JPH2_HUMAN - dbPTM
JPH2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JPH2_HUMAN
UniProt AC Q9BR39
Protein Name Junctophilin-2
Gene Name JPH2
Organism Homo sapiens (Human).
Sequence Length 696
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. JPH2 is necessary for proper intracellular Ca(2+) signaling in cardiac myocytes via its involvement in ryanodine receptor-mediated calcium ion release. Contributes to the construction of skeletal muscle triad junctions..
Protein Sequence MSGGRFDFDDGGAYCGGWEGGKAHGHGLCTGPKGQGEYSGSWNFGFEVAGVYTWPSGNTFEGYWSQGKRHGLGIETKGRWLYKGEWTHGFKGRYGIRQSSSSGAKYEGTWNNGLQDGYGTETYADGGTYQGQFTNGMRHGYGVRQSVPYGMAVVVRSPLRTSLSSLRSEHSNGTVAPDSPASPASDGPALPSPAIPRGGFALSLLANAEAAARAPKGGGLFQRGALLGKLRRAESRTSVGSQRSRVSFLKSDLSSGASDAASTASLGEAAEGADEAAPFEADIDATTTETYMGEWKNDKRSGFGVSERSSGLRYEGEWLDNLRHGYGCTTLPDGHREEGKYRHNVLVKDTKRRMLQLKSNKVRQKVEHSVEGAQRAAAIARQKAEIAASRTSHAKAKAEAAEQAALAANQESNIARTLARELAPDFYQPGPEYQKRRLLQEILENSESLLEPPDRGAGAAGLPQPPRESPQLHERETPRPEGGSPSPAGTPPQPKRPRPGVSKDGLLSPGAWNGEPSGEGSRSVTPSEGAGRRSPARPATERMAIEALQAPPAPSREPEVALYQGYHSYAVRTTPPEPPPFEDQPEPEVSGSESAPSSPATAPLQAPTLRGPEPARETPAKLEPKPIIPKAEPRAKARKTEARGLTKAGAKKKARKEAALAAEAEVEVEEVPNTILICMVILLNIGLAILFVHLLT
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
141PhosphorylationTNGMRHGYGVRQSVP
CCCCCCCCCCCCCCC		13.3126437602
146PhosphorylationHGYGVRQSVPYGMAV
CCCCCCCCCCCCEEE		17.9424719451
149PhosphorylationGVRQSVPYGMAVVVR
CCCCCCCCCEEEEEC		19.8524719451
157PhosphorylationGMAVVVRSPLRTSLS
CEEEEECCCHHHCHH		19.3723927012
161PhosphorylationVVRSPLRTSLSSLRS
EECCCHHHCHHHHHH		41.5223927012
162PhosphorylationVRSPLRTSLSSLRSE
ECCCHHHCHHHHHHC		21.5922167270
164PhosphorylationSPLRTSLSSLRSEHS
CCHHHCHHHHHHCCC		27.3922167270
165PhosphorylationPLRTSLSSLRSEHSN
CHHHCHHHHHHCCCC		32.8522167270
168PhosphorylationTSLSSLRSEHSNGTV
HCHHHHHHCCCCCCC		44.9823663014
171PhosphorylationSSLRSEHSNGTVAPD
HHHHHCCCCCCCCCC		32.6723663014
174PhosphorylationRSEHSNGTVAPDSPA
HHCCCCCCCCCCCCC		20.1123663014
179PhosphorylationNGTVAPDSPASPASD
CCCCCCCCCCCCCCC		22.7023663014
182PhosphorylationVAPDSPASPASDGPA
CCCCCCCCCCCCCCC		25.1223663014
185PhosphorylationDSPASPASDGPALPS
CCCCCCCCCCCCCCC		46.6223663014
192PhosphorylationSDGPALPSPAIPRGG
CCCCCCCCCCCCCCH		28.0121955146
235PhosphorylationGKLRRAESRTSVGSQ
HHHHHCCCCCCCCCH		39.6126437602
237PhosphorylationLRRAESRTSVGSQRS
HHHCCCCCCCCCHHH		36.7226437602
238PhosphorylationRRAESRTSVGSQRSR
HHCCCCCCCCCHHHH		24.3026437602
241PhosphorylationESRTSVGSQRSRVSF
CCCCCCCCHHHHHHH		21.9226437602
244PhosphorylationTSVGSQRSRVSFLKS
CCCCCHHHHHHHHHH		29.4226437602
247PhosphorylationGSQRSRVSFLKSDLS
CCHHHHHHHHHHHHC		24.6126437602
263PhosphorylationGASDAASTASLGEAA
CCCCHHHHHHHHHHH		18.6222210691
265PhosphorylationSDAASTASLGEAAEG
CCHHHHHHHHHHHCC		36.6822210691
306PhosphorylationKRSGFGVSERSSGLR
CCCCCCCCCCCCCCC		27.8924719451
309PhosphorylationGFGVSERSSGLRYEG
CCCCCCCCCCCCCCC		25.3824719451
310PhosphorylationFGVSERSSGLRYEGE
CCCCCCCCCCCCCCC		48.3324719451
359PhosphorylationRRMLQLKSNKVRQKV
HHHHHHHHHHHHHHH		50.9419664994
369PhosphorylationVRQKVEHSVEGAQRA
