TC159_ARATH - dbPTM
TC159_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TC159_ARATH
UniProt AC O81283
Protein Name Translocase of chloroplast 159, chloroplastic
Gene Name TOC159
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1503
Subcellular Localization Plastid, chloroplast outer membrane
Single-pass membrane protein. Cytoplasm. Cycles between the cytoplasm and chloroplast, probably as a soluble preprotein receptor. The anchoring to the chloroplast outer membrane required the GTPase activity and GD
Protein Description GTPase involved in protein precursor import into chloroplasts. Seems to recognize chloroplast-destined precursor proteins and regulate their presentation to the translocation channel through GTP hydrolysis. Required for chloroplast biogenesis. Probably specialized in the import of nuclear encoded photosynthetic preproteins from the cytoplasm to the chloroplast..
Protein Sequence MDSKSVTPEPTNPFYASSGQSGKTYASVVAAAAAAAADKEDGGAVSSAKELDSSSEAVSGNSDKVGADDLSDSEKEKPNLVGDGKVSDEVDGSLKEDSTTPEATPKPEVVSGETIGVDDVSSLSPKPEAVSDGVGVVEENKKVKEDVEDIKDDGESKIENGSVDVDVKQASTDGESESKVKDVEEEDVGTKKDDEGESELGGKVDVDDKSDNVIEEEGVELTDKGDVIVNSSPVESVHVDVAKPGVVVVGDAEGSEELKINADAETLEVANKFDQIGDDDSGEFEPVSDKAIEEVEEKFTSESDSIADSSKLESVDTSAVEPEVVAAESGSEPKDVEKANGLEKGMTYAEVIKAASAVADNGTKEEESVLGGIVDDAEEGVKLNNKGDFVVDSSAIEAVNVDVAKPGVVVVGDVEVSEVLETDGNIPDVHNKFDPIGQGEGGEVELESDKATEEGGGKLVSEGDSMVDSSVVDSVDADINVAEPGVVVVGAAKEAVIKEDDKDDEVDKTISNIEEPDDLTAAYDGNFELAVKEISEAAKVEPDEPKVGVEVEELPVSESLKVGSVDAEEDSIPAAESQFEVRKVVEGDSAEEDENKLPVEDIVSSREFSFGGKEVDQEPSGEGVTRVDGSESEEETEEMIFGSSEAAKQFLAELEKASSGIEAHSDEANISNNMSDRIDGQIVTDSDEDVDTEDEGEEKMFDTAALAALLKAATGGGSSEGGNFTITSQDGTKLFSMDRPAGLSSSLRPLKPAAAPRANRSNIFSNSNVTMADETEINLSEEEKQKLEKLQSLRVKFLRLLQRLGHSAEDSIAAQVLYRLALLAGRQAGQLFSLDAAKKKAVESEAEGNEELIFSLNILVLGKAGVGKSATINSILGNQIASIDAFGLSTTSVREISGTVNGVKITFIDTPGLKSAAMDQSTNAKMLSSVKKVMKKCPPDIVLYVDRLDTQTRDLNNLPLLRTITASLGTSIWKNAIVTLTHAASAPPDGPSGTPLSYDVFVAQCSHIVQQSIGQAVGDLRLMNPSLMNPVSLVENHPLCRKNREGVKVLPNGQTWRSQLLLLCYSLKVLSETNSLLRPQEPLDHRKVFGFRVRSPPLPYLLSWLLQSRAHPKLPGDQGGDSVDSDIEIDDVSDSEQEDGEDDEYDQLPPFKPLRKTQLAKLSNEQRKAYFEEYDYRVKLLQKKQWREELKRMKEMKKNGKKLGESEFGYPGEEDDPENGAPAAVPVPLPDMVLPPSFDSDNSAYRYRYLEPTSQLLTRPVLDTHGWDHDCGYDGVNAEHSLALASRFPATATVQVTKDKKEFNIHLDSSVSAKHGENGSTMAGFDIQNVGKQLAYVVRGETKFKNLRKNKTTVGGSVTFLGENIATGVKLEDQIALGKRLVLVGSTGTMRSQGDSAYGANLEVRLREADFPIGQDQSSFGLSLVKWRGDLALGANLQSQVSVGRNSKIALRAGLNNKMSGQITVRTSSSDQLQIALTAILPIAMSIYKSIRPEATNDKYSMY
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
15PhosphorylationPEPTNPFYASSGQSG
CCCCCCCCCCCCCCC		13.5630407730
