JPH1_HUMAN - dbPTM
JPH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JPH1_HUMAN
UniProt AC Q9HDC5
Protein Name Junctophilin-1
Gene Name JPH1
Organism Homo sapiens (Human).
Sequence Length 661
Subcellular Localization Cell membrane
Peripheral membrane protein. Endoplasmic reticulum membrane
Single-pass type IV membrane protein. Sarcoplasmic reticulum membrane
Single-pass type IV membrane protein. Localized predominantly on the plasma membrane. The transmembrane
Protein Description Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH1 contributes to the construction of the skeletal muscle triad by linking the t-tubule (transverse-tubule) and SR (sarcoplasmic reticulum) membranes..
Protein Sequence MTGGRFDFDDGGTYCGGWEEGKAHGHGICTGPKGQGEYSGSWSHGFEVVGGYTWPSGNTYQGYWAQGKRHGLGVETKGKWMYRGEWSHGFKGRYGVRQSLCTPARYEGTWSNGLQDGYGVETYGDGGTYQGQWAGGMRHGYGVRQSVPYGMATVIRSPLRTSLASLRSEQSNGSVLHDAAAAADSPAGTRGGFVLNFHADAELAGKKKGGLFRRGSLLGSMKLRKSESKSSISSKRSSVRSDAAMSRISSSDANSTISFGDVDCDFCPVEDHVDATTTETYMGEWKNDKRNGFGVSERSNGMKYEGEWANNKRHGYGCTVFPDGSKEEGKYKNNILVRGIRKQLIPIRHTKTREKVDRAIEGAQRAAAMARTKVEIANSRTAHARAKADAADQAALAARQECDIARAVARELSPDFYQPGPDYVKQRFQEGVDAKENPEEKVPEKPPTPKESPHFYRKGTTPPRSPEASPKHSHSPASSPKPLKKQNPSSGARLNQDKRSVADEQVTAIVNKPLMSKAPTKEAGAVVPQSKYSGRHHIPNPSNGELHSQYHGYYVKLNAPQHPPVDVEDGDGSSQSSSALVHKPSANKWSPSKSVTKPVAKESKAEPKAKKSELAIPKNPASNDSCPALEKEANSGPNSIMIVLVMLLNIGLAILFVHFLT
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
14PhosphorylationDFDDGGTYCGGWEEG
ECCCCCCCCCCCCCC		7.7427642862
38PhosphorylationGPKGQGEYSGSWSHG
CCCCCCCCCCCCCCC		25.7525072903
39PhosphorylationPKGQGEYSGSWSHGF
CCCCCCCCCCCCCCE		23.2725072903
41PhosphorylationGQGEYSGSWSHGFEV
CCCCCCCCCCCCEEE		21.3325072903
43PhosphorylationGEYSGSWSHGFEVVG
CCCCCCCCCCEEEEE		18.5425072903
52PhosphorylationGFEVVGGYTWPSGNT
CEEEEEEEECCCCCE		10.3325072903
53PhosphorylationFEVVGGYTWPSGNTY
EEEEEEEECCCCCEE		33.8925072903
56PhosphorylationVGGYTWPSGNTYQGY
EEEEECCCCCEECEE		35.9225072903
59PhosphorylationYTWPSGNTYQGYWAQ
EECCCCCEECEEECC		22.2825072903
60PhosphorylationTWPSGNTYQGYWAQG
ECCCCCEECEEECCC		12.1625072903
63PhosphorylationSGNTYQGYWAQGKRH
CCCEECEEECCCCCC		5.0925072903
77UbiquitinationHGLGVETKGKWMYRG
CCCCCCCCCCEEECC		45.01-
79AcetylationLGVETKGKWMYRGEW
CCCCCCCCEEECCCC		30.2826051181
87PhosphorylationWMYRGEWSHGFKGRY
EEECCCCCCCCCCCC		14.9426437602
91UbiquitinationGEWSHGFKGRYGVRQ
CCCCCCCCCCCEECC		47.2521890473
91UbiquitinationGEWSHGFKGRYGVRQ
CCCCCCCCCCCEECC		47.2521890473