HHHHHHHHHHHHHHH		14.3623403867
435UbiquitinationQPGPEYQKRRLLQEI
CCCHHHHHHHHHHHH		38.29-
446PhosphorylationLQEILENSESLLEPP
HHHHHHCCHHHCCCC		21.1327174698
448PhosphorylationEILENSESLLEPPDR
HHHHCCHHHCCCCCC		37.7727174698
469PhosphorylationLPQPPRESPQLHERE
CCCCCCCCCCCCCCC		21.1621712546
477PhosphorylationPQLHERETPRPEGGS
CCCCCCCCCCCCCCC		30.7130278072
484PhosphorylationTPRPEGGSPSPAGTP
CCCCCCCCCCCCCCC		32.8222167270
486PhosphorylationRPEGGSPSPAGTPPQ
CCCCCCCCCCCCCCC		29.1322167270
490PhosphorylationGSPSPAGTPPQPKRP
CCCCCCCCCCCCCCC		33.6230266825
502PhosphorylationKRPRPGVSKDGLLSP
CCCCCCCCCCCCCCC		30.83-
508PhosphorylationVSKDGLLSPGAWNGE
CCCCCCCCCCCCCCC		26.7421815630
523PhosphorylationPSGEGSRSVTPSEGA
CCCCCCCCCCCCCCC		31.8526437602
525PhosphorylationGEGSRSVTPSEGAGR
CCCCCCCCCCCCCCC		23.5027174698
527PhosphorylationGSRSVTPSEGAGRRS
CCCCCCCCCCCCCCC		39.0227174698
534PhosphorylationSEGAGRRSPARPATE
CCCCCCCCCCCCHHH		22.8826657352
540PhosphorylationRSPARPATERMAIEA
CCCCCCHHHHHHHHH		27.1427174698
563PhosphorylationREPEVALYQGYHSYA
CCCCEEEEEECCEEE		7.0827642862
568PhosphorylationALYQGYHSYAVRTTP
EEEEECCEEECCCCC		13.3024719451
569PhosphorylationLYQGYHSYAVRTTPP
EEEECCEEECCCCCC		8.8727642862
573PhosphorylationYHSYAVRTTPPEPPP
CCEEECCCCCCCCCC		36.7426437602
574PhosphorylationHSYAVRTTPPEPPPF
CEEECCCCCCCCCCC		26.7026437602
590PhosphorylationDQPEPEVSGSESAPS
CCCCCCCCCCCCCCC		34.6326657352
592PhosphorylationPEPEVSGSESAPSSP
CCCCCCCCCCCCCCC		22.3729449344
594PhosphorylationPEVSGSESAPSSPAT
CCCCCCCCCCCCCCC		47.3726657352
597PhosphorylationSGSESAPSSPATAPL
CCCCCCCCCCCCCCC		48.9829449344
598PhosphorylationGSESAPSSPATAPLQ
CCCCCCCCCCCCCCC		19.9326657352
601PhosphorylationSAPSSPATAPLQAPT
CCCCCCCCCCCCCCC		31.9929449344
618PhosphorylationGPEPARETPAKLEPK
CCCCCCCCCCCCCCC		24.0026437602
639AcetylationEPRAKARKTEARGLT
CHHHHHHHHHHHCCC		56.4226051181
647AcetylationTEARGLTKAGAKKKA
HHHHCCCHHHHHHHH		50.2823749302
647UbiquitinationTEARGLTKAGAKKKA
HHHHCCCHHHHHHHH		50.28-
651AcetylationGLTKAGAKKKARKEA
CCCHHHHHHHHHHHH		54.6223749302
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
165SPhosphorylationKinasePRKCAP17252
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
165SPhosphorylation

20095964
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 JPH2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of JPH2_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613873Cardiomyopathy, familial hypertrophic 17 (CMH17)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of JPH2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"S165F mutation of junctophilin 2 affects Ca2+ signalling in skeletalmuscle.";
Woo J.S., Hwang J.H., Ko J.K., Weisleder N., Kim do H., Ma J.,Lee E.H.;
Biochem. J. 427:125-134(2010).
Cited for: PHOSPHORYLATION AT SER-165, INTERACTION WITH TRPC3, FUNCTION, ANDCHARACTERIZATION OF VARIANT PHE-165.
"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-484; SER-486 ANDTHR-490, 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 SER-469; SER-486 ANDTHR-490, AND MASS SPECTROMETRY.

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