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Protein

5'-nucleotidase

Gene

NT5E

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities.1 Publication

Catalytic activityi

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Zinc 1
Metal bindingi38 – 381Zinc 1
Metal bindingi85 – 851Zinc 1
Metal bindingi85 – 851Zinc 2
Metal bindingi117 – 1171Zinc 2
Sitei118 – 1181Transition state stabilizer
Sitei121 – 1211Transition state stabilizerCurated
Metal bindingi220 – 2201Zinc 2
Metal bindingi243 – 2431Zinc 2
Binding sitei245 – 2451Substrate
Binding sitei354 – 3541Substrate
Binding sitei390 – 3901Substrate
Binding sitei395 – 3951Substrate
Binding sitei417 – 4171Substrate

GO - Molecular functioni

  1. 5'-nucleotidase activity Source: Reactome
  2. metal ion binding Source: UniProtKB-KW
  3. nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  1. adenosine biosynthetic process Source: Ensembl
  2. AMP catabolic process Source: Ensembl
  3. dephosphorylation Source: GOC
  4. DNA metabolic process Source: ProtInc
  5. negative regulation of inflammatory response Source: Ensembl
  6. nucleobase-containing small molecule metabolic process Source: Reactome
  7. purine nucleobase metabolic process Source: Reactome
  8. purine nucleotide catabolic process Source: Reactome
  9. pyrimidine nucleobase metabolic process Source: Reactome
  10. pyrimidine nucleoside catabolic process Source: Reactome
  11. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS05981-MONOMER.
RETL1328306-WGS:GSTH-3623-MONOMER.
ReactomeiREACT_1023. Pyrimidine catabolism.
REACT_2086. Purine catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-nucleotidase (EC:3.1.3.5)
Short name:
5'-NT
Alternative name(s):
Ecto-5'-nucleotidase
CD_antigen: CD73
Gene namesi
Name:NT5E
Synonyms:NT5, NTE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:8021. NT5E.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. cell surface Source: UniProtKB
  3. cytoplasm Source: HPA
  4. extracellular vesicular exosome Source: UniProtKB
  5. membrane Source: ProtInc
  6. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Calcification of joints and arteries1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA condition characterized by adult-onset calcification of the lower extremity arteries, including the iliac, femoral and tibial arteries, and hand and foot capsule joints. Age of onset has been reported as early as the second decade of life, usually involving intense joint pain or calcification in the hands.

See also OMIM:211800
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti358 – 3581C → Y in CALJA. 1 Publication
VAR_065185

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi211800. phenotype.
Orphaneti289601. Hereditary arterial and articular multiple calcification syndrome.
PharmGKBiPA31804.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 5495235'-nucleotidase1 PublicationPRO_0000000015Add
BLAST
Propeptidei550 – 57425Removed in mature formPRO_0000000016Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 571 Publication
Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi311 – 3111N-linked (GlcNAc...)2 Publications
Glycosylationi333 – 3331N-linked (GlcNAc...)2 Publications
Disulfide bondi353 ↔ 3581 Publication
Disulfide bondi365 ↔ 3871 Publication
Glycosylationi403 – 4031N-linked (GlcNAc...)1 Publication
Disulfide bondi476 ↔ 4791 Publication
Lipidationi549 – 5491GPI-anchor amidated serine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiP21589.
PaxDbiP21589.
PRIDEiP21589.

PTM databases

DEPODiP21589.
PhosphoSiteiP21589.

Expressioni

Gene expression databases

BgeeiP21589.
CleanExiHS_NT5E.
ExpressionAtlasiP21589. baseline and differential.
GenevestigatoriP21589.

Organism-specific databases

HPAiHPA017357.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi110962. 47 interactions.
DIPiDIP-59992N.
MINTiMINT-5002487.
STRINGi9606.ENSP00000257770.

