TROAP_HUMAN - dbPTM
TROAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TROAP_HUMAN
UniProt AC Q12815
Protein Name Tastin
Gene Name TROAP
Organism Homo sapiens (Human).
Sequence Length 778
Subcellular Localization Cytoplasm.
Protein Description Could be involved with bystin and trophinin in a cell adhesion molecule complex that mediates an initial attachment of the blastocyst to uterine epithelial cells at the time of the embryo implantation..
Protein Sequence MTTRQATKDPLLRGVSPTPSKIPVRSQKRTPFPTVTSCAVDQENQDPRRWVQKPPLNIQRPLVDSAGPRPKARHQAETSQRLVGISQPRNPLEELRPSPRGQNVGPGPPAQTEAPGTIEFVADPAALATILSGEGVKSCHLGRQPSLAKRVLVRGSQGGTTQRVQGVRASAYLAPRTPTHRLDPARASCFSRLEGPGPRGRTLCPQRLQALISPSGPSFHPSTRPSFQELRRETAGSSRTSVSQASGLLLETPVQPAFSLPKGEREVVTHSDEGGVASLGLAQRVPLRENREMSHTRDSHDSHLMPSPAPVAQPLPGHVVPCPSPFGRAQRVPSPGPPTLTSYSVLRRLTVQPKTRFTPMPSTPRVQQAQWLRGVSPQSCSEDPALPWEQVAVRLFDQESCIRSLEGSGKPPVATPSGPHSNRTPSLQEVKIQRIGILQQLLRQEVEGLVGGQCVPLNGGSSLDMVELQPLLTEISRTLNATEHNSGTSHLPGLLKHSGLPKPCLPEECGEPQPCPPAEPGPPEAFCRSEPEIPEPSLQEQLEVPEPYPPAEPRPLESCCRSEPEIPESSRQEQLEVPEPCPPAEPRPLESYCRIEPEIPESSRQEQLEVPEPCPPAEPGPLQPSTQGQSGPPGPCPRVELGASEPCTLEHRSLESSLPPCCSQWAPATTSLIFSSQHPLCASPPICSLQSLRPPAGQAGLSNLAPRTLALRERLKSCLTAIHCFHEARLDDECAFYTSRAPPSGPTRVCTNPVATLLEWQDALCFIPVGSAAPQGSP
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
13MethylationATKDPLLRGVSPTPS
HCCCCCCCCCCCCCC		51.67115368003
16PhosphorylationDPLLRGVSPTPSKIP
CCCCCCCCCCCCCCC		26.3625159151
18PhosphorylationLLRGVSPTPSKIPVR
CCCCCCCCCCCCCCC		32.4626055452
20PhosphorylationRGVSPTPSKIPVRSQ
CCCCCCCCCCCCCCC		45.7722199227
21AcetylationGVSPTPSKIPVRSQK
CCCCCCCCCCCCCCC		52.8425953088
26PhosphorylationPSKIPVRSQKRTPFP
CCCCCCCCCCCCCCC		40.0428555341
30PhosphorylationPVRSQKRTPFPTVTS
CCCCCCCCCCCCCCE		36.0029214152
34PhosphorylationQKRTPFPTVTSCAVD
CCCCCCCCCCEEEEC		36.4728555341
37PhosphorylationTPFPTVTSCAVDQEN
CCCCCCCEEEECCCC		8.8521815630
53UbiquitinationDPRRWVQKPPLNIQR
CCCHHCCCCCCCCCC		38.70-
65PhosphorylationIQRPLVDSAGPRPKA
CCCCCCCCCCCCCCH		27.8724719451
86PhosphorylationSQRLVGISQPRNPLE
HHHHHCCCCCCCHHH		28.3628555341
98PhosphorylationPLEELRPSPRGQNVG
HHHHHCCCCCCCCCC		22.3125159151
137UbiquitinationILSGEGVKSCHLGRQ
HHHCCCCCCCCCCCC		59.21-
146PhosphorylationCHLGRQPSLAKRVLV
CCCCCCCCCCEEEEE		32.4025159151
154MethylationLAKRVLVRGSQGGTT
CCEEEEECCCCCCCC		34.58115919025
156PhosphorylationKRVLVRGSQGGTTQR
EEEEECCCCCCCCCC		18.3229396449
160PhosphorylationVRGSQGGTTQRVQGV
ECCCCCCCCCCEECE		26.9520860994
161PhosphorylationRGSQGGTTQRVQGVR
CCCCCCCCCCEECEE		20.0426270265
170PhosphorylationRVQGVRASAYLAPRT
CEECEEEEEEECCCC		13.5921815630
172PhosphorylationQGVRASAYLAPRTPT
ECEEEEEEECCCCCC		10.8229396449
177PhosphorylationSAYLAPRTPTHRLDP
