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Q14542 (S29A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Equilibrative nucleoside transporter 2
Alternative name(s):
36 kDa nucleolar protein HNP36
Delayed-early response protein 12
Equilibrative nitrobenzylmercaptopurine riboside-insensitive nucleoside transporter
Short name=Equilibrative NBMPR-insensitive nucleoside transporter
Hydrophobic nucleolar protein, 36 kDa
Nucleoside transporter, ei-type
Solute carrier family 29 member 2
Gene names
Name:SLC29A2
Synonyms:DER12, ENT2, HNP36
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Subcellular location

Basolateral cell membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. Note: Localized at the basolateral cell membrane in polarized MDCK cells. Ref.4

Tissue specificity

Expressed in skeletal muscle, liver, lung, placenta, brain, heart, kidney and ovarian tissues. Ref.2 Ref.4

Induction

By PDGF/platelet derived growth factor and fibroblast growth factor (FGF).

Sequence similarities

Belongs to the SLC29A/ENT transporter (TC 2.A.57) family. [View classification]

Biophysicochemical properties

Kinetic parameters:

Vmax for adenosine uptake is about the same for SLC29A1 and SLC29A2.

KM=0.2 mM for uridine Ref.2 Ref.4

KM=0.75 mM for adenosine

Sequence caution

The sequence CAA60380.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14542-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14542-2)

Also known as: Short; HNP36;

The sequence of this isoform differs from the canonical sequence as follows:
     93-202: VPETVRILGS...LGYFITPCVG → AGQGGHEPRT...PEVCPLLPGQ
     203-456: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 3 (identifier: Q14542-3)

The sequence of this isoform differs from the canonical sequence as follows:
     290-301: IWLTALCLVLVF → SPCPSSPPSQPW
     302-456: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Equilibrative nucleoside transporter 2
PRO_0000209340

Regions

Transmembrane13 – 3321Helical; Potential
Transmembrane70 – 9021Helical; Potential
Transmembrane99 – 11921Helical; Potential
Transmembrane124 – 14421Helical; Potential
Transmembrane162 – 18221Helical; Potential
Transmembrane193 – 21321Helical; Potential
Transmembrane291 – 31121Helical; Potential
Transmembrane324 – 34421Helical; Potential
Transmembrane360 – 38021Helical; Potential
Transmembrane386 – 40621Helical; Potential
Transmembrane432 – 45221Helical; Potential

Amino acid modifications

Modified residue2521Phosphoserine Ref.11 Ref.12
Glycosylation481N-linked (GlcNAc...) Ref.9
Glycosylation571N-linked (GlcNAc...) Ref.9
Glycosylation2251N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence93 – 202110VPETV…TPCVG → AGQGGHEPRTLLLHHHGLRL LHQLLQCSPTGQPLRAAGHH ALHLQHPLPQRPGPGWDLCC PCHAPVHGQWRGRRDLCPGV LYHALCGHPHVHRVLPEPAS PEVCPLLPGQ in isoform 2.
VSP_040728
Alternative sequence203 – 456254Missing in isoform 2.
VSP_040729
Alternative sequence290 – 30112IWLTA…LVLVF → SPCPSSPPSQPW in isoform 3.
VSP_040730
Alternative sequence302 – 456155Missing in isoform 3.
VSP_040731
Natural variant51D → Y. Ref.13
Corresponds to variant rs8187643 [ dbSNP | Ensembl ].
VAR_029289
Natural variant681N → K. Ref.13
Corresponds to variant rs8187644 [ dbSNP | Ensembl ].
VAR_029290
Natural variant941P → L. Ref.13
Corresponds to variant rs8187648 [ dbSNP | Ensembl ].
VAR_029291
Natural variant184 – 1863SGV → M.
VAR_036822

Experimental info

Mutagenesis4551L → R: Reduces drastically localization at the cell surface. No effect on uptake of adenosine and thymidine. Reduces drastically localization at the cell surface and induces an significant reduction of adenosine or thymidine uptake; when associated with R-456. Ref.4
Mutagenesis4561L → R: Reduces drastically localization at the cell surface and induces an significant reduction of adenosine or thymidine uptake; when associated with R-455. Ref.4
Sequence conflict2001C → Y in CAA60380. Ref.1
Sequence conflict2001C → Y in AAC39526. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: ABCBD244306708E1

FASTA45650,113
        10         20         30         40         50         60 
MARGDAPRDS YHLVGISFFI LGLGTLLPWN FFITAIPYFQ ARLAGAGNST ARILSTNHTG 

        70         80         90        100        110        120 
PEDAFNFNNW VTLLSQLPLL LFTLLNSFLY QCVPETVRIL GSLLAILLLF ALTAALVKVD 

       130        140        150        160        170        180 
MSPGPFFSIT MASVCFINSF SAVLQGSLFG QLGTMPSTYS TLFLSGQGLA GIFAALAMLL 

       190        200        210        220        230        240 
SMASGVDAET SALGYFITPC VGILMSIVCY LSLPHLKFAR YYLANKSSQA QAQELETKAE 

       250        260        270        280        290        300 
LLQSDENGIP SSPQKVALTL DLDLEKEPES EPDEPQKPGK PSVFTVFQKI WLTALCLVLV 

       310        320        330        340        350        360 
FTVTLSVFPA ITAMVTSSTS PGKWSQFFNP ICCFLLFNIM DWLGRSLTSY FLWPDEDSRL 

       370        380        390        400        410        420 
LPLLVCLRFL FVPLFMLCHV PQRSRLPILF PQDAYFITFM LLFAVSNGYL VSLTMCLAPR 

       430        440        450 
QVLPHEREVA GALMTFFLAL GLSCGASLSF LFKALL 

« Hide

Isoform 2 (Short) (HNP36) [UniParc].

