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Q13822

- ENPP2_HUMAN

UniProt

Q13822 - ENPP2_HUMAN

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Protein
Ectonucleotide pyrophosphatase/phosphodiesterase family member 2
Gene
ENPP2, ATX, PDNP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Hydrolyzes lysophospholipids to produce lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine. Also can act on sphingosylphosphphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development. Tumor cell motility-stimulating factor.4 Publications

Catalytic activityi

1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine.1 Publication

Cofactori

Binds 2 zinc ions per subunit By similarity.
Binds 1 calcium ion per subunit By similarity.

Enzyme regulationi

Inhibited by lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P). Inhibited by EDTA and EGTA Inferred.3 Publications

Kineticsi

  1. KM=0.5 mM for 16:0-LPC (at pH 8.5)2 Publications
  2. KM=5.5 mM for pNP-TMP (at pH 8.5)
  3. KM=11.3 mM for pNppp (isoform 1)
  4. KM=5.7 mM for pNppp (isoform 2)
  5. KM=19.8 mM for pNppp (isoform 3)

Vmax=1.9 nmol/min/µg enzyme with pNppp as substrate (isoform 1)

Vmax=0.67 nmol/min/µg enzyme with pNppp as substrate (isoform 2)

Vmax=1.6 nmol/min/µg enzyme with pNppp as substrate (isoform 3)

pH dependencei

Optimum pH is 9.0 (isoform 1), 8.0 (isoform 3). Isoform 1 is less sensitive to pH. Isoform 1, isoform 2 and isoform 3 all retain some activity at pH 9.5.

Temperature dependencei

Isoform 1 and isoform 3 are active from 45 to 60 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi172 – 1721Zinc 1; catalytic By similarity
Active sitei210 – 2101Nucleophile By similarity
Metal bindingi210 – 2101Zinc 1; catalytic By similarity
Binding sitei231 – 2311Substrate By similarity
Binding sitei307 – 3071Substrate By similarity
Metal bindingi312 – 3121Zinc 2; catalytic By similarity
Metal bindingi316 – 3161Zinc 2; catalytic By similarity
Metal bindingi316 – 3161Zinc 2; via tele nitrogen; catalytic By similarity
Metal bindingi359 – 3591Zinc 1; catalytic By similarity
Metal bindingi360 – 3601Zinc 1; catalytic By similarity
Metal bindingi360 – 3601Zinc 1; via tele nitrogen; catalytic By similarity
Metal bindingi475 – 4751Zinc 2; catalytic By similarity
Metal bindingi475 – 4751Zinc 2; via tele nitrogen; catalytic By similarity
Metal bindingi740 – 7401Calcium By similarity
Metal bindingi744 – 7441Calcium By similarity
Metal bindingi746 – 7461Calcium; via carbonyl oxygen By similarity
Metal bindingi748 – 7481Calcium By similarity
Sitei853 – 8531Essential for catalytic activity By similarity

GO - Molecular functioni

  1. alkylglycerophosphoethanolamine phosphodiesterase activity Source: UniProtKB-EC
  2. calcium ion binding Source: UniProtKB
  3. hydrolase activity Source: UniProtKB
  4. lysophospholipase activity Source: UniProtKB
  5. nucleic acid binding Source: InterPro
  6. nucleotide diphosphatase activity Source: ProtInc
  7. phosphodiesterase I activity Source: ProtInc
  8. polysaccharide binding Source: InterPro
  9. scavenger receptor activity Source: InterPro
  10. transcription factor binding Source: ProtInc
  11. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: ProtInc
  2. cellular component movement Source: ProtInc
  3. chemotaxis Source: UniProtKB
  4. immune response Source: InterPro
  5. nucleic acid phosphodiester bond hydrolysis Source: GOC
  6. phosphate-containing compound metabolic process Source: ProtInc
  7. phosphatidylcholine catabolic process Source: UniProtKB
  8. phospholipid catabolic process Source: UniProt
  9. regulation of cell migration Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Chemotaxis, Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKQ13822.

Names & Taxonomyi

Protein namesi
Recommended name:
Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 (EC:3.1.4.39)
Short name:
E-NPP 2
Alternative name(s):
Autotaxin
Extracellular lysophospholipase D
Short name:
LysoPLD
Gene namesi
Name:ENPP2
Synonyms:ATX, PDNP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:3357. ENPP2.