EEEECCCCCCCCCCH		31.3230576142
179PhosphorylationYLAPRTPTHRLDPAR
EECCCCCCCCCCHHH		21.0021712546
188PhosphorylationRLDPARASCFSRLEG
CCCHHHHHHHHHCCC		15.3321712546
191PhosphorylationPARASCFSRLEGPGP
HHHHHHHHHCCCCCC		40.0421712546
192MethylationARASCFSRLEGPGPR
HHHHHHHHCCCCCCC		19.26115919029
199MethylationRLEGPGPRGRTLCPQ
HCCCCCCCCCCCCHH		53.8181453777
201MethylationEGPGPRGRTLCPQRL
CCCCCCCCCCCHHHH		26.29115919033
213PhosphorylationQRLQALISPSGPSFH
HHHHHHHCCCCCCCC		17.5426055452
215PhosphorylationLQALISPSGPSFHPS
HHHHHCCCCCCCCCC		57.4520068231
218PhosphorylationLISPSGPSFHPSTRP
HHCCCCCCCCCCCCC		39.4527732954
222PhosphorylationSGPSFHPSTRPSFQE
CCCCCCCCCCCCHHH		28.6020068231
223PhosphorylationGPSFHPSTRPSFQEL
CCCCCCCCCCCHHHH		51.5620068231
226PhosphorylationFHPSTRPSFQELRRE
CCCCCCCCHHHHHHH		35.9520068231
234PhosphorylationFQELRRETAGSSRTS
HHHHHHHHCCCCCCC		34.2121712546
237PhosphorylationLRRETAGSSRTSVSQ
HHHHHCCCCCCCHHH		17.7421712546
238PhosphorylationRRETAGSSRTSVSQA
HHHHCCCCCCCHHHH		38.36-
240PhosphorylationETAGSSRTSVSQASG
HHCCCCCCCHHHHCC		35.1121712546
241PhosphorylationTAGSSRTSVSQASGL
HCCCCCCCHHHHCCC		20.7521712546
243PhosphorylationGSSRTSVSQASGLLL
CCCCCCHHHHCCCEE		21.5726055452
246O-linked_GlycosylationRTSVSQASGLLLETP
CCCHHHHCCCEECCC		23.4930059200
246PhosphorylationRTSVSQASGLLLETP
CCCHHHHCCCEECCC		23.4921712546
252PhosphorylationASGLLLETPVQPAFS
HCCCEECCCCCCCCC		28.8226055452
259PhosphorylationTPVQPAFSLPKGERE
CCCCCCCCCCCCCEE		45.9621712546
262UbiquitinationQPAFSLPKGEREVVT
CCCCCCCCCCEEEEE		77.89-
269PhosphorylationKGEREVVTHSDEGGV
CCCEEEEEECCCCCC		22.3425159151
271PhosphorylationEREVVTHSDEGGVAS
CEEEEEECCCCCCCC		28.1725159151
278PhosphorylationSDEGGVASLGLAQRV
CCCCCCCCCCHHHCC		22.1425159151
299PhosphorylationEMSHTRDSHDSHLMP
CCCCCCCCCCCCCCC		26.3820068231
302PhosphorylationHTRDSHDSHLMPSPA
CCCCCCCCCCCCCCC		17.0722199227
307PhosphorylationHDSHLMPSPAPVAQP
CCCCCCCCCCCCCCC		21.5225159151
324PhosphorylationGHVVPCPSPFGRAQR
CCEEECCCCCCCCCC		39.3125159151
334PhosphorylationGRAQRVPSPGPPTLT
CCCCCCCCCCCCCCC		39.3625159151
339PhosphorylationVPSPGPPTLTSYSVL
CCCCCCCCCCCHHHH		45.8928387310
341PhosphorylationSPGPPTLTSYSVLRR
CCCCCCCCCHHHHHH		28.2625159151
342PhosphorylationPGPPTLTSYSVLRRL
CCCCCCCCHHHHHHC		20.6530576142
343PhosphorylationGPPTLTSYSVLRRLT
CCCCCCCHHHHHHCC		9.5028387310
344PhosphorylationPPTLTSYSVLRRLTV
CCCCCCHHHHHHCCC		17.9125159151
355PhosphorylationRLTVQPKTRFTPMPS
HCCCCCCCCCCCCCC		37.3821712546
358PhosphorylationVQPKTRFTPMPSTPR
CCCCCCCCCCCCCCH		18.5218669648
362PhosphorylationTRFTPMPSTPRVQQA
CCCCCCCCCCHHHHH		44.8025159151
363PhosphorylationRFTPMPSTPRVQQAQ
CCCCCCCCCHHHHHH		14.8325159151
373MethylationVQQAQWLRGVSPQSC
HHHHHHHCCCCCCCC		40.2797778427
376PhosphorylationAQWLRGVSPQSCSED
HHHHCCCCCCCCCCC		21.7525159151
379PhosphorylationLRGVSPQSCSEDPAL
HCCCCCCCCCCCCCC		24.0120068231
381PhosphorylationGVSPQSCSEDPALPW
CCCCCCCCCCCCCCH		50.7328464451
404PhosphorylationDQESCIRSLEGSGKP
CHHHHHHHCCCCCCC		15.7421712546
408PhosphorylationCIRSLEGSGKPPVAT
HHHHCCCCCCCCCCC		33.9828555341
410UbiquitinationRSLEGSGKPPVATPS
HHCCCCCCCCCCCCC		48.0921906983
415PhosphorylationSGKPPVATPSGPHSN
CCCCCCCCCCCCCCC		20.4428985074
417PhosphorylationKPPVATPSGPHSNRT
CCCCCCCCCCCCCCC		61.6825159151
421PhosphorylationATPSGPHSNRTPSLQ
CCCCCCCCCCCCCHH		31.0125159151
424PhosphorylationSGPHSNRTPSLQEVK
CCCCCCCCCCHHHHH		22.8321815630
426PhosphorylationPHSNRTPSLQEVKIQ
CCCCCCCCHHHHHHH		41.9121712546
431UbiquitinationTPSLQEVKIQRIGIL
CCCHHHHHHHHHHHH		32.1621906983
476PhosphorylationQPLLTEISRTLNATE
HHHHHHHHHHHCCCC		17.0021815630
486PhosphorylationLNATEHNSGTSHLPG
HCCCCCCCCCCCCCH		45.4121712546
488PhosphorylationATEHNSGTSHLPGLL
CCCCCCCCCCCCHHH		16.8821712546
489PhosphorylationTEHNSGTSHLPGLLK
CCCCCCCCCCCHHHH		26.9328555341
529PhosphorylationPPEAFCRSEPEIPEP
CCHHHCCCCCCCCCC		59.7028122231
537PhosphorylationEPEIPEPSLQEQLEV
CCCCCCCCHHHHCCC		40.8128122231
562PhosphorylationPLESCCRSEPEIPES
CHHHHCCCCCCCCCC		43.5221815630
644O-linked_GlycosylationPRVELGASEPCTLEH
CCEECCCCCCCCCCC		40.0330059200
717PhosphorylationALRERLKSCLTAIHC
HHHHHHHHHHHHHHH		20.9628555341
751PhosphorylationSGPTRVCTNPVATLL
CCCCCCCCCCCHHHH		39.4320068231
756PhosphorylationVCTNPVATLLEWQDA
CCCCCCHHHHHHCCE		31.9120068231
771PhosphorylationLCFIPVGSAAPQGSP
EEEEECCCCCCCCCC		22.8420068231
777PhosphorylationGSAAPQGSP------
CCCCCCCCC------		23.3720068231
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 TROAP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TROAP_HUMAN !!
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 TROAP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TROAP_HUMANTROAPphysical
9560222
BYST_HUMANBYSLphysical
9560222
TROP_HUMANTROphysical
9560222
K2C8_HUMANKRT8physical
9560222
TRI23_HUMANTRIM23physical
19060904
MARE1_HUMANMAPRE1physical
25416956
MARE3_HUMANMAPRE3physical
25416956
BANP_HUMANBANPphysical
25416956
K1C40_HUMANKRT40physical
25416956
MARE3_HUMANMAPRE3physical
21516116
BANP_HUMANBANPphysical
28514442
SUOX_HUMANSUOXphysical
28514442
MARE1_HUMANMAPRE1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TROAP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-18; SER-98;SER-307; SER-324; SER-334; THR-358; SER-362 AND THR-363, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-271; SER-334 ANDSER-376, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; SER-344 ANDSER-376, AND MASS SPECTROMETRY.

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