CHIP_ARATH - dbPTM
CHIP_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHIP_ARATH
UniProt AC Q9SRS9
Protein Name E3 ubiquitin-protein ligase CHIP {ECO:0000305}
Gene Name CHIP {ECO:0000303|PubMed:20028838}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 278
Subcellular Localization
Protein Description Has E3 ubiquitin-protein ligase activity and may target misfolded substrates towards proteasomal degradation. Regulates the activity of some serine/threonine-protein phosphatases by E3 ubiquitin-protein ligase activity. Required for responses to biotic and abiotic stresses such as auxin, abscisic acid (ABA), low and high temperature and darkness, probably through the activation of serine/threonine-protein phosphatase and the subsequent modification of the plasma membrane composition. Regulates the chloroplastic Clp proteolytic activity in response to stresses. Ubiquitylates FtsH1, a component of the chloroplast FtsH protease, and affects protein degradation in chloroplasts. Mediates plastid precursor degradation to prevent cytosolic precursor accumulation, together with the molecular chaperone HSC70-4. Mediates ubiquitination of transit peptides and thereby led to their degradation through the ubiquitin-proteasome system..
Protein Sequence MVTGVASAMAERLKEDGNNCFKKERFGAAIDAYTEAIALSPNVPAYWTNRALCHMKRKDWTKVEEDCRKAIQLVHNSVKAHYMLGLALLQKKEFTNGVKELQRALDLGRCSNPTGYMVEEIWEELSKAKYMEWELVSAMRSWELNSLKETCEAALNQQRALDMSRTEESSDEAYTAHTERLKALERVFKKAAEEDKPTEVPDYLCCNITLEIFRDPVISPSGVTYERAAILEHLKKVGKFDPITREKIDPANLVPNLAIKEAVAAYLEKHVWAYKMGC
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
9SulfoxidationVTGVASAMAERLKED
CCHHHHHHHHHHHHC
3.5425693801

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 CHIP_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHIP_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 CHIP_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC8_ARATHUBC8physical
16640601
UBC9_ARATHUBC9physical
16640601
UBC10_ARATHUBC10physical
16640601
R27AC_ARATHUBQ5physical
16640601
2AAG_ARATHPP2AA3physical
16640601
FTSH1_ARATHFTSH1physical
16640601
CLPP4_ARATHCLPP4physical
16640601
RBS3B_ARATHAT5G38410physical
16640601
2AAA_ARATHRCN1physical
16640601
MD37C_ARATHHSP70physical
20028838
FTSH1_ARATHFTSH1physical
17714429
MD37C_ARATHHSP70physical
17714429
CLPP4_ARATHCLPP4physical
17241447
ODPA1_ARATHE1 ALPHAphysical
24846764
ODP24_ARATHLTA2physical
24846764
CLPP3_ARATHCLPP3physical
26085677
CLPP5_ARATHCLPP5physical
26085677

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

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Related Literatures of Post-Translational Modification

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