CLD12_HUMAN - dbPTM
CLD12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
111PhosphorylationCLIGMCNTAFRSSVP
HHHHHHHHHHHHCCC
23.42-
115PhosphorylationMCNTAFRSSVPNIKL
HHHHHHHHCCCCHHH
29.2726657352
116PhosphorylationCNTAFRSSVPNIKLA
HHHHHHHCCCCHHHH
37.0226657352
121UbiquitinationRSSVPNIKLAKCLVN
HHCCCCHHHHHHHHH
49.372190698
125S-palmitoylationPNIKLAKCLVNSAGC
CCHHHHHHHHHHHHH
4.2229575903
211PhosphorylationSPFWQPLYSHPPSMH
CCCCCCHHCCCCCCC
16.18-
216PhosphorylationPLYSHPPSMHTYSQP
CHHCCCCCCCCCCCC
27.87-
220PhosphorylationHPPSMHTYSQPYSAR
CCCCCCCCCCCCCHH
7.22-
228PhosphorylationSQPYSARSRLSAIEI
CCCCCHHHHCCEEEE
36.9730266825
231PhosphorylationYSARSRLSAIEIDIP
CCHHHHCCEEEEEEC
26.5323927012
241PhosphorylationEIDIPVVSHTT----
EEEECEEECCC----
18.4923927012
243PhosphorylationDIPVVSHTT------
EECEEECCC------
27.0523927012
244PhosphorylationIPVVSHTT-------
ECEEECCC-------
31.0523927012

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

Oops, there are no upstream regulatory protein records of CLD12_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLD12_HUMAN !!

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 CLD12_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ECHM_HUMANECHS1physical
21988832
SEC13_HUMANSEC13physical
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.
Regulatory Network of CLD12_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

TOP