141PhosphorylationAGGMRHGYGVRQSVP
CCCCCCCCCCCCCCC		13.3124719451
146PhosphorylationHGYGVRQSVPYGMAT
CCCCCCCCCCCCCEE		17.9427174698
149PhosphorylationGVRQSVPYGMATVIR
CCCCCCCCCCEEECC		19.8527174698
153PhosphorylationSVPYGMATVIRSPLR
CCCCCCEEECCCHHH		13.9427174698
157PhosphorylationGMATVIRSPLRTSLA
CCEEECCCHHHHHHH		19.7023927012
161PhosphorylationVIRSPLRTSLASLRS
ECCCHHHHHHHHHHH		35.4630266825
162PhosphorylationIRSPLRTSLASLRSE
CCCHHHHHHHHHHHH		18.5930266825
165PhosphorylationPLRTSLASLRSEQSN
HHHHHHHHHHHHHCC		29.6130266825
168PhosphorylationTSLASLRSEQSNGSV
HHHHHHHHHHCCCCH		45.3323312004
171PhosphorylationASLRSEQSNGSVLHD
HHHHHHHCCCCHHHH		38.8223312004
174PhosphorylationRSEQSNGSVLHDAAA
HHHHCCCCHHHHHHH		26.2522496350
185PhosphorylationDAAAAADSPAGTRGG
HHHHHCCCCCCCCCE		16.3628985074
189PhosphorylationAADSPAGTRGGFVLN
HCCCCCCCCCEEEEE		28.3927174698
208AcetylationAELAGKKKGGLFRRG
HHHCCCCCCCCCCCC		62.7925825284
216PhosphorylationGGLFRRGSLLGSMKL
CCCCCCCCHHHCEEE		20.7122167270
220PhosphorylationRRGSLLGSMKLRKSE
CCCCHHHCEEECCCC		16.8322167270
226PhosphorylationGSMKLRKSESKSSIS
HCEEECCCCCCCCHH		40.4424719451
228PhosphorylationMKLRKSESKSSISSK
EEECCCCCCCCHHCC		44.9528985074
230PhosphorylationLRKSESKSSISSKRS
ECCCCCCCCHHCCHH		42.0322210691
231PhosphorylationRKSESKSSISSKRSS
CCCCCCCCHHCCHHH		30.1726437602
237PhosphorylationSSISSKRSSVRSDAA
CCHHCCHHHHHHHHH		36.6020873877
238PhosphorylationSISSKRSSVRSDAAM
CHHCCHHHHHHHHHH		26.1122496350
241PhosphorylationSKRSSVRSDAAMSRI
CCHHHHHHHHHHHHH		29.4626437602
246PhosphorylationVRSDAAMSRISSSDA
HHHHHHHHHHCCCCC		23.0322496350
296O-linked_GlycosylationKRNGFGVSERSNGMK
CCCCCCCCCCCCCCE		27.8930620550
373UbiquitinationAAAMARTKVEIANSR
HHHHHHHHHHHHHCC		32.11-
379PhosphorylationTKVEIANSRTAHARA
HHHHHHHCCHHHHHH		23.2226437602
413PhosphorylationRAVARELSPDFYQPG
HHHHHHHCCCCCCCC		20.0525159151
417PhosphorylationRELSPDFYQPGPDYV
HHHCCCCCCCCHHHH		22.6028796482
423PhosphorylationFYQPGPDYVKQRFQE
CCCCCHHHHHHHHHC		16.8128796482
425UbiquitinationQPGPDYVKQRFQEGV
CCCHHHHHHHHHCCC		29.53-
448PhosphorylationKVPEKPPTPKESPHF
CCCCCCCCCCCCCCC		56.3629255136
452PhosphorylationKPPTPKESPHFYRKG
CCCCCCCCCCCCCCC		29.7822167270
456PhosphorylationPKESPHFYRKGTTPP
CCCCCCCCCCCCCCC		14.3730266825
460PhosphorylationPHFYRKGTTPPRSPE
CCCCCCCCCCCCCCC		38.8829255136
461PhosphorylationHFYRKGTTPPRSPEA
CCCCCCCCCCCCCCC		39.7129255136
465PhosphorylationKGTTPPRSPEASPKH
CCCCCCCCCCCCCCC		32.6329255136
469PhosphorylationPPRSPEASPKHSHSP
CCCCCCCCCCCCCCC		32.5929255136
