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Q13822 (ENPP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ectonucleotide pyrophosphatase/phosphodiesterase family member 2

Short name=E-NPP 2
EC=3.1.4.39
Alternative name(s):
Autotaxin
Extracellular lysophospholipase D
Short name=LysoPLD
Gene names
Name:ENPP2
Synonyms:ATX, PDNP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length863 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10 Ref.11 Ref.12

Catalytic activity

1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine. Ref.12

Cofactor

Binds 2 zinc ions per subunit By similarity.

Binds 1 calcium ion per subunit By similarity.

Enzyme regulation

Inhibited by lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P). Inhibited by EDTA and EGTA Probable. Ref.4 Ref.5 Ref.12

Subcellular location

Secreted. Note: Secreted by most body fluids including serum and CSF. Also by adipocytes and numerous cancer cells. Ref.4

Tissue specificity

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. Ref.2 Ref.3 Ref.5

Induction

Up-regulated in massively obese subjects with glucose intolerance, and during adipogenesis. Ref.4 Ref.5 Ref.11 Ref.12

Post-translational modification

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

Sequence similarities

Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.

Contains 2 SMB (somatomedin-B) domains.

Biophysicochemical properties

Kinetic parameters:

KM=0.5 mM for 16:0-LPC (at pH 8.5) Ref.5 Ref.8

KM=5.5 mM for pNP-TMP (at pH 8.5)

KM=11.3 mM for pNppp (isoform 1)

KM=5.7 mM for pNppp (isoform 2)

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 dependence:

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 dependence:

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

Ontologies

Keywords
   Biological processChemotaxis
Lipid degradation
Lipid metabolism
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseObesity
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement Ref.9. Source: ProtInc

cellular component movement

Traceable author statement Ref.9. Source: ProtInc

chemotaxis

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

immune response

Inferred from electronic annotation. Source: InterPro

nucleic acid phosphodiester bond hydrolysis

Traceable author statement Ref.1. Source: GOC

phosphate-containing compound metabolic process

Traceable author statement Ref.3. Source: ProtInc

phosphatidylcholine catabolic process

Inferred from direct assay Ref.12. Source: UniProtKB

phospholipid catabolic process

Inferred from direct assay PubMed 15280042. Source: UniProt

regulation of cell migration

Inferred from direct assay Ref.9. Source: UniProtKB

   Cellular_componentextracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.9. Source: ProtInc

plasma membrane

Traceable author statement Ref.3. Source: ProtInc

   Molecular_functionalkylglycerophosphoethanolamine phosphodiesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

calcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

hydrolase activity

Traceable author statement Ref.1. Source: UniProtKB

lysophospholipase activity

Inferred from direct assay Ref.12. Source: UniProtKB

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

nucleotide diphosphatase activity

Traceable author statement Ref.3. Source: ProtInc

phosphodiesterase I activity

Traceable author statement Ref.1. Source: ProtInc

polysaccharide binding

Inferred from electronic annotation. Source: InterPro

scavenger receptor activity

Inferred from electronic annotation. Source: InterPro

transcription factor binding

Traceable author statement Ref.2. Source: ProtInc

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13822-1)

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.
Isoform 2 (identifier: Q13822-2)

Also known as: ATXmel; Alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     324-324: E → EESSYGSPFTPAKRPKRKVAPKRRQERPVAPPKKRRRKIHRMDHYAAETRQDK
Isoform 3 (identifier: Q13822-3)

Also known as: Gamma;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 By similarity
Propeptide28 – 358Removed by furin
PRO_0000281649
Chain36 – 863828Ectonucleotide pyrophosphatase/phosphodiesterase family member 2
PRO_0000188567

Regions

Domain55 – 9844SMB 1
Domain99 – 14345SMB 2
Region211 – 2144Substrate binding By similarity
Region244 – 25512Substrate binding By similarity
Region830 – 85122Required for secretion By similarity
Motif127 – 1293Cell attachment site Potential

Sites

Active site2101Nucleophile By similarity
Metal binding1721Zinc 1; catalytic By similarity
Metal binding2101Zinc 1; catalytic By similarity
Metal binding3121Zinc 2; catalytic By similarity
Metal binding3161Zinc 2; catalytic By similarity
Metal binding3161Zinc 2; via tele nitrogen; catalytic By similarity
Metal binding3591Zinc 1; catalytic By similarity
Metal binding3601Zinc 1; catalytic By similarity
Metal binding3601Zinc 1; via tele nitrogen; catalytic By similarity
Metal binding4751Zinc 2; catalytic By similarity
Metal binding4751Zinc 2; via tele nitrogen; catalytic By similarity
Metal binding7401Calcium By similarity
Metal binding7441Calcium By similarity
Metal binding7461Calcium; via carbonyl oxygen By similarity
Metal binding7481Calcium By similarity
Binding site2311Substrate By similarity
Binding site3071Substrate By similarity
Site8531Essential for catalytic activity By similarity