Checksum: E1E980B5CCC29586
Show »

FASTA20222,276
Isoform 3 [UniParc].

Checksum: 5DFD77C4226D4F15
Show »

FASTA30132,507

References

« Hide 'large scale' references
[1]"A mammalian delayed-early response gene encodes HNP36, a novel, conserved nucleolar protein."
Williams J.B., Lanahan A.A.
Biochem. Biophys. Res. Commun. 213:325-333(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Heart.
[2]"Molecular cloning and characterization of a nitrobenzylthioinosine-insensitive (ei) equilibrative nucleoside transporter from human placenta."
Griffiths M., Yao S.Y., Abidi F., Phillips S.E., Cass C.E., Young J.D., Baldwin S.A.
Biochem. J. 328:739-743(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Tissue: Placenta.
[3]"Cloning of the human equilibrative, nitrobenzylmercaptopurine riboside (NBMPR)-insensitive nucleoside transporter ei by functional expression in a transport-deficient cell line."
Crawford C.R., Patel D.H., Naeve C., Belt J.A.
J. Biol. Chem. 273:5288-5293(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RESPONSE TO NBMPR.
[4]"Localization of human equilibrative nucleoside transporters, hENT1 and hENT2, in renal epithelial cells."
Mangravite L.M., Xiao G., Giacomini K.M.
Am. J. Physiol. 284:F902-F910(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LEU-455 AND LEU-456.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[9]"Functional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2."
Ward J.L., Leung G.P., Toan S.V., Tse C.-M.
Arch. Biochem. Biophys. 411:19-26(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-48 AND ASN-57.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Functional characterization and haplotype analysis of polymorphisms in the human equilibrative nucleoside transporter, ENT2."
Owen R.P., Lagpacan L.L., Taylor T.R., De La Cruz M., Huang C.C., Kawamoto M., Johns S.J., Stryke D., Ferrin T.E., Giacomini K.M.
Drug Metab. Dispos. 34:12-15(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TYR-5; LYS-68; LEU-94 AND 184-SER--VAL-186 DELINS MET.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X86681 mRNA. Translation: CAA60380.1. Sequence problems.
AF029358 mRNA. Translation: AAC39526.1.
AF034102 mRNA. Translation: AAB97834.1.
AK057041 mRNA. Translation: BAG51849.1.
AF401235 mRNA. Translation: AAK92533.1.
AP001107 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74521.1.
CH471076 Genomic DNA. Translation: EAW74519.1.
BC093634 mRNA. Translation: AAH93634.1.
PIRJC4196.
RefSeqNP_001523.2. NM_001532.2.
UniGeneHs.569017.

3D structure databases

ProteinModelPortalQ14542.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109419. 1 interaction.
IntActQ14542. 1 interaction.
STRING9606.ENSP00000350024.

Protein family/group databases

TCDB2.A.57.1.8. the equilibrative nucleoside transporter (ent) family.

PTM databases

PhosphoSiteQ14542.

Polymorphism databases

DMDM116242781.

Proteomic databases

PaxDbQ14542.
PRIDEQ14542.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357440; ENSP00000350024; ENSG00000174669. [Q14542-1]
ENST00000540386; ENSP00000444870; ENSG00000174669. [Q14542-3]
ENST00000541567; ENSP00000442116; ENSG00000174669. [Q14542-2]
ENST00000544554; ENSP00000439456; ENSG00000174669. [Q14542-1]
ENST00000546034; ENSP00000440329; ENSG00000174669. [Q14542-1]
GeneID3177.
KEGGhsa:3177.
UCSCuc001oht.3. human. [Q14542-1]

Organism-specific databases

CTD3177.
GeneCardsGC11M066129.
HGNCHGNC:11004. SLC29A2.
HPAHPA018168.
MIM602110. gene.
neXtProtNX_Q14542.
PharmGKBPA191.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249415.
HOGENOMHOG000007684.
HOVERGENHBG074626.
InParanoidQ14542.
KOK15014.
OMAPEKPSVF.
PhylomeDBQ14542.
TreeFamTF313950.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ14542.
BgeeQ14542.
CleanExHS_SLC29A2.
GenevestigatorQ14542.

Family and domain databases

InterProIPR002259. Eqnu_transpt.
IPR016196. MFS_dom_general_subst_transpt.
[Graphical view]
PANTHERPTHR10332. PTHR10332. 1 hit.
PfamPF01733. Nucleoside_tran. 1 hit.
[Graphical view]
PIRSFPIRSF016379. ENT. 1 hit.
PRINTSPR01130. DERENTRNSPRT.
SUPFAMSSF103473. SSF103473. 2 hits.
TIGRFAMsTIGR00939. 2a57. 1 hit.
ProtoNetSearch...

Other

GeneWikiEquilibrative_nucleoside_transporter_2.
GenomeRNAi3177.
NextBio12610.
PROQ14542.
SOURCESearch...

Entry information

Entry nameS29A2_HUMAN
AccessionPrimary (citable) accession number: Q14542
Secondary accession number(s): B3KPY7 expand/collapse secondary AC list , O43530, Q52M84, Q96R00, Q9UPE0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM