TPR1_ARATH - dbPTM
TPR1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPR1_ARATH
UniProt AC Q0WV90
Protein Name Topless-related protein 1
Gene Name TPR1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1120
Subcellular Localization Nucleus .
Protein Description Transcriptional corepressor. Activates TIR-NB-LRR R protein-mediated immune responses through repression of negative regulators such as CNGC2/DND1. [PubMed: 20647385 Negative regulator of jasmonate responses (By similarity]
Protein Sequence MSSLSRELVFLILQFLDEEKFKETVHKLEQESGFFFNMKYFEDEVHNGNWDEVEKYLSGFTKVDDNRYSMKIFFEIRKQKYLEALDRHDRPKAVDILVKDLKVFSTFNEELFKEITQLLTLENFRENEQLSKYGDTKSARAIMLVELKKLIEANPLFRDKLQFPTLRTSRLRTLINQSLNWQHQLCKNPRPNPDIKTLFVDHSCRLPNDARAPSPVNNPLLGSLPKAEGFPPLGAHGPFQPTPSPVPTPLAGWMSSPSSVPHPAVSGGPIALGAPSIQAALKHPRTPPSNSAVDYPSGDSDHVSKRTRPMGISDEVSLGVNMLPMTFPGQAHGHNQTFKAPDDLPKTVARTLSQGSSPMSMDFHPIKQTLLLVGTNVGDIGLWEVGSRERLVQKTFKVWDLSKCSMPLQAALVKEPVVSVNRVIWSPDGSLFGVAYSRHIVQLYSYHGGEDMRQHLEIDAHVGGVNDIAFSTPNKQLCVTTCGDDKTIKVWDAATGVKRYTFEGHEAPVYSICPHYKENIQFIFSTALDGKIKAWLYDNMGSRVDYEAPGRWCTTMAYSADGTRLFSCGTSKDGESFIVEWNESEGAVKRTYQGFHKRSLGVVQFDTTKNRYLAAGDDFSIKFWDMDTIQLLTAIDADGGLQASPRIRFNKEGSLLAVSANDNMIKVMANSDGLRLLHTVENLSSESSKPAINSIPMVERPASVVSIPGMNGDSRNMVDVKPVITEESNDKSKVWKLTEVGEPSQCRSLRLPENMRVTKISRLIFTNSGNAILALASNAIHLLWKWQRNDRNATGKATASLPPQQWQPASGILMTNDVAETNPEEAVPCFALSKNDSYVMSASGGKISLFNMMTFKTMATFMPPPPAATFLAFHPQDNNIIAIGMDDSTIQIYNVRVDEVKSKLKGHSKRITGLAFSNVLNVLVSSGADAQLCVWNTDGWEKQKSKVLQIPQGRSTSSLSDTRVQFHQDQVHFLVVHETQLAIYETTKLECMKQWPVRESAAPITHATFSCDSQLIYTSFMDATICVFSSANLRLRCRVNPSAYLPASLSNSNVHPLVIAAHPQESNMFAVGLSDGGVHIFEPLESEGKWGVAPPPENGSASAVTATPSVGASASDQPQR
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
133PhosphorylationENEQLSKYGDTKSAR
HHHHHHHHCCCHHHH		19.5019880383
214PhosphorylationPNDARAPSPVNNPLL
CCCCCCCCCCCCCCC		40.2630291188
223PhosphorylationVNNPLLGSLPKAEGF
CCCCCCCCCCCCCCC		41.2823776212
285 (in isoform 1)Phosphorylation-60.6321768351
286PhosphorylationAALKHPRTPPSNSAV
HHHHCCCCCCCCCCC		43.9630291188
289PhosphorylationKHPRTPPSNSAVDYP
HCCCCCCCCCCCCCC		44.6223776212
291PhosphorylationPRTPPSNSAVDYPSG
CCCCCCCCCCCCCCC		33.7223776212
307PhosphorylationSDHVSKRTRPMGISD
CCCCCCCCCCCCCCC		42.7527545962
313PhosphorylationRTRPMGISDEVSLGV
CCCCCCCCCCEEECC		23.2227545962
317PhosphorylationMGISDEVSLGVNMLP
CCCCCCEEECCEEEE		19.8427545962
326PhosphorylationGVNMLPMTFPGQAHG
CCEEEECCCCCCCCC		25.4127545962
337PhosphorylationQAHGHNQTFKAPDDL
CCCCCCCCCCCCCCC		32.2127545962
706PhosphorylationERPASVVSIPGMNGD
ECCCEEEECCCCCCC		22.4025561503
725PhosphorylationVDVKPVITEESNDKS
EEEECEEECCCCCCC		33.6519880383
728PhosphorylationKPVITEESNDKSKVW
ECEEECCCCCCCCEE		44.0630291188
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 TPR1_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPR1_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 TPR1_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS902_ARATHHSP81-2physical
20856808
LBD41_ARATHLBD41physical
22065421
LBD37_ARATHLBD37physical
22065421
RVE7_ARATHEPR1physical
22065421
RAVL1_ARATHTEM1physical
22065421
HSFB1_ARATHHSF4physical
22065421
ERF82_ARATHERF3physical
22065421
ERF78_ARATHERF4physical
22065421
ERF83_ARATHERF7physical
22065421
ERF76_ARATHERF11physical
22065421
ZAT10_ARATHSTZphysical
22065421
GAT18_ARATHMNPphysical
22065421
MYB32_ARATHMYB32physical
22065421
MYB44_ARATHMYBR1physical
22065421
JMJ18_ARATHAT1G30810physical
22065421
TI11A_ARATHJAZ5physical
22065421
TI11B_ARATHJAZ6physical
22065421
IAA2_ARATHIAA2physical
22065421
IAA18_ARATHIAA18physical
22065421
IAA27_ARATHPAP2physical
22065421
Y2608_ARATHAT2G36080physical
22065421
TPR1_ARATHTPR1physical
22065421
AFP4_ARATHTMAC2physical
22065421
ARI1_ARATHARI1physical
22065421
SUMO3_ARATHSUMO3physical
22065421
RAP27_ARATHRAP2.7physical
22065421
IAA10_ARATHIAA10physical
22065421
ARFQ_ARATHARF17physical
22065421
TOE2_ARATHTOE2physical
22065421
IAA1_ARATHIAA1physical
22065421
IAA11_ARATHIAA11physical
22065421
AS1_ARATHAS1physical
22065421
WRK61_ARATHWRKY61physical
22065421
NFYC4_ARATHNF-YC4physical
22065421
DRE1D_ARATHCBF4physical
22065421
GATA9_ARATHGATA9physical
22065421
WRK32_ARATHWRKY32physical
22065421
BBM_ARATHBBMphysical
22065421
WOX5_ARATHWOX5physical
26028217
BZR1_ARATHBZR1physical
24938363
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPR1_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-214, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND MASSSPECTROMETRY.
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis.";
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.;
J. Proteome Res. 7:2458-2470(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND MASSSPECTROMETRY.

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