Structurei

Secondary structure

1
574
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 348Combined sources
Beta strandi48 – 503Combined sources
Helixi54 – 563Combined sources
Helixi61 – 7414Combined sources
Beta strandi76 – 827Combined sources
Beta strandi87 – 904Combined sources
Helixi91 – 966Combined sources
Helixi99 – 10810Combined sources
Beta strandi111 – 1144Combined sources
Helixi117 – 1204Combined sources
Helixi123 – 1286Combined sources
Turni129 – 1346Combined sources
Beta strandi142 – 1465Combined sources
Helixi150 – 1545Combined sources
Turni155 – 1573Combined sources
Beta strandi158 – 1669Combined sources
Beta strandi169 – 1779Combined sources
Helixi181 – 1844Combined sources
Beta strandi189 – 1935Combined sources
Helixi196 – 20914Combined sources
Beta strandi215 – 2217Combined sources
Helixi223 – 23210Combined sources
Beta strandi238 – 2403Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi263 – 2686Combined sources
Beta strandi274 – 2785Combined sources
Beta strandi285 – 29410Combined sources
Beta strandi300 – 3056Combined sources
Helixi318 – 33518Combined sources
Beta strandi337 – 3448Combined sources
Helixi350 – 3534Combined sources
Helixi359 – 37113Combined sources
Helixi379 – 3813Combined sources
Beta strandi386 – 3905Combined sources
Helixi391 – 3933Combined sources
Turni401 – 4044Combined sources
Beta strandi405 – 4073Combined sources
Helixi408 – 4147Combined sources
Beta strandi420 – 4278Combined sources
Helixi428 – 43912Combined sources
Turni440 – 4434Combined sources
Beta strandi450 – 45910Combined sources
Beta strandi469 – 4757Combined sources
Beta strandi477 – 4815Combined sources
Beta strandi484 – 4863Combined sources
Beta strandi492 – 4987Combined sources
Helixi499 – 5024Combined sources
Helixi505 – 5073Combined sources
Helixi509 – 5146Combined sources
Beta strandi516 – 5238Combined sources
Helixi524 – 53512Combined sources
Beta strandi536 – 5383Combined sources
Beta strandi544 – 5485Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4H1SX-ray2.20A/B27-549[»]
4H1YX-ray1.58P27-549[»]
4H2BX-ray1.70A27-549[»]
4H2FX-ray1.85A27-549[»]
4H2GX-ray1.55A27-549[»]
4H2IX-ray2.00A27-549[»]
ProteinModelPortaliP21589.
SMRiP21589. Positions 27-549.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni500 – 5067Substrate binding

Sequence similaritiesi

Belongs to the 5'-nucleotidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0737.
GeneTreeiENSGT00530000063775.
HOGENOMiHOG000247215.
HOVERGENiHBG000026.
KOiK01081.
OMAiRVPSYDP.
OrthoDBiEOG7TF78T.
PhylomeDBiP21589.
TreeFamiTF323589.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProiIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERiPTHR11575. PTHR11575. 1 hit.
PfamiPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR01607. APYRASEFAMLY.
SUPFAMiSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
PROSITEiPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P21589-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MCPRAARAPA TLLLALGAVL WPAAGAWELT ILHTNDVHSR LEQTSEDSSK
60 70 80 90 100
CVNASRCMGG VARLFTKVQQ IRRAEPNVLL LDAGDQYQGT IWFTVYKGAE
110 120 130 140 150
VAHFMNALRY DAMALGNHEF DNGVEGLIEP LLKEAKFPIL SANIKAKGPL
160 170 180 190 200
ASQISGLYLP YKVLPVGDEV VGIVGYTSKE TPFLSNPGTN LVFEDEITAL
210 220 230 240 250
QPEVDKLKTL NVNKIIALGH SGFEMDKLIA QKVRGVDVVV GGHSNTFLYT
260 270 280 290 300
GNPPSKEVPA GKYPFIVTSD DGRKVPVVQA YAFGKYLGYL KIEFDERGNV
310 320 330 340 350
ISSHGNPILL NSSIPEDPSI KADINKWRIK LDNYSTQELG KTIVYLDGSS
360 370 380 390 400
QSCRFRECNM GNLICDAMIN NNLRHTDEMF WNHVSMCILN GGGIRSPIDE
410 420 430 440 450
RNNGTITWEN LAAVLPFGGT FDLVQLKGST LKKAFEHSVH RYGQSTGEFL
460 470 480 490 500
QVGGIHVVYD LSRKPGDRVV KLDVLCTKCR VPSYDPLKMD EVYKVILPNF
510 520 530 540 550
LANGGDGFQM IKDELLRHDS GDQDINVVST YISKMKVIYP AVEGRIKFST
560 570
GSHCHGSFSL IFLSLWAVIF VLYQ
Length:574
Mass (Da):63,368
Last modified:May 1, 1991 - v1
Checksum:iA99AF170AB7EAECE
GO
Isoform 2 (identifier: P21589-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     404-453: Missing.

