S29A2_HUMAN - dbPTM
S29A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S29A2_HUMAN
UniProt AC Q14542
Protein Name Equilibrative nucleoside transporter 2
Gene Name SLC29A2
Organism Homo sapiens (Human).
Sequence Length 456
Subcellular Localization Basolateral cell membrane
Multi-pass membrane protein . Nucleus membrane
Multi-pass membrane protein . Localized at the basolateral cell membrane in polarized MDCK cells.
Protein Description Mediates equilibrative transport of purine, pyrimidine nucleosides and the purine base hypoxanthine. Very less sensitive than SLC29A1 to inhibition by nitrobenzylthioinosine (NBMPR), dipyridamole, dilazep and draflazine..
Protein Sequence MARGDAPRDSYHLVGISFFILGLGTLLPWNFFITAIPYFQARLAGAGNSTARILSTNHTGPEDAFNFNNWVTLLSQLPLLLFTLLNSFLYQCVPETVRILGSLLAILLLFALTAALVKVDMSPGPFFSITMASVCFINSFSAVLQGSLFGQLGTMPSTYSTLFLSGQGLAGIFAALAMLLSMASGVDAETSALGYFITPCVGILMSIVCYLSLPHLKFARYYLANKSSQAQAQELETKAELLQSDENGIPSSPQKVALTLDLDLEKEPESEPDEPQKPGKPSVFTVFQKIWLTALCLVLVFTVTLSVFPAITAMVTSSTSPGKWSQFFNPICCFLLFNIMDWLGRSLTSYFLWPDEDSRLLPLLVCLRFLFVPLFMLCHVPQRSRLPILFPQDAYFITFMLLFAVSNGYLVSLTMCLAPRQVLPHEREVAGALMTFFLALGLSCGASLSFLFKALL
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_GlycosylationARLAGAGNSTARILS
HHHCCCCCCCCEEEE		35.3412590919
48N-linked_GlycosylationARLAGAGNSTARILS
HHHCCCCCCCCEEEE		35.3412590919
49PhosphorylationRLAGAGNSTARILST
HHCCCCCCCCEEEEC		23.6423312004
50PhosphorylationLAGAGNSTARILSTN
HCCCCCCCCEEEECC		24.7723312004
57N-linked_GlycosylationTARILSTNHTGPEDA
CCEEEECCCCCHHHC		27.6112590919
57N-linked_GlycosylationTARILSTNHTGPEDA
CCEEEECCCCCHHHC		27.6112590919
96 (in isoform 2)Ubiquitination-14.7121906983
108 (in isoform 2)Ubiquitination-2.7821906983
225N-linked_GlycosylationFARYYLANKSSQAQA
HHHHHHHCCCHHHHH		41.99UniProtKB CARBOHYD
226 (in isoform 1)Ubiquitination-45.9721906983
226UbiquitinationARYYLANKSSQAQAQ
HHHHHHCCCHHHHHH		45.9721906983
226 (in isoform 3)Ubiquitination-45.97-
238 (in isoform 1)Ubiquitination-30.4121906983
238 (in isoform 3)Ubiquitination-30.41-
238UbiquitinationQAQELETKAELLQSD
HHHHHHHHHHHHHCC		30.412190698
244PhosphorylationTKAELLQSDENGIPS
HHHHHHHCCCCCCCC		47.0325159151
251PhosphorylationSDENGIPSSPQKVAL
CCCCCCCCCCCEEEE		53.3730266825
252PhosphorylationDENGIPSSPQKVALT
CCCCCCCCCCEEEEE		26.4630266825
312PhosphorylationLSVFPAITAMVTSST
HHHHHHHHHHHHCCC		15.71-
318PhosphorylationITAMVTSSTSPGKWS
HHHHHHCCCCCCHHH		24.44-
346PhosphorylationIMDWLGRSLTSYFLW
HHHHHCHHHHHHHCC		33.9126074081
348PhosphorylationDWLGRSLTSYFLWPD
HHHCHHHHHHHCCCC		23.7226074081
349PhosphorylationWLGRSLTSYFLWPDE
HHCHHHHHHHCCCCC		21.1226074081
350PhosphorylationLGRSLTSYFLWPDED
HCHHHHHHHCCCCCC		9.4726074081
358PhosphorylationFLWPDEDSRLLPLLV
HCCCCCCCCHHHHHH		23.8426074081
395PhosphorylationILFPQDAYFITFMLL
CCCCCHHHHHHHHHH		12.10-
409PhosphorylationLFAVSNGYLVSLTMC
HHHHHCCCHHEEEEE		14.26-
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

Oops, there are no upstream regulatory protein records of S29A2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S29A2_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 S29A2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBQL1_HUMANUBQLN1physical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D04931 Mercaptopurine (INN); Mercaptopurine anhydrous; Purinethol (TN)
DrugBank
DB00900Didanosine
DB00898Ethanol
DB00441Gemcitabine
DB01033Mercaptopurine
DB00943Zalcitabine
DB00495Zidovudine
Regulatory Network of S29A2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Functional analysis of site-directed glycosylation mutants of thehuman equilibrative nucleoside transporter-2.";
Ward J.L., Leung G.P., Toan S.V., Tse C.-M.;
Arch. Biochem. Biophys. 411:19-26(2003).
Cited for: GLYCOSYLATION AT ASN-48 AND ASN-57.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASSSPECTROMETRY.

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