Subcellular locationi

Secreted
Note: Secreted by most body fluids including serum and CSF. Also by adipocytes and numerous cancer cells.1 Publication

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
  2. integral component of plasma membrane Source: ProtInc
  3. plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi170 – 1701S → E: Reduces lysophospholipase activity by about 70%.
Mutagenesisi210 – 2101T → A: Loss of lysophospholipase activity. 1 Publication
Mutagenesisi211 – 2111F → Y: Reduces lysophospholipase activity by about 70%. 1 Publication
Mutagenesisi218 – 2181A → V: Reduces lysophospholipase activity by about 50%. 1 Publication
Mutagenesisi231 – 2311N → A: Strongly reduced lysophospholipase activity. 1 Publication
Mutagenesisi307 – 3071Y → Q: Reduces lysophospholipase activity by about 70%. 1 Publication

Keywords - Diseasei

Obesity

Organism-specific databases

PharmGKBiPA27792.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727 By similarity
Add
BLAST
Propeptidei28 – 358Removed by furin
PRO_0000281649
Chaini36 – 863828Ectonucleotide pyrophosphatase/phosphodiesterase family member 2
PRO_0000188567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi54 – 541N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi59 ↔ 76 By similarity
Disulfide bondi63 ↔ 94 By similarity
Disulfide bondi74 ↔ 87 By similarity
Disulfide bondi80 ↔ 86 By similarity
Disulfide bondi103 ↔ 120 By similarity
Disulfide bondi108 ↔ 138 By similarity
Disulfide bondi118 ↔ 131 By similarity
Disulfide bondi124 ↔ 130 By similarity
Disulfide bondi149 ↔ 195 By similarity
Disulfide bondi157 ↔ 351 By similarity
Disulfide bondi367 ↔ 469 By similarity
Glycosylationi411 – 4111N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi414 ↔ 806 By similarity
Glycosylationi525 – 5251N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi567 ↔ 667 By similarity
Disulfide bondi569 ↔ 652 By similarity
Disulfide bondi775 ↔ 785 By similarity
Glycosylationi807 – 8071N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

N-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity By similarity.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ13822.
PRIDEiQ13822.

PTM databases

PhosphoSiteiQ13822.

Expressioni

Tissue specificityi

Predominantly expressed in brain, placenta, ovary, and small intestine. Expressed in a number of carcinomas such as hepatocellular and prostate carcinoma, neuroblastoma and non-small-cell lung cancer. Expressed in body fluids such as plasma, cerebral spinal fluid (CSF), saliva, follicular and amniotic fluids. Not detected in leukocytes. Isoform 1 is more highly expressed in peripheral tissues than in the central nervous system (CNS). Adipocytes only express isoform 1. Isoform 3 is more highly expressed in the brain than in peripheral tissues.3 Publications

Inductioni

Up-regulated in massively obese subjects with glucose intolerance, and during adipogenesis.4 Publications

Gene expression databases

ArrayExpressiQ13822.
BgeeiQ13822.
CleanExiHS_ENPP2.
GenevestigatoriQ13822.

Organism-specific databases

HPAiHPA023700.

Interactioni

Protein-protein interaction databases

BioGridi111194. 2 interactions.
IntActiQ13822. 1 interaction.
MINTiMINT-7969086.

Structurei

3D structure databases

ProteinModelPortaliQ13822.
SMRiQ13822. Positions 52-860.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 9844SMB 1
Add
BLAST
Domaini99 – 14345SMB 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni211 – 2144Substrate binding By similarity
Regioni244 – 25512Substrate binding By similarity
Add
BLAST
Regioni830 – 85122Required for secretion By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi127 – 1293Cell attachment site Reviewed prediction

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG1524.
HOVERGENiHBG051484.
KOiK01122.
OMAiGYGPTFK.
OrthoDBiEOG7XM2X4.
PhylomeDBiQ13822.
TreeFamiTF330032.

Family and domain databases

Gene3Di3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR024873. E-NPP.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PfamiPF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 2 hits.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13822-1) [UniParc]FASTAAdd to Basket

