S29A1_HUMAN - dbPTM
S29A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S29A1_HUMAN
UniProt AC Q99808
Protein Name Equilibrative nucleoside transporter 1
Gene Name SLC29A1
Organism Homo sapiens (Human).
Sequence Length 456
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. Inhibited by dipyridamole and dilazep (anticancer chemotherapeutics drugs)..
Protein Sequence MTTSHQPQDRYKAVWLIFFMLGLGTLLPWNFFMTATQYFTNRLDMSQNVSLVTAELSKDAQASAAPAAPLPERNSLSAIFNNVMTLCAMLPLLLFTYLNSFLHQRIPQSVRILGSLVAILLVFLITAILVKVQLDALPFFVITMIKIVLINSFGAILQGSLFGLAGLLPASYTAPIMSGQGLAGFFASVAMICAIASGSELSESAFGYFITACAVIILTIICYLGLPRLEFYRYYQQLKLEGPGEQETKLDLISKGEEPRAGKEESGVSVSNSQPTNESHSIKAILKNISVLAFSVCFIFTITIGMFPAVTVEVKSSIAGSSTWERYFIPVSCFLTFNIFDWLGRSLTAVFMWPGKDSRWLPSLVLARLVFVPLLLLCNIKPRRYLTVVFEHDAWFIFFMAAFAFSNGYLASLCMCFGPKKVKPAEAETAGAIMAFFLCLGLALGAVFSFLFRAIV
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_GlycosylationNRLDMSQNVSLVTAE
HCCCCCCCEEEEEEE		20.31UniProtKB CARBOHYD
63O-linked_GlycosylationLSKDAQASAAPAAPL
CCHHHHHHCCCCCCC		16.9432574038
63PhosphorylationLSKDAQASAAPAAPL
CCHHHHHHCCCCCCC		16.94-
143PhosphorylationALPFFVITMIKIVLI
CHHHHHHHHHHHHHH		13.9320068231
239UbiquitinationYRYYQQLKLEGPGEQ
HHHHHHHCCCCCCCC		39.9123000965
248PhosphorylationEGPGEQETKLDLISK
CCCCCCCCHHHEEEC		36.2823312004
249UbiquitinationGPGEQETKLDLISKG
CCCCCCCHHHEEECC		38.9723000965
254PhosphorylationETKLDLISKGEEPRA
CCHHHEEECCCCCCC		41.7423401153
255UbiquitinationTKLDLISKGEEPRAG
CHHHEEECCCCCCCC		64.4523000965
263UbiquitinationGEEPRAGKEESGVSV
CCCCCCCCCCCCCCC		58.2721906983
264UbiquitinationEEPRAGKEESGVSVS
CCCCCCCCCCCCCCC		57.3823000965
265UbiquitinationEPRAGKEESGVSVSN
CCCCCCCCCCCCCCC		57.1723000965
266PhosphorylationPRAGKEESGVSVSNS
CCCCCCCCCCCCCCC		45.6630266825
269PhosphorylationGKEESGVSVSNSQPT
CCCCCCCCCCCCCCC		24.2923401153
271PhosphorylationEESGVSVSNSQPTNE
CCCCCCCCCCCCCCC		24.2130266825
273PhosphorylationSGVSVSNSQPTNESH
CCCCCCCCCCCCCCH		29.9923401153
274UbiquitinationGVSVSNSQPTNESHS
CCCCCCCCCCCCCHH		53.7623000965
275UbiquitinationVSVSNSQPTNESHSI
CCCCCCCCCCCCHHH		36.6923000965
276PhosphorylationSVSNSQPTNESHSIK
CCCCCCCCCCCHHHH		43.9430266825
279PhosphorylationNSQPTNESHSIKAIL
CCCCCCCCHHHHHHH		25.3030266825
280UbiquitinationSQPTNESHSIKAILK
CCCCCCCHHHHHHHH		27.6223000965
281UbiquitinationQPTNESHSIKAILKN
CCCCCCHHHHHHHHH		34.7523000965
281PhosphorylationQPTNESHSIKAILKN
CCCCCCHHHHHHHHH		34.7523403867
282UbiquitinationPTNESHSIKAILKNI
CCCCCHHHHHHHHHH		2.6723000965
283UbiquitinationTNESHSIKAILKNIS
CCCCHHHHHHHHHHH		32.1821906983
287UbiquitinationHSIKAILKNISVLAF
HHHHHHHHHHHHHHH		46.23-
288UbiquitinationSIKAILKNISVLAFS
HHHHHHHHHHHHHHH		28.4627667366
289UbiquitinationIKAILKNISVLAFSV
HHHHHHHHHHHHHHH		2.6227667366
