PSAN_ARATH - dbPTM
PSAN_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSAN_ARATH
UniProt AC P49107
Protein Name Photosystem I reaction center subunit N, chloroplastic
Gene Name PSAN
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 171
Subcellular Localization Plastid, chloroplast thylakoid membrane
Peripheral membrane protein
Lumenal side.
Protein Description May function in mediating the binding of the antenna complexes to the PSI reaction center and core antenna. Plays an important role in docking plastocyanin to the PSI complex. Does not bind pigments..
Protein Sequence MAAMNSSVLTCSYAIAGSGSVELNQKVGLVNSSVGFGQKKQMIMPVIKAQRVVGDDVDGSNGRRSAMVFLAATLFSTAAVSASANAGVIDEYLERSKTNKELNDKKRLATSGANFARAFTVQFGSCKFPENFTGCQDLAKQKKVPFISEDIALECEGKDKYKCGSNVFWKW
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
65PhosphorylationDGSNGRRSAMVFLAA
CCCCCHHHHHHHHHH
21.2525368622
73PhosphorylationAMVFLAATLFSTAAV
HHHHHHHHHHHHHHH
23.8025368622
76PhosphorylationFLAATLFSTAAVSAS
HHHHHHHHHHHHHHH
21.9025368622
77PhosphorylationLAATLFSTAAVSASA
HHHHHHHHHHHHHHC
15.9925368622
83PhosphorylationSTAAVSASANAGVID
HHHHHHHHCCCCHHH
17.9825368622
87AcetylationVSASANAGVIDEYLE
HHHHCCCCHHHHHHH
19.4018431481
92NitrationNAGVIDEYLERSKTN
CCCHHHHHHHHHCCC
15.32-
120PhosphorylationANFARAFTVQFGSCK
CCHHHEEEEECCCCC
16.6519376835
125PhosphorylationAFTVQFGSCKFPENF
EEEEECCCCCCCCCC
18.5419376835
133PhosphorylationCKFPENFTGCQDLAK
CCCCCCCCCHHHHHH
48.9424243849

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 PSAN_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSAN_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 PSAN_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PSAN_ARATH !!

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

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Sorting signals, N-terminal modifications and abundance of thechloroplast proteome.";
Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O.,Sun Q., van Wijk K.J.;
PLoS ONE 3:E1994-E1994(2008).
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, AND ACETYLATION AT GLY-87.

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