MUB1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MUB1_ARATH
• UniProt AC: Q9MAB9
• Protein Name: Membrane-anchored ubiquitin-fold protein 1
• Gene Name: MUB1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 117
• Subcellular Localization: Cell membrane ; Lipid-anchor .
• Protein Description: May serve as docking site to facilitate the association of other proteins to the plasma membrane..
• Protein Sequence: MAEVHNQLEIKFRLTDGSDIGPKAFPDATTVSALKETVISEWPREKENGPKTVKEVKLISAGKVLENSKTVKDYRSPVSNLAGAVTTMHVIIQAPVTEKEKKPKGDPKMNKCVCSVM

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
112	S-palmitoylation	GDPKMNKCVCSVM-- CCCCCCCCCEECC--	2.95	-
114	Methylation	PKMNKCVCSVM---- CCCCCCCEECC----	3.39	16831869
114	Farnesylation	PKMNKCVCSVM---- CCCCCCCEECC----	3.39	16831869
114	Farnesylation	PKMNKCVCSVM---- CCCCCCCEECC----	3.39	16831869

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of MUB1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MUB1_ARATH !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of MUB1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBC8_ARATH	UBC8	physical	21345795
UBC9_ARATH	UBC9	physical	21345795
UBC10_ARATH	UBC10	physical	21345795
NAC89_ARATH	NAC089	physical	21798944

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Prenylation

"MUBS: a family of ubiquitin-fold proteins that are plasma membrane-anchored by prenylation.";
Downes B.P., Saracco S.A., Lee S.S., Crowell D.N., Vierstra R.D.;
J. Biol. Chem. 281:27145-27157(2006).
Cited for: IDENTIFICATION, NOMENCLATURE, ISOPRENYLATION AT CYS-114, MUTAGENESISOF CYS-114, AND SUBCELLULAR LOCATION.
PubMed: 16831869