TCP10_ARATH - dbPTM
TCP10_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCP10_ARATH
UniProt AC O82277
Protein Name Transcription factor TCP10
Gene Name TCP10
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 361
Subcellular Localization Nucleus .
Protein Description Plays a pivotal role in the control of morphogenesis of shoot organs by negatively regulating the expression of boundary-specific genes such as CUC genes, probably through the induction of miRNA (e.g. miR164). Participates in ovule develpment. [PubMed: 25378179]
Protein Sequence MGLKGYSVGEGGGEIVEVQGGHIIRATGRKDRHSKVFTSKGPRDRRVRLSAHTAIQFYDVQDRLGYDRPSKAVDWLIKKAKTAIDKLELGETTTTTTRQEPVNTKPESPTLVFQRENNDQTQFVAANLDPEDAMKTFFPATTTTNGGGGTNINFQNYPHQDDNNMVSRTTTPPPNLSQDLGLSLHPFQGNNNTVVVPETNNFTTTHFDTFGRISGWNHHDLTMTSSSSSEHQQQEQEERSNGGFMVNHHPHHHHHQPSMMTLLNSQQQQVFLGGQQQQQQRGTLQSSLFPHSFRSWDHHQTTSDHHHHQNQASSMFASSSQYGSHGMMMMQGLSFPNTTRLLHGEEATQPNSSSSPPNSHL
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
104PhosphorylationTRQEPVNTKPESPTL
CCCCCCCCCCCCCEE
48.4823776212
108PhosphorylationPVNTKPESPTLVFQR
CCCCCCCCCEEEEEC
31.5423776212
110PhosphorylationNTKPESPTLVFQREN
CCCCCCCEEEEECCC
44.8523776212
353PhosphorylationEATQPNSSSSPPNSH
CCCCCCCCCCCCCCC
41.2823111157
354PhosphorylationATQPNSSSSPPNSHL
CCCCCCCCCCCCCCC
46.8423111157
355PhosphorylationTQPNSSSSPPNSHL-
CCCCCCCCCCCCCC-
46.4523111157
359PhosphorylationSSSSPPNSHL-----
CCCCCCCCCC-----
31.7527545962

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 TCP10_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TCP10_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 TCP10_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LBD6_ARATHAS2physical
22380849
TCP4_ARATHTCP4physical
24129704
TCP3_ARATHTCP3physical
24129704
TCP2_ARATHTCP2physical
24129704
TCP24_ARATHTCP24physical
24129704
TCP13_ARATHPTF1physical
24129704
TCP17_ARATHTCP17physical
24129704
TCP5_ARATHTCP5physical
24129704
TCP11_ARATHAT2G37000physical
24129704
TCP19_ARATHAT5G51910physical
24129704
TCP21_ARATHAT5G08330physical
24129704
TCP15_ARATHAT1G69690physical
24129704
TCP20_ARATHTCP20physical
24129704
TCP23_ARATHAT1G35560physical
24129704
TCP8_ARATHAT1G58100physical
24129704
TCP14_ARATHTCP14physical
24129704

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TCP10_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-108, AND MASSSPECTROMETRY.

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