UniProt ID | S22AG_HUMAN | |
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UniProt AC | Q86VW1 | |
Protein Name | Solute carrier family 22 member 16 | |
Gene Name | SLC22A16 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 577 | |
Subcellular Localization |
Membrane Multi-pass membrane protein . Cell membrane . Detected in the plasma membrane of Sertoli cells and in the luminal membrane of epithelial cells in the epididymis. |
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Protein Description | High affinity carnitine transporter; the uptake is partially sodium-ion dependent. Thought to mediate the L-carnitine secretion mechanism from testis epididymal epithelium into the lumen which is involved in the maturation of spermatozoa. Also transports organic cations such as tetraethylammonium (TEA) and doxorubicin. The uptake of TEA is inhibited by various organic cations. The uptake of doxorubicin is sodium-independent.. | |
Protein Sequence | MGSRHFEGIYDHVGHFGRFQRVLYFICAFQNISCGIHYLASVFMGVTPHHVCRPPGNVSQVVFHNHSNWSLEDTGALLSSGQKDYVTVQLQNGEIWELSRCSRNKRENTSSLGYEYTGSKKEFPCVDGYIYDQNTWKSTAVTQWNLVCDRKWLAMLIQPLFMFGVLLGSVTFGYFSDRLGRRVVLWATSSSMFLFGIAAAFAVDYYTFMAARFFLAMVASGYLVVGFVYVMEFIGMKSRTWASVHLHSFFAVGTLLVALTGYLVRTWWLYQMILSTVTVPFILCCWVLPETPFWLLSEGRYEEAQKIVDIMAKWNRASSCKLSELLSLDLQGPVSNSPTEVQKHNLSYLFYNWSITKRTLTVWLIWFTGSLGFYSFSLNSVNLGGNEYLNLFLLGVVEIPAYTFVCIAMDKVGRRTVLAYSLFCSALACGVVMVIPQKHYILGVVTAMVGKFAIGAAFGLIYLYTAELYPTIVRSLAVGSGSMVCRLASILAPFSVDLSSIWIFIPQLFVGTMALLSGVLTLKLPETLGKRLATTWEEAAKLESENESKSSKLLLTTNNSGLEKTEAITPRDSGLGE | |
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 |
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57 | N-linked_Glycosylation | HVCRPPGNVSQVVFH CCCCCCCCEEEEEEE | 35.72 | UniProtKB CARBOHYD | |
65 | N-linked_Glycosylation | VSQVVFHNHSNWSLE EEEEEEECCCCCCHH | 28.90 | UniProtKB CARBOHYD | |
68 | N-linked_Glycosylation | VVFHNHSNWSLEDTG EEEECCCCCCHHHHC | 25.46 | UniProtKB CARBOHYD | |
108 | N-linked_Glycosylation | CSRNKRENTSSLGYE ECCCCCCCCCCCCCE | 49.66 | UniProtKB CARBOHYD | |
238 | Phosphorylation | MEFIGMKSRTWASVH HHHHCCCCCCEEEHH | 26.50 | 24719451 | |
345 | N-linked_Glycosylation | PTEVQKHNLSYLFYN CHHHHHHCEEEEEEC | 37.40 | UniProtKB CARBOHYD | |
352 | N-linked_Glycosylation | NLSYLFYNWSITKRT CEEEEEECCCCCCCC | 20.77 | UniProtKB CARBOHYD | |
475 | Phosphorylation | LYPTIVRSLAVGSGS HHHHHHHHHCCCCCC | 15.13 | - | |
535 | Phosphorylation | LGKRLATTWEEAAKL HHHHHHHCHHHHHHH | 25.85 | - | |
546 | N-linked_Glycosylation | AAKLESENESKSSKL HHHHHCCCCCCCCCE | 69.03 | UniProtKB CARBOHYD | |
556 | Phosphorylation | KSSKLLLTTNNSGLE CCCCEEEEECCCCCC | 27.70 | - | |
558 | N-linked_Glycosylation | SKLLLTTNNSGLEKT CCEEEEECCCCCCEE | 35.12 | UniProtKB CARBOHYD | |
560 | Phosphorylation | LLLTTNNSGLEKTEA EEEEECCCCCCEEEC | 46.99 | - | |
569 | Phosphorylation | LEKTEAITPRDSGLG CCEEECCCCCCCCCC | 21.22 | 24719451 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of S22AG_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of S22AG_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of S22AG_HUMAN !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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