S39A7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: S39A7_HUMAN
• UniProt AC: Q92504
• Protein Name: Zinc transporter SLC39A7
• Gene Name: SLC39A7
• Organism: Homo sapiens (Human).
• Sequence Length: 469
• Subcellular Localization: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus, cis-Golgi network membrane.
• Protein Description: Zinc transporter, that transports Zn(2+) from the endoplasmic reticulum/Golgi apparatus to the cytosol. Transport is stimulated by growth factors, such as EGF, and Ca(2+), as well as by exogenous Zn(2+)..
• Protein Sequence: MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE

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
133	Phosphorylation	KQDLDAVTLWAYALG CCCHHHHHHHHHHHH	20.50	24043423
137	Phosphorylation	DAVTLWAYALGATVL HHHHHHHHHHHHHHH	7.26	24043423
142	Phosphorylation	WAYALGATVLISAAP HHHHHHHHHHHHHCC	17.66	24043423
146	Phosphorylation	LGATVLISAAPFFVL HHHHHHHHHCCEEEE	17.76	24043423
160	Phosphorylation	LFLIPVESNSPRHRS EEEEECCCCCHHHHH	42.73	24043423
162	Phosphorylation	LIPVESNSPRHRSLL EEECCCCCHHHHHHH	32.37	24043423
260	Phosphorylation	AHSHTRGSHGHGRQE CCCCCCCCCCCCHHC	24.01	26329039
275	Phosphorylation	RSTKEKQSSEEEEKE CCCCCCCCCHHHHHH	51.27	29255136
276	Phosphorylation	STKEKQSSEEEEKET CCCCCCCCHHHHHHH	46.67	29255136
283	Phosphorylation	SEEEEKETRGVQKRR CHHHHHHHHCCHHHC	43.73	29255136
293	Phosphorylation	VQKRRGGSTVPKDGP CHHHCCCCCCCCCCC	29.11	20068231
294	Phosphorylation	QKRRGGSTVPKDGPV HHHCCCCCCCCCCCC	44.07	20068231
297	Ubiquitination	RGGSTVPKDGPVRPQ CCCCCCCCCCCCCCC	71.61	-
310	Acetylation	PQNAEEEKRGLDLRV CCCHHHHHCCCCCHH	55.86	26051181
310	Ubiquitination	PQNAEEEKRGLDLRV CCCHHHHHCCCCCHH	55.86	21906983

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
275	S	Phosphorylation	Kinase	CK2	-	Uniprot
276	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of S39A7_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of S39A7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TYY1_HUMAN	YY1	physical	21988832

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND SER-276, ANDMASS SPECTROMETRY.
PubMed: 19369195

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND SER-276, ANDMASS SPECTROMETRY.
PubMed: 18691976

"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, AND MASSSPECTROMETRY.
PubMed: 18088087

"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND SER-276, ANDMASS SPECTROMETRY.
PubMed: 16083285