PECR_HUMAN - dbPTM
PECR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PECR_HUMAN
UniProt AC Q9BY49
Protein Name Peroxisomal trans-2-enoyl-CoA reductase
Gene Name PECR
Organism Homo sapiens (Human).
Sequence Length 303
Subcellular Localization Peroxisome .
Protein Description Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity..
Protein Sequence MASWAKGRSYLAPGLLQGQVAIVTGGATGIGKAIVKELLELGSNVVIASRKLERLKSAADELQANLPPTKQARVIPIQCNIRNEEEVNNLVKSTLDTFGKINFLVNNGGGQFLSPAEHISSKGWHAVLETNLTGTFYMCKAVYSSWMKEHGGSIVNIIVPTKAGFPLAVHSGAARAGVYNLTKSLALEWACSGIRINCVAPGVIYSQTAVENYGSWGQSFFEGSFQKIPAKRIGVPEEVSSVVCFLLSPAASFITGQSVDVDGGRSLYTHSYEVPDHDNWPKGAGDLSVVKKMKETFKEKAKL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
32SuccinylationGGATGIGKAIVKELL
CCCCHHHHHHHHHHH
32.78-
32SuccinylationGGATGIGKAIVKELL
CCCCHHHHHHHHHHH
32.78-
43PhosphorylationKELLELGSNVVIASR
HHHHHCCCCEEEEHH
38.7927251275
49PhosphorylationGSNVVIASRKLERLK
CCCEEEEHHHHHHHH
20.8724275569
57PhosphorylationRKLERLKSAADELQA
HHHHHHHHHHHHHHH
33.0329083192
69PhosphorylationLQANLPPTKQARVIP
HHHCCCCCCCCEEEE
33.5729083192
92UbiquitinationEEVNNLVKSTLDTFG
HHHHHHHHHHHHHCC
40.6729967540
179PhosphorylationGAARAGVYNLTKSLA
CCHHHCCCHHHHHHH
11.9721082442
182PhosphorylationRAGVYNLTKSLALEW
HHCCCHHHHHHHHHH
18.2328152594
184O-linked_GlycosylationGVYNLTKSLALEWAC
CCCHHHHHHHHHHHH
17.4030379171
288PhosphorylationPKGAGDLSVVKKMKE
CCCCCCHHHHHHHHH
29.6024702127
291AcetylationAGDLSVVKKMKETFK
CCCHHHHHHHHHHHH
45.0225953088
296PhosphorylationVVKKMKETFKEKAKL
HHHHHHHHHHHHHCC
34.1929457462

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PECR_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PECR_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PECR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTA_HUMANACTA2physical
26186194
ACY1_HUMANACY1physical
26186194
LCN1_HUMANLCN1physical
26186194
UBA5_HUMANUBA5physical
26186194
HNRPF_HUMANHNRNPFphysical
28514442
LCN1_HUMANLCN1physical
28514442
UBA5_HUMANUBA5physical
28514442
ACY1_HUMANACY1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00173Adenine
Regulatory Network of PECR_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-179, AND MASSSPECTROMETRY.

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