Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P49961

- ENTP1_HUMAN

UniProt

P49961 - ENTP1_HUMAN

Protein

Ectonucleoside triphosphate diphosphohydrolase 1

Gene

ENTPD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.1 Publication

    Catalytic activityi

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

    Cofactori

    Ca2+ or Mg2+.1 Publication

    pH dependencei

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei174 – 1741Proton acceptorBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. nucleoside-diphosphatase activity Source: Ensembl
    3. nucleoside-triphosphatase activity Source: Ensembl
    4. protein binding Source: IntAct

    GO - Biological processi

    1. ATP catabolic process Source: Ensembl
    2. blood coagulation Source: ProtInc
    3. cell adhesion Source: ProtInc
    4. G-protein coupled receptor signaling pathway Source: Ensembl
    5. platelet activation Source: Ensembl
    6. purine ribonucleoside diphosphate catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    ATP-binding, Calcium, Magnesium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06471-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ectonucleoside triphosphate diphosphohydrolase 1 (EC:3.6.1.5)
    Short name:
    NTPDase 1
    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 namesi
    Name:ENTPD1
    Synonyms:CD39
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:3363. ENTPD1.

    Subcellular locationi

    GO - Cellular componenti

    1. basal lamina Source: Ensembl
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of plasma membrane Source: ProtInc
    4. membrane Source: UniProtKB
    5. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Spastic paraplegia 64, autosomal recessive (SPG64) [MIM:615683]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti210 – 2101G → R in SPG64. 1 Publication
    VAR_071082

    Keywords - Diseasei

    Disease mutation, Hereditary spastic paraplegia, Neurodegeneration

    Organism-specific databases

    MIMi615683. phenotype.
    PharmGKBiPA27798.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 510510Ectonucleoside triphosphate diphosphohydrolase 1PRO_0000209902Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi13 – 131S-palmitoyl cysteine1 Publication
    Glycosylationi73 – 731N-linked (GlcNAc...)1 Publication
    Disulfide bondi84 ↔ 108By similarity
    Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi255 ↔ 301By similarity
    Disulfide bondi282 ↔ 325By similarity
    Glycosylationi292 – 2921N-linked (GlcNAc...)1 Publication
    Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi338 ↔ 343By similarity
    Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi390 ↔ 413By similarity
    Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The N-terminus is blocked.
    Palmitoylated in the N-terminal part.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Proteomic databases

    MaxQBiP49961.
    PaxDbiP49961.
    PRIDEiP49961.

    PTM databases

    PhosphoSiteiP49961.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    BgeeiP49961.
    CleanExiHS_ENTPD1.
    GenevestigatoriP49961.

    Organism-specific databases

    HPAiCAB002494.
    HPA014067.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RANBP9Q96S595EBI-8074749,EBI-636085

    Protein-protein interaction databases

    BioGridi107391. 1 interaction.
    IntActiP49961. 1 interaction.
    MINTiMINT-8215689.
    STRINGi9606.ENSP00000360248.

    Structurei

    3D structure databases

    ProteinModelPortaliP49961.
    SMRiP49961. Positions 46-461.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini38 – 478441ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini500 – 51011CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei17 – 3721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei479 – 49921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GDA1/CD39 NTPase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5371.
    HOVERGENiHBG018982.
    KOiK01510.
    OMAiCFSGAYI.
    OrthoDBiEOG754HPX.
    PhylomeDBiP49961.
    TreeFamiTF332859.

    Family and domain databases

    InterProiIPR000407. GDA1_CD39_NTPase.
    [Graphical view]
    PANTHERiPTHR11782. PTHR11782. 1 hit.
    PfamiPF01150. GDA1_CD39. 1 hit.
    [Graphical view]
    PROSITEiPS01238. GDA1_CD39_NTPASE. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49961-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEDTKESNVK TFCSKNILAI LGFSSIIAVI ALLAVGLTQN KALPENVKYG    50
    IVLDAGSSHT SLYIYKWPAE KENDTGVVHQ VEECRVKGPG ISKFVQKVNE 100
    IGIYLTDCME RAREVIPRSQ HQETPVYLGA TAGMRLLRME SEELADRVLD 150
    VVERSLSNYP FDFQGARIIT GQEEGAYGWI TINYLLGKFS QKTRWFSIVP 200
    YETNNQETFG ALDLGGASTQ VTFVPQNQTI ESPDNALQFR LYGKDYNVYT 250
    HSFLCYGKDQ ALWQKLAKDI QVASNEILRD PCFHPGYKKV VNVSDLYKTP 300
    CTKRFEMTLP FQQFEIQGIG NYQQCHQSIL ELFNTSYCPY SQCAFNGIFL 350
    PPLQGDFGAF SAFYFVMKFL NLTSEKVSQE KVTEMMKKFC AQPWEEIKTS 400
    YAGVKEKYLS EYCFSGTYIL SLLLQGYHFT ADSWEHIHFI GKIQGSDAGW 450
    TLGYMLNLTN MIPAEQPLST PLSHSTYVFL MVLFSLVLFT VAIIGLLIFH 500
    KPSYFWKDMV 510
    Length:510
    Mass (Da):57,965
    Last modified:October 1, 1996 - v1
    Checksum:iBAD87D2499649159
    GO
    Isoform 2 (identifier: P49961-2) [UniParc]FASTAAdd to Basket

    Also known as: Placental I

    The sequence of this isoform differs from the canonical sequence as follows:
         1-4: MEDT → MKGTKDLTSQQ

    Show »
    Length:517
    Mass (Da):58,706
    Checksum:i3E6C59E474010921
    GO
    Isoform 3 (identifier: P49961-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:306
    Mass (Da):34,175
    Checksum:iE0D3B642D3A5A6C8
    GO
    Isoform 4 (identifier: P49961-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-138: Missing.

