KEGG   PATHWAY: tps04141
Entry
tps04141                    Pathway                                
Name
Protein processing in endoplasmic reticulum - Thalassiosira pseudonana
Description
The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis.
Class
Genetic Information Processing; Folding, sorting and degradation
Pathway map
tps04141  Protein processing in endoplasmic reticulum
tps04141

Other DBs
GO: 0030433 0034976
Organism
Thalassiosira pseudonana [GN:tps]
Gene
THAPSDRAFT_10025  [KO:K14004]
THAPSDRAFT_10077  [KO:K03094]
THAPSDRAFT_105  [KO:K03237]
THAPSDRAFT_16926  [KO:K14016]
THAPSDRAFT_17859  [KO:K13989]
THAPSDRAFT_21756  [KO:K04523]
THAPSDRAFT_21965  [KO:K09584] [EC:5.3.4.1]
THAPSDRAFT_22140  [KO:K14016]
THAPSDRAFT_22248  [KO:K14006]
THAPSDRAFT_22319  [KO:K14018]
THAPSDRAFT_22432  [KO:K06689] [EC:2.3.2.23]
THAPSDRAFT_22477  [KO:K10661] [EC:2.3.2.27]
THAPSDRAFT_22579  [KO:K12275]
THAPSDRAFT_22766  [KO:K09487]
THAPSDRAFT_22963  [KO:K14005]
THAPSDRAFT_23857  [KO:K24348]
THAPSDRAFT_2409  [KO:K14015]
THAPSDRAFT_24902  [KO:K10601] [EC:2.3.2.27]
THAPSDRAFT_25024  [KO:K14012]
THAPSDRAFT_25599  [KO:K14001]
THAPSDRAFT_261059  [KO:K11718] [EC:2.4.1.-]
THAPSDRAFT_261109  [KO:K03283]
THAPSDRAFT_261702  [KO:K13993]
THAPSDRAFT_261710  STT3b; oliosaccharyl transferase [KO:K07151] [EC:2.4.99.18]
THAPSDRAFT_263031  Rad23; Rad23 like protein [KO:K10839]
THAPSDRAFT_267952  [KO:K13525]
THAPSDRAFT_267964  [KO:K03347]
THAPSDRAFT_268640  [KO:K01230] [EC:3.2.1.113]
THAPSDRAFT_269120  hsp70; heat shock protein 70 [KO:K03283]
THAPSDRAFT_269547  [KO:K09523]
THAPSDRAFT_26957  [KO:K09540]
THAPSDRAFT_269747  [KO:K14007]
THAPSDRAFT_27656  hsp70_4; heat shock protein/chaperone [KO:K09490] [EC:3.6.4.10]
THAPSDRAFT_28189  HSP70_3; heat shock protein, HSP70, hsc70 [KO:K03283]
THAPSDRAFT_28710  [KO:K10597] [EC:2.3.2.27]
THAPSDRAFT_28769  SEC61-2; protein transportor [KO:K10956]
THAPSDRAFT_3013  ubc; ubiquitin conjugating enzyme [KO:K10575] [EC:2.3.2.23]
THAPSDRAFT_30950  [KO:K10085]
THAPSDRAFT_34810  [KO:K08057]
THAPSDRAFT_34968  [KO:K23741]
THAPSDRAFT_35036  [KO:K13989]
THAPSDRAFT_36798  [KO:K08852] [EC:2.7.11.1 3.1.26.-]
THAPSDRAFT_37083  [KO:K09503]
THAPSDRAFT_38322  [KO:K07953] [EC:3.6.5.-]
THAPSDRAFT_38460  [KO:K03094]
THAPSDRAFT_38578  BIP2; luminal binding protein [KO:K09490] [EC:3.6.4.10]
THAPSDRAFT_39497  [KO:K07953] [EC:3.6.5.-]
THAPSDRAFT_40232  OAM1; mannosyl-oligosaccharide 1,2-alpha-mannosidase [KO:K01230] [EC:3.2.1.113]
THAPSDRAFT_40817  [KO:K03868] [EC:2.3.2.32]
THAPSDRAFT_4160  [KO:K07151] [EC:2.4.99.18]
THAPSDRAFT_41898  HSP70_2; heat shock protein [KO:K09486]
THAPSDRAFT_4224  [KO:K04523]
THAPSDRAFT_5036  [KO:K11863] [EC:3.4.22.-]
THAPSDRAFT_6285  HSP90_1; HSP90 family member [KO:K04079]
THAPSDRAFT_6534  [KO:K13989]
THAPSDRAFT_9466  [KO:K11519]
THAPS_17910  [KO:K04554] [EC:2.3.2.23]
THAPS_23368  [KO:K09562]
THAPS_25355  SEC61-1; protein translocase complex subunit [KO:K10956]
THAPS_35410  [KO:K01456] [EC:3.5.1.52]
THAPS_38207  [KO:K07342]
THAPS_41300  EXG1; glucosidase II alpha subunit [KO:K05546] [EC:3.2.1.207]
Compound
C00076  Calcium cation
G00009  
G00010  
G00011  
G00012  
G10694  
Reference
  Authors
Naidoo N
  Title
ER and aging-Protein folding and the ER stress response.
  Journal
Ageing Res Rev 8:150-9 (2009)
DOI:10.1016/j.arr.2009.03.001
Reference
  Authors
Malhotra JD, Kaufman RJ
  Title
The endoplasmic reticulum and the unfolded protein response.
  Journal
Semin Cell Dev Biol 18:716-31 (2007)
DOI:10.1016/j.semcdb.2007.09.003
Reference
  Authors
Maattanen P, Gehring K, Bergeron JJ, Thomas DY
  Title
Protein quality control in the ER: the recognition of misfolded proteins.
  Journal
Semin Cell Dev Biol 21:500-11 (2010)
DOI:10.1016/j.semcdb.2010.03.006
Reference
  Authors
Stolz A, Wolf DH
  Title
Endoplasmic reticulum associated protein degradation: a chaperone assisted journey to hell.
  Journal
Biochim Biophys Acta 1803:694-705 (2010)
DOI:10.1016/j.bbamcr.2010.02.005
Reference
  Authors
Dejgaard K, Theberge JF, Heath-Engel H, Chevet E, Tremblay ML, Thomas DY
  Title
Organization of the Sec61 translocon, studied by high resolution native electrophoresis.
  Journal
J Proteome Res 9:1763-71 (2010)
DOI:10.1021/pr900900x
Related
pathway
tps00510  N-Glycan biosynthesis
tps03050  Proteasome
tps03060  Protein export
KO pathway
ko04141   

DBGET integrated database retrieval system