Also known as: ATXter, Beta

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

MARRSSFQSC QIISLFTFAV GVNICLGFTA HRIKRAEGWE EGPPTVLSDS    50
PWTNISGSCK GRCFELQEAG PPDCRCDNLC KSYTSCCHDF DELCLKTARG 100
WECTKDRCGE VRNEENACHC SEDCLARGDC CTNYQVVCKG ESHWVDDDCE 150
EIKAAECPAG FVRPPLIIFS VDGFRASYMK KGSKVMPNIE KLRSCGTHSP 200
YMRPVYPTKT FPNLYTLATG LYPESHGIVG NSMYDPVFDA TFHLRGREKF 250
NHRWWGGQPL WITATKQGVK AGTFFWSVVI PHERRILTIL QWLTLPDHER 300
PSVYAFYSEQ PDFSGHKYGP FGPEMTNPLR EIDKIVGQLM DGLKQLKLHR 350
CVNVIFVGDH GMEDVTCDRT EFLSNYLTNV DDITLVPGTL GRIRSKFSNN 400
AKYDPKAIIA NLTCKKPDQH FKPYLKQHLP KRLHYANNRR IEDIHLLVER 450
RWHVARKPLD VYKKPSGKCF FQGDHGFDNK VNSMQTVFVG YGSTFKYKTK 500
VPPFENIELY NVMCDLLGLK PAPNNGTHGS LNHLLRTNTF RPTMPEEVTR 550
PNYPGIMYLQ SDFDLGCTCD DKVEPKNKLD ELNKRLHTKG STEERHLLYG 600
RPAVLYRTRY DILYHTDFES GYSEIFLMPL WTSYTVSKQA EVSSVPDHLT 650
SCVRPDVRVS PSFSQNCLAY KNDKQMSYGF LFPPYLSSSP EAKYDAFLVT 700
NMVPMYPAFK RVWNYFQRVL VKKYASERNG VNVISGPIFD YDYDGLHDTE 750
DKIKQYVEGS SIPVPTHYYS IITSCLDFTQ PADKCDGPLS VSSFILPHRP 800
DNEESCNSSE DESKWVEELM KMHTARVRDI EHLTSLDFFR KTSRSYPEIL 850
TLKTYLHTYE SEI 863
Length:863
Mass (Da):98,994
Last modified:March 2, 2010 - v3
Checksum:i94A7A2B3701F0993
GO
Isoform 2 (identifier: Q13822-2) [UniParc]FASTAAdd to Basket

Also known as: ATXmel, Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     324-324: E → EESSYGSPFTPAKRPKRKVAPKRRQERPVAPPKKRRRKIHRMDHYAAETRQDK

Show »
Length:915
Mass (Da):105,201
Checksum:i30C7CB1E60101B75
GO
Isoform 3 (identifier: Q13822-3) [UniParc]FASTAAdd to Basket

Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     593-593: E → EAETRKFRGSRNENKENINGNFEPRK

Show »
Length:888
Mass (Da):101,968
Checksum:i17A8986783028C4D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti493 – 4931S → P.7 Publications
Corresponds to variant rs10283100 [ dbSNP | Ensembl ].
VAR_060469
Natural varianti577 – 5771N → S.
Corresponds to variant rs2289886 [ dbSNP | Ensembl ].
VAR_057472
Natural varianti726 – 7261S → L.
Corresponds to variant rs16892767 [ dbSNP | Ensembl ].
VAR_057473

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei324 – 3241E → EESSYGSPFTPAKRPKRKVA PKRRQERPVAPPKKRRRKIH RMDHYAAETRQDK in isoform 2.
VSP_006750
Alternative sequencei593 – 5931E → EAETRKFRGSRNENKENING NFEPRK in isoform 3.
VSP_036398

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231N → S in AAA64785. 1 Publication
Sequence conflicti23 – 231N → S in ABW38316. 1 Publication
Sequence conflicti73 – 731D → H in BAA08260. 1 Publication
Sequence conflicti100 – 1001G → A in AAB00855. 1 Publication
Sequence conflicti291 – 2911Q → R in AAA64785. 1 Publication
Sequence conflicti291 – 2911Q → R in ABW38316. 1 Publication
Sequence conflicti349 – 3491H → R in AAA64785. 1 Publication
Sequence conflicti349 – 3491H → R in ABW38316. 1 Publication
Sequence conflicti457 – 4571K → P AA sequence 1 Publication
Sequence conflicti501 – 5011V → S AA sequence 1 Publication
Sequence conflicti508 – 5081E → N AA sequence 1 Publication
Sequence conflicti554 – 5541P → L AA sequence 1 Publication
Sequence conflicti629 – 6291P → L in AAA64785. 1 Publication
Sequence conflicti629 – 6291P → L in ABW38316. 1 Publication
Sequence conflicti644 – 6441S → R in BAA08260. 1 Publication
Sequence conflicti703 – 7031V → A in BAA08260. 1 Publication
Sequence conflicti769 – 7691Y → H in BAA08260. 1 Publication
Isoform 3 (identifier: Q13822-3)
Sequence conflicti23 – 231N → S in ABW38316. 1 Publication
Sequence conflicti291 – 2911Q → R in ABW38316. 1 Publication
Sequence conflicti349 – 3491H → R in ABW38316. 1 Publication
Sequence conflicti493 – 4931S → P in ABW38316. 1 Publication
Sequence conflicti599 – 5991F → Y in ABW38316. 1 Publication
Sequence conflicti602 – 6021S → T in ABW38316. 1 Publication
Sequence conflicti654 – 6541P → L in ABW38316. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L35594 mRNA. Translation: AAA64785.1.
D45421 mRNA. Translation: BAA08260.1.
D45914 Genomic DNA. Translation: BAA08342.1.
L46720 mRNA. Translation: AAB00855.1.
EU131011 mRNA. Translation: ABW38316.2.
AC099818 Genomic DNA. No translation available.
AC107960 Genomic DNA. No translation available.
BC034961 mRNA. Translation: AAH34961.1.
CCDSiCCDS34936.1. [Q13822-1]
CCDS47914.1. [Q13822-3]
CCDS6329.1. [Q13822-2]
PIRiA55144.
RefSeqiNP_001035181.1. NM_001040092.2. [Q13822-1]
NP_001124335.1. NM_001130863.2. [Q13822-3]
NP_006200.3. NM_006209.4. [Q13822-2]
UniGeneiHs.190977.

