S29A1_MOUSE - dbPTM
S29A1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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..
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
48N-linked_GlycosylationNRLDVSQNVSSDTDQ
CCCCCCCCCCCCCCC
28.2919349973
249UbiquitinationGPAEQETKLDLISKG
CCCCCCHHHHHHHCC
38.97-
249 (in isoform 2)Ubiquitination-38.97-
254PhosphorylationETKLDLISKGEEPKG
CHHHHHHHCCCCCCC
41.7417520485
255UbiquitinationTKLDLISKGEEPKGR
HHHHHHHCCCCCCCC
64.45-
266PhosphorylationPKGRREESGVPGPNS
CCCCCCCCCCCCCCC
40.1021809900
273PhosphorylationSGVPGPNSPPTNRNQ
CCCCCCCCCCCCCHH
35.0821809900
276PhosphorylationPGPNSPPTNRNQSIK
CCCCCCCCCCHHHHH
50.6321809900
281PhosphorylationPPTNRNQSIKAILKS
CCCCCHHHHHHHHHH
29.6121809900
288PhosphorylationSIKAILKSICVPALS
HHHHHHHHCHHHHHH
20.1321809900
351S-palmitoylationGRSLTAVCMWPGQDS
CCCCEEEEECCCCCC
1.8828526873
378S-palmitoylationFIPLLMLCNVKARHC
HHHHHHHCCHHCCCC
3.2428526873
381AcetylationLLMLCNVKARHCGAQ
HHHHCCHHCCCCCCC
26.226565833
381UbiquitinationLLMLCNVKARHCGAQ
HHHHCCHHCCCCCCC
26.22-

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
254SPhosphorylationKinaseCK2A1P68400
PSP
266SPhosphorylationKinasePKACAP05132
PSP
273SPhosphorylationKinasePKACAP05132
PSP
276TPhosphorylationKinasePKACAP05132
PSP
276TPhosphorylationKinasePRKCAP17252
GPS
281SPhosphorylationKinasePKACAP05132
PSP
281SPhosphorylationKinasePRKCAP17252
GPS
288SPhosphorylationKinasePKACAP05132
PSP
288SPhosphorylationKinasePRKCAP17252
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S29A1_MOUSE !!

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 S29A1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of S29A1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of S29A1_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.

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