PTM Viewer PTM Viewer

AT3G63190.1

Arabidopsis thaliana [ath]

ribosome recycling factor, chloroplast precursor

11 PTM sites : 4 PTM types

PLAZA: AT3G63190
Gene Family: HOM05D002713
Other Names: AtcpRRF,Arabidopsis thaliana chloroplast ribosome recycling factor,HFP108,HIGH CHLOROPHYLL FLUORESCENCE AND PALE GREEN MUTANT 108,cpRRF,chloroplast ribosome recycling factor; RRF
Uniprot
Q9M1X0

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 83 ATIEEIEAEKSAIETDVKSKMEKTIETL167b
ATIEEIEAEKSAIETD119
ac K 100 SAIETDVKSK101
ph S 101 SAIETDVKSK88
ac K 166 SSLKAIEK101
ph S 197 LSLPPLTSDR88
ac K 205 ELSKVVAK98a
ac K 227 DALKSYDKLEK98e
ac K 231 SYDKLEK98a
101
ac K 234 SYDKLEKEK101
mox M 258 LIDVYMK62a
62b
ac K 266 KIEELYKQK101
IEELYKQK101

Sequence

Length: 275

MAASFSSTAPTTPVLRFRANYSKPLLSLPDSCLRIISSAISPSTRLIACSFKTDKLPLGAGVNLSGGPVVKRSLQKRLVIRSATIEEIEAEKSAIETDVKSKMEKTIETLRTSFNSIRTGRSNAAMLDKIEVEYYGSPVSLKSIAQISTPDGSSLLLQPYDKSSLKAIEKAIVNSDLGVTPNNDGDVIRLSLPPLTSDRRKELSKVVAKQSEEGKVALRNIRRDALKSYDKLEKEKKLSEDNVKDLSSDLQKLIDVYMKKIEELYKQKEKELMKV

ID PTM Type Color
nt N-terminus Proteolysis X
ac Acetylation X
ph Phosphorylation X
mox Methionine Oxidation X
Multiple types X

Domains & Sites

Clear highlighted range 
Interpro Domains
Show IPR ID From To
IPR023584 111 273
Molecule Processing
Show Type From To
Transit Peptide 1 82

BLAST


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