TJAP1_MOUSE - dbPTM
TJAP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TJAP1_MOUSE
UniProt AC Q9DCD5
Protein Name Tight junction-associated protein 1
Gene Name Tjap1
Organism Mus musculus (Mouse).
Sequence Length 539
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.
Protein Description
Protein Sequence MSSAAPAKKPYRKAPPEHRELRLEIPVSRLEQEESLTDAERMKLLQQENEELRKRLASATRRTEALERELEIGQDCLELELGQSREELDKFKDKFRRLQNSYTASQRTNQELEDKLHALIKKAEMDRKTLDWEIVELTNKLLDARNTINKLEELNERYRLDCNLAVQLLKCNKSHFRNHKLADLPCELQDMVRKHLRSGQEVASPSPSPSSSLSPGAVVPTSVIARVLEKPESLLLNSAQSGSAGRPLAEDVFVHVDMSGGDPASPPAPGSPNGECCSVSTAGGSPEEELPLPAFDKLSPYPTPSPPHPLYPGRKVIEFSEDKIRIPRNSPLPNCTYATRQAISLSLVEDGSERAHRSSVPSSPASAQGSPHHQPSPAPSALSAPASSASSEEDLLASWQRAFVDRTPPPAAVVQRTAFGRDSLPELQLHFSPGHSTAPPPSPHRERGLVLPAEPDSGFPQDEEEEMLNLPVSPEEERQSLLPDKEGTEEASGPSHVDGRAWPLPSPSRPQRSPKRMGVHHLHRKDSLTQAQEQGTVLS
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
58PhosphorylationELRKRLASATRRTEA
HHHHHHHHHHHHHHH		34.46-
198PhosphorylationMVRKHLRSGQEVASP
HHHHHHHCCCCCCCC		51.7126643407
204PhosphorylationRSGQEVASPSPSPSS
HCCCCCCCCCCCCCC		30.9626643407
206PhosphorylationGQEVASPSPSPSSSL
CCCCCCCCCCCCCCC		35.2025293948
208PhosphorylationEVASPSPSPSSSLSP
CCCCCCCCCCCCCCC		41.5725293948
210PhosphorylationASPSPSPSSSLSPGA
CCCCCCCCCCCCCCC		36.5825293948
211PhosphorylationSPSPSPSSSLSPGAV
CCCCCCCCCCCCCCC		38.3925293948
212PhosphorylationPSPSPSSSLSPGAVV
CCCCCCCCCCCCCCC		36.8824453211
214PhosphorylationPSPSSSLSPGAVVPT
CCCCCCCCCCCCCCH		24.2024453211
221PhosphorylationSPGAVVPTSVIARVL
CCCCCCCHHHHHHHH		24.8225293948
222PhosphorylationPGAVVPTSVIARVLE
CCCCCCHHHHHHHHH		12.8825293948
285PhosphorylationSVSTAGGSPEEELPL
EEECCCCCCHHHCCC		28.37-
295PhosphorylationEELPLPAFDKLSPYP
HHCCCCCCCCCCCCC		8.87-
303PhosphorylationDKLSPYPTPSPPHPL
CCCCCCCCCCCCCCC		30.4726745281
305PhosphorylationLSPYPTPSPPHPLYP
CCCCCCCCCCCCCCC		54.2427600695
311PhosphorylationPSPPHPLYPGRKVIE
CCCCCCCCCCCEEEE		14.2123984901
313PhosphorylationPPHPLYPGRKVIEFS
CCCCCCCCCEEEEEC		28.60-
315PhosphorylationHPLYPGRKVIEFSED
CCCCCCCEEEEECCC		54.18-
320PhosphorylationGRKVIEFSEDKIRIP
CCEEEEECCCCCCCC		31.9028066266
330PhosphorylationKIRIPRNSPLPNCTY
CCCCCCCCCCCCCCH		29.1524899341
336PhosphorylationNSPLPNCTYATRQAI
CCCCCCCCHHHCCEE		23.8825777480
337PhosphorylationSPLPNCTYATRQAIS
CCCCCCCHHHCCEEE		14.2622817900
339PhosphorylationLPNCTYATRQAISLS
CCCCCHHHCCEEEEE		16.9525777480
340PhosphorylationPNCTYATRQAISLSL
