IGSF8_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IGSF8_MOUSE
• UniProt AC: Q8R366
• Protein Name: Immunoglobulin superfamily member 8
• Gene Name: Igsf8
• Organism: Mus musculus (Mouse).
• Sequence Length: 611
• Subcellular Localization: Cell membrane ; Single-pass membrane protein .
• Protein Description: May play a key role in diverse functions ascribed to CD81 and CD9 such as oocytes fertilization or hepatitis C virus function. May regulate proliferation and differentiation of keratinocytes. May be a negative regulator of cell motility: suppresses T-cell mobility coordinately with CD81, associates with CD82 to suppress prostate cancer cell migration, regulates epidermoid cell reaggregation and motility on laminin-5 with CD9 and CD81 as key linkers. May also play a role on integrin-dependent morphology and motility functions. May participate in the regulation of neurite outgrowth and maintenance of the neural network in the adult brain..
• Protein Sequence: MGVPSPTPLSSLLLLLLILGTRCYARQVHVPRGPLYRVAGTAVSISCNVSDYEGPAQQDFEWFMYRPEAPATSLGIVSTKDSQFSYAVFGPRVASGDLQVQRLKGDSVVLKIARLQAQDSGFYECYTPSTDTQYLGNYSAKVELRVLPDELQVSAAPPGPRGRQAATSPSRLTVHEGQELALGCLAQTKTKKHTHLSVSFGRAIPEAPVGRATLQEVVGLRSDMAVEAGAPYAERLASGELRLSKEGTDRYRMVVGGAQAGDSGTYHCTAAEWIQDPDGSWVQVAEKRAVLAHVDVQTLSSQLAVTVGPGERRIGPGEPLELLCNVSGALPPPGRHAAYSVGWEMAPAGAPGPGRLVAQLDTEGIGSLGPGYEDRHIAMEKVASRTYRLRLEAARPADAGTYRCLAKAYVRGSGTRLREAASARSRPLPVHVREEGVVLEAVAWLAGGTVYRGETASLLCNISVRGGPPGLRLAASWWVERPEEGELSSGPAQLVGGVGQDGVAELGVRPGGGPVSVELVGPRSHRLRLHGLGPEDEGIYHCAPSAWVQHADYSWYQAGSARSGPVTVYPYTHAVDTLFVPLLVGTGVALVTGASVLATITCCFMKRMRKR

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
5	Phosphorylation	---MGVPSPTPLSSL ---CCCCCCCHHHHH	38.71	17203969
7	Phosphorylation	-MGVPSPTPLSSLLL -CCCCCCCHHHHHHH	40.99	28576409
10	Phosphorylation	VPSPTPLSSLLLLLL CCCCCHHHHHHHHHH	21.83	17203969
21	Phosphorylation	LLLLILGTRCYARQV HHHHHHCCCCEEECC	17.70	28576409
48	N-linked_Glycosylation	TAVSISCNVSDYEGP EEEEEEEECCCCCCC	29.54	-
137	N-linked_Glycosylation	TDTQYLGNYSAKVEL CCCEECCCCEEEEEE	25.62	-
184	S-nitrosylation	GQELALGCLAQTKTK CCHHHHHHEEECCCC	2.71	24895380
325	N-linked_Glycosylation	EPLELLCNVSGALPP CCHHHHEECCCCCCC	30.84	-
516	Phosphorylation	RPGGGPVSVELVGPR CCCCCCEEEEEECCC	17.01	-
602	S-palmitoylation	SVLATITCCFMKRMR HHHHHHHHHHHHHHH	1.17	21609323
603	S-palmitoylation	VLATITCCFMKRMRK HHHHHHHHHHHHHHC	2.53	21609323

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

Oops, there are no upstream regulatory protein records of IGSF8_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IGSF8_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of IGSF8_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of IGSF8_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Palmitoylation

"Differential functions of phospholipid binding and palmitoylation oftumour suppressor EWI2/PGRL.";
He B., Zhang Y.H., Richardson M.M., Zhang J.S., Rubinstein E.,Zhang X.A.;
Biochem. J. 437:399-411(2011).
Cited for: PALMITOYLATION AT CYS-602 AND CYS-603, DOMAIN, AND SUBCELLULARLOCATION.
PubMed: 21609323

Phosphorylation

"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-10, AND MASSSPECTROMETRY.
PubMed: 17203969