Genome annotation databases

EnsembliENST00000075322; ENSP00000075322; ENSG00000136960. [Q13822-1]
ENST00000259486; ENSP00000259486; ENSG00000136960. [Q13822-2]
ENST00000522826; ENSP00000428291; ENSG00000136960. [Q13822-3]
GeneIDi5168.
KEGGihsa:5168.
UCSCiuc003yos.2. human. [Q13822-2]
uc003yot.2. human. [Q13822-1]

Polymorphism databases

DMDMi290457674.

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:
EMBL
GenBank
DDBJ
Links Updated
L35594 mRNA. Translation: AAA64785.1 .
D45421 mRNA. Translation: BAA08260.1 .
D45914 Genomic DNA. Translation: BAA08342.1 .
L46720 mRNA. Translation: AAB00855.1 .
EU131011 mRNA. Translation: ABW38316.2 .
AC099818 Genomic DNA. No translation available.
AC107960 Genomic DNA. No translation available.
BC034961 mRNA. Translation: AAH34961.1 .
CCDSi CCDS34936.1. [Q13822-1 ]
CCDS47914.1. [Q13822-3 ]
CCDS6329.1. [Q13822-2 ]
PIRi A55144.
RefSeqi NP_001035181.1. NM_001040092.2. [Q13822-1 ]
NP_001124335.1. NM_001130863.2. [Q13822-3 ]
NP_006200.3. NM_006209.4. [Q13822-2 ]
UniGenei Hs.190977.

3D structure databases

ProteinModelPortali Q13822.
SMRi Q13822. Positions 52-860.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111194. 2 interactions.
IntActi Q13822. 1 interaction.
MINTi MINT-7969086.

Chemistry

ChEMBLi CHEMBL3691.

PTM databases

PhosphoSitei Q13822.

Polymorphism databases

DMDMi 290457674.

Proteomic databases

PaxDbi Q13822.
PRIDEi Q13822.

Protocols and materials databases

DNASUi 5168.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000075322 ; ENSP00000075322 ; ENSG00000136960 . [Q13822-1 ]
ENST00000259486 ; ENSP00000259486 ; ENSG00000136960 . [Q13822-2 ]
ENST00000522826 ; ENSP00000428291 ; ENSG00000136960 . [Q13822-3 ]
GeneIDi 5168.
KEGGi hsa:5168.
UCSCi uc003yos.2. human. [Q13822-2 ]
uc003yot.2. human. [Q13822-1 ]

Organism-specific databases

CTDi 5168.
GeneCardsi GC08M120569.
H-InvDB HIX0025550.
HGNCi HGNC:3357. ENPP2.
HPAi HPA023700.
MIMi 601060. gene.
neXtProti NX_Q13822.
PharmGKBi PA27792.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1524.
HOVERGENi HBG051484.
KOi K01122.
OMAi GYGPTFK.
OrthoDBi EOG7XM2X4.
PhylomeDBi Q13822.
TreeFami TF330032.

Enzyme and pathway databases

SABIO-RK Q13822.

Miscellaneous databases

ChiTaRSi ENPP2. human.
GeneWikii Autotaxin.
GenomeRNAii 5168.
NextBioi 19994.
PROi Q13822.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13822.
Bgeei Q13822.
CleanExi HS_ENPP2.
Genevestigatori Q13822.

