TMED4_HUMAN - dbPTM
TMED4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TMED4_HUMAN
UniProt AC Q7Z7H5
Protein Name Transmembrane emp24 domain-containing protein 4
Gene Name TMED4
Organism Homo sapiens (Human).
Sequence Length 227
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein.
Protein Description Involved in vesicular protein trafficking, mainly in the early secretory pathway. targeting. Involved in the maintenance of the Golgi apparatus. Appears to play a role in the biosynthesis of secreted cargo including processing. Involved in endoplasmic reticulum stress response. May play a role in the regulation of heat-shock response and apoptosis (By similarity)..
Protein Sequence MAGVGAGPLRAMGRQALLLLALCATGAQGLYFHIGETEKRCFIEEIPDETMVIGNYRTQMWDKQKEVFLPSTPGLGMHVEVKDPDGKVVLSRQYGSEGRFTFTSHTPGDHQICLHSNSTRMALFAGGKLRVHLDIQVGEHANNYPEIAAKDKLTELQLRARQLLDQVEQIQKEQDYQRYREERFRLTSESTNQRVLWWSIAQTVILILTGIWQMRHLKSFFEAKKLV
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
41GlutathionylationIGETEKRCFIEEIPD
CCCCCCEEEEEECCC
6.2822555962
63UbiquitinationYRTQMWDKQKEVFLP
CCCCCHHCCCCEECC
47.99-
65UbiquitinationTQMWDKQKEVFLPST
CCCHHCCCCEECCCC
62.68-
71PhosphorylationQKEVFLPSTPGLGMH
CCCEECCCCCCCCEE
49.7525278378
71O-linked_GlycosylationQKEVFLPSTPGLGMH
CCCEECCCCCCCCEE
49.75OGP
72PhosphorylationKEVFLPSTPGLGMHV
CCEECCCCCCCCEEE
21.3125278378
82UbiquitinationLGMHVEVKDPDGKVV
CCEEEEEECCCCCEE
50.46-
87UbiquitinationEVKDPDGKVVLSRQY
EEECCCCCEEEEEEE
36.23-
91PhosphorylationPDGKVVLSRQYGSEG
CCCCEEEEEEECCCC
13.0125278378
117N-linked_GlycosylationHQICLHSNSTRMALF
CEEEEECCCCEEEEE
36.3319159218
128UbiquitinationMALFAGGKLRVHLDI
EEEEECCEEEEEEEE
32.00-
128AcetylationMALFAGGKLRVHLDI
EEEEECCEEEEEEEE
32.0025953088
136 (in isoform 2)Ubiquitination-36.5121890473
150UbiquitinationNYPEIAAKDKLTELQ
CCHHHHHHCHHHHHH
46.50-
152 (in isoform 3)Ubiquitination-57.5121890473
152 (in isoform 1)Ubiquitination-57.5121890473
152UbiquitinationPEIAAKDKLTELQLR
HHHHHHCHHHHHHHH
57.5121890473
154PhosphorylationIAAKDKLTELQLRAR
HHHHCHHHHHHHHHH
40.1521406692
156 (in isoform 2)Ubiquitination-4.9721890473
172 (in isoform 3)Ubiquitination-60.0021890473
172 (in isoform 1)Ubiquitination-60.0021890473
172UbiquitinationDQVEQIQKEQDYQRY
HHHHHHHHHHHHHHH
60.0021906983
172AcetylationDQVEQIQKEQDYQRY
HHHHHHHHHHHHHHH
60.0026051181
199PhosphorylationNQRVLWWSIAQTVIL
CHHHHHHHHHHHHHH
9.1020068231
218UbiquitinationIWQMRHLKSFFEAKK
HHHHHHHHHHHHHHH
38.8121890473
218AcetylationIWQMRHLKSFFEAKK
HHHHHHHHHHHHHHH
38.8125825284
224UbiquitinationLKSFFEAKKLV----
HHHHHHHHHCC----
39.17-

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 TMED4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TMED4_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 TMED4_HUMAN !!

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

Oops, there are no PPI records of TMED4_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 TMED4_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-117, AND MASSSPECTROMETRY.

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