JAM1_MOUSE - dbPTM
JAM1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
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 Orthologous
Protein Cluster
42N-linked_GlycosylationSDVQVPENESIKLTC
CCCCCCCCCCEEEEE
42.0919349973
49GlutathionylationNESIKLTCTYSGFSS
CCCEEEEEEECCCCC
4.9524333276
90PhosphorylationADRVTFSSSGITFSS
CCEEEEECCCEEEEE
28.5228285833
96PhosphorylationSSSGITFSSVTRKDN
ECCCEEEEEEEECCC
18.4328285833
97PhosphorylationSSGITFSSVTRKDNG
CCCEEEEEEEECCCC
24.2628285833
152GlutathionylationGNRAVLTCSEHDGSP
CCEEEEEEECCCCCC
3.8224333276
171PhosphorylationSWFKDGISMLTADAK
CHHHCCEEEEECCHH
17.17-
174PhosphorylationKDGISMLTADAKKTR
HCCEEEEECCHHHHH
17.53-
185N-linked_GlycosylationKKTRAFMNSSFTIDP
HHHHHHHHCCEEECC
28.2219656770
277UbiquitinationKKGTAPGKKVIYSQP
CCCCCCCCEEEEECC
42.6927667366
278UbiquitinationKGTAPGKKVIYSQPS
CCCCCCCEEEEECCC
39.5222790023
281PhosphorylationAPGKKVIYSQPSTRS
CCCCEEEEECCCCCC
12.3025177544
282PhosphorylationPGKKVIYSQPSTRSE
CCCEEEEECCCCCCC
25.2125521595
285PhosphorylationKVIYSQPSTRSEGEF
EEEEECCCCCCCCCC
28.9025521595
286PhosphorylationVIYSQPSTRSEGEFK
EEEECCCCCCCCCCC
44.9225521595
288PhosphorylationYSQPSTRSEGEFKQT
EECCCCCCCCCCCCC
50.4725521595
293UbiquitinationTRSEGEFKQTSSFLV
CCCCCCCCCCCCCCC
48.65-
295PhosphorylationSEGEFKQTSSFLV--
CCCCCCCCCCCCC--
27.2525293948
296PhosphorylationEGEFKQTSSFLV---
CCCCCCCCCCCC---
19.3217242355
297PhosphorylationGEFKQTSSFLV----
CCCCCCCCCCC----
26.4526239621

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
285SPhosphorylationKinasePRKCZQ05513
GPS
285SPhosphorylationKinasePKCZQ02956
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_HUMANCASKphysical
11120739

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of JAM1_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.
"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.
Phosphorylation
ReferencePubMed
"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.

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