SDCB1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SDCB1_MOUSE
• UniProt AC: O08992
• Protein Name: Syntenin-1
• Gene Name: Sdcbp
• Organism: Mus musculus (Mouse).
• Sequence Length: 299
• Subcellular Localization: Cell junction, focal adhesion . Cell junction, adherens junction . Cell membrane ; Peripheral membrane protein . Endoplasmic reticulum membrane ; Peripheral membrane protein . Nucleus . Melanosome . Cytoplasm, cytosol . Cytoplasm, cytoskeleton . Secreted,
• Protein Description: Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis. Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1. In concert with SDC1/4 and PDCD6IP, regulates exosome biogenesis (By similarity). Regulates migration, growth, proliferation, and cell cycle progression in a variety of cancer types. [PubMed: 26539120 In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway (By similarity]
• Protein Sequence: MSLYPSLEDLKVDKVIQAQTAYSANPASQAFVLVDASAALPPDGNLYPKLYPELSQYMGLSLNEAEICESMPMVSGAPAQGQLVARPSSVNYMVAPVTGNDAGIRRAEIKQGIREVILCKDQDGKIGLRLKSIDNGIFVQLVQANSPASLVGLRFGDQVLQINGENCAGWSSDKAHKVLKQAFGEKITMTIRDRPFERTVTMHKDSSGHVGFIFKSGKITSIVKDSSAARNGLLTDHHICEINGQNVIGLKDAQIADILSTAGTVVTITIMPTFIFEHIIKRMAPSIMKSLMDHTIPEV

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
2	Phosphorylation	------MSLYPSLED ------CCCCCCHHH	36.29	28066266
2	Acetylation	------MSLYPSLED ------CCCCCCHHH	36.29	-
4	Phosphorylation	----MSLYPSLEDLK ----CCCCCCHHHCC	5.40	27742792
6	Phosphorylation	--MSLYPSLEDLKVD --CCCCCCHHHCCCC	30.73	26824392
22	Phosphorylation	VIQAQTAYSANPASQ EEECCCCCCCCCHHC	16.23	-
47	Phosphorylation	LPPDGNLYPKLYPEL CCCCCCCCHHHHHHH	11.43	-
57	Phosphorylation	LYPELSQYMGLSLNE HHHHHHHHCCCCCCH	6.97	-
68	Glutathionylation	SLNEAEICESMPMVS CCCHHHHHHCCCCCC	2.08	24333276
88	Phosphorylation	GQLVARPSSVNYMVA CCEEECCCCCCEEEE	41.17	22817900
89	Phosphorylation	QLVARPSSVNYMVAP CEEECCCCCCEEEEC	19.64	22817900
92	Phosphorylation	ARPSSVNYMVAPVTG ECCCCCCEEEECCCC	7.27	22817900
119	S-nitrosocysteine	GIREVILCKDQDGKI CCCEEEEEECCCCCE	2.91	-
119	S-nitrosylation	GIREVILCKDQDGKI CCCEEEEEECCCCCE	2.91	20925432
132	Phosphorylation	KIGLRLKSIDNGIFV CEEEEEEEECCCEEE	39.50	29899451
177	Acetylation	WSSDKAHKVLKQAFG CCCHHHHHHHHHHHC	54.87	23864654
186	Ubiquitination	LKQAFGEKITMTIRD HHHHHCCCEEEEECC	43.80	22790023
206	Phosphorylation	TVTMHKDSSGHVGFI EEEEECCCCCCEEEE	42.92	22871156
207	Phosphorylation	VTMHKDSSGHVGFIF EEEECCCCCCEEEEE	42.95	22871156
216	Phosphorylation	HVGFIFKSGKITSIV CEEEEEECCEEEEEE	34.27	23684622
240	S-nitrosocysteine	LLTDHHICEINGQNV CCCCEEEEEECCEEE	3.59	-
240	S-nitrosylation	LLTDHHICEINGQNV CCCCEEEEEECCEEE	3.59	20925432

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

Oops, there are no upstream regulatory protein records of SDCB1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SDCB1_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 SDCB1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of SDCB1_MOUSE !!

Drug and Disease Associations

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