Amino acid modifications

Glycosylation541N-linked (GlcNAc...) Potential
Glycosylation4111N-linked (GlcNAc...) Potential
Glycosylation5251N-linked (GlcNAc...) Potential
Glycosylation8071N-linked (GlcNAc...) Potential
Disulfide bond59 ↔ 76 By similarity
Disulfide bond63 ↔ 94 By similarity
Disulfide bond74 ↔ 87 By similarity
Disulfide bond80 ↔ 86 By similarity
Disulfide bond103 ↔ 120 By similarity
Disulfide bond108 ↔ 138 By similarity
Disulfide bond118 ↔ 131 By similarity
Disulfide bond124 ↔ 130 By similarity
Disulfide bond149 ↔ 195 By similarity
Disulfide bond157 ↔ 351 By similarity
Disulfide bond367 ↔ 469 By similarity
Disulfide bond414 ↔ 806 By similarity
Disulfide bond567 ↔ 667 By similarity
Disulfide bond569 ↔ 652 By similarity
Disulfide bond775 ↔ 785 By similarity

Natural variations

Alternative sequence3241E → EESSYGSPFTPAKRPKRKVA PKRRQERPVAPPKKRRRKIH RMDHYAAETRQDK in isoform 2.
VSP_006750
Alternative sequence5931E → EAETRKFRGSRNENKENING NFEPRK in isoform 3.
VSP_036398
Natural variant4931S → P. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.9
Corresponds to variant rs10283100 [ dbSNP | Ensembl ].
VAR_060469
Natural variant5771N → S.
Corresponds to variant rs2289886 [ dbSNP | Ensembl ].
VAR_057472
Natural variant7261S → L.
Corresponds to variant rs16892767 [ dbSNP | Ensembl ].
VAR_057473

Experimental info

Mutagenesis1701S → E: Reduces lysophospholipase activity by about 70%.
Mutagenesis2101T → A: Loss of lysophospholipase activity. Ref.12
Mutagenesis2111F → Y: Reduces lysophospholipase activity by about 70%. Ref.12
Mutagenesis2181A → V: Reduces lysophospholipase activity by about 50%. Ref.12
Mutagenesis2311N → A: Strongly reduced lysophospholipase activity. Ref.12
Mutagenesis3071Y → Q: Reduces lysophospholipase activity by about 70%. Ref.12
Sequence conflict231N → S in AAA64785. Ref.1
Sequence conflict231N → S in ABW38316. Ref.5
Sequence conflict731D → H in BAA08260. Ref.2
Sequence conflict1001G → A in AAB00855. Ref.3
Sequence conflict2911Q → R in AAA64785. Ref.1
Sequence conflict2911Q → R in ABW38316. Ref.5
Sequence conflict3491H → R in AAA64785. Ref.1
Sequence conflict3491H → R in ABW38316. Ref.5
Sequence conflict4571K → P AA sequence Ref.9
Sequence conflict5011V → S AA sequence Ref.9
Sequence conflict5081E → N AA sequence Ref.9
Sequence conflict5541P → L AA sequence Ref.9
Sequence conflict6291P → L in AAA64785. Ref.1
Sequence conflict6291P → L in ABW38316. Ref.5
Sequence conflict6441S → R in BAA08260. Ref.2
Sequence conflict7031V → A in BAA08260. Ref.2
Sequence conflict7691Y → H in BAA08260. Ref.2
Isoform 3:
Sequence conflict231N → S in ABW38316. Ref.5
Sequence conflict2911Q → R in ABW38316. Ref.5
Sequence conflict3491H → R in ABW38316. Ref.5
Sequence conflict4931S → P in ABW38316. Ref.5
Sequence conflict5991F → Y in ABW38316. Ref.5
Sequence conflict6021S → T in ABW38316. Ref.5
Sequence conflict6541P → L in ABW38316. Ref.5

Sequences

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

Last modified March 2, 2010. Version 3.
Checksum: 94A7A2B3701F0993

FASTA86398,994
        10         20         30         40         50         60 
MARRSSFQSC QIISLFTFAV GVNICLGFTA HRIKRAEGWE EGPPTVLSDS PWTNISGSCK 

        70         80         90        100        110        120 
GRCFELQEAG PPDCRCDNLC KSYTSCCHDF DELCLKTARG WECTKDRCGE VRNEENACHC 

       130        140        150        160        170        180 
SEDCLARGDC CTNYQVVCKG ESHWVDDDCE EIKAAECPAG FVRPPLIIFS VDGFRASYMK 

       190        200        210        220        230        240 
KGSKVMPNIE KLRSCGTHSP YMRPVYPTKT FPNLYTLATG LYPESHGIVG NSMYDPVFDA 

       250        260        270        280        290        300 
TFHLRGREKF NHRWWGGQPL WITATKQGVK AGTFFWSVVI PHERRILTIL QWLTLPDHER 

       310        320        330        340        350        360 
PSVYAFYSEQ PDFSGHKYGP FGPEMTNPLR EIDKIVGQLM DGLKQLKLHR CVNVIFVGDH 

       370        380        390        400        410        420 
GMEDVTCDRT EFLSNYLTNV DDITLVPGTL GRIRSKFSNN AKYDPKAIIA NLTCKKPDQH 