Family and domain databases

Gene3Di 3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR024873. E-NPP.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view ]
PANTHERi PTHR10151. PTHR10151. 1 hit.
Pfami PF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 2 hits.
PF01033. Somatomedin_B. 2 hits.
[Graphical view ]
PRINTSi PR00022. SOMATOMEDINB.
SMARTi SM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view ]
SUPFAMi SSF53649. SSF53649. 1 hit.
PROSITEi PS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of the human tumor motility-stimulating protein, autotaxin, reveals a homology with phosphodiesterases."
    Murata J., Lee H.Y., Clair T., Krutzsch H.C., Arestad A.A., Sobel M.E., Liotta L.A., Stracke M.L.
    J. Biol. Chem. 269:30479-30484(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, VARIANT PRO-493.
    Tissue: Melanoma.
  2. "Molecular cloning and chromosomal assignment of the human brain-type phosphodiesterase I/nucleotide pyrophosphatase gene (PDNP2)."
    Kawagoe H., Soma O., Goji J., Nishimura N., Narita M., Inazawa J., Nakamura H., Sano K.
    Genomics 30:380-384(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45, TISSUE SPECIFICITY, VARIANT PRO-493.
  3. "Cloning, chromosomal localization, and tissue expression of autotaxin from human teratocarcinoma cells."
    Lee H.Y., Murata J., Clair T., Polymeropoulos M.H., Torres R., Manrow R.E., Liotta L.A., Stracke M.L.
    Biochem. Biophys. Res. Commun. 218:714-719(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT PRO-493.
    Tissue: Teratocarcinoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, ENZYME REGULATION, VARIANT PRO-493.
  5. "Murine and human autotaxin alpha, beta, and gamma isoforms: gene organization, tissue distribution, and biochemical characterization."
    Giganti A., Rodriguez M., Fould B., Moulharat N., Coge F., Chomarat P., Galizzi J.-P., Valet P., Saulnier-Blache J.-S., Boutin J.A., Ferry G.
    J. Biol. Chem. 283:7776-7789(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), PROTEIN SEQUENCE OF 36-42 AND 49-54, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, VARIANT PRO-493.
    Tissue: Brain and Melanoma.
  6. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    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 1), VARIANT PRO-493.
    Tissue: Testis.
  8. "Identification of human plasma lysophospholipase D, a lysophosphatidic acid-producing enzyme, as autotaxin, a multifunctional phosphodiesterase."
    Tokumura A., Majima E., Kariya Y., Tominaga K., Kogure K., Yasuda K., Fukuzawa K.
    J. Biol. Chem. 277:39436-39442(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 36-49; 318-330; 335-344; 440-450 AND 854-863, IDENTIFICATION, BIOPHYSICOCHEMICAL PROPERTIES.
  9. "Identification, purification, and partial sequence analysis of autotaxin, a novel motility-stimulating protein."
    Stracke M.L., Krutzsch H.C., Unsworth E.J., Aarestad A., Cioce V., Schiffmann E., Liotta L.A.
    J. Biol. Chem. 267:2524-2529(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 256-266; 370-392; 457-463; 481-496; 501-510; 545-554; 639-643; 706-710 AND 829-840, FUNCTION, VARIANT PRO-493.
    Tissue: Melanoma.
  10. "Autotaxin (NPP-2), a metastasis-enhancing mitogen, is an angiogenic factor."
    Nam S.W., Clair T., Kim Y.S., McMarlin A., Schiffmann E., Liotta L.A., Stracke M.L.
    Cancer Res. 61:6938-6944(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANGIOGENESIS.
  11. "Potential involvement of adipocyte insulin resistance in obesity-associated up-regulation of adipocyte lysophospholipase D/autotaxin expression."
    Boucher J., Quilliot D., Pradere J.P., Simon M.F., Gres S., Guigne C., Prevot D., Ferry G., Boutin J.A., Carpene C., Valet P., Saulnier-Blache J.S.
    Diabetologia 48:569-577(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, POSSIBLE FUNCTION IN OBESITY.
  12. Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, MUTAGENESIS OF THR-210; PHE-211; ALA-218; ASN-231 AND TYR-307.

Entry informationi

Entry nameiENPP2_HUMAN
AccessioniPrimary (citable) accession number: Q13822
Secondary accession number(s): A8UHA1
, E9PHP7, Q13827, Q14555, Q15117, Q9UCQ8, Q9UCR0, Q9UCR1, Q9UCR2, Q9UCR3, Q9UCR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 2, 2010
Last modified: July 9, 2014
This is version 136 of the entry and version 3 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 chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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