TMED8_HUMAN - dbPTM
TMED8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TMED8_HUMAN
UniProt AC Q6PL24
Protein Name Protein TMED8
Gene Name TMED8
Organism Homo sapiens (Human).
Sequence Length 325
Subcellular Localization
Protein Description
Protein Sequence MSDLQAAEGPGSWSPTARPGSAGGVGDCQGVEGSQAAASENEDLENKDTSLLASATDPEPCSSPHRPQMVSPVSKDATEDLRKATGPLEAQALVKQDLLPADQAQVLNEMAKYQVPQRSGDIVMIQSEHTGAIDVLSADLESADLLGDHRKVSPPLMAPPCIWTFAKVKEFKSKLGKEKNSRLVVKRGEVVTIRVPTHPEGKRVCWEFATDDYDIGFGVYFDWTPVTSTDITVQVSDSSDDEDEEEEEEEEIEEPVPAGDVERGSRSSLRGRYGEVMPVYRRDSHRDVQAGSHDYPGEGIYLLKFDNSYSLLRNKTLYFHIYYTS
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
2Phosphorylation------MSDLQAAEG
------CCCCCCCCC
47.2128270605
12PhosphorylationQAAEGPGSWSPTARP
CCCCCCCCCCCCCCC
27.7526074081
14PhosphorylationAEGPGSWSPTARPGS
CCCCCCCCCCCCCCC
17.6725849741
16PhosphorylationGPGSWSPTARPGSAG
CCCCCCCCCCCCCCC
29.7726074081
21PhosphorylationSPTARPGSAGGVGDC
CCCCCCCCCCCCCCC
26.8223401153
27UbiquitinationGSAGGVGDCQGVEGS
CCCCCCCCCCCCCCC
21.1129967540
34PhosphorylationDCQGVEGSQAAASEN
CCCCCCCCHHCHHCC
11.7926074081
39PhosphorylationEGSQAAASENEDLEN
CCCHHCHHCCCCCCC
35.9130576142
44UbiquitinationAASENEDLENKDTSL
CHHCCCCCCCCCCCH
6.7829967540
49PhosphorylationEDLENKDTSLLASAT
CCCCCCCCCHHHCCC
23.9220873877
50PhosphorylationDLENKDTSLLASATD
CCCCCCCCHHHCCCC
31.3625159151
54PhosphorylationKDTSLLASATDPEPC
CCCCHHHCCCCCCCC
31.5030576142
56PhosphorylationTSLLASATDPEPCSS
CCHHHCCCCCCCCCC
49.9828450419
62PhosphorylationATDPEPCSSPHRPQM
CCCCCCCCCCCCCCC
58.5825159151
63PhosphorylationTDPEPCSSPHRPQMV
CCCCCCCCCCCCCCC
31.2925159151
71PhosphorylationPHRPQMVSPVSKDAT
CCCCCCCCCCCCCHH
17.7825159151
74PhosphorylationPQMVSPVSKDATEDL
CCCCCCCCCCHHHHH
28.3628450419
75AcetylationQMVSPVSKDATEDLR
CCCCCCCCCHHHHHH
52.1719821541
78PhosphorylationSPVSKDATEDLRKAT
CCCCCCHHHHHHHHH
39.9226074081
83UbiquitinationDATEDLRKATGPLEA
CHHHHHHHHHCCHHH
58.5629967540
85PhosphorylationTEDLRKATGPLEAQA
HHHHHHHHCCHHHHH
42.2227050516
95UbiquitinationLEAQALVKQDLLPAD
HHHHHHHHCCCCCHH
38.6629967540
110SulfoxidationQAQVLNEMAKYQVPQ
HHHHHHHHHCCCCCC
3.6621406390
112UbiquitinationQVLNEMAKYQVPQRS
HHHHHHHCCCCCCCC
34.6029967540
113PhosphorylationVLNEMAKYQVPQRSG
HHHHHHCCCCCCCCC
12.7627642862
151UbiquitinationDLLGDHRKVSPPLMA
HHHCCCCCCCCCCCC
43.5829967540
153PhosphorylationLGDHRKVSPPLMAPP
HCCCCCCCCCCCCCC
24.6828450419
156UbiquitinationHRKVSPPLMAPPCIW
CCCCCCCCCCCCCEE
5.3329967540
169AcetylationIWTFAKVKEFKSKLG
EEEHHHHHHHHHHHC
57.6419608861
172AcetylationFAKVKEFKSKLGKEK
HHHHHHHHHHHCCCC
48.0119608861
181PhosphorylationKLGKEKNSRLVVKRG
HHCCCCCCCEEEECC
37.75-
192PhosphorylationVKRGEVVTIRVPTHP
EECCCEEEEECCCCC
14.29-
197PhosphorylationVVTIRVPTHPEGKRV
EEEEECCCCCCCCEE
47.40-
236UbiquitinationTDITVQVSDSSDDED
CEEEEEECCCCCCCC
18.0621890473
241UbiquitinationQVSDSSDDEDEEEEE
EECCCCCCCCHHHHH
68.1621890473
265PhosphorylationAGDVERGSRSSLRGR
CCCCCCCCCHHHCCC
34.90-
267PhosphorylationDVERGSRSSLRGRYG
CCCCCCCHHHCCCCC
35.11-
268PhosphorylationVERGSRSSLRGRYGE
CCCCCCHHHCCCCCC
22.45-
284PhosphorylationMPVYRRDSHRDVQAG
EEEEECCCCCCCCCC
20.7121406692
292PhosphorylationHRDVQAGSHDYPGEG
CCCCCCCCCCCCCCE
19.0521406692
295PhosphorylationVQAGSHDYPGEGIYL
CCCCCCCCCCCEEEE
14.0221406692
301PhosphorylationDYPGEGIYLLKFDNS
CCCCCEEEEEEECCC
19.4821406692
304UbiquitinationGEGIYLLKFDNSYSL
CCEEEEEEECCCCHH
48.3421890473
309UbiquitinationLLKFDNSYSLLRNKT
EEEECCCCHHHCCCE
15.0221890473
309PhosphorylationLLKFDNSYSLLRNKT
EEEECCCCHHHCCCE
15.02-
406Ubiquitination----------------------------------------------------------------------------------------
----------------------------------------------------------------------------------------
21890473

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 TMED8_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TMED8_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 TMED8_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TMED8_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 TMED8_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-169, AND MASS SPECTROMETRY.

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