SMAGP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SMAGP_HUMAN
• UniProt AC: Q0VAQ4
• Protein Name: Small cell adhesion glycoprotein
• Gene Name: SMAGP
• Organism: Homo sapiens (Human).
• Sequence Length: 97
• Subcellular Localization: Cell membrane ; Single-pass type III membrane protein . Cytoplasmic vesicle membrane ; Single-pass type III membrane protein . Predominantly on lateral parts of the membrane, at cell-cell epithelial junctions (PubMed:15021913). Detected on cytoplasmi
• Protein Description: May play a role in epithelial cell-cell contacts. May play a role in tumor invasiveness and metastasis formation..
• Protein Sequence: MTSLLTTPSPREELMTTPILQPTEALSPEDGASTALIAVVITVVFLTLLSVVILIFFYLYKNKGSYVTYEPTEGEPSAIVQMESDLAKGSEKEEYFI

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	O-linked_Glycosylation	------MTSLLTTPS ------CCCCCCCCC	28.25	UniProtKB CARBOHYD
2	Phosphorylation	------MTSLLTTPS ------CCCCCCCCC	28.25	29759185
3	O-linked_Glycosylation	-----MTSLLTTPSP -----CCCCCCCCCC	21.78	UniProtKB CARBOHYD
3	Phosphorylation	-----MTSLLTTPSP -----CCCCCCCCCC	21.78	29759185
6	O-linked_Glycosylation	--MTSLLTTPSPREE --CCCCCCCCCCHHH	41.79	UniProtKB CARBOHYD
7	O-linked_Glycosylation	-MTSLLTTPSPREEL -CCCCCCCCCCHHHH	23.03	UniProtKB CARBOHYD
9	O-linked_Glycosylation	TSLLTTPSPREELMT CCCCCCCCCHHHHCC	34.20	UniProtKB CARBOHYD
16	O-linked_Glycosylation	SPREELMTTPILQPT CCHHHHCCCCCCCCC	41.88	UniProtKB CARBOHYD
17	O-linked_Glycosylation	PREELMTTPILQPTE CHHHHCCCCCCCCCC	8.38	UniProtKB CARBOHYD
23	O-linked_Glycosylation	TTPILQPTEALSPED CCCCCCCCCCCCCCC	22.41	UniProtKB CARBOHYD
65	Phosphorylation	YLYKNKGSYVTYEPT HHHHCCCCEEEEECC	20.31	20873877
66	Phosphorylation	LYKNKGSYVTYEPTE HHHCCCCEEEEECCC	12.89	20873877
68	Phosphorylation	KNKGSYVTYEPTEGE HCCCCEEEEECCCCC	17.59	20873877
69	Phosphorylation	NKGSYVTYEPTEGEP CCCCEEEEECCCCCC	15.18	20873877
72	Phosphorylation	SYVTYEPTEGEPSAI CEEEEECCCCCCCEE	44.69	26657352
77	Phosphorylation	EPTEGEPSAIVQMES ECCCCCCCEEEEECC	26.73	26657352
84	Phosphorylation	SAIVQMESDLAKGSE CEEEEECCHHHCCCC	32.36	20873877
88	Ubiquitination	QMESDLAKGSEKEEY EECCHHHCCCCCCCC	70.98	23000965
90	Phosphorylation	ESDLAKGSEKEEYFI CCHHHCCCCCCCCCC	44.80	29514088
92	Ubiquitination	DLAKGSEKEEYFI-- HHHCCCCCCCCCC--	58.50	23000965
95	Phosphorylation	KGSEKEEYFI----- CCCCCCCCCC-----	13.99	28796482

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SMAGP_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 SMAGP_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of SMAGP_HUMAN !!

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

"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-95, AND MASSSPECTROMETRY.
PubMed: 19534553