473PhosphorylationPEASPKHSHSPASSP
CCCCCCCCCCCCCCC		31.6123927012
475PhosphorylationASPKHSHSPASSPKP
CCCCCCCCCCCCCCC		25.7730278072
478PhosphorylationKHSHSPASSPKPLKK
CCCCCCCCCCCCCCC		51.0230278072
479PhosphorylationHSHSPASSPKPLKKQ
CCCCCCCCCCCCCCC		38.7623927012
489PhosphorylationPLKKQNPSSGARLNQ
CCCCCCCCCCCCCCC		49.2925690035
500PhosphorylationRLNQDKRSVADEQVT
CCCCCCCCCCHHHHH		27.6526437602
530PhosphorylationAGAVVPQSKYSGRHH
CCCCCCCCCCCCCCC		27.7324719451
532PhosphorylationAVVPQSKYSGRHHIP
CCCCCCCCCCCCCCC		22.9226852163
533PhosphorylationVVPQSKYSGRHHIPN
CCCCCCCCCCCCCCC		32.8426437602
542PhosphorylationRHHIPNPSNGELHSQ
CCCCCCCCCCCEECE		65.2028796482
548PhosphorylationPSNGELHSQYHGYYV
CCCCCEECEEEEEEE		45.0928796482
550PhosphorylationNGELHSQYHGYYVKL
CCCEECEEEEEEEEE		10.5428796482
553PhosphorylationLHSQYHGYYVKLNAP
EECEEEEEEEEECCC		7.5628796482
554PhosphorylationHSQYHGYYVKLNAPQ
ECEEEEEEEEECCCC		8.8328796482
573PhosphorylationDVEDGDGSSQSSSAL
CCCCCCCCCCCCCEE		29.9125159151
574PhosphorylationVEDGDGSSQSSSALV
CCCCCCCCCCCCEEE		39.3420873877
576PhosphorylationDGDGSSQSSSALVHK
CCCCCCCCCCEEEEC		28.3620873877
577PhosphorylationGDGSSQSSSALVHKP
CCCCCCCCCEEEECC		16.4025022875
578PhosphorylationDGSSQSSSALVHKPS
CCCCCCCCEEEECCC		30.7620873877
585PhosphorylationSALVHKPSANKWSPS
CEEEECCCCCCCCCC		49.6421082442
590PhosphorylationKPSANKWSPSKSVTK
CCCCCCCCCCCCCCC		22.3925159151
592PhosphorylationSANKWSPSKSVTKPV
CCCCCCCCCCCCCCC		31.8621082442
594PhosphorylationNKWSPSKSVTKPVAK
CCCCCCCCCCCCCCC		39.0826437602
596PhosphorylationWSPSKSVTKPVAKES
CCCCCCCCCCCCCCC		36.4028634120
611UbiquitinationKAEPKAKKSELAIPK
CCCCCCCCCCCCCCC		54.76-
622PhosphorylationAIPKNPASNDSCPAL
CCCCCCCCCCCCHHH		42.2928102081
625PhosphorylationKNPASNDSCPALEKE
CCCCCCCCCHHHHHH		26.6730278072
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 JPH1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JPH1_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 JPH1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of JPH1_HUMAN !!
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 JPH1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-460; THR-461; SER-465AND SER-469, AND MASS SPECTROMETRY.
"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-157; SER-216; SER-220;THR-448; SER-452; THR-461; SER-465 AND SER-469, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-448 AND SER-452, ANDMASS SPECTROMETRY.

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