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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
31 (in isoform 2) | Phosphorylation | - | 21.78 | 25072903 | |
32 (in isoform 2) | Phosphorylation | - | 3.65 | 25072903 | |
35 (in isoform 2) | Phosphorylation | - | 3.42 | 25072903 | |
36 (in isoform 2) | Phosphorylation | - | 46.96 | 25072903 | |
39 (in isoform 2) | Phosphorylation | - | 4.47 | 25072903 | |
41 (in isoform 2) | Phosphorylation | - | 13.17 | 25072903 | |
44 (in isoform 2) | Phosphorylation | - | 19.94 | 25072903 | |
94 | Phosphorylation | VSLGFFGSIFALFGM HHHHHHHHHHHHHCC | 14.91 | 22817900 | |
192 | Phosphorylation | DNNKTPRYTYNGATS CCCCCCCEEECCCCC | 18.12 | - | |
193 | Phosphorylation | NNKTPRYTYNGATSV CCCCCCEEECCCCCC | 16.28 | - | |
194 | Phosphorylation | NKTPRYTYNGATSVM CCCCCEEECCCCCCC | 11.58 | 22817900 | |
198 | Phosphorylation | RYTYNGATSVMSSRT CEEECCCCCCCCCCC | 24.21 | 28857561 | |
199 | Phosphorylation | YTYNGATSVMSSRTK EEECCCCCCCCCCCC | 18.45 | 28857561 | |
202 | Phosphorylation | NGATSVMSSRTKYHG CCCCCCCCCCCCCCC | 17.95 | 23401153 | |
203 | Phosphorylation | GATSVMSSRTKYHGG CCCCCCCCCCCCCCC | 26.35 | 22617229 | |
205 | Phosphorylation | TSVMSSRTKYHGGED CCCCCCCCCCCCCCC | 37.59 | - | |
207 | Phosphorylation | VMSSRTKYHGGEDFK CCCCCCCCCCCCCCC | 12.70 | - | |
219 | Phosphorylation | DFKTTNPSKQFDKNA CCCCCCCCCCCCCCC | 40.95 | 28857561 | |
227 | Phosphorylation | KQFDKNAYV------ CCCCCCCCC------ | 18.98 | - |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CLD10_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 CLD10_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ATE1_HUMAN | ATE1 | physical | 26186194 | |
FGF1_HUMAN | FGF1 | physical | 26186194 | |
FGF1_HUMAN | FGF1 | physical | 28514442 | |
ATE1_HUMAN | ATE1 | physical | 28514442 |
Kegg Disease | ||||||
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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 |
"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. |