R27AA_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: R27AA_ARATH
• UniProt AC: P59271
• Protein Name: Ubiquitin-40S ribosomal protein S27a-1
• Gene Name: RPS27AA
• 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).; Ribosomal protein RSP27a-1 is a component of the 40S subunit of the ribosome..
• Protein Sequence: MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGAKKRKKKTYTKPKKIKHTHKKVKLAVLQFYKVDGSGKVQRLKKECPSVSCGPGTFMASHFDRHYCGKCGTTYVFKKADEE

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
1	Sulfoxidation	-------MQIFVKTL -------CEEEEEEC	6.60	25693801
11	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEE	31.36	17272265
22	Phosphorylation	LEVESSDTIDNVKAK EEEECCCCHHHHHHH	31.98	19880383
29	Ubiquitination	TIDNVKAKIQDKEGI CHHHHHHHEECCCCC	34.87	17272265
33	Ubiquitination	VKAKIQDKEGIPPDQ HHHHEECCCCCCHHH	41.27	17272265
48	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	17272265
63	Ubiquitination	LADYNIQKESTLHLV HHCCCCCCCHHHHHH	50.24	17272265
65	Phosphorylation	DYNIQKESTLHLVLR CCCCCCCHHHHHHHH	43.22	25561503
66	Phosphorylation	YNIQKESTLHLVLRL CCCCCCHHHHHHHHH	21.20	25561503
111	Phosphorylation	QFYKVDGSGKVQRLK EEEEECCCCHHHHCH	30.86	19880383

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

Oops, there are no upstream regulatory protein records of R27AA_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of R27AA_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 R27AA_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of R27AA_ARATH !!

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