CLD10_HUMAN - dbPTM
CLD10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CLD10_HUMAN
UniProt AC P78369
Protein Name Claudin-10
Gene Name CLDN10
Organism Homo sapiens (Human).
Sequence Length 228
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. Involved in the regulation of paracellular epithelia permeability to ions in multiple organs. It acts as a paracellular ion channel probably forming permselective pores; isoform 1 appears to create pores preferentially permeable to cations and isoform 2 for anions. In sweat glands and in the thick ascending limb (TAL) of Henle's loop in kidney, it controls paracellular sodium permeability which is essential for proper sweat production and renal function. [PubMed: 19383724]
Protein Sequence MASTASEIIAFMVSISGWVLVSSTLPTDYWKVSTIDGTVITTATYWANLWKACVTDSTGVSNCKDFPSMLALDGYIQACRGLMIAAVSLGFFGSIFALFGMKCTKVGGSDKAKAKIACLAGIVFILSGLCSMTGCSLYANKITTEFFDPLFVEQKYELGAALFIGWAGASLCIIGGVIFCFSISDNNKTPRYTYNGATSVMSSRTKYHGGEDFKTTNPSKQFDKNAYV
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
31 (in isoform 2)Phosphorylation-21.7825072903
32 (in isoform 2)Phosphorylation-3.6525072903
35 (in isoform 2)Phosphorylation-3.4225072903
36 (in isoform 2)Phosphorylation-46.9625072903
39 (in isoform 2)Phosphorylation-4.4725072903
41 (in isoform 2)Phosphorylation-13.1725072903
44 (in isoform 2)Phosphorylation-19.9425072903
94PhosphorylationVSLGFFGSIFALFGM
HHHHHHHHHHHHHCC
14.9122817900
192PhosphorylationDNNKTPRYTYNGATS
CCCCCCCEEECCCCC
18.12-
193PhosphorylationNNKTPRYTYNGATSV
CCCCCCEEECCCCCC
16.28-
194PhosphorylationNKTPRYTYNGATSVM
CCCCCEEECCCCCCC
11.5822817900
198PhosphorylationRYTYNGATSVMSSRT
CEEECCCCCCCCCCC
24.2128857561
199PhosphorylationYTYNGATSVMSSRTK
EEECCCCCCCCCCCC
18.4528857561
202PhosphorylationNGATSVMSSRTKYHG
CCCCCCCCCCCCCCC
17.9523401153
203PhosphorylationGATSVMSSRTKYHGG
CCCCCCCCCCCCCCC
26.3522617229
205PhosphorylationTSVMSSRTKYHGGED
CCCCCCCCCCCCCCC
37.59-
207PhosphorylationVMSSRTKYHGGEDFK
CCCCCCCCCCCCCCC
12.70-
219PhosphorylationDFKTTNPSKQFDKNA
CCCCCCCCCCCCCCC
40.9528857561
227PhosphorylationKQFDKNAYV------
CCCCCCCCC------
18.98-

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 CLD10_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CLD10_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 CLD10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATE1_HUMANATE1physical
26186194
FGF1_HUMANFGF1physical
26186194
FGF1_HUMANFGF1physical
28514442
ATE1_HUMANATE1physical
28514442

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 CLD10_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASSSPECTROMETRY.

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