UniProt ID | S29A1_MOUSE | |
---|---|---|
UniProt AC | Q9JIM1 | |
Protein Name | Equilibrative nucleoside transporter 1 | |
Gene Name | Slc29a1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 460 | |
Subcellular Localization |
Basolateral cell membrane Multi-pass membrane protein. Apical cell membrane Multi-pass membrane protein. Cell membrane Multi-pass membrane protein. Predominantly localized in the basolateral membrane in polarized MDCK cells.. |
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Protein Description | Mediates both influx and efflux of nucleosides across the membrane (equilibrative transporter). It is sensitive (ES) to low concentrations of the inhibitor nitrobenzylmercaptopurine riboside (NBMPR) and is sodium-independent. It has a higher affinity for adenosine. Resistant to dipyridamole and dilazep inhibition (anticancer chemotherapeutics drugs).. | |
Protein Sequence | MTTSHQPQDRYKAVWLIFFVLGLGTLLPWNFFMTATKYFTNRLDVSQNVSSDTDQSCESTKALADPTVALPARSSLSAIFNNVMTLCAMLPLLVFTCLNSFLHQRISQSVRILGSLLAILLVFLVTAALVKVEMDALIFFVITMIKIVLINSFGAILQASLFGLAGVLPANYTAPIMSGQGLAGFFTSVAMICAIASGSELSESAFGYFITACAVVILAILCYLALPRTEFYRHYLQLNLAGPAEQETKLDLISKGEEPKGRREESGVPGPNSPPTNRNQSIKAILKSICVPALSVCFIFTVTIGLFPAVTAEVESSIAGTSPWKSYFIPVACFLNFNVFDWLGRSLTAVCMWPGQDSRWLPVLVASRIVFIPLLMLCNVKARHCGAQRHHFVFKHDAWFIAFMAAFAFSNGYLASLCMCFGPKKVKPAEAETAGNIMSFFLCLGLALGAVLSFLLRALV | |
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 |
---|---|---|---|---|---|
48 | N-linked_Glycosylation | NRLDVSQNVSSDTDQ CCCCCCCCCCCCCCC | 28.29 | 19349973 | |
249 | Ubiquitination | GPAEQETKLDLISKG CCCCCCHHHHHHHCC | 38.97 | - | |
249 (in isoform 2) | Ubiquitination | - | 38.97 | - | |
254 | Phosphorylation | ETKLDLISKGEEPKG CHHHHHHHCCCCCCC | 41.74 | 17520485 | |
255 | Ubiquitination | TKLDLISKGEEPKGR HHHHHHHCCCCCCCC | 64.45 | - | |
266 | Phosphorylation | PKGRREESGVPGPNS CCCCCCCCCCCCCCC | 40.10 | 21809900 | |
273 | Phosphorylation | SGVPGPNSPPTNRNQ CCCCCCCCCCCCCHH | 35.08 | 21809900 | |
276 | Phosphorylation | PGPNSPPTNRNQSIK CCCCCCCCCCHHHHH | 50.63 | 21809900 | |
281 | Phosphorylation | PPTNRNQSIKAILKS CCCCCHHHHHHHHHH | 29.61 | 21809900 | |
288 | Phosphorylation | SIKAILKSICVPALS HHHHHHHHCHHHHHH | 20.13 | 21809900 | |
351 | S-palmitoylation | GRSLTAVCMWPGQDS CCCCEEEEECCCCCC | 1.88 | 28526873 | |
378 | S-palmitoylation | FIPLLMLCNVKARHC HHHHHHHCCHHCCCC | 3.24 | 28526873 | |
381 | Acetylation | LLMLCNVKARHCGAQ HHHHCCHHCCCCCCC | 26.22 | 6565833 | |
381 | Ubiquitination | LLMLCNVKARHCGAQ HHHHCCHHCCCCCCC | 26.22 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
254 | S | Phosphorylation | Kinase | CK2A1 | P68400 | PSP |
266 | S | Phosphorylation | Kinase | PKACA | P05132 | PSP |
273 | S | Phosphorylation | Kinase | PKACA | P05132 | PSP |
276 | T | Phosphorylation | Kinase | PKACA | P05132 | PSP |
276 | T | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
281 | S | Phosphorylation | Kinase | PKACA | P05132 | PSP |
281 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
288 | S | Phosphorylation | Kinase | PKACA | P05132 | PSP |
288 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of S29A1_MOUSE !! |
* 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 S29A1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of S29A1_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-48, AND MASS SPECTROMETRY. |