dbPTM

TSN12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TSN12_HUMAN
UniProt AC	O95859
Protein Name	Tetraspanin-12
Gene Name	TSPAN12
Organism	Homo sapiens (Human).
Sequence Length	305
Subcellular Localization	Cell membrane Multi-pass membrane protein.
Protein Description	Regulator of cell surface receptor signal transduction. Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activate the norrin (NDP)-dependent activation of FZD4, while it does not activate the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1) (By similarity). Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP). Activates MMP14/MT1-MMP-dependent cleavage activity..
Protein Sequence	MAREDSVKCLRCLLYALNLLFWLMSISVLAVSAWMRDYLNNVLTLTAETRVEEAVILTYFPVVHPVMIAVCCFLIIVGMLGYCGTVKRNLLLLAWYFGSLLVIFCVELACGVWTYEQELMVPVQWSDMVTLKARMTNYGLPRYRWLTHAWNFFQREFKCCGVVYFTDWLEMTEMDWPPDSCCVREFPGCSKQAHQEDLSDLYQEGCGKKMYSFLRGTKQLQVLRFLGISIGVTQILAMILTITLLWALYYDRREPGTDQMMSLKNDNSQHLSCPSVELLKPSLSRIFEHTSMANSFNTHFEMEEL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	S-palmitoylation	AREDSVKCLRCLLYA CHHHHHHHHHHHHHH	2.44	19587294
12	S-palmitoylation	DSVKCLRCLLYALNL HHHHHHHHHHHHHHH	1.66	19587294
83	S-palmitoylation	IVGMLGYCGTVKRNL HHHHHCHHCHHHHHH	3.32	19587294
136	Phosphorylation	VTLKARMTNYGLPRY EEHHHHHHHCCCCHH	21.53	23403867
138	Phosphorylation	LKARMTNYGLPRYRW HHHHHHHCCCCHHHH	15.75	23403867
143	Phosphorylation	TNYGLPRYRWLTHAW HHCCCCHHHHHHHHH	12.28	-
208	Ubiquitination	LYQEGCGKKMYSFLR HHHCCCCHHHHHHHH	38.14	-
280	Ubiquitination	CPSVELLKPSLSRIF CCCHHHHCHHHHHHH	45.22	-

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 TSN12_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
9	C	Palmitoylation	19587294
The precise position of palmitoylated residues is unclear and occurs either on Cys-9, Cys-12 and/or Cys-83.
12	C	Palmitoylation	19587294
The precise position of palmitoylated residues is unclear and occurs either on Cys-9, Cys-12 and/or Cys-83.
83	C	Palmitoylation	19587294
The precise position of palmitoylated residues is unclear and occurs either on Cys-9, Cys-12 and/or Cys-83.

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 TSN12_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TSN12_HUMAN !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TSN12_HUMAN

Related Literatures of Post-Translational Modification