PTM Viewer PTM Viewer

AT5G66570.1

Arabidopsis thaliana [ath]

PS II oxygen-evolving complex 1

62 PTM sites : 11 PTM types

PLAZA: AT5G66570
Gene Family: HOM05D003002
Other Names: MSP-1,MANGANESE-STABILIZING PROTEIN 1,OE33,OXYGEN EVOLVING COMPLEX 33 KILODALTON PROTEIN,OEE1,33 KDA OXYGEN EVOLVING POLYPEPTIDE 1,OEE33,OXYGEN EVOLVING ENHANCER PROTEIN 33,PSBO-1,PS II OXYGEN-EVOLVING COMPLEX 1; PSBO1

Link out to other resources with this protein ID : TAIR   |   PeptideAtlas   |   ARAPORT   |   PhosPhAt

For each protein all PTMs are highlighted by default in the respective protein sequence (right-hand side). One can adjust a selection of PTMs in the PTM table on the left-hand side. In addition, functional protein domains and sites can be underlined if desired.

In the PTM table per PTM the PTM position and type is indicated, as well as the plain peptide sequence that was identified by mass spectrometry. The respective proteomics study is indicated by a number, providing a link to consult the experimental details. Additional PTM meta-data includes various confidence measures such as peptide score provided by search algorithms, posterior error probability (PEP), precursor mass deviation (in ppm) and modification site probability. The available confidence meta-data can be consulted in the extended PTM table by clicking SHOW CONFIDENCE. However, in the default PTM table, a color-coding of confidence is provided with green indicating high confidence, olive medium confidence, grey low confidence, and no color an unassigned confidence. More details regarding this confidence assignment can be consulted in the tutorial or the Plant PTM Viewer manuscript.

Besides confidence measures, log2 fold changes between two conditions with significance values (P- or Q-values) are shown if provided in the respective publication. Log2 fold changes are colored in heatmap-like gradient (green = induced, red = repressed) and significant values are highlighted in green. To determine significance, we employed the threshold used in the respective publication. For more details on the quantitative measurements we refer to the experimental details and respective publication, as methodologies can differ.

On the bottom of the page one can send the whole protein or a part of the protein (i.e. a functional domain) to PTM Blast. This will display aligned protein sequences that potentially report aligned PTMs.