17PhosphorylationPTNPFYASSGQSGKT
CCCCCCCCCCCCCCC		24.5030407730
18PhosphorylationTNPFYASSGQSGKTY
CCCCCCCCCCCCCCH		32.4530407730
21PhosphorylationFYASSGQSGKTYASV
CCCCCCCCCCCHHHH		45.8727532006
53PhosphorylationSSAKELDSSSEAVSG
CCHHHCCCCCCCCCC		48.6823776212
54PhosphorylationSAKELDSSSEAVSGN
CHHHCCCCCCCCCCC		31.6823776212
55PhosphorylationAKELDSSSEAVSGNS
HHHCCCCCCCCCCCC		33.2623776212
59PhosphorylationDSSSEAVSGNSDKVG
CCCCCCCCCCCCCCC		39.0323776212
62PhosphorylationSEAVSGNSDKVGADD
CCCCCCCCCCCCCCC		42.1923776212
71PhosphorylationKVGADDLSDSEKEKP
CCCCCCCCCCCCCCC		46.1930291188
73PhosphorylationGADDLSDSEKEKPNL
CCCCCCCCCCCCCCC		47.3824601666
93PhosphorylationVSDEVDGSLKEDSTT
CCCCCCCCCCCCCCC		31.6325561503
122PhosphorylationIGVDDVSSLSPKPEA
ECCCCHHHCCCCCCH		32.4919376835
162PhosphorylationESKIENGSVDVDVKQ
CCCCCCCCEEEEEEE		27.0719880383
171PhosphorylationDVDVKQASTDGESES
EEEEEECCCCCCCHH		25.2425561503
172PhosphorylationVDVKQASTDGESESK
EEEEECCCCCCCHHH		51.5525561503
198PhosphorylationKKDDEGESELGGKVD
CCCCCCCCCCCCEEC		49.3225561503
210PhosphorylationKVDVDDKSDNVIEEE
EECCCCCCCCCEEEC		41.2223776212
222PhosphorylationEEEGVELTDKGDVIV
EECCCEECCCCCEEE		23.3523776212
231PhosphorylationKGDVIVNSSPVESVH
CCCEEECCCCCCEEE		25.7327532006
266PhosphorylationKINADAETLEVANKF
EECCCHHHHHHHHCC		29.9119376835
281PhosphorylationDQIGDDDSGEFEPVS
CCCCCCCCCCEEECC		47.4130291188
288PhosphorylationSGEFEPVSDKAIEEV
CCCEEECCHHHHHHH		44.0723776212
300PhosphorylationEEVEEKFTSESDSIA
HHHHHHHCCCCCCCC		42.5323776212
301PhosphorylationEVEEKFTSESDSIAD
HHHHHHCCCCCCCCC		37.9330291188
303PhosphorylationEEKFTSESDSIADSS
HHHHCCCCCCCCCHH		36.1023776212
305PhosphorylationKFTSESDSIADSSKL
HHCCCCCCCCCHHHC		29.0223776212
309PhosphorylationESDSIADSSKLESVD
CCCCCCCHHHCEECC		21.9823776212
310PhosphorylationSDSIADSSKLESVDT
CCCCCCHHHCEECCC		41.6323776212
346SulfoxidationANGLEKGMTYAEVIK
HCCCCCCCCHHHHHH		3.7125693801
448PhosphorylationGGEVELESDKATEEG
CCCEEECCCCCCCCC		57.9723776212
452PhosphorylationELESDKATEEGGGKL
EECCCCCCCCCCCCE		40.0723776212
461PhosphorylationEGGGKLVSEGDSMVD
CCCCCEECCCCCCCC		46.42-
557PhosphorylationEVEELPVSESLKVGS
EEEECCCCCCEEECC		21.3823776212
559PhosphorylationEELPVSESLKVGSVD
EECCCCCCEEECCCC		26.4523776212
564PhosphorylationSESLKVGSVDAEEDS
CCCEEECCCCCCCCC		21.5830291188
571PhosphorylationSVDAEEDSIPAAESQ
CCCCCCCCCCHHHHH		33.4830291188
589PhosphorylationRKVVEGDSAEEDENK
EEHHCCCCCCCCCCC		48.7330291188
604PhosphorylationLPVEDIVSSREFSFG
CCHHHHCCCCEEEEC		24.8225561503
605PhosphorylationPVEDIVSSREFSFGG
CHHHHCCCCEEEECC		25.5719880383
609PhosphorylationIVSSREFSFGGKEVD
HCCCCEEEECCEECC		20.4430291188
620PhosphorylationKEVDQEPSGEGVTRV
EECCCCCCCCCCCCC		49.0419376835
625PhosphorylationEPSGEGVTRVDGSES
CCCCCCCCCCCCCCC		35.5127532006
630PhosphorylationGVTRVDGSESEEETE
CCCCCCCCCCHHHHH		33.2230291188
632PhosphorylationTRVDGSESEEETEEM
CCCCCCCCHHHHHHH		52.5930291188
636PhosphorylationGSESEEETEEMIFGS
CCCCHHHHHHHHHCC		40.2923776212
643PhosphorylationTEEMIFGSSEAAKQF
HHHHHHCCHHHHHHH		17.7923776212
644PhosphorylationEEMIFGSSEAAKQFL
HHHHHCCHHHHHHHH		31.4723776212
658PhosphorylationLAELEKASSGIEAHS
HHHHHHHHCCCHHCC		39.9227532006
659PhosphorylationAELEKASSGIEAHSD
HHHHHHHCCCHHCCC		48.9627532006
665PhosphorylationSSGIEAHSDEANISN
HCCCHHCCCCCCCCC		44.1630291188
671PhosphorylationHSDEANISNNMSDRI
CCCCCCCCCCCCCCC		23.2023776212
675PhosphorylationANISNNMSDRIDGQI
CCCCCCCCCCCCCEE		26.3423776212
684PhosphorylationRIDGQIVTDSDEDVD
CCCCEEECCCCCCCC		31.2630291188
686PhosphorylationDGQIVTDSDEDVDTE
CCEEECCCCCCCCCC		33.2730291188
692PhosphorylationDSDEDVDTEDEGEEK
CCCCCCCCCCCCHHH		45.2230291188
703PhosphorylationGEEKMFDTAALAALL
CHHHHHHHHHHHHHH		11.5423776212
746PhosphorylationRPAGLSSSLRPLKPA
CCCCCCCCCCCCCCC		25.6425561503
1125PhosphorylationQGGDSVDSDIEIDDV
CCCCCCCCCCEECCC		38.0329654922
1133PhosphorylationDIEIDDVSDSEQEDG
CCEECCCCHHCCCCC		42.2727531888
1135PhosphorylationEIDDVSDSEQEDGED
EECCCCHHCCCCCCC		33.4027531888
1464PhosphorylationNKMSGQITVRTSSSD
CCCCCEEEEECCCHH		8.9619880383
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 TC159_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TC159_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 TC159_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TI110_ARATHTIC110physical
15829604
SUMO3_ARATHSUMO3physical
20855607
TOC33_ARATHTOC33physical
19010773
DRTS1_ARATHTHY-1physical
15138290
RK11_ARATHPRPL11physical
15138290
PORA_ARATHPORAphysical
15138290
TC753_ARATHTOC75-IIIphysical
19188370
TOC33_ARATHTOC33physical
19188370
TI110_ARATHTIC110physical
14765117
TC753_ARATHTOC75-IIIphysical
14765117
TIC40_ARATHTIC40physical
14765117
OEP37_ARATHOEP37physical
14765117
GGR_ARATHGGRphysical
14765117
TOC34_ARATHTOC34physical
14765117
TOC33_ARATHTOC33physical
12460988
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TC159_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-71; SER-73; SER-122;SER-210; SER-281; SER-288; SER-448; SER-589; SER-609; SER-630;SER-632; SER-659; THR-684; SER-686 AND THR-692, AND MASS SPECTROMETRY.
"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-71, AND MASSSPECTROMETRY.

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