dbPTM

SL9A4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SL9A4_HUMAN
UniProt AC	Q6AI14
Protein Name	Sodium/hydrogen exchanger 4
Gene Name	SLC9A4
Organism	Homo sapiens (Human).
Sequence Length	798
Subcellular Localization	Apical cell membrane Multi-pass membrane protein. Basolateral cell membrane Multi-pass membrane protein. Cytoplasmic granule membrane Multi-pass membrane protein. Found in zymogen granule membranes..
Protein Description	Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient. Plays an important role in signal transduction. May play a specialized role in the kidney in rectifying cell volume in response to extreme fluctuations of hyperosmolar-stimulated cell shrinkage. Is relatively amiloride and ethylisopropylamiloride (EIPA) insensitive. Can be activated under conditions of hyperosmolar-induced cell shrinkage in a sustained intracellular acidification-dependence manner. Activated by 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS) in a sustained intracellular acidification-dependence manner. Affects potassium/proton exchange as well as sodium/proton and lithium/proton exchange. In basolateral cell membrane, participates in homeostatic control of intracellular pH, and may play a role in proton extrusion in order to achieve transepithelial HCO3(-) secretion. In apical cell membrane may be involved in mediating sodium absorption. Requires for normal levels of gastric acid secretion, secretory membrane development, parietal cell maturation and/or differentiation and at least secondarily for chief cell differentiation (By similarity)..
Protein Sequence	MALQMFVTYSPWNCLLLLVALECSEASSDLNESANSTAQYASNAWFAAASSEPEEGISVFELDYDYVQIPYEVTLWILLASLAKIGFHLYHRLPGLMPESCLLILVGALVGGIIFGTDHKSPPVMDSSIYFLYLLPPIVLEGGYFMPTRPFFENIGSILWWAVLGALINALGIGLSLYLICQVKAFGLGDVNLLQNLLFGSLISAVDPVAVLAVFEEARVNEQLYMMIFGEALLNDGITVVLYNMLIAFTKMHKFEDIETVDILAGCARFIVVGLGGVLFGIVFGFISAFITRFTQNISAIEPLIVFMFSYLSYLAAETLYLSGILAITACAVTMKKYVEENVSQTSYTTIKYFMKMLSSVSETLIFIFMGVSTVGKNHEWNWAFICFTLAFCQIWRAISVFALFYISNQFRTFPFSIKDQCIIFYSGVRGAGSFSLAFLLPLSLFPRKKMFVTATLVVIYFTVFIQGITVGPLVRYLDVKKTNKKESINEELHIRLMDHLKAGIEDVCGHWSHYQVRDKFKKFDHRYLRKILIRKNLPKSSIVSLYKKLEMKQAIEMVETGILSSTAFSIPHQAQRIQGIKRLSPEDVESIRDILTSNMYQVRQRTLSYNKYNLKPQTSEKQAKEILIRRQNTLRESMRKGHSLPWGKPAGTKNIRYLSYPYGNPQSAGRDTRAAGFSDDDSSDPGSPSITFSACSRIGSLQKQEAQEIIPMKSLHRGRKAFSFGYQRNTSQEEYLGGVRRVALRPKPLFHAVDEEGESGGESEGKASLVEVRSRWTADHGHGRDHHRSHSPLLQKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
342	N-linked_Glycosylation	MKKYVEENVSQTSYT HHHHHHHCCCCCCHH	25.82	UniProtKB CARBOHYD
352	Ubiquitination	QTSYTTIKYFMKMLS CCCHHHHHHHHHHHH	30.28	22817900
356	Ubiquitination	TTIKYFMKMLSSVSE HHHHHHHHHHHCCCH	27.13	22817900
463	Phosphorylation	TLVVIYFTVFIQGIT HHHHHHHHHHHCCCC	9.49	-
541	Phosphorylation	IRKNLPKSSIVSLYK HHCCCCHHHHHHHHH	24.29	23312004
542	Phosphorylation	RKNLPKSSIVSLYKK HCCCCHHHHHHHHHH	32.89	23312004
613	Phosphorylation	RTLSYNKYNLKPQTS HHHHCCCCCCCCCCC	23.30	21712546
619	Phosphorylation	KYNLKPQTSEKQAKE CCCCCCCCCHHHHHH	47.59	21712546
634	Phosphorylation	ILIRRQNTLRESMRK HHHHHHHHHHHHHHC	20.89	-
638	Phosphorylation	RQNTLRESMRKGHSL HHHHHHHHHHCCCCC	19.90	22468782
644	Phosphorylation	ESMRKGHSLPWGKPA HHHHCCCCCCCCCCC	44.81	-
660	Phosphorylation	TKNIRYLSYPYGNPQ CCEEEEEECCCCCCC	18.35	28857561
673	Phosphorylation	PQSAGRDTRAAGFSD CCCCCCCCCCCCCCC	22.35	-
688	Phosphorylation	DDSSDPGSPSITFSA CCCCCCCCCCEEHHH	22.36	22210691
701	Phosphorylation	SACSRIGSLQKQEAQ HHHHHCCCCCHHHHH	25.84	22210691
724	Phosphorylation	HRGRKAFSFGYQRNT CCCCCHHHCCCCCCC	23.71	-
732	Phosphorylation	FGYQRNTSQEEYLGG CCCCCCCCHHHHCCC	38.86	26657352
792	Phosphorylation	RDHHRSHSPLLQKK- CCCCCCCCHHHCCC-	20.63	26657352

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 SL9A4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SL9A4_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 SL9A4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SL9A4_HUMAN !!

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 SL9A4_HUMAN

Related Literatures of Post-Translational Modification

Ubiquitylation
Reference	PubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-352, AND MASSSPECTROMETRY.	17370265 [Abstract]