Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P49961 (ENTP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ectonucleoside triphosphate diphosphohydrolase 1

Short name=NTPDase 1
EC=3.6.1.5
Alternative name(s):
Ecto-ATP diphosphohydrolase 1
Short name=Ecto-ATPDase 1
Short name=Ecto-ATPase 1
Ecto-apyrase
Lymphoid cell activation antigen
CD_antigen=CD39
Gene names
Name:ENTPD1
Synonyms:CD39
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well. Ref.10

Catalytic activity

A nucleoside 5'-triphosphate + 2 H2O = a nucleoside 5'-phosphate + 2 phosphate.

Cofactor

Ca2+ or Mg2+. Ref.10

Subunit structure

Homodimer; disulfide-linked By similarity.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

Expressed primarily on activated lymphoid cells. Also expressed in endothelial tissues. Isoform 1 and isoform 3 are present in both placenta and umbilical vein, whereas isoform 2 is present in placenta only.

Post-translational modification

The N-terminus is blocked.

Palmitoylated in the N-terminal part. Ref.12

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0-7.5 with ATP as substrate, and 7.5-8.0 with ADP as substrate.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Magnesium
Nucleotide-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from electronic annotation. Source: Ensembl

G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement Ref.10. Source: ProtInc

cell adhesion

Non-traceable author statement Ref.1. Source: ProtInc

platelet activation

Inferred from electronic annotation. Source: Ensembl

purine ribonucleoside diphosphate catabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasal lamina

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Non-traceable author statement Ref.10. Source: ProtInc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside-diphosphatase activity

Inferred from electronic annotation. Source: Ensembl

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 16478441. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RANBP9Q96S595EBI-8074749,EBI-636085

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49961-1)

Also known as: Vascular;

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: P49961-2)

Also known as: Placental I;

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MEDT → MKGTKDLTSQQ
Isoform 3 (identifier: P49961-3)

Also known as: Placental II;

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MEDT → MKGTKDLTSQQ
     272-299: VASNEILRDPCFHPGYKKVVNVSDLYKT → ASITQSRPAPFTSAPPAPTSCCFLFQIQ
     300-510: Missing.
Isoform 4 (identifier: P49961-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: Missing.
Isoform 5 (identifier: P49961-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.
Isoform 6 (identifier: P49961-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MEDTK → MGREELFLTFSFSSGFQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 510510Ectonucleoside triphosphate diphosphohydrolase 1
PRO_0000209902

Regions

Topological domain1 – 1616Cytoplasmic Potential
Transmembrane17 – 3721Helical; Potential
Topological domain38 – 478441Extracellular Potential
Transmembrane479 – 49921Helical; Potential
Topological domain500 – 51011Cytoplasmic Potential

Sites

Active site1741Proton acceptor By similarity

Amino acid modifications

Lipidation131S-palmitoyl cysteine Probable
Glycosylation731N-linked (GlcNAc...) Ref.13
Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation2921N-linked (GlcNAc...) Ref.13
Glycosylation3341N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential
Disulfide bond84 ↔ 108 By similarity
Disulfide bond255 ↔ 301 By similarity
Disulfide bond282 ↔ 325 By similarity
Disulfide bond338 ↔ 343 By similarity
Disulfide bond390 ↔ 413 By similarity

Natural variations

Alternative sequence1 – 138138Missing in isoform 4.
VSP_044284
Alternative sequence1 – 108108Missing in isoform 5.
VSP_044283
Alternative sequence1 – 55MEDTK → MGREELFLTFSFSSGFQ in isoform 6.
VSP_046050
Alternative sequence1 – 44MEDT → MKGTKDLTSQQ in isoform 2 and isoform 3.
VSP_003607
Alternative sequence272 – 29928VASNE…DLYKT → ASITQSRPAPFTSAPPAPTS CCFLFQIQ in isoform 3.
VSP_003608
Alternative sequence300 – 510211Missing in isoform 3.
VSP_003609
Natural variant2931V → I.
Corresponds to variant rs3793744 [ dbSNP | Ensembl ].
VAR_022099

Experimental info

Sequence conflict57 – 582SS → G AA sequence Ref.9
Sequence conflict1621D → K AA sequence Ref.8
Sequence conflict2081T → TGET AA sequence Ref.9
Sequence conflict2481V → Y AA sequence Ref.9
Sequence conflict4811M → I in BAG62981. Ref.4

Sequences

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

Last modified October 1, 1996. Version 1.
Checksum: BAD87D2499649159

FASTA51057,965
        10         20         30         40         50         60 
MEDTKESNVK TFCSKNILAI LGFSSIIAVI ALLAVGLTQN KALPENVKYG IVLDAGSSHT 

        70         80         90        100        110        120 
SLYIYKWPAE KENDTGVVHQ VEECRVKGPG ISKFVQKVNE IGIYLTDCME RAREVIPRSQ 

       130        140        150        160        170        180 
HQETPVYLGA TAGMRLLRME SEELADRVLD VVERSLSNYP FDFQGARIIT GQEEGAYGWI 

       190        200        210        220        230        240 
TINYLLGKFS QKTRWFSIVP YETNNQETFG ALDLGGASTQ VTFVPQNQTI ESPDNALQFR 

       250        260        270        280        290        300 
LYGKDYNVYT HSFLCYGKDQ ALWQKLAKDI QVASNEILRD PCFHPGYKKV VNVSDLYKTP 

       310        320        330        340        350        360 
CTKRFEMTLP FQQFEIQGIG NYQQCHQSIL ELFNTSYCPY SQCAFNGIFL PPLQGDFGAF 

       370        380        390        400        410        420 
SAFYFVMKFL NLTSEKVSQE KVTEMMKKFC AQPWEEIKTS YAGVKEKYLS EYCFSGTYIL 

       430        440        450        460        470        480 
SLLLQGYHFT ADSWEHIHFI GKIQGSDAGW TLGYMLNLTN MIPAEQPLST PLSHSTYVFL 

       490        500        510 
MVLFSLVLFT VAIIGLLIFH KPSYFWKDMV 

« Hide

Isoform 2 (Placental I) [UniParc].

Checksum: 3E6C59E474010921
Show »

FASTA51758,706
Isoform 3 (Placental II) [UniParc].

Checksum: E0D3B642D3A5A6C8
Show »

FASTA30634,175
Isoform 4 [UniParc].

Checksum: A8B1DE1366356EE3
Show »

FASTA37242,731
Isoform 5 [UniParc].

Checksum: F5CE35BD50FF7DB3
Show »

FASTA40246,180
Isoform 6 [UniParc].

Checksum: 5D160D81F02277B7
Show »

FASTA52259,325

References

« Hide 'large scale' references
[1]"The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization."
Maliszewski C.R., Delespesse G.J.T., Schoenborn M.A., Armitage R.J., Fanslow W.C., Nakajima T., Baker E., Sutherland G.R., Poindexter K., Birks C., Alpert A., Friend D., Gimpel S.D., Gayle R.B. III
J. Immunol. 153:3574-3583(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Loss of ATP diphosphohydrolase activity with endothelial cell activation."
Robson S.C., Kaczmarek E., Siegel J.B., Candinas D., Koziak K., Millan M., Hancock W.W., Bach F.H.
J. Exp. Med. 185:153-163(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Umbilical vein.
[3]"The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II."
Matsumoto M., Sakurai Y., Kokubo T., Yagi H., Makita K., Matsui T., Titani K., Fujimura Y., Narita N.
FEBS Lett. 453:335-340(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Tissue: Placenta.
[4]"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] (ISOFORMS 1; 4; 5 AND 6).
Tissue: Brain, Synovium, Trachea and Uterus.
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM 4).
Tissue: Lung.
[8]"Purification and properties of human placental ATP diphosphohydrolase."
Christoforidis S., Papamarcaki T., Galaris D., Kellner R., Tsolas O.
Eur. J. Biochem. 234:66-74(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 240-242; 162-166; 185-189; 210-223; 243-249 AND 288-297.
Tissue: Placenta.
[9]"Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation."
Makita K., Shimoyama T., Sakurai Y., Yagi H., Matsumoto M., Narita N., Sakamoto Y., Saito S., Ikeda Y., Suzuki M., Titani K., Fujimura Y.
Int. J. Hematol. 68:297-310(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-30; 49-65; 94-97; 88-93; 193-223; 245-265; 382-385 AND 399-405 (ISOFORM 2).
Tissue: Placenta.
[10]"Identification and characterization of CD39/vascular ATP diphosphohydrolase."
Kaczmarek E., Koziak K., Sevigny J., Siegel J.B., Anrather J., Beaudoin A.R., Bach F.H., Robson S.C.
J. Biol. Chem. 271:33116-33122(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COFACTOR.
[11]"CD39 is an ecto-(Ca2+,Mg2+)-apyrase."
Wang T.F., Guidotti G.
J. Biol. Chem. 271:9898-9901(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[12]"Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae."
Koziak K., Kaczmarek E., Kittel A., Sevigny J., Blusztajn J.K., Schulte Am Esch J. II, Imai M., Guckelberger O., Goepfert C., Qawi I., Robson S.C.
J. Biol. Chem. 275:2057-2062(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-13.
[13]"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-73 AND ASN-292.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S73813 mRNA. Translation: AAB32152.1.
U87967 mRNA. Translation: AAB47572.1.
AK304836 mRNA. Translation: BAG65580.1.
AJ133133 mRNA. Translation: CAB41886.1.
AJ133134 mRNA. Translation: CAB41887.1.
AK298648 mRNA. Translation: BAH12835.1.
AK301459 mRNA. Translation: BAG62981.1.
AK304018 mRNA. Translation: BAG64933.1.
AK316009 mRNA. Translation: BAH14380.1.
AL356632, AL365273 Genomic DNA. Translation: CAI16771.1.
AL365273 Genomic DNA. Translation: CAH73752.1.
AL365273, AL356632 Genomic DNA. Translation: CAH73753.1.
AL365273, AL356632 Genomic DNA. Translation: CAH73754.1.
AL356632, AL365273 Genomic DNA. Translation: CAI16770.1.
CH471066 Genomic DNA. Translation: EAW49988.1.
CH471066 Genomic DNA. Translation: EAW49989.1.
CH471066 Genomic DNA. Translation: EAW49990.1.
BC047664 mRNA. Translation: AAH47664.1.
CCDSCCDS41554.1. [P49961-2]
CCDS53556.1. [P49961-6]
CCDS53557.1. [P49961-5]
CCDS53558.1. [P49961-4]
CCDS7444.1. [P49961-1]
PIRI56242.
RefSeqNP_001091645.1. NM_001098175.1. [P49961-2]
NP_001157650.1. NM_001164178.1. [P49961-6]
NP_001157653.1. NM_001164181.1. [P49961-5]
NP_001157654.1. NM_001164182.1. [P49961-4]
NP_001157655.1. NM_001164183.1. [P49961-4]
NP_001767.3. NM_001776.5. [P49961-1]
UniGeneHs.576612.

