PDZD8_HUMAN - dbPTM
PDZD8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDZD8_HUMAN
UniProt AC Q8NEN9
Protein Name PDZ domain-containing protein 8 {ECO:0000305}
Gene Name PDZD8 {ECO:0000312|HGNC:HGNC:26974}
Organism Homo sapiens (Human).
Sequence Length 1154
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein . Localizes at mitochondria-endoplasmic reticulum contact sites.
Protein Description Molecular tethering protein that connects endoplasmic reticulum and mitochondria membranes. [PubMed: 29097544 PDZD8-dependent endoplasmic reticulum-mitochondria membrane tethering is essential for endoplasmic reticulum-mitochondria Ca(2+) transfer]
Protein Sequence MGLLLMILASAVLGSFLTLLAQFFLLYRRQPEPPADEAARAGEGFRYIKPVPGLLLREYLYGGGRDEEPSGAAPEGGATPTAAPETPAPPTRETCYFLNATILFLFRELRDTALTRRWVTKKIKVEFEELLQTKTAGRLLEGLSLRDVFLGETVPFIKTIRLVRPVVPSATGEPDGPEGEALPAACPEELAFEAEVEYNGGFHLAIDVDLVFGKSAYLFVKLSRVVGRLRLVFTRVPFTHWFFSFVEDPLIDFEVRSQFEGRPMPQLTSIIVNQLKKIIKRKHTLPNYKIRFKPFFPYQTLQGFEEDEEHIHIQQWALTEGRLKVTLLECSRLLIFGSYDREANVHCTLELSSSVWEEKQRSSIKTVELIKGNLQSVGLTLRLVQSTDGYAGHVIIETVAPNSPAAIADLQRGDRLIAIGGVKITSTLQVLKLIKQAGDRVLVYYERPVGQSNQGAVLQDNFGQLEENFLSSSCQSGYEEEAAGLTVDTESRELDSEFEDLASDVRAQNEFKDEAQSLSHSPKRVPTTLSIKPLGAISPVLNRKLAVGSHPLPPKIQSKDGNKPPPLKTSEITDPAQVSKPTQGSAFKPPVPPRPQAKVPLPSADAPNQAEPDVLVEKPEKVVPPPLVDKSAEKQAKNVDAIDDAAAPKQFLAKQEVAKDVTSETSCPTKDSSDDRQTWESSEILYRNKLGKWTRTRASCLFDIEACHRYLNIALWCRDPFKLGGLICLGHVSLKLEDVALGCLATSNTEYLSKLRLEAPSPKAIVTRTALRNLSMQKGFNDKFCYGDITIHFKYLKEGESDHHVVTNVEKEKEPHLVEEVSVLPKEEQFVGQMGLTENKHSFQDTQFQNPTWCDYCKKKVWTKAASQCMFCAYVCHKKCQEKCLAETSVCGATDRRIDRTLKNLRLEGQETLLGLPPRVDAEASKSVNKTTGLTRHIINTSSRLLNLRQVSKTRLSEPGTDLVEPSPKHTPNTSDNEGSDTEVCGPNSPSKRGNSTGIKLVRKEGGLDDSVFIAVKEIGRDLYRGLPTEERIQKLEFMLDKLQNEIDQELEHNNSLVREEKETTDTRKKSLLSAALAKSGERLQALTLLMIHYRAGIEDIETLESLSLDQHSKKISKYTDDTEEDLDNEISQLIDSQPFSSISDDLFGPSESV
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
49UbiquitinationGEGFRYIKPVPGLLL
CCCCCCCCCCCCCHH		30.9123000965
61PhosphorylationLLLREYLYGGGRDEE
CHHHHHHHCCCCCCC		16.90-
79PhosphorylationAAPEGGATPTAAPET
CCCCCCCCCCCCCCC		25.1726657352
81PhosphorylationPEGGATPTAAPETPA
CCCCCCCCCCCCCCC		30.9726471730
134UbiquitinationFEELLQTKTAGRLLE
HHHHHCCCCHHHHCC		24.3429967540
158UbiquitinationGETVPFIKTIRLVRP
CCCCCHHEEEEEEEC		37.9721890473
282AcetylationLKKIIKRKHTLPNYK
HHHHHHCCCCCCCCE		35.6212430075
288PhosphorylationRKHTLPNYKIRFKPF
CCCCCCCCEEEEEEC		13.07-
289AcetylationKHTLPNYKIRFKPFF
CCCCCCCEEEEEECC		33.7612430085
376PhosphorylationLIKGNLQSVGLTLRL
EHHCCHHHHCEEEEE		22.7125599653
391UbiquitinationVQSTDGYAGHVIIET
EECCCCCCCEEEEEE		13.7223000965
394UbiquitinationTDGYAGHVIIETVAP
CCCCCCEEEEEEECC		4.6323000965
432UbiquitinationTSTLQVLKLIKQAGD
CCHHHHHHHHHHHCC		49.6723000965
435UbiquitinationLQVLKLIKQAGDRVL
HHHHHHHHHHCCEEE		44.5223000965
496PhosphorylationTESRELDSEFEDLAS
CCHHHHHHHHHHHHH		57.7322617229
503PhosphorylationSEFEDLASDVRAQNE
HHHHHHHHHHHHHHH		43.8923403867
517PhosphorylationEFKDEAQSLSHSPKR
HHHHHHHHHCCCCCC		38.6023927012
519PhosphorylationKDEAQSLSHSPKRVP
HHHHHHHCCCCCCCC		27.4530266825
521PhosphorylationEAQSLSHSPKRVPTT
HHHHHCCCCCCCCCE		28.8329255136
527PhosphorylationHSPKRVPTTLSIKPL
CCCCCCCCEEECCCC		37.2023403867
528PhosphorylationSPKRVPTTLSIKPLG
CCCCCCCEEECCCCC		16.6723403867
530PhosphorylationKRVPTTLSIKPLGAI
CCCCCEEECCCCCCC		26.8630206219
538PhosphorylationIKPLGAISPVLNRKL
CCCCCCCHHHHCCCC		14.3919664994
603PhosphorylationQAKVPLPSADAPNQA
CCCCCCCCCCCCCCC		46.60-
631PhosphorylationPPPLVDKSAEKQAKN
CCCCCCCCHHHHHCC		36.8828674419
663PhosphorylationEVAKDVTSETSCPTK
HHHCCCCCCCCCCCC		38.43-
669PhosphorylationTSETSCPTKDSSDDR
CCCCCCCCCCCCCCC		52.38-
670UbiquitinationSETSCPTKDSSDDRQ
CCCCCCCCCCCCCCH		40.5333845483
672PhosphorylationTSCPTKDSSDDRQTW
CCCCCCCCCCCCHHH		36.90-
673PhosphorylationSCPTKDSSDDRQTWE
CCCCCCCCCCCHHHH		54.38-
761PhosphorylationKLRLEAPSPKAIVTR
HHCCCCCCCCEEHHH		46.1925159151
763UbiquitinationRLEAPSPKAIVTRTA
CCCCCCCCEEHHHHH		55.9033845483
775PhosphorylationRTALRNLSMQKGFND
HHHHHHHHCCCCCCC		23.79-
795PhosphorylationDITIHFKYLKEGESD
CEEEEEEEECCCCCC		23.2818452278
842PhosphorylationGLTENKHSFQDTQFQ
CCCCCCCCCCCCCCC		26.64-
846PhosphorylationNKHSFQDTQFQNPTW
CCCCCCCCCCCCCCH		22.09-
852PhosphorylationDTQFQNPTWCDYCKK
CCCCCCCCHHHHCHH		46.40-
856PhosphorylationQNPTWCDYCKKKVWT
CCCCHHHHCHHHHHH		11.75-
941PhosphorylationLTRHIINTSSRLLNL
CHHHHHHHHHHHHCH		20.0523312004
942PhosphorylationTRHIINTSSRLLNLR
HHHHHHHHHHHHCHH		14.6923312004
943PhosphorylationRHIINTSSRLLNLRQ
HHHHHHHHHHHCHHH		25.5523312004
952PhosphorylationLLNLRQVSKTRLSEP
HHCHHHHHCCCCCCC		21.7027067055
957PhosphorylationQVSKTRLSEPGTDLV
HHHCCCCCCCCCCCC		38.1523927012
961PhosphorylationTRLSEPGTDLVEPSP
CCCCCCCCCCCCCCC		36.5523927012
967PhosphorylationGTDLVEPSPKHTPNT
CCCCCCCCCCCCCCC		32.8330266825
971PhosphorylationVEPSPKHTPNTSDNE
CCCCCCCCCCCCCCC		25.1022167270
974PhosphorylationSPKHTPNTSDNEGSD
CCCCCCCCCCCCCCC		38.3722167270
975PhosphorylationPKHTPNTSDNEGSDT
CCCCCCCCCCCCCCC		45.1126503892
980PhosphorylationNTSDNEGSDTEVCGP
CCCCCCCCCCCCCCC		34.8726503892
982PhosphorylationSDNEGSDTEVCGPNS
CCCCCCCCCCCCCCC		31.8222167270
989PhosphorylationTEVCGPNSPSKRGNS
CCCCCCCCCCCCCCC		33.4122167270
991PhosphorylationVCGPNSPSKRGNSTG
CCCCCCCCCCCCCCC		34.5023663014
1017UbiquitinationDSVFIAVKEIGRDLY
CCEEEEEHHHCHHHH		34.2932015554
1071PhosphorylationTTDTRKKSLLSAALA
CCCHHHHHHHHHHHH		37.2622985185
1106PhosphorylationEDIETLESLSLDQHS
CCHHHHHHCCCHHHH		26.7724173317
1108PhosphorylationIETLESLSLDQHSKK
HHHHHHCCCHHHHHH		38.9028270605
1113PhosphorylationSLSLDQHSKKISKYT
HCCCHHHHHHHHHCC		29.9728270605
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 PDZD8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDZD8_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 PDZD8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PDZD8_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 PDZD8_HUMAN

loading...

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-496, 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-496 AND SER-538, 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-538, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory