dbPTM

TMED9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TMED9_HUMAN
UniProt AC	Q9BVK6
Protein Name	Transmembrane emp24 domain-containing protein 9
Gene Name	TMED9
Organism	Homo sapiens (Human).
Sequence Length	235
Subcellular Localization	Endoplasmic reticulum membrane Single-pass type I membrane protein. Golgi apparatus, cis-Golgi network membrane Single-pass type I membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane Single-pass type I membrane protein. Golg
Protein Description	Appears to be involved in vesicular protein trafficking, mainly in the early secretory pathway. In COPI vesicle-mediated retrograde transport involved in the coatomer recruitment to membranes of the early secretory pathway. Increases coatomer-dependent activity of ARFGAP2. Thought to play a crucial role in the specific retention of p24 complexes in cis-Golgi membranes; specifically contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network. May be involved in organization of intracellular membranes, such as of the ER-Golgi intermediate compartment and the Golgi apparatus. Involved in ER localization of PTPN2 isoform PTPB..
Protein Sequence	MAVELGVLLVRPRPGTGLGRVMRTLLLVLWLATRGSALYFHIGETEKKCFIEEIPDETMVIGNYRTQLYDKQREEYQPATPGLGMFVEVKDPEDKVILARQYGSEGRFTFTSHTPGEHQICLHSNSTKFSLFAGGMLRVHLDIQVGEHANDYAEIAAKDKLSELQLRVRQLVEQVEQIQKEQNYQRWREERFRQTSESTNQRVLWWSILQTLILVAIGVWQMRHLKSFFEAKKLV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
49	Glutathionylation	IGETEKKCFIEEIPD CCCCCCEEEEEECCC	6.51	22555962
71	Ubiquitination	YRTQLYDKQREEYQP EECCCHHHCHHHHCC	37.38	-
71	2-Hydroxyisobutyrylation	YRTQLYDKQREEYQP EECCCHHHCHHHHCC	37.38	-
80	Phosphorylation	REEYQPATPGLGMFV HHHHCCCCCCCCEEE	25.27	25022875
90	Ubiquitination	LGMFVEVKDPEDKVI CCEEEEECCHHCCEE	54.80	21906983
95	2-Hydroxyisobutyrylation	EVKDPEDKVILARQY EECCHHCCEEEEEEC	29.52	-
95	Ubiquitination	EVKDPEDKVILARQY EECCHHCCEEEEEEC	29.52	-
125	N-linked_Glycosylation	HQICLHSNSTKFSLF CEEEEECCCCEEEEE	42.84	12754519
125	N-linked_Glycosylation	HQICLHSNSTKFSLF CEEEEECCCCEEEEE	42.84	12754519
136	Sulfoxidation	FSLFAGGMLRVHLDI EEEECCCEEEEEEEE	1.80	28465586
152	Phosphorylation	VGEHANDYAEIAAKD CCCCCCCHHHHHHHH	13.12	-
158	Ubiquitination	DYAEIAAKDKLSELQ CHHHHHHHHHHHHHH	46.50	-
160	Acetylation	AEIAAKDKLSELQLR HHHHHHHHHHHHHHH	53.88	26051181
160	Ubiquitination	AEIAAKDKLSELQLR HHHHHHHHHHHHHHH	53.88	21906983
162	Phosphorylation	IAAKDKLSELQLRVR HHHHHHHHHHHHHHH	41.84	-
180	Acetylation	EQVEQIQKEQNYQRW HHHHHHHHHHHHHHH	64.00	26051181
180	Ubiquitination	EQVEQIQKEQNYQRW HHHHHHHHHHHHHHH	64.00	21906983
198	Phosphorylation	RFRQTSESTNQRVLW HHHHCCHHHHHHHHH	32.21	-
226	Ubiquitination	VWQMRHLKSFFEAKK HHHHHHHHHHHHHHH	38.81	21906983
226	2-Hydroxyisobutyrylation	VWQMRHLKSFFEAKK HHHHHHHHHHHHHHH	38.81	-
226	Acetylation	VWQMRHLKSFFEAKK HHHHHHHHHHHHHHH	38.81	24575541
232	Ubiquitination	LKSFFEAKKLV---- HHHHHHHHHCC----	39.17	-
232	2-Hydroxyisobutyrylation	LKSFFEAKKLV---- 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 TMED9_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TMED9_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 TMED9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TMEDA_HUMAN	TMED10	physical	22939629
MA2A1_HUMAN	MAN2A1	physical	9472029
STX5_HUMAN	STX5	physical	9472029
TMED1_HUMAN	TMED1	physical	9472029
TMED2_HUMAN	TMED2	physical	9472029
TMEDA_HUMAN	TMED10	physical	9472029
GALT_HUMAN	GALT	physical	9472029
P53_HUMAN	TP53	physical	9472029

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 TMED9_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-125, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-125.	12754519 [Abstract]