TM2D3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TM2D3_HUMAN
• UniProt AC: Q9BRN9
• Protein Name: TM2 domain-containing protein 3
• Gene Name: TM2D3
• Organism: Homo sapiens (Human).
• Sequence Length: 247
• Subcellular Localization: Membrane ; Multi-pass membrane protein .
• Protein Sequence: MAGGVLPLRGLRALCRVLLFLSQFCILSGGEQSQALAQSIKDPGPTRTFTVVPRAAESTEIPPYVMKCPSNGLCSRLPADCIDCTTNFSCTYGKPVTFDCAVKPSVTCVDQDFKSQKNFIINMTCRFCWQLPETDYECTNSTSCMTVSCPRQRYPANCTVRDHVHCLGNRTFPKMLYCNWTGGYKWSTALALSITLGGFGADRFYLGQWREGLGKLFSFGGLGIWTLIDVLLIGVGYVGPADGSLYI

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
28	Phosphorylation	LSQFCILSGGEQSQA HHHHHHHCCCHHHHH	25.49	22817900
28 (in isoform 2)	Phosphorylation	-	25.49	17287340
46	O-linked_Glycosylation	SIKDPGPTRTFTVVP HCCCCCCCCEEEEEC	48.53	55825235
58	Phosphorylation	VVPRAAESTEIPPYV EECCCCCCCCCCCEE	26.98	17287340
59	O-linked_Glycosylation	VPRAAESTEIPPYVM ECCCCCCCCCCCEEE	29.46	OGP
64	Phosphorylation	ESTEIPPYVMKCPSN CCCCCCCEEEECCCC	14.07	-
94	Ubiquitination	NFSCTYGKPVTFDCA CEECCCCCCEEEECE	26.38	-
103	Ubiquitination	VTFDCAVKPSVTCVD EEEECEECCCEEEEC	17.04	-
114	Ubiquitination	TCVDQDFKSQKNFII EEECCCHHHCCCEEE	61.33	-
140	N-linked_Glycosylation	ETDYECTNSTSCMTV CCCCEECCCCCEEEE	55.75	UniProtKB CARBOHYD
148	Phosphorylation	STSCMTVSCPRQRYP CCCEEEEECCCCCCC	14.83	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TM2D3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TM2D3_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TM2D3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CQ080_HUMAN	C17orf80	physical	26186194
OAF_HUMAN	OAF	physical	26186194
CSTN1_HUMAN	CLSTN1	physical	26186194
SPCS2_HUMAN	SPCS2	physical	26186194
DX39A_HUMAN	DDX39A	physical	26186194
MTFP1_HUMAN	MTFP1	physical	26186194
COT2_HUMAN	NR2F2	physical	26186194
SPCS1_HUMAN	SPCS1	physical	26186194
SPCS2_HUMAN	SPCS2	physical	28514442
SPCS1_HUMAN	SPCS1	physical	28514442
DX39A_HUMAN	DDX39A	physical	28514442
OAF_HUMAN	OAF	physical	28514442
CQ080_HUMAN	C17orf80	physical	28514442
NPTX1_HUMAN	NPTX1	physical	28514442
FSTL1_HUMAN	FSTL1	physical	28514442
MTFP1_HUMAN	MTFP1	physical	28514442
COT2_HUMAN	NR2F2	physical	28514442
AAAT_HUMAN	SLC1A5	physical	28514442
TOIP2_HUMAN	TOR1AIP2	physical	28514442
IFG15_HUMAN	TOR1AIP2	physical	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-58, AND MASSSPECTROMETRY.
PubMed: 17287340