TRDN_HUMAN - dbPTM
TRDN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRDN_HUMAN
UniProt AC Q13061
Protein Name Triadin
Gene Name TRDN
Organism Homo sapiens (Human).
Sequence Length 729
Subcellular Localization Cell membrane . Sarcoplasmic reticulum membrane
Single-pass type II membrane protein .
Protein Description Contributes to the regulation of lumenal Ca2+ release via the sarcoplasmic reticulum calcium release channels RYR1 and RYR2, a key step in triggering skeletal and heart muscle contraction. Required for normal organization of the triad junction, where T-tubules and the sarcoplasmic reticulum terminal cisternae are in close contact (By similarity). Required for normal skeletal muscle strength. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats..
Protein Sequence MTEITAEGNASTTTTVIDSKNGSVPKSPGKVLKRTVTEDIVTTFSSPAAWLLVIALIITWSAVAIVMFDLVDYKNFSASSIAKIGSDPLKLVRDAMEETTDWIYGFFSLLSDIISSEDEEDDDGDEDTDKGEIDEPPLRKKEIHKDKTEKQEKPERKIQTKVTHKEKEKGKEKVREKEKPEKKATHKEKIEKKEKPETKTLAKEQKKAKTAEKSEEKTKKEVKGGKQEKVKQTAAKVKEVQKTPSKPKEKEDKEKAAVSKHEQKDQYAFCRYMIDIFVHGDLKPGQSPAIPPPLPTEQASRPTPASPALEEKEGEKKKAEKKVTSETKKKEKEDIKKKSEKETAIDVEKKEPGKASETKQGTVKIAAQAAAKKDEKKEDSKKTKKPAEVEQPKGKKQEKKEKHVEPAKSPKKEHSVPSDKQVKAKTERAKEEIGAVSIKKAVPGKKEEKTTKTVEQEIRKEKSGKTSSILKDKEPIKGKEEKVPASLKEKEPETKKDEKMSKAGKEVKPKPPQLQGKKEEKPEPQIKKEAKPAISEKVQIHKQDIVKPEKTVSHGKPEEKVLKQVKAVTIEKTAKPKPTKKAEHREREPPSIKTDKPKPTPKGTSEVTESGKKKTEISEKESKEKADMKHLREEKVSTRKESLQLHNVTKAEKPARVSKDVEDVPASKKAKEGTEDVSPTKQKSPISFFQCVYLDGYNGYGFQFPFTPADRPGESSGQANSPGQKQQGQ
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
11PhosphorylationITAEGNASTTTTVID
EEECCCCCEEEEEEE		30.2230576142
15PhosphorylationGNASTTTTVIDSKNG
CCCCEEEEEEECCCC		17.2418187866
27PhosphorylationKNGSVPKSPGKVLKR
CCCCCCCCCCCEEEE		32.5818452278
75N-linked_GlycosylationFDLVDYKNFSASSIA
HHHCCCCCCCHHHHH		29.85UniProtKB CARBOHYD
77PhosphorylationLVDYKNFSASSIAKI
HCCCCCCCHHHHHHH		36.3119413330
86PhosphorylationSSIAKIGSDPLKLVR
HHHHHHCCCHHHHHH		39.2622673903
160PhosphorylationKPERKIQTKVTHKEK
CCCHHHCHHCCHHHH		30.8423312004
195AcetylationEKIEKKEKPETKTLA
HHHHHHCCHHHHHHH		57.977408777
199AcetylationKKEKPETKTLAKEQK
HHCCHHHHHHHHHHH		39.6219657435
220AcetylationKSEEKTKKEVKGGKQ
HHHHHHHHHHCCCHH		73.337692099
226AcetylationKKEVKGGKQEKVKQT
HHHHCCCHHHHHHHH		65.0420167786
229AcetylationVKGGKQEKVKQTAAK
HCCCHHHHHHHHHHH		52.8420167786
233PhosphorylationKQEKVKQTAAKVKEV
HHHHHHHHHHHHHHH		23.9028258704
303O-linked_GlycosylationTEQASRPTPASPALE
CHHCCCCCCCCHHHH		30.31OGP
325PhosphorylationKAEKKVTSETKKKEK
HHHHHCCHHHHHHHH		46.38-
339PhosphorylationKEDIKKKSEKETAID
HHHHHHHHHHHCCCC		63.8826437602
343PhosphorylationKKKSEKETAIDVEKK
HHHHHHHCCCCCCCC		39.7326437602
356PhosphorylationKKEPGKASETKQGTV
CCCCCCCCCCCCHHH		49.6529083192
358PhosphorylationEPGKASETKQGTVKI
CCCCCCCCCCHHHHH		26.6029083192
362PhosphorylationASETKQGTVKIAAQA
CCCCCCHHHHHHHHH		19.0129083192
409PhosphorylationKHVEPAKSPKKEHSV
HCCCCCCCCCCCCCC		44.0226437602
415PhosphorylationKSPKKEHSVPSDKQV
CCCCCCCCCCCHHHH		36.4926437602
418PhosphorylationKKEHSVPSDKQVKAK
CCCCCCCCHHHHHHH		56.1126437602
437PhosphorylationKEEIGAVSIKKAVPG
HHHHCCCEEEECCCC		28.3128258704
439UbiquitinationEIGAVSIKKAVPGKK
HHCCCEEEECCCCCC		27.46-
446UbiquitinationKKAVPGKKEEKTTKT
