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
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	-

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
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

Functions of PTM Sites

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.

Oops, there are no SNP-PTM records of S29A1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of S29A1_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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.
PubMed: 19349973