       430        440        450        460        470        480 
FKPYLKQHLP KRLHYANNRR IEDIHLLVER RWHVARKPLD VYKKPSGKCF FQGDHGFDNK 

       490        500        510        520        530        540 
VNSMQTVFVG YGSTFKYKTK VPPFENIELY NVMCDLLGLK PAPNNGTHGS LNHLLRTNTF 

       550        560        570        580        590        600 
RPTMPEEVTR PNYPGIMYLQ SDFDLGCTCD DKVEPKNKLD ELNKRLHTKG STEERHLLYG 

       610        620        630        640        650        660 
RPAVLYRTRY DILYHTDFES GYSEIFLMPL WTSYTVSKQA EVSSVPDHLT SCVRPDVRVS 

       670        680        690        700        710        720 
PSFSQNCLAY KNDKQMSYGF LFPPYLSSSP EAKYDAFLVT NMVPMYPAFK RVWNYFQRVL 

       730        740        750        760        770        780 
VKKYASERNG VNVISGPIFD YDYDGLHDTE DKIKQYVEGS SIPVPTHYYS IITSCLDFTQ 

       790        800        810        820        830        840 
PADKCDGPLS VSSFILPHRP DNEESCNSSE DESKWVEELM KMHTARVRDI EHLTSLDFFR 

       850        860 
KTSRSYPEIL TLKTYLHTYE SEI 

« Hide

Isoform 2 (ATXmel) (Alpha) [UniParc].

Checksum: 30C7CB1E60101B75
Show »

FASTA915105,201
Isoform 3 (Gamma) [UniParc].

Checksum: 17A8986783028C4D
Show »

FASTA888101,968

References

« Hide 'large scale' references
[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]"Inhibition of autotaxin by lysophosphatidic acid and sphingosine 1-phosphate."
van Meeteren L.A., Ruurs P., Christodoulou E., Goding J.W., Takakusa H., Kikuchi K., Perrakis A., Nagano T., Moolenaar W.H.
J. Biol. Chem. 280:21155-21161(2005) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Structural basis of substrate discrimination and integrin binding by autotaxin."
Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z., Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S., Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K., Kooi C.W. expand/collapse author list , Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H., Perrakis A.
Nat. Struct. Mol. Biol. 18:198-204(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, MUTAGENESIS OF THR-210; PHE-211; ALA-218; ASN-231 AND TYR-307.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA55144.
RefSeqNP_001035181.1. NM_001040092.2.
NP_001124335.1. NM_001130863.2.
NP_006200.3. NM_006209.4.
UniGeneHs.190977.

3D structure databases

ProteinModelPortalQ13822.
SMRQ13822. Positions 23-860.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111194. 2 interactions.
IntActQ13822. 1 interaction.
MINTMINT-7969086.

Chemistry

ChEMBLCHEMBL3691.

PTM databases

PhosphoSiteQ13822.

Polymorphism databases

DMDM290457674.

Proteomic databases

PaxDbQ13822.
PRIDEQ13822.

Protocols and materials databases

DNASU5168.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000075322; ENSP00000075322; ENSG00000136960. [Q13822-1]
ENST00000259486; ENSP00000259486; ENSG00000136960. [Q13822-2]
ENST00000522826; ENSP00000428291; ENSG00000136960. [Q13822-3]
GeneID5168.
KEGGhsa:5168.
UCSCuc003yos.2. human. [Q13822-2]
uc003yot.2. human. [Q13822-1]

Organism-specific databases

CTD5168.
GeneCardsGC08M120569.
H-InvDBHIX0025550.
HGNCHGNC:3357. ENPP2.
HPAHPA023700.
MIM601060. gene.
neXtProtNX_Q13822.
PharmGKBPA27792.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1524.
HOVERGENHBG051484.
KOK01122.
OMAGDHGMED.
OrthoDBEOG7XM2X4.
PhylomeDBQ13822.
TreeFamTF330032.

Enzyme and pathway databases

SABIO-RKQ13822.

Gene expression databases

ArrayExpressQ13822.
BgeeQ13822.
CleanExHS_ENPP2.
GenevestigatorQ13822.

Family and domain databases

Gene3D3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProIPR017849. 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]
PANTHERPTHR10151. PTHR10151. 1 hit.
PfamPF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 2 hits.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
PRINTSPR00022. SOMATOMEDINB.
SMARTSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view]
SUPFAMSSF53649. SSF53649. 1 hit.
PROSITEPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSENPP2. human.
GeneWikiAutotaxin.
GenomeRNAi5168.
NextBio19994.
PROQ13822.
SOURCESearch...

Entry information

Entry nameENPP2_HUMAN
AccessionPrimary (citable) accession number: Q13822
Secondary accession number(s): A8UHA1 expand/collapse secondary AC list , E9PHP7, Q13827, Q14555, Q15117, Q9UCQ8, Q9UCR0, Q9UCR1, Q9UCR2, Q9UCR3, Q9UCR4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 2, 2010
Last modified: April 16, 2014
This is version 133 of the entry and version 3 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 8

Human chromosome 8: entries, gene names and cross-references to MIM