PSAD2_ARATH - dbPTM
PSAD2_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSAD2_ARATH
UniProt AC Q9SA56
Protein Name Photosystem I reaction center subunit II-2, chloroplastic
Gene Name PSAD2
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 204
Subcellular Localization Plastid, chloroplast thylakoid membrane
Peripheral membrane protein
Stromal side.
Protein Description PSAD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein (By similarity)..
Protein Sequence MATQAAGIFSPAITTTTSAVKKLHLFSSSHRPKSLSFTKTAIRAEKTESSSAAPAVKEAPVGFTPPQLDPNTPSPIFAGSTGGLLRKAQVEEFYVITWNSPKEQIFEMPTGGAAIMREGPNLLKLARKEQCLALGTRLRSKYKITYQFYRVFPNGEVQYLHPKDGVYPEKANPGREGVGLNMRSIGKNVSPIEVKFTGKQSYDL
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
15PhosphorylationIFSPAITTTTSAVKK
CCCCCEECCHHHHHH
23.2025368622
16PhosphorylationFSPAITTTTSAVKKL
CCCCEECCHHHHHHH
15.3125368622
17PhosphorylationSPAITTTTSAVKKLH
CCCEECCHHHHHHHH
16.7625368622
18PhosphorylationPAITTTTSAVKKLHL
CCEECCHHHHHHHHH
29.0425368622
36PhosphorylationSHRPKSLSFTKTAIR
CCCCCCCCEECHHHH
37.6519880383
47PhosphorylationTAIRAEKTESSSAAP
HHHHHHHCCCCCCCC
32.3819376835
49PhosphorylationIRAEKTESSSAAPAV
HHHHHCCCCCCCCCC
34.5219880383
50PhosphorylationRAEKTESSSAAPAVK
HHHHCCCCCCCCCCC
20.1219880383
64PhosphorylationKEAPVGFTPPQLDPN
CCCCCCCCCCCCCCC
28.2922092075
72PhosphorylationPPQLDPNTPSPIFAG
CCCCCCCCCCCCCCC
30.4527029354
74PhosphorylationQLDPNTPSPIFAGST
CCCCCCCCCCCCCCC
28.7027029354
80PhosphorylationPSPIFAGSTGGLLRK
CCCCCCCCCCCHHHH
22.0527029354
81PhosphorylationSPIFAGSTGGLLRKA
CCCCCCCCCCHHHHC
34.0627029354
110PhosphorylationEQIFEMPTGGAAIMR
HHEEECCCCCCHHHC
47.1122092075
145PhosphorylationLRSKYKITYQFYRVF
HHHCEEEEEEEEEEC
13.7129654922
190PhosphorylationRSIGKNVSPIEVKFT
CCCCCCCCCEEEEEE
29.5625561503

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 PSAD2_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSAD2_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 PSAD2_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUT1C_ARATHAT1G52220physical
18813226
CDC23_ARATHAPC8physical
21798944
KNAT1_ARATHKNAT1physical
21798944
BOI_ARATHRINGphysical
21798944
CLAH2_ARATHAT3G08530physical
21798944
HS157_ARATHAT5G37670physical
21798944
BH027_ARATHAT4G29930physical
21798944
TCP13_ARATHPTF1physical
21798944

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSAD2_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 THR-47, AND MASSSPECTROMETRY.

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