dbPTM

PSMD4_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSMD4_ARATH
UniProt AC	P55034
Protein Name	26S proteasome non-ATPase regulatory subunit 4 homolog
Gene Name	RPN10
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	386
Subcellular Localization
Protein Description	Plays a role in maintaining the structural integrity of the 19S regulatory particle (RP), subcomplex of the 26S proteasome. Plays a major role in both the direct and indirect recognition of ubiquitinated substrates of ubiquitin/26S proteasome-mediated proteolysis (UPP). Binds and presumably selects ubiquitin-conjugates for destruction. Prefers multiubiquitin chains rather than single ubiquitins, with a binding affinity for 'Lys-48'-linked ubiquitin chains. Acts as a potential docking subunit for both ubiquitin receptors RAD23s and DSK2s. Plays a role in the growth and development via the proteasome-dependent degradation of the ABA-signaling protein ABI5/DPBF1. Plays an important role for balancing cell expansion with cell proliferation rates during shoot development..
Protein Sequence	MVLEATMICIDNSEWMRNGDYSPSRLQAQTEAVNLLCGAKTQSNPENTVGILTMAGKGVRVLTTPTSDLGKILACMHGLDVGGEINLTAAIQIAQLALKHRQNKNQRQRIIVFAGSPIKYEKKALEIVGKRLKKNSVSLDIVNFGEDDDEEKPQKLEALLTAVNNNDGSHIVHVPSGANALSDVLLSTPVFTGDEGASGYVSAAAAAAAAGGDFDFGVDPNIDPELALALRVSMEEERARQEAAAKKAADEAGQKDKDGDTASASQETVARTTDKNAEPMDEDSALLDQAIAMSVGDVNMSEAADEDQDLALALQMSMSGEESSEATGAGNNLLGNQAFISSVLSSLPGVDPNDPAVKELLASLPDESKRTEEEESSSKKGEDEKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
22	Phosphorylation	WMRNGDYSPSRLQAQ HHHCCCCCHHHHHHH	22.57	29654922
24	Phosphorylation	RNGDYSPSRLQAQTE HCCCCCHHHHHHHHH	39.42	25561503
261	Phosphorylation	QKDKDGDTASASQET CCCCCCCCCCCCHHH	28.21	23776212
263	Phosphorylation	DKDGDTASASQETVA CCCCCCCCCCHHHHH	30.46	30291188
265	Phosphorylation	DGDTASASQETVART CCCCCCCCHHHHHHC	26.50	23776212
268	Phosphorylation	TASASQETVARTTDK CCCCCHHHHHHCCCC	16.30	23776212
363	Phosphorylation	AVKELLASLPDESKR HHHHHHHCCCCHHHC	40.16	30291188
378	Phosphorylation	TEEEESSSKKGEDEK CHHHHHHHCCCCCCC	47.90	25561503

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 PSMD4_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSMD4_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 PSMD4_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATG8A_ARATH	APG8A	physical	26004230
DSK2B_ARATH	DSK2	physical	26004230
PS13A_ARATH	AT5G45620	physical	26004230

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PSMD4_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis."; de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.; J. Proteome Res. 7:2458-2470(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASSSPECTROMETRY.	18433157 [Abstract]