CCCCHHHCCEEEEEE		18.76-
344PhosphorylationYATRQAISLSLVEDG
HHHCCEEEEEEECCC		18.2130635358
346PhosphorylationTRQAISLSLVEDGSE
HCCEEEEEEECCCCC		24.4723970565
352PhosphorylationLSLVEDGSERAHRSS
EEEECCCCCCCCCCC		35.9122802335
358PhosphorylationGSERAHRSSVPSSPA
CCCCCCCCCCCCCCC		26.3125338131
359PhosphorylationSERAHRSSVPSSPAS
CCCCCCCCCCCCCCC		37.6925338131
362PhosphorylationAHRSSVPSSPASAQG
CCCCCCCCCCCCCCC		46.9625338131
366PhosphorylationSVPSSPASAQGSPHH
CCCCCCCCCCCCCCC		25.2225338131
376PhosphorylationGSPHHQPSPAPSALS
CCCCCCCCCCCCCCC		27.4221183079
380PhosphorylationHQPSPAPSALSAPAS
CCCCCCCCCCCCCCC		43.9021183079
383PhosphorylationSPAPSALSAPASSAS
CCCCCCCCCCCCCCC		31.7425338131
388PhosphorylationALSAPASSASSEEDL
CCCCCCCCCCCHHHH		33.9922817900
390PhosphorylationSAPASSASSEEDLLA
CCCCCCCCCHHHHHH		39.9821183079
391PhosphorylationAPASSASSEEDLLAS
CCCCCCCCHHHHHHH		44.7321183079
407PhosphorylationQRAFVDRTPPPAAVV
HHHHHCCCCCCCCEE		35.3726824392
417PhosphorylationPAAVVQRTAFGRDSL
CCCEEEECCCCCCCC		14.8419131326
423PhosphorylationRTAFGRDSLPELQLH
ECCCCCCCCCCCEEE		44.4528507225
432PhosphorylationPELQLHFSPGHSTAP
CCCEEECCCCCCCCC		21.1525619855
436PhosphorylationLHFSPGHSTAPPPSP
EECCCCCCCCCCCCC		31.9825619855
437PhosphorylationHFSPGHSTAPPPSPH
ECCCCCCCCCCCCCC		37.1925619855
442PhosphorylationHSTAPPPSPHRERGL
CCCCCCCCCCCCCCC		38.8326824392
473PhosphorylationEMLNLPVSPEEERQS
HHHCCCCCHHHHHHH		25.3427180971
480PhosphorylationSPEEERQSLLPDKEG
CHHHHHHHCCCCCCC		37.7925338131
483PhosphorylationEERQSLLPDKEGTEE
HHHHHCCCCCCCCCC		56.79-
506PhosphorylationGRAWPLPSPSRPQRS
CCCCCCCCCCCCCCC		43.1028725479
508PhosphorylationAWPLPSPSRPQRSPK
CCCCCCCCCCCCCCC		62.0128638064
513PhosphorylationSPSRPQRSPKRMGVH
CCCCCCCCCCCCCCC		29.5328507225
527PhosphorylationHHLHRKDSLTQAQEQ
CEECCCCCCHHHHHH		36.0327087446
529PhosphorylationLHRKDSLTQAQEQGT
ECCCCCCHHHHHHCC		26.3027087446
536PhosphorylationTQAQEQGTVLS----
HHHHHHCCCCC----		20.2628285833
537PhosphorylationQAQEQGTVLS-----
HHHHHCCCCC-----		6.7221183079
539PhosphorylationQEQGTVLS-------
HHHCCCCC-------		33.5621659605
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TJAP1_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TJAP1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TJAP1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527, AND MASSSPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-407, AND MASSSPECTROMETRY.

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