MASS SPECTROMETRY.

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