dbPTM

CLD4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CLD4_HUMAN
UniProt AC	O14493
Protein Name	Claudin-4
Gene Name	CLDN4
Organism	Homo sapiens (Human).
Sequence Length	209
Subcellular Localization	Cell junction, tight junction . Cell membrane Multi-pass membrane protein . CLDN4 is required for tight junction localization in the kidney.
Protein Description	Channel-forming tight junction protein that mediates paracellular chloride transport in the kidney. Plays a critical role in the paracellular reabsorption of filtered chloride in the kidney collecting ducts. Claudins play a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity..
Protein Sequence	MASMGLQVMGIALAVLGWLAVMLCCALPMWRVTAFIGSNIVTSQTIWEGLWMNCVVQSTGQMQCKVYDSLLALPQDLQAARALVIISIIVAALGVLLSVVGGKCTNCLEDESAKAKTMIVAGVVFLLAGLMVIVPVSWTAHNIIQDFYNPLVASGQKREMGASLYVGWAASGLLLLGGGLLCCNCPPRTDKPYSAKYSAARSAAASNYV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASMGLQVMG -----CCCHHHHHHH	16.46	24043423
189	Phosphorylation	CCNCPPRTDKPYSAK ECCCCCCCCCCCCHH	54.90	23312004
193	Phosphorylation	PPRTDKPYSAKYSAA CCCCCCCCCHHHHHH	27.31	22817900
194	Phosphorylation	PRTDKPYSAKYSAAR CCCCCCCCHHHHHHH	27.15	25849741
197	Phosphorylation	DKPYSAKYSAARSAA CCCCCHHHHHHHHHH	11.85	22817900
198	Phosphorylation	KPYSAKYSAARSAAA CCCCHHHHHHHHHHH	18.10	25849741
202	Phosphorylation	AKYSAARSAAASNYV HHHHHHHHHHHHCCC	19.96	25849741
206	Phosphorylation	AARSAAASNYV---- HHHHHHHHCCC----	24.78	24670416
208	Phosphorylation	RSAAASNYV------ HHHHHHCCC------	12.68	22322096

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
189	T	Phosphorylation	Kinase	PRKCE	Q02156	GPS
194	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
194	S	Phosphorylation	Kinase	PRKCE	Q02156	GPS
208	Y	Phosphorylation	Kinase	EPHA2	P29317	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CLD4_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 CLD4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
ZO1_HUMAN	TJP1	physical	10601346

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 CLD4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"EphA2 phosphorylates the cytoplasmic tail of Claudin-4 and mediatesparacellular permeability."; Tanaka M., Kamata R., Sakai R.; J. Biol. Chem. 280:42375-42382(2005). Cited for: INTERACTION WITH EPHA2 AND TJP1, MUTAGENESIS OF TYR-208, ANDPHOSPHORYLATION AT TYR-208 BY EPHA2.	16236711 [Abstract]