TR120_YEAST - dbPTM
TR120_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TR120_YEAST
UniProt AC Q04183
Protein Name Trafficking protein particle complex II-specific subunit 120
Gene Name TRS120
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1289
Subcellular Localization Golgi apparatus, cis-Golgi network .
Protein Description Specific subunit of the TRAPP II complex, a highly conserved vesicle tethering complex that functions in the late Golgi as a guanine nucleotide exchanger (GEF) for the Golgi YPT1 GTPase. TRS120 plays a role in the YPT GEF activity of TRAPP II in concert with the two other TRAPP II-specific subunits TRS65 and TRS130..
Protein Sequence MNILKHFPSYVGPSKIRTLVIPIGHWTRKEFNNAVQKLSEFNEIHLSDVTPIDSPIFTPQGFPHGKLFFDFLTIDHDDALELFLYDFEPFRKTFVIIGLVNDYSDPLTNLNFMKEKYPTLISPNLVYASSTPTKELEQTIDTMENVFASSPDMQKNIETIMCDIARNFLTALNSYYSSYKHVTLRSPGAIGGNAVLKTTLIRQNSYTSSSSSTPMSAVQSSVSSSSKAGSVTTASKRLSSFEMTTNSLKRSASLKLATTLSTSENRSQQKSLGRQMKILGNFQLLAGRYVDALNSFVDAITTLYKVRDYLWLGSALDGISICFLLLSYLGLSYQIPQIVSLICPVEKLNFESSSTGISPVDSNSKATASTTASSTPRNSISIAAMQSPRNSIMSLSAPALNIDVENINLPLLIKCISDKVLYYYDLSLMHNSEYAPQVVYCEFLLKTLTFMTSCYKSSEFSKDVLDNIVKNQHRALSDIPNSPMFPRFEVYFYSNKLFELQLKEMQVEAQIKIYSTMAEVYRLLGYKRKQLFVLRLLMVALLATPNKIAWHPDYRTLIDTIIELLNINESEAKINVDDPSQSTWLILQKKILQLCIKVSRKINDFEYVAKFSSILITKYTHLLNQSEQDALFKEYIQPSITNESITSYWDPFILREVVINRILDSDPTSNEIPLESDVSSLESLENRQKTQDINPQEVFNPFKRVQPTSFVSNNSTKVPILVFLVGDKAEFTCRVQNPFKFDFTINDIQLDEEISEFCEIDRKAVSYSGPYNVKAESIRSITLPLIIKKPTYKKIYEISCLKISILKLPLQKFDIINDSRRSNPVEEEAEYSKCIYGKLKIKILPEQPQLELLSTSKMTRNSWMMLDGTKTDFHITVRNKSLSCAINHIKIIPMNNIEQMLKPDYWKKMPPDDLYIMEKQLDWLSKSCVRIIKLPTVIKPNETITFDLELDNTAVPFNFTGFDLLIEYGMSATDESCIYLKKLSIPYEVTLRRTIEVPSMDIIPLNELFSSQVENVDWIEYVMSKIRAESNLHSRDFILLLLDFRNSWIDGIKLNVQFEDFTSNEYHVEASHTSRIIVPIKKIDYKKYNFENTPIPRIYPGRQFIQSGLNEEQTIEMRQKFWCREHIISKLKCNWKLTTDQSVTGSVDFNKFIEKFDHKMVYTIYPGRLFYGVQLLLDEPKVKVGEIINLKIITEPTSTCRRKQNSTVNFLDIVIFDSKTSKILPRSNRRILYNGSLTKPISTTKVSEINLEIIPIEKGRYEFSVCISKSNNQDGIIQFDSENVILSVI
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
149PhosphorylationTMENVFASSPDMQKN
HHHHHHHCCHHHHHC		30.8228889911
150PhosphorylationMENVFASSPDMQKNI
HHHHHHCCHHHHHCH		22.8428889911
186PhosphorylationYKHVTLRSPGAIGGN
CCEEEEECCCCCCCC		30.6928889911
198PhosphorylationGGNAVLKTTLIRQNS
CCCEEEEEEEEECCC		23.7521440633
199PhosphorylationGNAVLKTTLIRQNSY
CCEEEEEEEEECCCC		20.7128889911
205PhosphorylationTTLIRQNSYTSSSSS
EEEEECCCCCCCCCC		22.8123749301
207PhosphorylationLIRQNSYTSSSSSTP
EEECCCCCCCCCCCC		23.1928889911
208PhosphorylationIRQNSYTSSSSSTPM
EECCCCCCCCCCCCC		21.7128889911
209PhosphorylationRQNSYTSSSSSTPMS
ECCCCCCCCCCCCCH		26.8328889911
210PhosphorylationQNSYTSSSSSTPMSA
CCCCCCCCCCCCCHH		28.2428889911
211PhosphorylationNSYTSSSSSTPMSAV
CCCCCCCCCCCCHHH		39.9328889911
212PhosphorylationSYTSSSSSTPMSAVQ
CCCCCCCCCCCHHHH		38.1828889911
213PhosphorylationYTSSSSSTPMSAVQS
CCCCCCCCCCHHHHH		25.5928889911
221PhosphorylationPMSAVQSSVSSSSKA
CCHHHHHHCCCCCCC		14.6628889911
233PhosphorylationSKAGSVTTASKRLSS
CCCCCCCHHHHHHHC		27.1228889911
239PhosphorylationTTASKRLSSFEMTTN
CHHHHHHHCCCCCCH		36.6924961812
240PhosphorylationTASKRLSSFEMTTNS
HHHHHHHCCCCCCHH		29.8020377248
251PhosphorylationTTNSLKRSASLKLAT
CCHHHHHHHHHHHHH		22.1827017623
253PhosphorylationNSLKRSASLKLATTL
HHHHHHHHHHHHHHH		27.5521440633
262PhosphorylationKLATTLSTSENRSQQ
HHHHHHCCCCCHHHH		43.0827017623
352PhosphorylationVEKLNFESSSTGISP
HHHCCCCCCCCCCCC		26.0028889911
353PhosphorylationEKLNFESSSTGISPV
HHCCCCCCCCCCCCC		25.4022369663
354PhosphorylationKLNFESSSTGISPVD
HCCCCCCCCCCCCCC		39.6722369663
355PhosphorylationLNFESSSTGISPVDS