291UbiquitinationAILKNISVLAFSVCF
HHHHHHHHHHHHHHH		3.8623000965
292UbiquitinationILKNISVLAFSVCFI
HHHHHHHHHHHHHHH		2.9623000965
297UbiquitinationSVLAFSVCFIFTITI
HHHHHHHHHHHHHHC		1.7823000965
298UbiquitinationVLAFSVCFIFTITIG
HHHHHHHHHHHHHCC		4.8923000965
305UbiquitinationFIFTITIGMFPAVTV
HHHHHHCCCCCCEEE		11.7427667366
306UbiquitinationIFTITIGMFPAVTVE
HHHHHCCCCCCEEEE		3.0027667366
308UbiquitinationTITIGMFPAVTVEVK
HHHCCCCCCEEEEEH		19.5432015554
309UbiquitinationITIGMFPAVTVEVKS
HHCCCCCCEEEEEHH		9.8032015554
318UbiquitinationTVEVKSSIAGSSTWE
EEEEHHHHCCCCCCH		6.9423000965
319UbiquitinationVEVKSSIAGSSTWER
EEEHHHHCCCCCCHH		17.4823000965
325UbiquitinationIAGSSTWERYFIPVS
HCCCCCCHHCEEEHH		37.2825015289
326UbiquitinationAGSSTWERYFIPVSC
CCCCCCHHCEEEHHH		24.1925015289
328UbiquitinationSSTWERYFIPVSCFL
CCCCHHCEEEHHHHH		6.7923000965
329UbiquitinationSTWERYFIPVSCFLT
CCCHHCEEEHHHHHH		2.1423000965
334UbiquitinationYFIPVSCFLTFNIFD
CEEEHHHHHHHCHHH		5.8423000965
335UbiquitinationFIPVSCFLTFNIFDW
EEEHHHHHHHCHHHH		6.6623000965
342UbiquitinationLTFNIFDWLGRSLTA
HHHCHHHHHCCCCEE		7.0327667366
342UbiquitinationLTFNIFDWLGRSLTA
HHHCHHHHHCCCCEE		7.0321890473
343UbiquitinationTFNIFDWLGRSLTAV
HHCHHHHHCCCCEEE		4.3827667366
356UbiquitinationAVFMWPGKDSRWLPS
EEEECCCCCCCCHHH		48.7529967540
362UbiquitinationGKDSRWLPSLVLARL
CCCCCCHHHHHHHHH		20.7521890473
362UbiquitinationGKDSRWLPSLVLARL
CCCCCCHHHHHHHHH		20.7532015554
363UbiquitinationKDSRWLPSLVLARLV
CCCCCHHHHHHHHHH		29.0125015289
381UbiquitinationLLLLCNIKPRRYLTV
HHHHCCCCCCCEEEE		20.6229967540
382UbiquitinationLLLCNIKPRRYLTVV
HHHCCCCCCCEEEEE		23.3721890473
398UbiquitinationEHDAWFIFFMAAFAF
ECHHHHHHHHHHHHH		2.2021890473
399UbiquitinationHDAWFIFFMAAFAFS
CHHHHHHHHHHHHHC		2.5221890473
435UbiquitinationETAGAIMAFFLCLGL
HHHHHHHHHHHHHHH		5.9721890473
436UbiquitinationTAGAIMAFFLCLGLA
HHHHHHHHHHHHHHH		2.3821890473
460UbiquitinationRAIV-----------
HHHC-----------		21890473
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
281SPhosphorylationKinasePRKCDQ05655
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S29A1_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRC_HUMANSRCphysical
28514442
GBB2_HUMANGNB2physical
28514442
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
DB00987Cytarabine
DB00900Didanosine
DB00898Ethanol
DB01073Fludarabine
DB00544Fluorouracil
DB00441Gemcitabine
DB01033Mercaptopurine
DB00642Pemetrexed
DB00811Ribavirin
DB00943Zalcitabine
Regulatory Network of S29A1_HUMAN

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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.
Phosphorylation
ReferencePubMed
"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-254, AND MASSSPECTROMETRY.

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