PTMs



PTM Type

Mod AA

Pos

Peptide

Exp ID

Conf
nt A 2 AASLQSTATFLQSAKIATAPSR92
nta A 2 AASLQSTATFLQSAKIATAPSR92
119
nt E 86 EGAPKRLTYDEIQSKTYMEVKGTGTANQCPTIDGGSE119
EGAPKRLTYDEIQSKTYMEVKGTGTAN119
EGAPKRLTYDEIQSKTYME119
EGAPKRLTYDEIQSKTY167b
ph T 93 RLTYDEIQSK86a
ph Y 94 RLTYDEIQSK86a
86b
86c
ph S 99 RLTYDEIQSK86a
86b
86c
88
ac K 100 RLTYDEIQSKTYMEVK101
LTYDEIQSKTYMEVK101
mox M 103 TYMEVK62a
62b
nt V 105 VKGTGTANQCPTIDGGSE119
nt K 106 KGTGTANQCPTIDGGSE99
acy C 114 GTGTANQCPTIDGGSETFSFK163c
sno C 114 GTGTANQCPTIDGGSETFSFKPGK169
GTGTANQCPTIDGGSETFSFK65
169
ph T 116 GTGTANQCPTIDGGSETFSFKPGK114
ph S 121 GTGTANQCPTIDGGSETFSFKPGK114
GTGTANQCPTIDGGSETFSFK114
ph T 123 GTGTANQCPTIDGGSETFSFKPGK114
fuc S 125 GTGTANQCPTIDGGSETFSFKPGKYAGK162
ph S 125 GTGTANQCPTIDGGSETFSFKPGK114
GTGTANQCPTIDGGSETFSFK114
136
ac K 127 GTGTANQCPTIDGGSETFSFKPGK98b
cr K 127 GTGTANQCPTIDGGSETFSFKPGK164c
ac K 130 GTGTANQCPTIDGGSETFSFKPGKYAGK98d
ac K 135 KFCFEPTSFTVK98d
cr K 135 KFCFEPTSFTVK164c
acy C 137 FCFEPTSFTVK163c
sno C 137 FCFEPTSFTVK65
169
ph S 142 KFCFEPTSFTVK114
cr K 146 KFCFEPTSFTVKADSVSK164c
hib K 146 KFCFEPTSFTVKADSVSK164e
ph S 149 ADSVSKNAPPEFQNTK114
ph S 151 ADSVSKNAPPEFQNTK114
ac K 152 ADSVSKNAPPEFQNTK101
cr K 152 ADSVSKNAPPEFQNTK164c
hib K 152 ADSVSKNAPPEFQNTK164e
ac K 162 NAPPEFQNTKLMTR98d
101
ph S 182 LTYTLDEIEGPFEVASDGSVNFK100
nt E 190 EEDGIDYAAVTVQLPGGER51c
ac K 216 VPFLFTVKQLDASGKPDSFTGK36
98d
cr K 216 VPFLFTVKQLDASGKPDSFTGK164c
ph S 221 QLDASGKPDSFTGK114
ac K 223 QLDASGKPDSFTGK98b
98d
cr K 223 QLDASGKPDSFTGK164c
hib K 223 QLDASGKPDSFTGK164e
ph S 226 QLDASGKPDSFTGK88
114
ac K 230 QLDASGKPDSFTGKFLVPSYR98a
98d
101
cr K 230 QLDASGKPDSFTGKFLVPSYR164c
hib K 230 QLDASGKPDSFTGKFLVPSYR164e
ph S 239 GSSFLDPK88
ac K 245 GSSFLDPKGR98d
98e
101
me1 R 247 GRGGSTGYDNAVALPAGGRGDEEELVKENVK123
nt S 250 STGYDNAVALPAGGRGDEEE119
STGYDNAVALPAGGR119
nt G 262 GGRGDEEELVKE92
ac K 272 GDEEELVKENVK98a
98e
cr K 272 GDEEELVKENVK164c
ac K 276 GDEEELVKENVKNTAASVGEITLK101
ENVKNTAASVGEITLK101
cr K 276 ENVKNTAASVGEITLK164c
ph S 281 NTAASVGEITLK88
100
114
136
ph T 286 NTAASVGEITLK114
ac K 288 NTAASVGEITLKVTK98d
101
NTAASVGEITLK101
cr K 288 NTAASVGEITLKVTK164c
hib K 288 NTAASVGEITLKVTK164e
cr K 291 VTKSKPETGEVIGVFESLQPSDTDLGAK164c
fuc S 292 SKPETGEVIGVFESLQPSDTDLGAKVPKDVK162
SKPETGEVIGVFESLQPSDTDLGAKVPK162
cr K 316 SKPETGEVIGVFESLQPSDTDLGAKVPK164c

Sequence

Length: 332

MAASLQSTATFLQSAKIATAPSRGSSHLRSTQAVGKSFGLETSSARLTCSFQSDFKDFTGKCSDAVKIAGFALATSALVVSGASAEGAPKRLTYDEIQSKTYMEVKGTGTANQCPTIDGGSETFSFKPGKYAGKKFCFEPTSFTVKADSVSKNAPPEFQNTKLMTRLTYTLDEIEGPFEVASDGSVNFKEEDGIDYAAVTVQLPGGERVPFLFTVKQLDASGKPDSFTGKFLVPSYRGSSFLDPKGRGGSTGYDNAVALPAGGRGDEEELVKENVKNTAASVGEITLKVTKSKPETGEVIGVFESLQPSDTDLGAKVPKDVKIQGVWYGQLE

ID PTM Type Color
nt N-terminus Proteolysis X
nta N-terminal Acetylation X
ph Phosphorylation X
ac Acetylation X
mox Methionine Oxidation X
acy S-Acylation X
sno S-nitrosylation X
fuc O-Fucosylation X
cr Crotonylation X
hib 2-Hydroxyisobutyrylation X
me1 Monomethylation X
Multiple types X

Domains & Sites

Clear highlighted range 
Molecule Processing
Show Type From To
Transit Peptide 1 58
Transit Peptide 59 85

BLAST


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