dbPTM

JAM1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	JAM1_MOUSE
UniProt AC	O88792
Protein Name	Junctional adhesion molecule A
Gene Name	F11r
Organism	Mus musculus (Mouse).
Sequence Length	300
Subcellular Localization	Cell junction, tight junction . Cell membrane Single-pass type I membrane protein . Localized at tight junctions of both epithelial and endothelial cells.
Protein Description	Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. [PubMed: 11447115 The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly]
Protein Sequence	MGTEGKAGRKLLFLFTSMILGSLVQGKGSVYTAQSDVQVPENESIKLTCTYSGFSSPRVEWKFVQGSTTALVCYNSQITAPYADRVTFSSSGITFSSVTRKDNGEYTCMVSEEGGQNYGEVSIHLTVLVPPSKPTISVPSSVTIGNRAVLTCSEHDGSPPSEYSWFKDGISMLTADAKKTRAFMNSSFTIDPKSGDLIFDPVTAFDSGEYYCQAQNGYGTAMRSEAAHMDAVELNVGGIVAAVLVTLILLGLLIFGVWFAYSRGYFERTKKGTAPGKKVIYSQPSTRSEGEFKQTSSFLV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
42	N-linked_Glycosylation	SDVQVPENESIKLTC CCCCCCCCCCEEEEE	42.09	19349973
49	Glutathionylation	NESIKLTCTYSGFSS CCCEEEEEEECCCCC	4.95	24333276
90	Phosphorylation	ADRVTFSSSGITFSS CCEEEEECCCEEEEE	28.52	28285833
96	Phosphorylation	SSSGITFSSVTRKDN ECCCEEEEEEEECCC	18.43	28285833
97	Phosphorylation	SSGITFSSVTRKDNG CCCEEEEEEEECCCC	24.26	28285833
152	Glutathionylation	GNRAVLTCSEHDGSP CCEEEEEEECCCCCC	3.82	24333276
171	Phosphorylation	SWFKDGISMLTADAK CHHHCCEEEEECCHH	17.17	-
174	Phosphorylation	KDGISMLTADAKKTR HCCEEEEECCHHHHH	17.53	-
185	N-linked_Glycosylation	KKTRAFMNSSFTIDP HHHHHHHHCCEEECC	28.22	19656770
277	Ubiquitination	KKGTAPGKKVIYSQP CCCCCCCCEEEEECC	42.69	27667366
278	Ubiquitination	KGTAPGKKVIYSQPS CCCCCCCEEEEECCC	39.52	22790023
281	Phosphorylation	APGKKVIYSQPSTRS CCCCEEEEECCCCCC	12.30	25177544
282	Phosphorylation	PGKKVIYSQPSTRSE CCCEEEEECCCCCCC	25.21	25521595
285	Phosphorylation	KVIYSQPSTRSEGEF EEEEECCCCCCCCCC	28.90	25521595
286	Phosphorylation	VIYSQPSTRSEGEFK EEEECCCCCCCCCCC	44.92	25521595
288	Phosphorylation	YSQPSTRSEGEFKQT EECCCCCCCCCCCCC	50.47	25521595
293	Ubiquitination	TRSEGEFKQTSSFLV CCCCCCCCCCCCCCC	48.65	-
295	Phosphorylation	SEGEFKQTSSFLV-- CCCCCCCCCCCCC--	27.25	25293948
296	Phosphorylation	EGEFKQTSSFLV--- CCCCCCCCCCCC---	19.32	17242355
297	Phosphorylation	GEFKQTSSFLV---- CCCCCCCCCCC----	26.45	26239621

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
285	S	Phosphorylation	Kinase	PRKCZ	Q05513	GPS
285	S	Phosphorylation	Kinase	PKCZ	Q02956	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of JAM1_MOUSE !!

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 JAM1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CSKP_HUMAN	CASK	physical	11120739

Drug and Disease Associations

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

Regulatory Network of JAM1_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-42 AND ASN-185, AND MASSSPECTROMETRY.	19349973 [Abstract]
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation."; Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.; Mol. Cell. Proteomics 8:2555-2569(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185, AND MASSSPECTROMETRY.	19656770 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-288, ANDMASS SPECTROMETRY.	17242355 [Abstract]