PTM Viewer PTM Viewer

AT5G64300.1

Arabidopsis thaliana [ath]

GTP cyclohydrolase II

5 PTM sites : 4 PTM types

PLAZA: AT5G64300
Gene Family: HOM05D000723
Other Names: ATGCH,ARABIDOPSIS THALIANA GTP CYCLOHYDROLASE II,ATRIBA1,Arabidopsis thaliana riboflavin A1,RFD1,RED FLUORESCENT IN DARKNESS 1,RIBA1,riboflavin A1; GCH

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 57 AAVISREDDLLSFTN119
nt S 80 SLIDDRTEEPLE99
sno C 384 VHSECLTGDIFGSAR90a
90b
169
so C 384 VHSECLTGDIFGSAR108
ph S 539 FKGDVVEKIESESES85
114
GDVVEKIESESES109

Sequence

Length: 543

MSSINLSSSSPSTISLSRSRLSQSSTTLLHGLHRVTLPSNHPLSTFSIKTNTGKVKAAVISREDDLLSFTNGNTPLSNGSLIDDRTEEPLEADSVSLGTLAADSAPAPANGFVAEDDDFELDLPTPGFSSIPEAIEDIRQGKLVVVVDDEDRENEGDLVMAAQLATPEAMAFIVRHGTGIVCVSMKEDDLERLHLPLMVNQKENEEKLSTAFTVTVDAKHGTTTGVSARDRATTILSLASRDSKPEDFNRPGHIFPLKYREGGVLKRAGHTEASVDLTVLAGLDPVGVLCEIVDDDGSMARLPKLREFAAENNLKVVSIADLIRYRRKRDKLVERASAARIPTMWGPFTAYCYRSILDGIEHIAMVKGEIGDGQDILVRVHSECLTGDIFGSARCDCGNQLALSMQQIEATGRGVLVYLRGHEGRGIGLGHKLRAYNLQDAGRDTVEANEELGLPVDSREYGIGAQIIRDLGVRTMKLMTNNPAKYVGLKGYGLAIVGRVPLLSLITKENKRYLETKRTKMGHMYGLKFKGDVVEKIESESES

ID PTM Type Color
nt N-terminus Proteolysis X
sno S-nitrosylation X
so S-sulfenylation X
ph Phosphorylation X
Multiple types X

Domains & Sites

Clear highlighted range 
Interpro Domains
Show IPR ID From To
IPR032677 335 501
Molecule Processing
Show Type From To
Transit Peptide 1 56
Sites
Show Type Position
Metal Ion-binding Site 253
Metal Ion-binding Site 291
Site 457
Site 459
Active Site 152
Active Site 157
Active Site 267
Active Site 291
Active Site 153
Active Site 153
Active Site 270
Active Site 379
Active Site 400
Active Site 423
Active Site 445
Active Site 480
Active Site 485
Active Site 384
Active Site 395
Active Site 397

BLAST


Perform a BLAST search for this sequence, or a part of this sequence (minimum 50 characters)
A downloadable tutorial can be found here