UniProt ID | S39A3_HUMAN | |
---|---|---|
UniProt AC | Q9BRY0 | |
Protein Name | Zinc transporter ZIP3 | |
Gene Name | SLC39A3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 314 | |
Subcellular Localization |
Membrane Multi-pass membrane protein . |
|
Protein Description | Acts as a zinc-influx transporter.. | |
Protein Sequence | MVKLLVAKILCMVGVFFFMLLGSLLPVKIIETDFEKAHRSKKILSLCNTFGGGVFLATCFNALLPAVREKLQKVLSLGHISTDYPLAETILLLGFFMTVFLEQLILTFRKEKPSFIDLETFNAGSDVGSDSEYESPFMGGARGHALYVEPHGHGPSLSVQGLSRASPVRLLSLAFALSAHSVFEGLALGLQEEGEKVVSLFVGVAVHETLVAVALGISMARSAMPLRDAAKLAVTVSAMIPLGIGLGLGIESAQGVPGSVASVLLQGLAGGTFLFITFLEILAKELEEKSDRLLKVLFLVLGYTVLAGMVFLKW | |
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 |
---|---|---|---|---|---|
36 | Ubiquitination | IIETDFEKAHRSKKI EHHCCHHHHHHCHHH | 49.87 | 33845483 | |
98 (in isoform 2) | Phosphorylation | - | 11.71 | - | |
99 (in isoform 2) | Phosphorylation | - | 3.28 | - | |
112 | Ubiquitination | ILTFRKEKPSFIDLE HHHHHHCCCCCEECE | 49.34 | - | |
114 | Phosphorylation | TFRKEKPSFIDLETF HHHHCCCCCEECEEE | 45.99 | 27422710 | |
120 | Phosphorylation | PSFIDLETFNAGSDV CCCEECEEECCCCCC | 29.50 | 25693802 | |
125 | Phosphorylation | LETFNAGSDVGSDSE CEEECCCCCCCCCCC | 27.06 | 26503892 | |
129 | Phosphorylation | NAGSDVGSDSEYESP CCCCCCCCCCCCCCC | 37.50 | 26055452 | |
131 | Phosphorylation | GSDVGSDSEYESPFM CCCCCCCCCCCCCCC | 43.72 | 26503892 | |
133 | Phosphorylation | DVGSDSEYESPFMGG CCCCCCCCCCCCCCC | 26.17 | 25693802 | |
135 | Phosphorylation | GSDSEYESPFMGGAR CCCCCCCCCCCCCCC | 23.65 | 20873877 | |
147 | Phosphorylation | GARGHALYVEPHGHG CCCCEEEEEECCCCC | 11.98 | 25884760 | |
156 | Phosphorylation | EPHGHGPSLSVQGLS ECCCCCCCCCCCCCC | 37.56 | 26356563 | |
158 | Phosphorylation | HGHGPSLSVQGLSRA CCCCCCCCCCCCCCC | 19.41 | 26356563 | |
163 | Phosphorylation | SLSVQGLSRASPVRL CCCCCCCCCCCHHHH | 32.40 | 23401153 | |
164 | Methylation | LSVQGLSRASPVRLL CCCCCCCCCCHHHHH | 44.09 | 115917117 | |
166 | Phosphorylation | VQGLSRASPVRLLSL CCCCCCCCHHHHHHH | 23.87 | 24719451 | |
222 | Phosphorylation | LGISMARSAMPLRDA HHHHHHHHCCCHHHH | 21.27 | 18691976 |
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 S39A3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of S39A3_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 S39A3_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of S39A3_HUMAN !! |
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. |
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Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASSSPECTROMETRY. | |
"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-125 AND SER-129, ANDMASS SPECTROMETRY. | |
"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-125 AND SER-129, ANDMASS SPECTROMETRY. | |
"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-125 AND SER-129, ANDMASS SPECTROMETRY. |