Note: No experimental confirmation available.

Show »
Length:524
Mass (Da):57,949
Checksum:i98A11D22CFC7C610
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti358 – 3581C → Y in CALJA. 1 Publication
VAR_065185
Natural varianti376 – 3761T → A.1 Publication
Corresponds to variant rs2229523 [ dbSNP | Ensembl ].
VAR_022091
Natural varianti379 – 3791M → T.
Corresponds to variant rs2229524 [ dbSNP | Ensembl ].
VAR_048103

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei404 – 45350Missing in isoform 2. 1 PublicationVSP_043076Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55740 mRNA. Translation: CAA39271.1.
AK075008 mRNA. Translation: BAG52050.1.
AL135903, AL589666 Genomic DNA. Translation: CAH72337.1.
AL589666, AL135903 Genomic DNA. Translation: CAI40168.1.
U21730 Genomic DNA. Translation: AAA96950.1.
AF069067 Genomic DNA. Translation: AAC98672.1.
CCDSiCCDS5002.1. [P21589-1]
CCDS56439.1. [P21589-2]
PIRiS11032.
RefSeqiNP_001191742.1. NM_001204813.1. [P21589-2]
NP_002517.1. NM_002526.3. [P21589-1]
UniGeneiHs.153952.

Genome annotation databases

EnsembliENST00000257770; ENSP00000257770; ENSG00000135318. [P21589-1]
ENST00000369651; ENSP00000358665; ENSG00000135318. [P21589-2]
GeneIDi4907.
KEGGihsa:4907.
UCSCiuc003pko.4. human. [P21589-1]
uc010kbr.3. human. [P21589-2]

Polymorphism databases

DMDMi112825.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55740 mRNA. Translation: CAA39271.1.
AK075008 mRNA. Translation: BAG52050.1.
AL135903, AL589666 Genomic DNA. Translation: CAH72337.1.
AL589666, AL135903 Genomic DNA. Translation: CAI40168.1.
U21730 Genomic DNA. Translation: AAA96950.1.
AF069067 Genomic DNA. Translation: AAC98672.1.
CCDSiCCDS5002.1. [P21589-1]
CCDS56439.1. [P21589-2]
PIRiS11032.
RefSeqiNP_001191742.1. NM_001204813.1. [P21589-2]
NP_002517.1. NM_002526.3. [P21589-1]
UniGeneiHs.153952.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4H1SX-ray2.20A/B27-549[»]
4H1YX-ray1.58P27-549[»]
4H2BX-ray1.70A27-549[»]
4H2FX-ray1.85A27-549[»]
4H2GX-ray1.55A27-549[»]
4H2IX-ray2.00A27-549[»]
ProteinModelPortaliP21589.
SMRiP21589. Positions 27-549.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110962. 47 interactions.
DIPiDIP-59992N.
MINTiMINT-5002487.
STRINGi9606.ENSP00000257770.

Chemistry

BindingDBiP21589.
ChEMBLiCHEMBL5957.
DrugBankiDB00987. Cytarabine.
DB00806. Pentoxifylline.
GuidetoPHARMACOLOGYi1232.

PTM databases

DEPODiP21589.
PhosphoSiteiP21589.

Polymorphism databases

DMDMi112825.

Proteomic databases

MaxQBiP21589.
PaxDbiP21589.
PRIDEiP21589.

