PER34_ARATH - dbPTM
PER34_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PER34_ARATH
UniProt AC Q9SMU8
Protein Name Peroxidase 34
Gene Name PER34
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 353
Subcellular Localization Secreted . Vacuole . Carboxy-terminal extension appears to target the protein to vacuoles.
Protein Description Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.; May be implicated in the systemic acquired resistance response via the salicylic acid signal transduction pathway. Exhibits a Ca(2+)-pectate binding affinity which could be interpreted in vivo as a specificity to interact with the pectic structure of the cell wall..
Protein Sequence MHFSSSSTSSTWTILITLGCLMLHASLSAAQLTPTFYDRSCPNVTNIVRETIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGNANSARGFPVIDRMKAAVERACPRTVSCADMLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLELANANLPAPFFTLPQLKASFRNVGLDRPSDLVALSGGHTFGKNQCQFILDRLYNFSNTGLPDPTLNTTYLQTLRGLCPLNGNRSALVDFDLRTPTVFDNKYYVNLKERKGLIQSDQELFSSPNATDTIPLVRAYADGTQTFFNAFVEAMNRMGNITPTTGTQGQIRLNCRVVNSNSLLHDVVDIVDFVSSM
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
31Pyrrolidone_carboxylic_acidHASLSAAQLTPTFYD
HHHHHHHHCCCCCCC
45.65-
31Pyrrolidone_carboxylic_acidHASLSAAQLTPTFYD
HHHHHHHHCCCCCCC
45.65-
43N-linked_GlycosylationFYDRSCPNVTNIVRE
CCCCCCCCHHHHHHH
58.53-
87N-linked_GlycosylationDASILLDNTTSFRTE
CCCCCCCCCCCCCCC
45.27-
197PhosphorylationPSDLVALSGGHTFGK
HHHEEEECCCCCCCH
32.7522092075
216N-linked_GlycosylationFILDRLYNFSNTGLP
HHHHHHHHCCCCCCC
38.16-
228N-linked_GlycosylationGLPDPTLNTTYLQTL
CCCCCCCCHHHHHHH
32.62-
244N-linked_GlycosylationGLCPLNGNRSALVDF
HCCCCCCCCCEEEEE
33.39-
285N-linked_GlycosylationQELFSSPNATDTIPL
HHHHCCCCCCCCCCC
58.37-

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 PER34_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PER34_ARATH !!

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 PER34_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PER34_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PER34_ARATH

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Related Literatures of Post-Translational Modification

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