3D structure databases

ProteinModelPortalP49961.
SMRP49961. Positions 46-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107391. 1 interaction.
IntActP49961. 1 interaction.
MINTMINT-8215689.
STRING9606.ENSP00000360248.

Chemistry

BindingDBP49961.
ChEMBLCHEMBL5722.

PTM databases

PhosphoSiteP49961.

Polymorphism databases

DMDM1705710.

Proteomic databases

MaxQBP49961.
PaxDbP49961.
PRIDEP49961.

Protocols and materials databases

DNASU953.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371203; ENSP00000360246; ENSG00000138185. [P49961-4]
ENST00000371205; ENSP00000360248; ENSG00000138185. [P49961-1]
ENST00000371207; ENSP00000360250; ENSG00000138185. [P49961-6]
ENST00000453258; ENSP00000390955; ENSG00000138185. [P49961-2]
ENST00000539125; ENSP00000440027; ENSG00000138185. [P49961-4]
ENST00000543964; ENSP00000442968; ENSG00000138185. [P49961-5]
GeneID953.
KEGGhsa:953.
UCSCuc001kle.1. human. [P49961-3]
uc001klh.4. human. [P49961-1]
uc001kli.4. human. [P49961-2]
uc010qoj.2. human.

Organism-specific databases

CTD953.
GeneCardsGC10P097505.
HGNCHGNC:3363. ENTPD1.
HPACAB002494.
HPA014067.
MIM601752. gene.
neXtProtNX_P49961.
PharmGKBPA27798.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5371.
HOVERGENHBG018982.
KOK01510.
OMACFSGAYI.
OrthoDBEOG754HPX.
PhylomeDBP49961.
TreeFamTF332859.

Enzyme and pathway databases

BioCycMetaCyc:HS06471-MONOMER.

Gene expression databases

BgeeP49961.
CleanExHS_ENTPD1.
GenevestigatorP49961.

Family and domain databases

InterProIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERPTHR11782. PTHR11782. 1 hit.
PfamPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSENTPD1. human.
GeneWikiENTPD1.
GenomeRNAi953.
NextBio3966.
PROP49961.
SOURCESearch...

Entry information

Entry nameENTP1_HUMAN
AccessionPrimary (citable) accession number: P49961
Secondary accession number(s): A9Z1X8 expand/collapse secondary AC list , B4DWB9, B4E1X1, B7Z599, G3XAF6, Q5T561, Q5T562, Q86VV3, Q9UQQ9, Q9Y3Q9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 142 of the entry and version 1 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 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries