TJAP1_HUMAN - dbPTM
TJAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TJAP1_HUMAN
UniProt AC Q5JTD0
Protein Name Tight junction-associated protein 1
Gene Name TJAP1
Organism Homo sapiens (Human).
Sequence Length 557
Subcellular Localization Golgi apparatus. Cell junction, tight junction. Recruited to tight junctions (TJ) during late stages of maturation of the TJ complexes. Excluded from adherens junctions and desmosomes (By similarity)..
Protein Description
Protein Sequence MTSAAPAKKPYRKAPPEHRELRLEIPGSRLEQEEPLTDAERMKLLQEENEELRRRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHTLASLSHSWIFAIKKAEMDRKTLDWEIVELTNKLLDAKNTINKLEELNERYRLDCNLAVQLLKCNKSHFRNHKFADLPCELQDMVRKHLHSGQEAASPGPAPSLAPGAVVPTSVIARVLEKPESLLLNSAQSGSAGRPLAEDVFVHVDMSEGVPGDPASPPAPGSPTPQPNGECHSLGTARGSPEEELPLPAFEKLNPYPTPSPPHPLYPGRRVIEFSEDKVRIPRNSPLPNCTYATRQAISLSLVEEGSERARPSPVPSTPASAQASPHHQPSPAPLTLSAPASSASSEEDLLVSWQRAFVDRTPPPAAVAQRTAFGRDALPELQRHFAHSPADRDEVVQAPSARPEESELLLPTEPDSGFPREEEELNLPISPEEERQSLLPINRGTEEGPGTSHTEGRAWPLPSSSRPQRSPKRMGVHHLHRKDSLTQAQEQGNLLN
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
2Acetylation------MTSAAPAKK
------CCCCCCCCC		27.3722814378
3Phosphorylation-----MTSAAPAKKP
-----CCCCCCCCCC		22.5724719451
11PhosphorylationAAPAKKPYRKAPPEH
CCCCCCCCCCCCHHH		33.3624719451
28PhosphorylationLRLEIPGSRLEQEEP
EEEECCCCHHCCCCC		28.47-
37PhosphorylationLEQEEPLTDAERMKL
HCCCCCCCHHHHHHH		43.83-
58PhosphorylationELRRRLASATRRTEA
HHHHHHHHHHHHHHH		34.4622817900
60PhosphorylationRRRLASATRRTEALE
HHHHHHHHHHHHHHH		20.4223312004
63PhosphorylationLASATRRTEALEREL
HHHHHHHHHHHHHHH		23.48-
147 (in isoform 2)Phosphorylation-4.41-
155UbiquitinationTNKLLDAKNTINKLE
HHHHHHHHHHHHHHH		55.05-
157PhosphorylationKLLDAKNTINKLEEL
HHHHHHHHHHHHHHH		25.8123403867
160UbiquitinationDAKNTINKLEELNER
HHHHHHHHHHHHHHH		54.12-
198 (in isoform 2)Phosphorylation-7.15-
204UbiquitinationELQDMVRKHLHSGQE
HHHHHHHHHHHCCCC		38.82-
208PhosphorylationMVRKHLHSGQEAASP
HHHHHHHCCCCCCCC		48.8321712546
214PhosphorylationHSGQEAASPGPAPSL
HCCCCCCCCCCCCCC		37.1225159151
220PhosphorylationASPGPAPSLAPGAVV
CCCCCCCCCCCCCCC		38.9920873877
229PhosphorylationAPGAVVPTSVIARVL
CCCCCCCHHHHHHHH		24.8223312004
230PhosphorylationPGAVVPTSVIARVLE
CCCCCCHHHHHHHHH		12.8823312004
290 (in isoform 2)Phosphorylation-35.38-
293PhosphorylationQPNGECHSLGTARGS
CCCCCCCCCCCCCCC		39.9026074081
296PhosphorylationGECHSLGTARGSPEE
CCCCCCCCCCCCCHH		20.6226074081
300PhosphorylationSLGTARGSPEEELPL
CCCCCCCCCHHCCCC		24.4719664994
308 (in isoform 2)Phosphorylation-32.72-
310 (in isoform 2)Phosphorylation-8.86-
316PhosphorylationAFEKLNPYPTPSPPH
HHHHCCCCCCCCCCC		20.7522167270
316 (in isoform 2)Phosphorylation-20.75-
318PhosphorylationEKLNPYPTPSPPHPL
HHCCCCCCCCCCCCC		30.4722167270
320PhosphorylationLNPYPTPSPPHPLYP
CCCCCCCCCCCCCCC		54.2422167270
326PhosphorylationPSPPHPLYPGRRVIE
CCCCCCCCCCCCEEE		14.2122167270
335PhosphorylationGRRVIEFSEDKVRIP
CCCEEECCCCCCCCC		31.9021815630
335 (in isoform 2)Phosphorylation-31.90-
345PhosphorylationKVRIPRNSPLPNCTY
CCCCCCCCCCCCCCH		29.1521945579
351PhosphorylationNSPLPNCTYATRQAI
CCCCCCCCHHHHHHH		23.8821945579
352PhosphorylationSPLPNCTYATRQAIS
CCCCCCCHHHHHHHE		14.2621945579
354PhosphorylationLPNCTYATRQAISLS
CCCCCHHHHHHHEEH		16.9521945579
359PhosphorylationYATRQAISLSLVEEG
HHHHHHHEEHHHHCC		18.2122199227
361PhosphorylationTRQAISLSLVEEGSE
HHHHHEEHHHHCCCC		24.4722199227
367PhosphorylationLSLVEEGSERARPSP
EHHHHCCCCCCCCCC		27.4720068231
381PhosphorylationPVPSTPASAQASPHH
CCCCCCCCCCCCCCC		23.3228348404
385PhosphorylationTPASAQASPHHQPSP
CCCCCCCCCCCCCCC		16.8228348404
391PhosphorylationASPHHQPSPAPLTLS
CCCCCCCCCCCEEEE		27.4228348404
398PhosphorylationSPAPLTLSAPASSAS
CCCCEEEECCCCCCC		27.2828348404
402PhosphorylationLTLSAPASSASSEED
EEEECCCCCCCCHHH		25.9427251275
403PhosphorylationTLSAPASSASSEEDL
EEECCCCCCCCHHHH		33.9927251275
405PhosphorylationSAPASSASSEEDLLV
ECCCCCCCCHHHHHH		39.9828348404
406PhosphorylationAPASSASSEEDLLVS
CCCCCCCCHHHHHHH		44.7328348404
412 (in isoform 2)Phosphorylation-7.70-
422PhosphorylationQRAFVDRTPPPAAVA
HHHHHCCCCCHHHHH		35.3729255136
449PhosphorylationLQRHFAHSPADRDEV
HHHHHCCCCCCHHHH		20.5327794612
481 (in isoform 2)Phosphorylation-62.79-
491PhosphorylationEELNLPISPEEERQS
HHHCCCCCHHHHHHC		25.0719664994
504MethylationQSLLPINRGTEEGPG
HCCCCCCCCCCCCCC		54.88115918521
506PhosphorylationLLPINRGTEEGPGTS
CCCCCCCCCCCCCCC		27.8528555341
524PhosphorylationGRAWPLPSSSRPQRS
CCCCCCCCCCCCCCC		48.9423403867
525PhosphorylationRAWPLPSSSRPQRSP
CCCCCCCCCCCCCCC		28.5523403867
526PhosphorylationAWPLPSSSRPQRSPK
CCCCCCCCCCCCCCC		52.9323403867
531PhosphorylationSSSRPQRSPKRMGVH
CCCCCCCCCCCCCCC		29.5322617229
535 (in isoform 2)Phosphorylation-9.08-
537 (in isoform 2)Phosphorylation-1.56-
545PhosphorylationHHLHRKDSLTQAQEQ
CCCCCCHHHHHHHHH		36.0319664994
547PhosphorylationLHRKDSLTQAQEQGN
CCCCHHHHHHHHHCC		26.3029255136
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 TJAP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TJAP1_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 TJAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DLG1_HUMANDLG1physical
11602598
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 TJAP1_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-300 AND SER-545, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, 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-300; THR-318; SER-320;SER-345; THR-422 AND SER-545, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-352, AND MASSSPECTROMETRY.

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