    Show »
    Length:372
    Mass (Da):42,731
    Checksum:iA8B1DE1366356EE3
    GO
    Isoform 5 (identifier: P49961-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-108: Missing.

    Show »
    Length:402
    Mass (Da):46,180
    Checksum:iF5CE35BD50FF7DB3
    GO
    Isoform 6 (identifier: P49961-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-5: MEDTK → MGREELFLTFSFSSGFQ

    Note: No experimental confirmation available.

    Show »
    Length:522
    Mass (Da):59,325
    Checksum:i5D160D81F02277B7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti57 – 582SS → G AA sequence (PubMed:9846014)Curated
    Sequence conflicti162 – 1621D → K AA sequence (PubMed:8529670)Curated
    Sequence conflicti208 – 2081T → TGET AA sequence (PubMed:9846014)Curated
    Sequence conflicti248 – 2481V → Y AA sequence (PubMed:9846014)Curated
    Sequence conflicti481 – 4811M → I in BAG62981. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti210 – 2101G → R in SPG64. 1 Publication
    VAR_071082
    Natural varianti293 – 2931V → I.
    Corresponds to variant rs3793744 [ dbSNP | Ensembl ].
    VAR_022099

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 138138Missing in isoform 4. 2 PublicationsVSP_044284Add
    BLAST
    Alternative sequencei1 – 108108Missing in isoform 5. 1 PublicationVSP_044283Add
    BLAST
    Alternative sequencei1 – 55MEDTK → MGREELFLTFSFSSGFQ in isoform 6. 1 PublicationVSP_046050
    Alternative sequencei1 – 44MEDT → MKGTKDLTSQQ in isoform 2 and isoform 3. 1 PublicationVSP_003607
    Alternative sequencei272 – 29928VASNE…DLYKT → ASITQSRPAPFTSAPPAPTS CCFLFQIQ in isoform 3. 1 PublicationVSP_003608Add
    BLAST
    Alternative sequencei300 – 510211Missing in isoform 3. 1 PublicationVSP_003609Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS41554.1. [P49961-2]
    CCDS53556.1. [P49961-6]
    CCDS53557.1. [P49961-5]
    CCDS53558.1. [P49961-4]
    CCDS7444.1. [P49961-1]
    PIRiI56242.
    RefSeqiNP_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]
    UniGeneiHs.576612.

    Genome annotation databases

    EnsembliENST00000371203; 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]
    GeneIDi953.
    KEGGihsa:953.
    UCSCiuc001kle.1. human. [P49961-3]
    uc001klh.4. human. [P49961-1]
    uc001kli.4. human. [P49961-2]
    uc010qoj.2. human.

    Polymorphism databases

    DMDMi1705710.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS41554.1. [P49961-2 ]
    CCDS53556.1. [P49961-6 ]
    CCDS53557.1. [P49961-5 ]
    CCDS53558.1. [P49961-4 ]
    CCDS7444.1. [P49961-1 ]
    PIRi I56242.
    RefSeqi NP_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 ]
    UniGenei Hs.576612.

    3D structure databases

    ProteinModelPortali P49961.
    SMRi P49961. Positions 46-461.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107391. 1 interaction.
    IntActi P49961. 1 interaction.
    MINTi MINT-8215689.
    STRINGi 9606.ENSP00000360248.

    Chemistry

    BindingDBi P49961.
    ChEMBLi CHEMBL5722.

    PTM databases

    PhosphoSitei P49961.

    Polymorphism databases

    DMDMi 1705710.

    Proteomic databases

    MaxQBi P49961.
    PaxDbi P49961.
    PRIDEi P49961.

    Protocols and materials databases

    DNASUi 953.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371203 ; 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 ]
    GeneIDi 953.
    KEGGi hsa:953.
    UCSCi uc001kle.1. human. [P49961-3 ]
    uc001klh.4. human. [P49961-1 ]
    uc001kli.4. human. [P49961-2 ]
    uc010qoj.2. human.

    Organism-specific databases

    CTDi 953.
    GeneCardsi GC10P097505.
    HGNCi HGNC:3363. ENTPD1.
    HPAi CAB002494.
    HPA014067.
    MIMi 601752. gene.
    615683. phenotype.
    neXtProti NX_P49961.
    PharmGKBi PA27798.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5371.
    HOVERGENi HBG018982.
    KOi K01510.
    OMAi CFSGAYI.
    OrthoDBi EOG754HPX.
    PhylomeDBi P49961.
    TreeFami TF332859.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06471-MONOMER.

    Miscellaneous databases

    ChiTaRSi ENTPD1. human.
    GeneWikii ENTPD1.
    GenomeRNAii 953.
    NextBioi 3966.
    PROi P49961.
    SOURCEi Search...

    Gene expression databases

    Bgeei P49961.
    CleanExi HS_ENTPD1.
    Genevestigatori P49961.

    Family and domain databases

    InterProi IPR000407. GDA1_CD39_NTPase.
    [Graphical view ]
    PANTHERi PTHR11782. PTHR11782. 1 hit.
    Pfami PF01150. GDA1_CD39. 1 hit.
    [Graphical view ]
    PROSITEi PS01238. GDA1_CD39_NTPASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. Cited for: CHARACTERIZATION.
    12. 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.
    14. Cited for: VARIANT SPG64 ARG-210.

    Entry informationi

    Entry nameiENTP1_HUMAN
    AccessioniPrimary (citable) accession number: P49961
    Secondary accession number(s): A9Z1X8
    , B4DWB9, B4E1X1, B7Z599, G3XAF6, Q5T561, Q5T562, Q86VV3, Q9UQQ9, Q9Y3Q9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 144 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

    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 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3