TIC_ARATH - dbPTM
TIC_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TIC_ARATH
UniProt AC Q94KE2
Protein Name Protein TIME FOR COFFEE
Gene Name TIC
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1550
Subcellular Localization Nucleus .
Protein Description Regulator of normal clock function. Acts in the mid to late night. Contributes to the amplitude of circadian clocks. May act on the transcriptional induction of LATE ELONGATED HYPOCOTYL (LHY). Inhibits MYC2 protein accumulation, acting as a negative factor in the JA-signaling pathway..
Protein Sequence MDRNREARRVPMAAAGNGLSRRRHRAGSFRDSPEEEGPVELPEAARLRDRGGSNKKDRDRERDRDRERERERDRERDRLNSRSKRRRGERLMMVHGNLDDGGDDSSEESVNDDEEYDDGGVGPPSSLKMLPPTSNNISAASFSSSLSNHHNGGSGNLHHHHHSHNNNHQRKNNFPPTKVFRSSPSPAPVSPLVSTWKAADEMIGVSVPRKARSACTKRPHESWASSTTGGGVFASGEQIHRQISSTSPANRVSPASILASPSPPAPTSPSSSSISVRKKLPSGTKQKPLPPKSSSSKLSSPVAVQDEIEIEIAEVLYGMMRMPSTSKQEAAGNDLTEAAKSTVEVKSRVSSPISNPQTLPQSSITLAANSSSSNVSAIAPKRKKPRHVKYEDDNSSRVTTIKSEAEAPSKSQVPFSNQLKSSGSGEGNSSVLDSIIPLTRESNASLDSEKKENNLSKDETILPKVESSSGFRSDGEGAKSSSPEKEKFEIDLMAPPPVRSSSERGGEMMECVAAEAKPKVTEVETEAKPLLKEDRSDPAIHDSQEKKRPRMVAEAEHHKFERNCELKLDLDKSDHVGLVNKHHVQKPPPQQQLSVPDKTAQASHLPLHMSMPGWPGGLPTMGYMAPTQGVVPTDTSSLSAAAMQPPPHLLFNQPRPKRCATHCYIARNIQSHQQFTKMNPFWPAAAGSAPMYGTKACNLSLMPPTELQGSVLGRSSNPVQDKNSQSTSKSSETAQRNQLMLQQALPPGAANSILHGPTFIFPLGQQPHAAATIAAASVRPPNSGITSSGPTATSTSMNGSASATPAGAPTMSFSYPAMPGNETQYLAILQNNGYPFPVPAHVGAQPAYRGAPGQPMPFFNGSFYSSQMIQPPHHQPQKQHQQQLTGQMLQSHAPNNQNGSASTGSSAAQKHLQNQQLRPPINHGNSQGFPTHKVQSQPLNFQQRQQPRENATQHSETVGEDSPSTADSRGSRSNVAYGQNYGMQMQPTNLGLMSSPAPGGGVVGSSSSHGEKKSQQQVSKAGVESFQSPGYAMTFATFNGANTAPTLNMSSIAQNHAMFHSMPEAARQGYQMMAAQAAQQKMNYGASLEDGKSGSIGGAATANNTPEEQRKSGGGAIGKTSGGNGGQSIAFSNKQDLADASVSAVTSGSIVDSSSRLLNLGSALPQSSGSLPTSHHQQLLQQQQQQHMQRSQSQQPYTTMYLQKQQRYATSVAASAARTKGPVVSNGSGFPDHNMTTSPAGTTKFANANSGFPQNLVQSSSNQVQSQQWKNNSPRTTNTTQAQSPSMLSPSTSVAAASSLRNIPHKQQSRPQQSQISFAANSKPMTSGSPMQQVQGGTNHQAPSPPMLVGSPSTSSVSKNASGSPRTTASASSAANKGGQASTTTHSASQPSKNLQPASAASSAGGRNNGPSVLGNPTTSSGSKSQQQQQLPKHGLQPQAQLFFSNPYMQAQHQHQQQQITISPSGGYYIQRHQQQSGSAPAVPVTGAVTATSDPAKAIAAASAANNMKGGGGMGKTQQHQLGPPGFTNVHAVSSAVQVKPVDQKQQAGE
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
20PhosphorylationAAAGNGLSRRRHRAG
HHCCCCCCCCCCCCC		25.7424894044
28PhosphorylationRRRHRAGSFRDSPEE
CCCCCCCCCCCCCCC		19.0030291188
32PhosphorylationRAGSFRDSPEEEGPV
CCCCCCCCCCCCCCC		29.9230291188
105PhosphorylationLDDGGDDSSEESVND
CCCCCCCCCCCCCCC		44.3727531888
106PhosphorylationDDGGDDSSEESVNDD
CCCCCCCCCCCCCCC		52.9927531888
109PhosphorylationGDDSSEESVNDDEEY
