JAM1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: JAM1_HUMAN
• UniProt AC: Q9Y624
• Protein Name: Junctional adhesion molecule A
• Gene Name: F11R
• Organism: Homo sapiens (Human).
• Sequence Length: 299
• 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: 11489913 The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly (By similarity Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier (By similarity Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration]
• Protein Sequence: MGTKAQVERKLLCLFILAILLCSLALGSVTVHSSEPEVRIPENNPVKLSCAYSGFSSPRVEWKFDQGDTTRLVCYNNKITASYEDRVTFLPTGITFKSVTREDTGTYTCMVSEEGGNSYGEVKVKLIVLVPPSKPTVNIPSSATIGNRAVLTCSEQDGSPPSEYTWFKDGIVMPTNPKSTRAFSNSSYVLNPTTGELVFDPLSASDTGEYSCEARNGYGTPMTSNAVRMEAVERNVGVIVAAVLVTLILLGILVFGIWFAYSRGHFDRTKKGTSSKKVIYSQPSARSEGEFKQTSSFLV

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
34	Phosphorylation	GSVTVHSSEPEVRIP CCCEECCCCCCEECC	42.14	7646439
52	Phosphorylation	PVKLSCAYSGFSSPR CEEEEEECCCCCCCC	17.41	28152594
53	Phosphorylation	VKLSCAYSGFSSPRV EEEEEECCCCCCCCE	18.16	28152594
56	Phosphorylation	SCAYSGFSSPRVEWK EEECCCCCCCCEEEE	42.85	28152594
57	Phosphorylation	CAYSGFSSPRVEWKF EECCCCCCCCEEEEE	17.92	28152594
70	Phosphorylation	KFDQGDTTRLVCYNN EECCCCCEEEEEECC	27.09	7646439
86	Methylation	ITASYEDRVTFLPTG ECCCHHHCEEEECCC	19.89	115480717
88	Phosphorylation	ASYEDRVTFLPTGIT CCHHHCEEEECCCEE	21.98	20068231
92	Phosphorylation	DRVTFLPTGITFKSV HCEEEECCCEEEEEE	43.28	20068231
95	Phosphorylation	TFLPTGITFKSVTRE EEECCCEEEEEEECC	26.76	20068231
97	Ubiquitination	LPTGITFKSVTREDT ECCCEEEEEEECCCC	35.05	21890473
98	Phosphorylation	PTGITFKSVTREDTG CCCEEEEEEECCCCC	25.24	-
100	Phosphorylation	GITFKSVTREDTGTY CEEEEEEECCCCCEE	35.12	-
104	Phosphorylation	KSVTREDTGTYTCMV EEEECCCCCEEEEEE	27.03	20068231
107	Phosphorylation	TREDTGTYTCMVSEE ECCCCCEEEEEEECC	10.17	22817900
110	Sulfoxidation	DTGTYTCMVSEEGGN CCCEEEEEEECCCCC	2.61	28465586
133	Phosphorylation	LIVLVPPSKPTVNIP EEEEECCCCCCCCCC	45.24	20068231
136	Phosphorylation	LVPPSKPTVNIPSSA EECCCCCCCCCCCCC	29.89	20068231
141	Phosphorylation	KPTVNIPSSATIGNR CCCCCCCCCCEECCE	28.89	20068231
142	Phosphorylation	PTVNIPSSATIGNRA CCCCCCCCCEECCEE	24.87	20068231
144	Phosphorylation	VNIPSSATIGNRAVL CCCCCCCEECCEEEE	31.22	20068231
159	Phosphorylation	TCSEQDGSPPSEYTW EEECCCCCCCCCCEE	41.76	28348404
175	O-linked_Glycosylation	KDGIVMPTNPKSTRA ECCEECCCCCCCCCC	46.16	55824299
178	Ubiquitination	IVMPTNPKSTRAFSN EECCCCCCCCCCCCC	67.54	21890473
185	N-linked_Glycosylation	KSTRAFSNSSYVLNP CCCCCCCCCCEEECC	28.64	19159218
191	N-linked_Glycosylation	SNSSYVLNPTTGELV CCCCEEECCCCCCEE	23.10	19159218
224	Phosphorylation	GYGTPMTSNAVRMEA CCCCCCCCCCHHHHH	19.28	30576142
228	Ubiquitination	PMTSNAVRMEAVERN CCCCCCHHHHHHHHH	18.14	21890473
273	Phosphorylation	FDRTKKGTSSKKVIY CCCCCCCCCCCEEEE	38.41	18669648
274	Phosphorylation	DRTKKGTSSKKVIYS CCCCCCCCCCEEEEC	49.15	24719451
275	Phosphorylation	RTKKGTSSKKVIYSQ CCCCCCCCCEEEECC	36.01	18669648
277	Ubiquitination	KKGTSSKKVIYSQPS CCCCCCCEEEECCCC	35.49	21890473
280	Phosphorylation	TSSKKVIYSQPSARS CCCCEEEECCCCCCC	12.30	23927012
281	Phosphorylation	SSKKVIYSQPSARSE CCCEEEECCCCCCCC	25.21	21945579
284	Phosphorylation	KVIYSQPSARSEGEF EEEECCCCCCCCCCC	28.77	19664994
287	Phosphorylation	YSQPSARSEGEFKQT ECCCCCCCCCCCCCC	50.06	23927012
292	Ubiquitination	ARSEGEFKQTSSFLV CCCCCCCCCCCCCCC	48.65	21890473
294	Phosphorylation	SEGEFKQTSSFLV-- CCCCCCCCCCCCC--	27.25	28152594
295	Phosphorylation	EGEFKQTSSFLV--- CCCCCCCCCCCC---	19.32	23401153
296	Phosphorylation	GEFKQTSSFLV---- CCCCCCCCCCC----	26.45	23927012

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
284	S	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of JAM1_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 JAM1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZO1_HUMAN	TJP1	physical	10856295
PARD3_MOUSE	Pard3	physical	11447115
CSKP_HUMAN	CASK	physical	11120739
AFAD_HUMAN	MLLT4	physical	10856295
CSKP_HUMAN	CASK	physical	10856295
PEX19_HUMAN	PEX19	physical	21988832
SGTA_HUMAN	SGTA	physical	21516116

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

N-linked Glycosylation

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185 AND ASN-191, AND MASSSPECTROMETRY.
PubMed: 19159218

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; SER-287 ANDSER-296, AND MASS SPECTROMETRY.
PubMed: 19413330

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273; SER-275; TYR-280;SER-281; SER-284 AND SER-287, AND MASS SPECTROMETRY.
PubMed: 18669648

"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASSSPECTROMETRY.
PubMed: 18088087

"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-280, AND MASSSPECTROMETRY.
PubMed: 19534553

"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-280, AND MASSSPECTROMETRY.
PubMed: 18083107