RUB1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RUB1_ARATH
• UniProt AC: Q9SHE7
• Protein Name: Ubiquitin-NEDD8-like protein RUB1
• Gene Name: RUB1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 156
• Subcellular Localization: Ubiquitin: Cytoplasm. Nucleus.
• Protein Description: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).; NEDD8-like protein RUB1: Appears to function as a stable post-translational protein modifier. An AMP-RUB1 intermediate is formed by an activating enzyme, distinct from the ubiquitin activating enzyme E1, which is composed of a heterodimer AXR1/ECR1. Auxin response is mediated, at least in part, through modification of the cullin AtCUL1 by the attachment of RUB1 to 'Lys-692'..
• Protein Sequence: MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGTMIKVKTLTGKEIEIDIEPTDTIDRIKERVEEKEGIPPVQQRLIYAGKQLADDKTAKDYNIEGGSVLHLVLALRGGFGLL

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
11	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEE	31.36	-
22	Phosphorylation	LEVESSDTIDNVKAK EEEECCCCHHHHHHH	31.98	19880383
29	Ubiquitination	TIDNVKAKIQDKEGI CHHHHHHHEECCCCC	34.87	-
33	Ubiquitination	VKAKIQDKEGIPPDQ HHHHEECCCCCCHHH	41.27	-
48	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
63	Ubiquitination	LADYNIQKESTLHLV HHCCCCCCCCEEEEE	50.24	-
65	Phosphorylation	DYNIQKESTLHLVLR CCCCCCCCEEEEEEE	43.22	25561503
66	Phosphorylation	YNIQKESTLHLVLRL CCCCCCCEEEEEEEE	21.20	25561503
135	Phosphorylation	DDKTAKDYNIEGGSV CCCCCCCCCCCCHHH	19.82	19880383

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

Oops, there are no upstream regulatory protein records of RUB1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RUB1_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 RUB1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CUL1_ARATH	CUL1	physical	15319484
CUL3A_ARATH	CUL3	physical	15618422
CUL3B_ARATH	CUL3B	physical	15618422

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Ubiquitylation

"Multidimensional protein identification technology (MudPIT) analysisof ubiquitinated proteins in plants.";
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
Mol. Cell. Proteomics 6:601-610(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-29; LYS-33;LYS-48 AND LYS-63, AND MASS SPECTROMETRY.
PubMed: 17272265