UBQ10_ARATH - dbPTM
UBQ10_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBQ10_ARATH
UniProt AC Q8H159
Protein Name Polyubiquitin 10
Gene Name UBQ10
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 457
Subcellular Localization 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)..
Protein Sequence MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGF
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
11UbiquitinationFVKTLTGKTITLEVE
EEEECCCCEEEEEEE		31.36-
22PhosphorylationLEVESSDTIDNVKAK
EEEECCCCHHHHHHH		31.9819880383
29UbiquitinationTIDNVKAKIQDKEGI
CHHHHHHHEECCCCC		34.87-
33UbiquitinationVKAKIQDKEGIPPDQ
HHHHEECCCCCCHHH		41.27-
48UbiquitinationQRLIFAGKQLEDGRT
HEEEEEECCCCCCCC		48.56-
63UbiquitinationLADYNIQKESTLHLV
HHCCCCCCHHEEEEE		50.24-
65PhosphorylationDYNIQKESTLHLVLR
CCCCCCHHEEEEEEE		43.2225561503
66PhosphorylationYNIQKESTLHLVLRL
CCCCCHHEEEEEEEE		21.2025561503
98PhosphorylationLEVESSDTIDNVKAK
EEEECCCCHHHHHHH		31.9819880383
141PhosphorylationDYNIQKESTLHLVLR
CCCCCCHHEEEEEEE		43.2225561503
142PhosphorylationYNIQKESTLHLVLRL
CCCCCHHEEEEEEEE		21.2025561503
174PhosphorylationLEVESSDTIDNVKAK
EEEECCCCHHHHHHH		31.9819880383
217PhosphorylationDYNIQKESTLHLVLR
CCCCCCHHEEEEEEE		43.2225561503
218PhosphorylationYNIQKESTLHLVLRL
CCCCCHHEEEEEEEE		21.2025561503
250PhosphorylationLEVESSDTIDNVKAK
EEEECCCCHHHHHHH		31.9819880383
293PhosphorylationDYNIQKESTLHLVLR
CCCCCCHHEEEEEEE		43.2225561503
294PhosphorylationYNIQKESTLHLVLRL
CCCCCHHEEEEEEEE		21.2025561503
326PhosphorylationLEVESSDTIDNVKAK
EEEECCCCHHHHHHH		31.9819880383
369PhosphorylationDYNIQKESTLHLVLR
CCCCCCHHEEEEEEE		43.2225561503
370PhosphorylationYNIQKESTLHLVLRL
CCCCCHHEEEEEEEE		21.2025561503
402PhosphorylationLEVESSDTIDNVKAK
EEEECCCCHHHHHHH		31.9819880383
445PhosphorylationDYNIQKESTLHLVLR
CCCCCCHHEEEHEEE		43.2225561503
446PhosphorylationYNIQKESTLHLVLRL
CCCCCHHEEEHEEEE		21.2025561503
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 UBQ10_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBQ10_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 UBQ10_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UBQ10_ARATH !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBQ10_ARATH

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Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"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.

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