UniProt ID | CLD12_HUMAN | |
---|---|---|
UniProt AC | P56749 | |
Protein Name | Claudin-12 | |
Gene Name | CLDN12 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 244 | |
Subcellular Localization |
Cell junction, tight junction. Cell membrane Multi-pass membrane protein . |
|
Protein Description | Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.. | |
Protein Sequence | MGCRDVHAATVLSFLCGIASVAGLFAGTLLPNWRKLRLITFNRNEKNLTVYTGLWVKCARYDGSSDCLMYDTTWYSSVDQLDLRVLQFALPLSMLIAMGALLLCLIGMCNTAFRSSVPNIKLAKCLVNSAGCHLVAGLLFFLAGTVSLSPSIWVIFYNIHLNKKFEPVFSFDYAVYVTIASAGGLFMTSLILFIWYCTCKSLPSPFWQPLYSHPPSMHTYSQPYSARSRLSAIEIDIPVVSHTT | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
111 | Phosphorylation | CLIGMCNTAFRSSVP HHHHHHHHHHHHCCC | 23.42 | - | |
115 | Phosphorylation | MCNTAFRSSVPNIKL HHHHHHHHCCCCHHH | 29.27 | 26657352 | |
116 | Phosphorylation | CNTAFRSSVPNIKLA HHHHHHHCCCCHHHH | 37.02 | 26657352 | |
121 | Ubiquitination | RSSVPNIKLAKCLVN HHCCCCHHHHHHHHH | 49.37 | 2190698 | |
125 | S-palmitoylation | PNIKLAKCLVNSAGC CCHHHHHHHHHHHHH | 4.22 | 29575903 | |
211 | Phosphorylation | SPFWQPLYSHPPSMH CCCCCCHHCCCCCCC | 16.18 | - | |
216 | Phosphorylation | PLYSHPPSMHTYSQP CHHCCCCCCCCCCCC | 27.87 | - | |
220 | Phosphorylation | HPPSMHTYSQPYSAR CCCCCCCCCCCCCHH | 7.22 | - | |
228 | Phosphorylation | SQPYSARSRLSAIEI CCCCCHHHHCCEEEE | 36.97 | 30266825 | |
231 | Phosphorylation | YSARSRLSAIEIDIP CCHHHHCCEEEEEEC | 26.53 | 23927012 | |
241 | Phosphorylation | EIDIPVVSHTT---- EEEECEEECCC---- | 18.49 | 23927012 | |
243 | Phosphorylation | DIPVVSHTT------ EECEEECCC------ | 27.05 | 23927012 | |
244 | Phosphorylation | IPVVSHTT------- ECEEECCC------- | 31.05 | 23927012 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of CLD12_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CLD12_HUMAN !! |
* 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 CLD12_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ECHM_HUMAN | ECHS1 | physical | 21988832 | |
SEC13_HUMAN | SEC13 | physical | 21988832 |
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. |
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Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASSSPECTROMETRY. |