TTHL_ARATH - dbPTM
TTHL_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTHL_ARATH
UniProt AC Q9LVM5
Protein Name Uric acid degradation bifunctional protein TTL
Gene Name TTL
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 324
Subcellular Localization Cell membrane
Peripheral membrane protein. Peroxisome .
Protein Description Involved in the last two steps of the degradation of uric acid, i.e. the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) and its stereoselective decarboxylation to (S)-allantoin. Might function as a negative regulator to modulate brassinosteroid-mediated plant growth..
Protein Sequence MAMEIGEDEWKVCCGSSEFAKQMSTSGPLTSQEAIYTARDIWFNQVNVTDWLEAFSAHPQIGNTPSPSINSDFARRSVSEQSTAFATTSASALQELAEWNVLYKKKFGFIFIICASGRTHAEMLHALKERYENRPIVELEIAAMEQMKITELRMAKLFSDKAKVISETDSSSSPVSTKPQDRLRIIGGHLNVAAEAKAPKRSRPPITTHVLDVSRGAPAAGVEVHLEVWSGTTGPSFVHGGGGVWSSVGTSATDRDGRSGPLMDLVDALNPGTYRISFDTAKYSPGCFFPYVSIVFQVTESQKWEHFHVPLLLAPFSFSTYRGS
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
2Acetylation------MAMEIGEDE
------CCCCCCCCC
12.3322223895
166PhosphorylationSDKAKVISETDSSSS
CCCCEEEECCCCCCC
37.1123776212
168PhosphorylationKAKVISETDSSSSPV
CCEEEECCCCCCCCC
34.1023776212
170PhosphorylationKVISETDSSSSPVST
EEEECCCCCCCCCCC
39.2723776212
170 (in isoform 2)Phosphorylation-39.2723776212
171PhosphorylationVISETDSSSSPVSTK
EEECCCCCCCCCCCC
37.3323776212
171 (in isoform 2)Phosphorylation-37.3323776212
171 (in isoform 3)Phosphorylation-37.3319880383
172PhosphorylationISETDSSSSPVSTKP
EECCCCCCCCCCCCC
42.4823776212
172 (in isoform 2)Phosphorylation-42.4823776212
173PhosphorylationSETDSSSSPVSTKPQ
ECCCCCCCCCCCCCH
31.1323776212
173 (in isoform 2)Phosphorylation-31.1323776212
176PhosphorylationDSSSSPVSTKPQDRL
CCCCCCCCCCCHHCE
33.8123776212
176 (in isoform 2)Phosphorylation-33.8123776212
177PhosphorylationSSSSPVSTKPQDRLR
CCCCCCCCCCHHCEE
47.1523776212

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 TTHL_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TTHL_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 TTHL_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TTHL_ARATHTTLphysical
21798944
SUMO3_ARATHSUMO3physical
20855607

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TTHL_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND SER-173, ANDMASS SPECTROMETRY.

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