JAM2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: JAM2_HUMAN
• UniProt AC: P57087
• Protein Name: Junctional adhesion molecule B
• Gene Name: JAM2
• Organism: Homo sapiens (Human).
• Sequence Length: 298
• 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: May play a role in the processes of lymphocyte homing to secondary lymphoid organs..
• Protein Sequence: MARRSRHRLLLLLLRYLVVALGYHKAYGFSAPKDQQVVTAVEYQEAILACKTPKKTVSSRLEWKKLGRSVSFVYYQQTLQGDFKNRAEMIDFNIRIKNVTRSDAGKYRCEVSAPSEQGQNLEEDTVTLEVLVAPAVPSCEVPSSALSGTVVELRCQDKEGNPAPEYTWFKDGIRLLENPRLGSQSTNSSYTMNTKTGTLQFNTVSKLDTGEYSCEARNSVGYRRCPGKRMQVDDLNISGIIAAVVVVALVISVCGLGVCYAQRKGYFSKETSFQKSNSSSKATTMSENDFKHTKSFII

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
51	Acetylation	QEAILACKTPKKTVS HHHHHHCCCCCCCHH	63.35	7364695
55	Acetylation	LACKTPKKTVSSRLE HHCCCCCCCHHHHHC	56.19	22362433
98	N-linked_Glycosylation	DFNIRIKNVTRSDAG EEEEEEECCCHHHCC	37.71	16335952
187	N-linked_Glycosylation	RLGSQSTNSSYTMNT CCCCCCCCCCEEEEC	33.92	UniProtKB CARBOHYD
233	Ubiquitination	PGKRMQVDDLNISGI CCCCEECCCCCHHHH	37.48	32142685
236	N-linked_Glycosylation	RMQVDDLNISGIIAA CEECCCCCHHHHHHH	33.12	UniProtKB CARBOHYD
238	Phosphorylation	QVDDLNISGIIAAVV ECCCCCHHHHHHHHH	23.90	24043423
239	Ubiquitination	VDDLNISGIIAAVVV CCCCCHHHHHHHHHH	16.12	32142685
245	Ubiquitination	SGIIAAVVVVALVIS HHHHHHHHHHHHHHH	2.16	32142685
252	Phosphorylation	VVVALVISVCGLGVC HHHHHHHHHHCHHHH	12.13	24043423
260	Phosphorylation	VCGLGVCYAQRKGYF HHCHHHHHHHHCCCC	11.90	24043423
269	Ubiquitination	QRKGYFSKETSFQKS HHCCCCCCCCCCCCC	55.93	32142685
275	Ubiquitination	SKETSFQKSNSSSKA CCCCCCCCCCCCCCC	49.98	32142685
276	Phosphorylation	KETSFQKSNSSSKAT CCCCCCCCCCCCCCE	31.03	-
278	Phosphorylation	TSFQKSNSSSKATTM CCCCCCCCCCCCEEC	42.98	-
280	Phosphorylation	FQKSNSSSKATTMSE CCCCCCCCCCEECCH	26.57	12953056
281	Ubiquitination	QKSNSSSKATTMSEN CCCCCCCCCEECCHH	52.26	32142685
283	Phosphorylation	SNSSSKATTMSENDF CCCCCCCEECCHHHC	27.11	24173317
284	Phosphorylation	NSSSKATTMSENDFK CCCCCCEECCHHHCC	24.45	29514088
286	Phosphorylation	SSKATTMSENDFKHT CCCCEECCHHHCCCC	31.02	29514088
291	Ubiquitination	TMSENDFKHTKSFII ECCHHHCCCCCCCCC	53.91	-
295	Phosphorylation	NDFKHTKSFII---- HHCCCCCCCCC----	23.88	24719451

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

Oops, there are no upstream regulatory protein records of JAM2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of JAM2_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 JAM2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PARD3_HUMAN	PARD3	physical	12953056
JAM3_HUMAN	JAM3	physical	21982860
JAM2_HUMAN	JAM2	physical	21982860
TYDP2_HUMAN	TDP2	physical	21988832
NDK3_HUMAN	NME3	physical	21988832
YBOX1_HUMAN	YBX1	physical	21988832
SOX8_HUMAN	SOX8	physical	21988832

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

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98, AND MASS SPECTROMETRY.
PubMed: 16335952