Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ectonucleoside triphosphate diphosphohydrolase 1

Gene

ENTPD1

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

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+1 Publication, 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

GO - Biological processi

  • blood coagulation Source: ProtInc
  • cell adhesion Source: ProtInc
  • G-protein coupled receptor signaling pathway Source: Ensembl
  • platelet activation Source: Ensembl
  • purine ribonucleoside diphosphate catabolic process Source: Ensembl
Complete GO annotation...

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 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:3363. ENTPD1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei17 – 3721HelicalSequence AnalysisAdd
BLAST
Topological domaini38 – 478441ExtracellularSequence AnalysisAdd
BLAST
Transmembranei479 – 49921HelicalSequence AnalysisAdd
BLAST
Topological domaini500 – 51011CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • basal lamina Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • membrane Source: UniProtKB
  • plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Spastic paraplegia 64, autosomal recessive (SPG64)1 Publication

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

Disease descriptionA 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.

See also OMIM:615683
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.
Orphaneti401810. Autosomal recessive spastic paraplegia type 64.
PharmGKBiPA27798.

Polymorphism and mutation databases

BioMutaiENTPD1.
DMDMi1705710.

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.
GenevisibleiP49961. HS.

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. 2 interactions.
IntActiP49961. 1 interaction.
MINTiMINT-8215689.

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the GDA1/CD39 NTPase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5371.
GeneTreeiENSGT00550000074435.
HOGENOMiHOG000059572.
HOVERGENiHBG018982.
InParanoidiP49961.
KOiK01510.
OMAiECKLKGP.
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. AlignAdd to basket

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

        10         20         30         40         50
MEDTKESNVK TFCSKNILAI LGFSSIIAVI ALLAVGLTQN KALPENVKYG
60 70 80 90 100
IVLDAGSSHT SLYIYKWPAE KENDTGVVHQ VEECRVKGPG ISKFVQKVNE
110 120 130 140 150
IGIYLTDCME RAREVIPRSQ HQETPVYLGA TAGMRLLRME SEELADRVLD
160 170 180 190 200
VVERSLSNYP FDFQGARIIT GQEEGAYGWI TINYLLGKFS QKTRWFSIVP
210 220 230 240 250
YETNNQETFG ALDLGGASTQ VTFVPQNQTI ESPDNALQFR LYGKDYNVYT
260 270 280 290 300
HSFLCYGKDQ ALWQKLAKDI QVASNEILRD PCFHPGYKKV VNVSDLYKTP
310 320 330 340 350
CTKRFEMTLP FQQFEIQGIG NYQQCHQSIL ELFNTSYCPY SQCAFNGIFL
360 370 380 390 400
PPLQGDFGAF SAFYFVMKFL NLTSEKVSQE KVTEMMKKFC AQPWEEIKTS
410 420 430 440 450
YAGVKEKYLS EYCFSGTYIL SLLLQGYHFT ADSWEHIHFI GKIQGSDAGW
460 470 480 490 500
TLGYMLNLTN MIPAEQPLST PLSHSTYVFL MVLFSLVLFT VAIIGLLIFH
510
KPSYFWKDMV
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi107391. 2 interactions.
IntActiP49961. 1 interaction.
MINTiMINT-8215689.

Chemistry

BindingDBiP49961.
ChEMBLiCHEMBL5722.

PTM databases

PhosphoSiteiP49961.

Polymorphism and mutation databases

BioMutaiENTPD1.
DMDMi1705710.

Proteomic databases

MaxQBiP49961.
PaxDbiP49961.
PRIDEiP49961.

Protocols and materials databases

DNASUi953.
Structural Biology KnowledgebaseSearch...

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.

Organism-specific databases

CTDi953.
GeneCardsiGC10P097471.
HGNCiHGNC:3363. ENTPD1.
HPAiCAB002494.
HPA014067.
MIMi601752. gene.
615683. phenotype.
neXtProtiNX_P49961.
Orphaneti401810. Autosomal recessive spastic paraplegia type 64.
PharmGKBiPA27798.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5371.
GeneTreeiENSGT00550000074435.
HOGENOMiHOG000059572.
HOVERGENiHBG018982.
InParanoidiP49961.
KOiK01510.
OMAiECKLKGP.
OrthoDBiEOG754HPX.
PhylomeDBiP49961.
TreeFamiTF332859.

Enzyme and pathway databases

BioCyciMetaCyc:HS06471-MONOMER.

Miscellaneous databases

ChiTaRSiENTPD1. human.
GeneWikiiENTPD1.
GenomeRNAii953.
NextBioi3966.
PROiP49961.
SOURCEiSearch...

Gene expression databases

BgeeiP49961.
CleanExiHS_ENTPD1.
GenevisibleiP49961. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 151 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

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.