TMEDA_HUMAN - dbPTM
TMEDA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TMEDA_HUMAN
UniProt AC P49755
Protein Name Transmembrane emp24 domain-containing protein 10
Gene Name TMED10
Organism Homo sapiens (Human).
Sequence Length 219
Subcellular Localization Golgi apparatus, cis-Golgi network membrane
Single-pass type I membrane protein. Melanosome. Endoplasmic reticulum membrane
Single-pass type I membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane
Single-pass type I membrane p
Protein Description Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1 (By similarity). In COPI vesicle-mediated retrograde transport involved in the biogenesis of COPI vesicles and vesicle coat recruitment. On Golgi membranes, acts as primary receptor for ARF1-GDP which is involved in COPI-vesicle formation. Increases coatomer-dependent GTPase-activating activity of ARFGAP2. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2LR1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent of modulation of gamma-secretase activity). As part of the presenilin-dependent gamma-secretase complex regulates gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40 (Abeta40). Involved in organization of the Golgi apparatus..
Protein Sequence MSGLSGPPARRGPFPLALLLLFLLGPRLVLAISFHLPINSRKCLREEIHKDLLVTGAYEISDQSGGAGGLRSHLKITDSAGHILYSKEDATKGKFAFTTEDYDMFEVCFESKGTGRIPDQLVILDMKHGVEAKNYEEIAKVEKLKPLEVELRRLEDLSESIVNDFAYMKKREEEMRDTNESTNTRVLYFSIFSMFCLIGLATWQVFYLRRFFKAKKLIE
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
40PhosphorylationSFHLPINSRKCLREE
HCCCCCCCCHHHHHH
33.56-
42UbiquitinationHLPINSRKCLREEIH
CCCCCCCHHHHHHHH
37.12-
502-HydroxyisobutyrylationCLREEIHKDLLVTGA
HHHHHHHHHHEEECC
56.59-
50UbiquitinationCLREEIHKDLLVTGA
HHHHHHHHHHEEECC
56.59-
55O-linked_GlycosylationIHKDLLVTGAYEISD
HHHHHEEECCEEECC
18.9655830839
58PhosphorylationDLLVTGAYEISDQSG
HHEEECCEEECCCCC
18.36-
75UbiquitinationGGLRSHLKITDSAGH
CCHHHEEEEECCCCC
37.8321890473
752-HydroxyisobutyrylationGGLRSHLKITDSAGH
CCHHHEEEEECCCCC
37.83-
75UbiquitinationGGLRSHLKITDSAGH
CCHHHEEEEECCCCC
37.8321890473
77O-linked_GlycosylationLRSHLKITDSAGHIL
HHHEEEEECCCCCEE
23.4755825583
79PhosphorylationSHLKITDSAGHILYS
HEEEEECCCCCEEEE
27.7428152594
85PhosphorylationDSAGHILYSKEDATK
CCCCCEEEEHHHCCC
19.6628152594
86PhosphorylationSAGHILYSKEDATKG
CCCCEEEEHHHCCCC
26.5628152594
87UbiquitinationAGHILYSKEDATKGK
CCCEEEEHHHCCCCE
46.1621890473
87AcetylationAGHILYSKEDATKGK
CCCEEEEHHHCCCCE
46.1626822725
872-HydroxyisobutyrylationAGHILYSKEDATKGK
CCCEEEEHHHCCCCE
46.16-
87UbiquitinationAGHILYSKEDATKGK
CCCEEEEHHHCCCCE
46.1621890473
91PhosphorylationLYSKEDATKGKFAFT
EEEHHHCCCCEEEEE
53.2928152594
92UbiquitinationYSKEDATKGKFAFTT
EEHHHCCCCEEEEEC
62.92-
94UbiquitinationKEDATKGKFAFTTED
HHHCCCCEEEEECCC
34.77-
114O-linked_GlycosylationVCFESKGTGRIPDQL
HHHCCCCCCCCCCEE
27.33OGP
126SulfoxidationDQLVILDMKHGVEAK
CEEEEEECCCCCCCC
2.8628465586
1272-HydroxyisobutyrylationQLVILDMKHGVEAKN
EEEEEECCCCCCCCC
36.55-
127AcetylationQLVILDMKHGVEAKN
EEEEEECCCCCCCCC
36.5526051181
127UbiquitinationQLVILDMKHGVEAKN
EEEEEECCCCCCCCC
36.5521890473
133UbiquitinationMKHGVEAKNYEEIAK
CCCCCCCCCHHHHHH
46.70-
133SuccinylationMKHGVEAKNYEEIAK
CCCCCCCCCHHHHHH
46.7023954790
135PhosphorylationHGVEAKNYEEIAKVE
CCCCCCCHHHHHHHH
17.7728152594
140AcetylationKNYEEIAKVEKLKPL
CCHHHHHHHHHCCCH
57.5025825284
140UbiquitinationKNYEEIAKVEKLKPL
CCHHHHHHHHHCCCH
57.5021890473
143UbiquitinationEEIAKVEKLKPLEVE
HHHHHHHHCCCHHHH
65.87-
1432-HydroxyisobutyrylationEEIAKVEKLKPLEVE
HHHHHHHHCCCHHHH
65.87-
145UbiquitinationIAKVEKLKPLEVELR
HHHHHHCCCHHHHHH
59.6321890473
152MethylationKPLEVELRRLEDLSE
CCHHHHHHHHHHHHH
27.86115918609
167PhosphorylationSIVNDFAYMKKREEE
HHHHHHHHHHHHHHH
14.95-
168SulfoxidationIVNDFAYMKKREEEM
HHHHHHHHHHHHHHH
3.5628183972
169AcetylationVNDFAYMKKREEEMR
HHHHHHHHHHHHHHH
35.6826051181
169UbiquitinationVNDFAYMKKREEEMR
HHHHHHHHHHHHHHH
35.6821890473
170UbiquitinationNDFAYMKKREEEMRD
HHHHHHHHHHHHHHC
48.81-
171MethylationDFAYMKKREEEMRDT
HHHHHHHHHHHHHCC
51.55-
176MethylationKKREEEMRDTNESTN
HHHHHHHHCCCCCCC
51.38-
179N-linked_GlycosylationEEEMRDTNESTNTRV
HHHHHCCCCCCCHHH
45.57UniProtKB CARBOHYD
182PhosphorylationMRDTNESTNTRVLYF
HHCCCCCCCHHHHHH
34.1422210691
184PhosphorylationDTNESTNTRVLYFSI
CCCCCCCHHHHHHHH
23.42-

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 TMEDA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TMEDA_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 TMEDA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VAMP2_HUMANVAMP2physical
22939629
TMED1_HUMANTMED1physical
26186194
GOGB1_HUMANGOLGB1physical
26186194
TMED4_HUMANTMED4physical
26186194
TMED2_HUMANTMED2physical
26186194
TMED7_HUMANTMED7physical
26186194
TMED3_HUMANTMED3physical
26186194
TMED5_HUMANTMED5physical
26186194
EMC7_HUMANEMC7physical
26186194
TMED4_HUMANTMED4physical
26344197
TMED9_HUMANTMED9physical
26344197
COPG2_HUMANCOPG2physical
11056392
COPG1_HUMANCOPG1physical
11056392
TMED4_HUMANTMED4physical
28514442
GOGB1_HUMANGOLGB1physical
28514442
TMED1_HUMANTMED1physical
28514442
TMED3_HUMANTMED3physical
28514442
TMED7_HUMANTMED7physical
28514442

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 TMEDA_HUMAN

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Related Literatures of Post-Translational Modification

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