CCCCCCCCCCCCCCC		23.3627531888
182PhosphorylationPPTKVFRSSPSPAPV
CCCCCCCCCCCCCCC		34.8323111157
183PhosphorylationPTKVFRSSPSPAPVS
CCCCCCCCCCCCCCC		25.7430407730
185PhosphorylationKVFRSSPSPAPVSPL
CCCCCCCCCCCCCCC		35.3230407730
190PhosphorylationSPSPAPVSPLVSTWK
CCCCCCCCCCHHHHH		16.0930291188
244PhosphorylationEQIHRQISSTSPANR
HHHHHHHHCCCCCCC		21.1619376835
245PhosphorylationQIHRQISSTSPANRV
HHHHHHHCCCCCCCC		34.2419376835
246PhosphorylationIHRQISSTSPANRVS
HHHHHHCCCCCCCCC		31.7527531888
247PhosphorylationHRQISSTSPANRVSP
HHHHHCCCCCCCCCH		24.7819376835
256PhosphorylationANRVSPASILASPSP
CCCCCHHHHHCCCCC		22.8630407730
260PhosphorylationSPASILASPSPPAPT
CHHHHHCCCCCCCCC		23.5930407730
262PhosphorylationASILASPSPPAPTSP
HHHHCCCCCCCCCCC		40.8130291188
267PhosphorylationSPSPPAPTSPSSSSI
CCCCCCCCCCCCCCC		56.2130291188
268PhosphorylationPSPPAPTSPSSSSIS
CCCCCCCCCCCCCCE		23.0227531888
270PhosphorylationPPAPTSPSSSSISVR
CCCCCCCCCCCCEEE		42.4927288362
271PhosphorylationPAPTSPSSSSISVRK
CCCCCCCCCCCEEEE		31.3327288362
272PhosphorylationAPTSPSSSSISVRKK
CCCCCCCCCCEEEEC		35.7127288362
273PhosphorylationPTSPSSSSISVRKKL
CCCCCCCCCEEEECC		22.3427288362
275PhosphorylationSPSSSSISVRKKLPS
CCCCCCCEEEECCCC		20.1627288362
299PhosphorylationKSSSSKLSSPVAVQD
CCCCCCCCCCCEECC		36.0124243849
300PhosphorylationSSSSKLSSPVAVQDE
CCCCCCCCCCEECCH		33.5524243849
347PhosphorylationKSTVEVKSRVSSPIS
HHHHHHHHHCCCCCC		42.9925561503
351PhosphorylationEVKSRVSSPISNPQT
HHHHHCCCCCCCCCC		24.3226658240
402SumoylationSSRVTTIKSEAEAPS
CCCCEEEEECCCCCC		39.90-
421PhosphorylationPFSNQLKSSGSGEGN
CCCCCCCCCCCCCCC		48.8223776212
422PhosphorylationFSNQLKSSGSGEGNS
CCCCCCCCCCCCCCC		35.0823776212
424PhosphorylationNQLKSSGSGEGNSSV
CCCCCCCCCCCCCHH		35.3023776212
429PhosphorylationSGSGEGNSSVLDSII
CCCCCCCCHHHHHHH		32.4523776212
430PhosphorylationGSGEGNSSVLDSIIP
CCCCCCCHHHHHHHH		30.6023776212
434PhosphorylationGNSSVLDSIIPLTRE
CCCHHHHHHHHCCCC		20.4623776212
442PhosphorylationIIPLTRESNASLDSE
HHHCCCCCCCCCCHH		34.1130407730
445PhosphorylationLTRESNASLDSEKKE
CCCCCCCCCCHHHHH		36.6430407730
448PhosphorylationESNASLDSEKKENNL
CCCCCCCHHHHHCCC		57.5230407730
467PhosphorylationTILPKVESSSGFRSD
CCHHHHHCCCCCCCC		32.5627545962
468PhosphorylationILPKVESSSGFRSDG
CHHHHHCCCCCCCCC		22.4525561503
469PhosphorylationLPKVESSSGFRSDGE
HHHHHCCCCCCCCCC		51.7530407730
473PhosphorylationESSSGFRSDGEGAKS
HCCCCCCCCCCCCCC		47.9423111157
480PhosphorylationSDGEGAKSSSPEKEK
CCCCCCCCCCCCHHC		35.2023776212
481PhosphorylationDGEGAKSSSPEKEKF
CCCCCCCCCCCHHCE		49.5623776212
482PhosphorylationGEGAKSSSPEKEKFE
CCCCCCCCCCHHCEE		44.1423776212
500PhosphorylationMAPPPVRSSSERGGE
CCCCCCCCCCCCCCC		38.1523776212
501PhosphorylationAPPPVRSSSERGGEM
CCCCCCCCCCCCCCH		26.1723776212
502PhosphorylationPPPVRSSSERGGEMM
CCCCCCCCCCCCCHH		32.3423776212
536PhosphorylationPLLKEDRSDPAIHDS
CCCCCCCCCCCCCCC		61.3425561503
543PhosphorylationSDPAIHDSQEKKRPR
CCCCCCCCHHHCCCC		26.5230407730
573PhosphorylationLKLDLDKSDHVGLVN
EEECCCCCCCEEEEC		32.3930291188
962PhosphorylationSETVGEDSPSTADSR
CCCCCCCCCCCCCCC		19.2227545962
964PhosphorylationTVGEDSPSTADSRGS
CCCCCCCCCCCCCCC		39.9325561503
965PhosphorylationVGEDSPSTADSRGSR
CCCCCCCCCCCCCCC		37.5625561503
1112PhosphorylationTPEEQRKSGGGAIGK
CHHHHHHCCCCCCCC		44.8825561503
1120PhosphorylationGGGAIGKTSGGNGGQ
CCCCCCCCCCCCCCC		27.6525561503
1121PhosphorylationGGAIGKTSGGNGGQS
CCCCCCCCCCCCCCE		48.4625561503
1382PhosphorylationANKGGQASTTTHSAS
HHCCCCCCCCCCCCC		20.5623776212
1383PhosphorylationNKGGQASTTTHSASQ
HCCCCCCCCCCCCCC		38.4423776212
1384PhosphorylationKGGQASTTTHSASQP
CCCCCCCCCCCCCCC		21.7323776212
1385PhosphorylationGGQASTTTHSASQPS
CCCCCCCCCCCCCCC		17.5823776212
1387PhosphorylationQASTTTHSASQPSKN
CCCCCCCCCCCCCCC		27.7623776212
1389PhosphorylationSTTTHSASQPSKNLQ
CCCCCCCCCCCCCCC		45.7123776212
1392PhosphorylationTHSASQPSKNLQPAS
CCCCCCCCCCCCCCH		26.9223776212
1403PhosphorylationQPASAASSAGGRNNG
CCCHHHHHCCCCCCC		26.6323111157
1419PhosphorylationSVLGNPTTSSGSKSQ
CCCCCCCCCCCCHHH		23.3525561503
1420PhosphorylationVLGNPTTSSGSKSQQ
CCCCCCCCCCCHHHH		34.8725561503
1421PhosphorylationLGNPTTSSGSKSQQQ
CCCCCCCCCCHHHHH		45.0225561503
1423PhosphorylationNPTTSSGSKSQQQQQ
CCCCCCCCHHHHHHH		30.9525561503
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 TIC_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TIC_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 TIC_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ELF4_ARATHELF4genetic
17496120
ELF3_ARATHELF3genetic
17496120
APRR1_ARATHTOC1genetic
17496120
GIGAN_ARATHGIgenetic
17496120
ELF3_ARATHELF3genetic
14555691
MYC2_ARATHMYC2physical
22693280
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TIC_ARATH

loading...

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-247, AND MASSSPECTROMETRY.
"Temporal analysis of sucrose-induced phosphorylation changes inplasma membrane proteins of Arabidopsis.";
Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B.,Schulze W.X.;
Mol. Cell. Proteomics 6:1711-1726(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1112, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory