Difference between revisions of "Sequence-based predictions TSD"
(→Transmembrane helices) |
|||
Line 4: | Line 4: | ||
'''Thor:''' ...He's adopted |
'''Thor:''' ...He's adopted |
||
+ | <!-- seit wann zitieren wir denn ami kinofilme ;)? gut der film is aber auch nice ... --> |
||
If not noted otherwise, the sequence for all predictions is the [[HEXA Reference sequence]]. A protocol for this task can be found [[Sequence-based predictions Protocol TSD|here]]. |
If not noted otherwise, the sequence for all predictions is the [[HEXA Reference sequence]]. A protocol for this task can be found [[Sequence-based predictions Protocol TSD|here]]. |
||
Line 18: | Line 19: | ||
<br> |
<br> |
||
Dopamine D3 receptor, KvAP and AQP-4 are multi-pass membrane proteins. |
Dopamine D3 receptor, KvAP and AQP-4 are multi-pass membrane proteins. |
||
+ | <figtable id="tab:gopetgo"> |
||
+ | {| class="wikitable", style="width:750px; border-collapse: collapse; border-style: solid; border-width:0px; border-color: #000" |
||
+ | |- |
||
+ | ! style="border-style: solid; border-width: 0 0 0 0;" colspan="8" | Positions of transmembrane helices |
||
+ | |- |
||
+ | ! style="border-style: solid; border-width: 0 0 0 0" | Drd3 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" | 33–35 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" |66–88 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" | 105–126 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" |150–170 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" |188–212 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" |330–351 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" |367–388 |
||
+ | |- |
||
+ | ! style="border-style: solid; border-width: 0 0 0 0" | KvAP |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" | 39–63 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" | 68–92 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" |109–125 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" | 129–145 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" | 160–184 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" | 222–253 |
||
+ | |||
+ | |- |
||
+ | ! style="border-style: solid; border-width: 0 0 0 0" |AQP-4 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" | 37–57 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" |65–85 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" |116–136 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" |156–176 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" |185–205 |
||
+ | | style="border-style: solid; border-width: 0 0 0 0" |232–252 |
||
+ | |- |
||
+ | |} |
||
+ | '''Table TODO''': Assigned transmembrane regions in Uniprot |
||
+ | </figtable> |
||
+ | |||
== Signal peptides == |
== Signal peptides == |
Revision as of 17:21, 14 May 2012
Thor: He's my brother
Natasha Romanoff: He killed 80 people in 2 days
Thor: ...He's adopted
If not noted otherwise, the sequence for all predictions is the HEXA Reference sequence. A protocol for this task can be found here.
Contents
Secondary structure
Proteins: Ribonuclease inhibitor P10775 , CutA Q9X0E6 , CAM-PRP catalytic subunit Q08209
Ribonuclease inhibitor and CutA are located in the cytoplasm whereas the CAM-PRP catalytic subunit is located in the nucleus.
Disorder
Transmembrane helices
Proteins: Dopamine D3 receptor P35462 , KvAP Q9YDF8 , AQP-4 P47863
Dopamine D3 receptor, KvAP and AQP-4 are multi-pass membrane proteins.
<figtable id="tab:gopetgo">
Positions of transmembrane helices | |||||||
---|---|---|---|---|---|---|---|
Drd3 | 33–35 | 66–88 | 105–126 | 150–170 | 188–212 | 330–351 | 367–388 |
KvAP | 39–63 | 68–92 | 109–125 | 129–145 | 160–184 | 222–253 | |
AQP-4 | 37–57 | 65–85 | 116–136 | 156–176 | 185–205 | 232–252 |
Table TODO: Assigned transmembrane regions in Uniprot </figtable>
Signal peptides
Proteins: Serum albumin P02768, LAMP-1 P11279, AQP-4 P47863
HEXA LAMP-1 and Serum albumin contain a signal peptide. HEXA has an assigned peptide between position 1 and 22, LAMP-1 between 1 and 28 and Serum albumin between position 1 and 18.
LAMP-1 is a membrane protein which passes the membrane with one helix. Serum albumin, the main protein of plasma, is a secreted extracellular protein.
AQP-4 is a multi-pass membrane protein which forms a waterspecific channel and functions in transport.
The prediction of the displayed results was performed with SignalP version 4.0.
SignalP employs 3 main scores for the prediction of signal peptides, C, S and Y. The S-score stands for the actual signal peptide prediction, with high scores indicating that the corresponding amino acid is part of a signal peptide, and low scores indicating that the amino acid is part of a mature protein.
The C-score is the cleavage score, which indicates the best cleavage cite when significantly high. (When a cleavage site position is referred to by a single number, the number indicates the first residue in the mature protein.)
Y-max is a derivative of the C-score combined with the S-score calculated to give a better cleavage site prediction than the raw C-score alone.
There are two additional scores reported in the SignalP output, namely the S-mean and the D-score. The S-mean is the average of the S-score, ranging from the N-terminal amino acid to the amino acid assigned with the highest Y-max score. The D-score is implemented as a weighted average of the S-mean and the Y-max scores.
For non-secretory proteins all scores are supposed to be very low.
<figtable id="tbl:signalp">
Table : Signal peptide predictions. |
</figtable>
The <xr id="tbl:signalp"/> displays the results of the SignalP predictions. HEXA, LAMP-1 and Serum albumin are correctly predicted one signal peptide at the beginning of the sequence and AQP-4 is identified as a mature protein.
GO terms
GOpet
<figtable id="tab:gopetgo">
GO-Term ID | Type | Confidence | GO-Term description |
---|---|---|---|
GO:0003824 | Molecular function | 97% | catalytic activity |
GO:0004563 | Molecular function | 96% | beta-N-acetylhexosaminidase activity |
GO:0015929 | Molecular function | 96% | hexosaminidase activity |
GO:0016787 | Molecular function | 96% | hydrolase activity |
GO:0016798 | Molecular function | 96% | hydrolase activity acting on glycosyl bonds |
GO:0004553 | Molecular function | 96% | hydrolase activity hydrolyzing O-glycosyl compounds |
GO:0016799 | Molecular function | 77% | hydrolase activity hydrolyzing N-glycosyl compounds |
GO:0046982 | Molecular function | 61% | protein heterodimerization activity |
Table TODO: </figtable>