dbPTM

S26A2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	S26A2_HUMAN
UniProt AC	P50443
Protein Name	Sulfate transporter
Gene Name	SLC26A2
Organism	Homo sapiens (Human).
Sequence Length	739
Subcellular Localization	Cell membrane Multi-pass membrane protein .
Protein Description	Sulfate transporter. May play a role in endochondral bone formation..
Protein Sequence	MSSESKEQHNVSPRDSAEGNDSYPSGIHLELQRESSTDFKQFETNDQCRPYHRILIERQEKSDTNFKEFVIKKLQKNCQCSPAKAKNMILGFLPVLQWLPKYDLKKNILGDVMSGLIVGILLVPQSIAYSLLAGQEPVYGLYTSFFASIIYFLLGTSRHISVGIFGVLCLMIGETVDRELQKAGYDNAHSAPSLGMVSNGSTLLNHTSDRICDKSCYAIMVGSTVTFIAGVYQVAMGFFQVGFVSVYLSDALLSGFVTGASFTILTSQAKYLLGLNLPRTNGVGSLITTWIHVFRNIHKTNLCDLITSLLCLLVLLPTKELNEHFKSKLKAPIPIELVVVVAATLASHFGKLHENYNSSIAGHIPTGFMPPKVPEWNLIPSVAVDAIAISIIGFAITVSLSEMFAKKHGYTVKANQEMYAIGFCNIIPSFFHCFTTSAALAKTLVKESTGCHTQLSGVVTALVLLLVLLVIAPLFYSLQKSVLGVITIVNLRGALRKFRDLPKMWSISRMDTVIWFVTMLSSALLSTEIGLLVGVCFSIFCVILRTQKPKSSLLGLVEESEVFESVSAYKNLQIKPGIKIFRFVAPLYYINKECFKSALYKQTVNPILIKVAWKKAAKRKIKEKVVTLGGIQDEMSVQLSHDPLELHTIVIDCSAIQFLDTAGIHTLKEVRRDYEAIGIQVLLAQCNPTVRDSLTNGEYCKKEEENLLFYSVYEAMAFAEVSKNQKGVCVPNGLSLSSD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSESKEQH ------CCHHHHHHC	42.69	25002506
3	Phosphorylation	-----MSSESKEQHN -----CCHHHHHHCC	44.59	25002506
5	Phosphorylation	---MSSESKEQHNVS ---CCHHHHHHCCCC	43.36	25002506
6	Ubiquitination	--MSSESKEQHNVSP --CCHHHHHHCCCCC	58.29	33845483
12	Phosphorylation	SKEQHNVSPRDSAEG HHHHCCCCCCCCCCC	21.38	30266825
16	Phosphorylation	HNVSPRDSAEGNDSY CCCCCCCCCCCCCCC	29.51	27273156
22	Phosphorylation	DSAEGNDSYPSGIHL CCCCCCCCCCCCEEE	42.83	23927012
23	Phosphorylation	SAEGNDSYPSGIHLE CCCCCCCCCCCEEEE	12.32	23927012
25	Phosphorylation	EGNDSYPSGIHLELQ CCCCCCCCCEEEEEE	41.99	23927012
35	Phosphorylation	HLELQRESSTDFKQF EEEEEECCCCCHHHH	40.50	23401153
36	Phosphorylation	LELQRESSTDFKQFE EEEEECCCCCHHHHC	27.52	23401153
37	Phosphorylation	ELQRESSTDFKQFET EEEECCCCCHHHHCC	55.52	27273156
40	Ubiquitination	RESSTDFKQFETNDQ ECCCCCHHHHCCCCC	57.81	22817900
44	Phosphorylation	TDFKQFETNDQCRPY CCHHHHCCCCCCCCH	45.44	26699800
51	Phosphorylation	TNDQCRPYHRILIER CCCCCCCHHHEEEEC	5.60	22817900
67	Ubiquitination	EKSDTNFKEFVIKKL HHCCCCHHHHHHHHH	52.92	29967540
199	N-linked_Glycosylation	PSLGMVSNGSTLLNH CCCCCCCCCCHHCCC	36.70	UniProtKB CARBOHYD
205	N-linked_Glycosylation	SNGSTLLNHTSDRIC CCCCHHCCCCCCCCC	39.23	UniProtKB CARBOHYD
271	Phosphorylation	ILTSQAKYLLGLNLP EHHHHHHHHHCCCCC	15.35	-
357	N-linked_Glycosylation	GKLHENYNSSIAGHI HHHHHCCCCCCCCCC	40.64	UniProtKB CARBOHYD
358	Phosphorylation	KLHENYNSSIAGHIP HHHHCCCCCCCCCCC	16.86	-
359	Phosphorylation	LHENYNSSIAGHIPT HHHCCCCCCCCCCCC	16.90	-
506	Phosphorylation	RDLPKMWSISRMDTV HCCCCCCCCCCHHHH	13.74	29083192
508	Phosphorylation	LPKMWSISRMDTVIW CCCCCCCCCHHHHHH	18.94	29083192
588	Phosphorylation	FRFVAPLYYINKECF EEECCCHHHCCHHHH	10.97	-
589	Phosphorylation	RFVAPLYYINKECFK EECCCHHHCCHHHHH	13.00	-
596	Ubiquitination	YINKECFKSALYKQT HCCHHHHHHHHHHHC	46.61	29967540
600	Phosphorylation	ECFKSALYKQTVNPI HHHHHHHHHHCCCHH	10.77	-
601	Ubiquitination	CFKSALYKQTVNPIL HHHHHHHHHCCCHHH	40.10	33845483
603	Phosphorylation	KSALYKQTVNPILIK HHHHHHHCCCHHHHH	20.35	-
726	Ubiquitination	AEVSKNQKGVCVPNG HHHCCCCCCEECCCC	63.81	29967540
735	Phosphorylation	VCVPNGLSLSSD--- EECCCCCCCCCC---	27.83	25002506
737	Phosphorylation	VPNGLSLSSD----- CCCCCCCCCC-----	29.14	25002506
738	Phosphorylation	PNGLSLSSD------ CCCCCCCCC------	53.27	25002506

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 S26A2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of S26A2_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 S26A2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of S26A2_HUMAN !!

Drug and Disease Associations

Kegg Disease
H00476	Multiple epiphyseal dysplasia (MED)
H00515	The DTDST-related disorders, including: Achondrogenesis IB (ACG IB); Atelosteogenesis II (AO II); Di
OMIM Disease
222600	Diastrophic dysplasia (DTD)
600972	Achondrogenesis 1B (ACG1B)
256050	Atelosteogenesis 2 (AO2)
226900	Multiple epiphyseal dysplasia 4 (EDM4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of S26A2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-16, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASSSPECTROMETRY.	17081983 [Abstract]