Protocols and materials databases

DNASUi4907.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257770; ENSP00000257770; ENSG00000135318. [P21589-1]
ENST00000369651; ENSP00000358665; ENSG00000135318. [P21589-2]
GeneIDi4907.
KEGGihsa:4907.
UCSCiuc003pko.4. human. [P21589-1]
uc010kbr.3. human. [P21589-2]

Organism-specific databases

CTDi4907.
GeneCardsiGC06P086216.
HGNCiHGNC:8021. NT5E.
HPAiHPA017357.
MIMi129190. gene.
211800. phenotype.
neXtProtiNX_P21589.
Orphaneti289601. Hereditary arterial and articular multiple calcification syndrome.
PharmGKBiPA31804.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0737.
GeneTreeiENSGT00530000063775.
HOGENOMiHOG000247215.
HOVERGENiHBG000026.
KOiK01081.
OMAiRVPSYDP.
OrthoDBiEOG7TF78T.
PhylomeDBiP21589.
TreeFamiTF323589.

Enzyme and pathway databases

BioCyciMetaCyc:HS05981-MONOMER.
RETL1328306-WGS:GSTH-3623-MONOMER.
ReactomeiREACT_1023. Pyrimidine catabolism.
REACT_2086. Purine catabolism.

Miscellaneous databases

ChiTaRSiNT5E. human.
GeneWikiiNT5E.
GenomeRNAii4907.
NextBioi18883.
PROiP21589.
SOURCEiSearch...

Gene expression databases

BgeeiP21589.
CleanExiHS_NT5E.
ExpressionAtlasiP21589. baseline and differential.
GenevestigatoriP21589.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProiIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERiPTHR11575. PTHR11575. 1 hit.
PfamiPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR01607. APYRASEFAMLY.
SUPFAMiSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
PROSITEiPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of human placental 5'-nucleotidase and identification of the glycolipid anchor in the mature form."
    Misumi Y., Ogata S., Ohkubo K., Hirose S., Ikehara Y.
    Eur. J. Biochem. 191:563-569(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, GPI-ANCHOR AT SER-549.
    Tissue: Placenta.
  2. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Isolation and characterization of the promoter of the human 5'-nucleotidase (CD73)-encoding gene."
    Hansen K.R., Resta R., Webb C.F., Thompson L.F.
    Gene 167:307-312(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-113.
    Tissue: Placenta.
  5. Zanoni L., Rosi F., Pagani R., Marinello E.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 359-489, VARIANT ALA-376.
    Tissue: Leukocyte.
  6. "Characterization of soluble vs membrane-bound human placental 5'-nucleotidase."
    Klemens M.R., Sherman W.R., Holmberg N.J., Ruedi J.M., Low M.G., Thompson L.F.
    Biochem. Biophys. Res. Commun. 172:1371-1377(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-40.
    Tissue: Placenta.
  7. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-311; ASN-333 AND ASN-403.
    Tissue: Liver.
  8. "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) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-333.
    Tissue: Leukemic T-cell.
  9. "The high-resolution crystal structure of periplasmic Haemophilus influenzae NAD nucleotidase reveals a novel enzymatic function of human CD73 related to NAD metabolism."
    Garavaglia S., Bruzzone S., Cassani C., Canella L., Allegrone G., Sturla L., Mannino E., Millo E., De Flora A., Rizzi M.
    Biochem. J. 441:131-141(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Crystal structure of the human ecto-5'-nucleotidase (CD73): insights into the regulation of purinergic signaling."
    Knapp K., Zebisch M., Pippel J., El-Tayeb A., Muller C.E., Strater N.
    Structure 20:2161-2173(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 27-549 IN COMPLEXES WITH ATP ANALOG AND ZINC IONS, SUBUNIT, GLYCOSYLATION AT ASN-311, DISULFIDE BONDS.
  12. Cited for: VARIANT CALJA TYR-358.

Entry informationi

Entry namei5NTD_HUMAN
AccessioniPrimary (citable) accession number: P21589
Secondary accession number(s): B3KQI8, O75520, Q5W116
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: March 4, 2015
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.