CCCCCCCCCCCCCCC		40.2522369663
358PhosphorylationESSSTGISPVDSNSK
CCCCCCCCCCCCCCC		21.8822369663
362PhosphorylationTGISPVDSNSKATAS
CCCCCCCCCCCCCCC		43.1422369663
364PhosphorylationISPVDSNSKATASTT
CCCCCCCCCCCCCCC		27.8520377248
369PhosphorylationSNSKATASTTASSTP
CCCCCCCCCCCCCCC		23.1830377154
370PhosphorylationNSKATASTTASSTPR
CCCCCCCCCCCCCCC		24.7419779198
371PhosphorylationSKATASTTASSTPRN
CCCCCCCCCCCCCCC		23.2616445868
373PhosphorylationATASTTASSTPRNSI
CCCCCCCCCCCCCCE		32.4328152593
374PhosphorylationTASTTASSTPRNSIS
CCCCCCCCCCCCCEE		39.7128152593
375PhosphorylationASTTASSTPRNSISI
CCCCCCCCCCCCEEE		24.6316445868
379PhosphorylationASSTPRNSISIAAMQ
CCCCCCCCEEEEEEC		20.9923749301
381PhosphorylationSTPRNSISIAAMQSP
CCCCCCEEEEEECCC		13.1415665377
387PhosphorylationISIAAMQSPRNSIMS
EEEEEECCCCCCCHH		16.8522369663
449PhosphorylationEFLLKTLTFMTSCYK
HHHHHHHHHHHHHHC		19.3221551504
455PhosphorylationLTFMTSCYKSSEFSK
HHHHHHHHCCCCCCH		17.4221551504
458PhosphorylationMTSCYKSSEFSKDVL
HHHHHCCCCCCHHHH		38.2121551504
514PhosphorylationVEAQIKIYSTMAEVY
HHHHHHHHHHHHHHH		7.9630377154
516PhosphorylationAQIKIYSTMAEVYRL
HHHHHHHHHHHHHHH		11.9330377154
521PhosphorylationYSTMAEVYRLLGYKR
HHHHHHHHHHHCCCH		6.2530377154
526PhosphorylationEVYRLLGYKRKQLFV
HHHHHHCCCHHHHHH		13.9530377154
676PhosphorylationSNEIPLESDVSSLES
CCCCCCCCCCHHHHH		51.5021440633
679PhosphorylationIPLESDVSSLESLEN
CCCCCCCHHHHHHHH		33.9119779198
680PhosphorylationPLESDVSSLESLENR
CCCCCCHHHHHHHHH		35.6823749301
683PhosphorylationSDVSSLESLENRQKT
CCCHHHHHHHHHHCC		46.4021440633
708PhosphorylationPFKRVQPTSFVSNNS
CCCCCCCCCCCCCCC		20.0821440633
709PhosphorylationFKRVQPTSFVSNNST
CCCCCCCCCCCCCCC		30.2727214570
905PhosphorylationEQMLKPDYWKKMPPD
HHHHCCHHHHHCCHH		27.8827017623
1162PhosphorylationKFDHKMVYTIYPGRL
HCCCCEEEEECCCCC		5.5030377154
1165PhosphorylationHKMVYTIYPGRLFYG
CCEEEEECCCCCEEE		7.5830377154
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 TR120_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TR120_YEAST !!
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 TR120_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BET3_YEASTBET3physical
11239471
BET3_YEASTBET3physical
10727015
YPT31_YEASTYPT31genetic
12210902
YPT32_YEASTYPT32genetic
12210902
BET3_YEASTBET3physical
16554755
TRS33_YEASTTRS33physical
16554755
YPT31_YEASTYPT31genetic
19843283
TR130_YEASTTRS130physical
20375281
TRS65_YEASTTRS65physical
20375281
TR130_YEASTTRS130physical
20972447
TRS65_YEASTTRS65physical
20972447
TRS33_YEASTTRS33physical
20972447
TRS31_YEASTTRS31physical
20972447
BET3_YEASTBET3physical
20972447
TRS23_YEASTTRS23physical
20972447
TRS20_YEASTTRS20physical
20972447
BET5_YEASTBET5physical
20972447
TRS65_YEASTTRS65genetic
21813735
SSB1_YEASTSSB1physical
22940862
TRS33_YEASTTRS33physical
22940862
TR120_YEASTTRS120physical
22940862
HSP71_YEASTSSA1physical
22940862
YPT31_YEASTYPT31genetic
15574876
THIL_YEASTERG10genetic
23891562
BET3_YEASTBET3physical
21813735
TRS31_YEASTTRS31physical
23465091
TR130_YEASTTRS130physical
27872253
TRS65_YEASTTRS65physical
27872253
TRS33_YEASTTRS33physical
27872253
TRS31_YEASTTRS31physical
27872253
TRS23_YEASTTRS23physical
27872253
BET3_YEASTBET3physical
27872253
TRS20_YEASTTRS20physical
27872253
BET5_YEASTBET5physical
27872253
TCA17_YEASTTCA17physical
27872253
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TR120_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND MASSSPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-371 AND THR-375, ANDMASS SPECTROMETRY.

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