EECCCCCCCCCCCHH		76.62-
463PhosphorylationQEIRKEKSGKTSSIL
HHHHHHHCCCCCHHH		46.76-
466PhosphorylationRKEKSGKTSSILKDK
HHHHCCCCCHHHCCC		31.09-
468PhosphorylationEKSGKTSSILKDKEP
HHCCCCCHHHCCCCC		36.8524719451
477UbiquitinationLKDKEPIKGKEEKVP
HCCCCCCCCCCCCCC		74.72-
486PhosphorylationKEEKVPASLKEKEPE
CCCCCCCCCCCCCCC		33.63-
496UbiquitinationEKEPETKKDEKMSKA
CCCCCCHHHHHHHHC		77.77-
575AcetylationVTIEKTAKPKPTKKA
EEEECCCCCCCCCCH		59.82134035
581AcetylationAKPKPTKKAEHRERE
CCCCCCCCHHHCCCC		62.58134033
591PhosphorylationHREREPPSIKTDKPK
HCCCCCCCCCCCCCC		47.6422985185
605PhosphorylationKPTPKGTSEVTESGK
CCCCCCCCCCCCCCC		38.4426437602
610PhosphorylationGTSEVTESGKKKTEI
CCCCCCCCCCCCCCC		46.6926437602
615PhosphorylationTESGKKKTEISEKES
CCCCCCCCCCCHHHH		47.6428258704
625TrimethylationSEKESKEKADMKHLR
CHHHHHHHHHHHHHH		54.12-
625MethylationSEKESKEKADMKHLR
CHHHHHHHHHHHHHH		54.1223644510
642PhosphorylationKVSTRKESLQLHNVT
HHHHHHHHHHHHCCC		25.1726437602
647N-linked_GlycosylationKESLQLHNVTKAEKP
HHHHHHHCCCCCCCC		52.31UniProtKB CARBOHYD
667PhosphorylationDVEDVPASKKAKEGT
CHHHCCHHHHHCCCC		28.7226437602
674PhosphorylationSKKAKEGTEDVSPTK
HHHHCCCCCCCCCCC		30.06-
678PhosphorylationKEGTEDVSPTKQKSP
CCCCCCCCCCCCCCC		38.8917924679
680PhosphorylationGTEDVSPTKQKSPIS
CCCCCCCCCCCCCCC		38.3017924679
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 TRDN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRDN_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 TRDN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RYR1_HUMANRYR1physical
9890886
RYR1_HUMANRYR1physical
7721813
CASQ2_HUMANCASQ2physical
7721813
RYR1_HUMANRYR1physical
10212196
CASQ2_HUMANCASQ2physical
10748065
MRP5_HUMANABCC5physical
28514442
TM205_HUMANTMEM205physical
28514442
GOLI4_HUMANGOLIM4physical
28514442
JPH1_HUMANJPH1physical
28514442
ABCBA_HUMANABCB10physical
28514442
ZFPL1_HUMANZFPL1physical
28514442
TM223_HUMANTMEM223physical
28514442
TMM9B_HUMANTMEM9Bphysical
28514442
EMC3_HUMANEMC3physical
28514442
VTI1B_HUMANVTI1Bphysical
28514442
MANEA_HUMANMANEAphysical
28514442
EMC4_HUMANEMC4physical
28514442
GOSR2_HUMANGOSR2physical
28514442
EMC8_HUMANEMC8physical
28514442
EMC10_HUMANEMC10physical
28514442
EXOG_HUMANEXOGphysical
28514442
STX12_HUMANSTX12physical
28514442
PCYOX_HUMANPCYOX1physical
28514442
EMC7_HUMANEMC7physical
28514442
BET1_HUMANBET1physical
28514442
PDIA5_HUMANPDIA5physical
28514442
EMC2_HUMANEMC2physical
28514442
LMA2L_HUMANLMAN2Lphysical
28514442
NAT14_HUMANNAT14physical
28514442
GP1BB_HUMANGP1BBphysical
28514442
TM192_HUMANTMEM192physical
28514442
LRP10_HUMANLRP10physical
28514442
CGT_HUMANUGT8physical
28514442
STX8_HUMANSTX8physical
28514442
PXMP2_HUMANPXMP2physical
28514442
M17L2_HUMANMPV17L2physical
28514442
Drug and Disease Associations
Kegg Disease
OMIM Disease
615441Ventricular tachycardia, catecholaminergic polymorphic, 5, with or without muscle weakness (CPVT5)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRDN_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678 AND THR-680, ANDMASS 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-409, 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 THR-15, AND MASSSPECTROMETRY.

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