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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 2

Gene

ENPP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.3 Publications

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity
  • Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Enzyme regulationi

Inhibited by lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P). Inhibited by EDTA and EGTA (Probable).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)2 Publications
  3. KM=11.3 mM for pNppp (isoform 1)2 Publications
  4. KM=5.7 mM for pNppp (isoform 2)2 Publications
  5. KM=19.8 mM for pNppp (isoform 3)2 Publications
  1. Vmax=1.9 nmol/min/µg enzyme with pNppp as substrate (isoform 1)2 Publications
  2. Vmax=0.67 nmol/min/µg enzyme with pNppp as substrate (isoform 2)2 Publications
  3. Vmax=1.6 nmol/min/µg enzyme with pNppp as substrate (isoform 3)2 Publications

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 9.5.2 Publications

Temperature dependencei

Isoform 1 and isoform 3 are active from 45 to 60 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi172Zinc 1; catalyticBy similarity1
Active sitei210NucleophileBy similarity1
Metal bindingi210Zinc 1; catalyticBy similarity1
Binding sitei231SubstrateBy similarity1
Binding sitei307SubstrateBy similarity1
Metal bindingi312Zinc 2; catalyticBy similarity1
Metal bindingi316Zinc 2; catalyticBy similarity1
Metal bindingi316Zinc 2; via tele nitrogen; catalyticBy similarity1
Metal bindingi359Zinc 1; catalyticBy similarity1
Metal bindingi360Zinc 1; catalyticBy similarity1
Metal bindingi360Zinc 1; via tele nitrogen; catalyticBy similarity1
Metal bindingi475Zinc 2; catalyticBy similarity1
Metal bindingi475Zinc 2; via tele nitrogen; catalyticBy similarity1
Metal bindingi740CalciumBy similarity1
Metal bindingi744CalciumBy similarity1
Metal bindingi746Calcium; via carbonyl oxygenBy similarity1
Metal bindingi748CalciumBy similarity1
Sitei853Essential for catalytic activityBy similarity1

GO - Molecular functioni

  • alkylglycerophosphoethanolamine phosphodiesterase activity Source: UniProtKB-EC
  • calcium ion binding Source: UniProtKB
  • hydrolase activity Source: UniProtKB
  • lysophospholipase activity Source: UniProtKB
  • nucleic acid binding Source: InterPro
  • nucleotide diphosphatase activity Source: ProtInc
  • phosphodiesterase I activity Source: ProtInc
  • polysaccharide binding Source: InterPro
  • scavenger receptor activity Source: InterPro
  • transcription factor binding Source: ProtInc
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • chemotaxis Source: UniProtKB
  • G-protein coupled receptor signaling pathway Source: ProtInc
  • immune response Source: InterPro
  • movement of cell or subcellular component Source: ProtInc
  • phosphate-containing compound metabolic process Source: ProtInc
  • phosphatidylcholine catabolic process Source: UniProtKB
  • phospholipid catabolic process Source: UniProtKB
  • positive regulation of epithelial cell migration Source: UniProtKB
  • positive regulation of lamellipodium morphogenesis Source: UniProtKB
  • positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  • regulation of angiogenesis Source: InterPro
  • 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

BioCyciMetaCyc:HS06258-MONOMER.
ZFISH:HS06258-MONOMER.
BRENDAi3.1.4.39. 2681.
SABIO-RKQ13822.

Chemistry databases

SwissLipidsiSLP:000000393.
SLP:000000641. [Q13822-1]

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
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:3357. ENPP2.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi170S → E: Reduces lysophospholipase activity by about 70%. 1
Mutagenesisi210T → A: Loss of lysophospholipase activity. 1 Publication1
Mutagenesisi211F → Y: Reduces lysophospholipase activity by about 70%. 1 Publication1
Mutagenesisi218A → V: Reduces lysophospholipase activity by about 50%. 1 Publication1
Mutagenesisi231N → A: Strongly reduced lysophospholipase activity. 1 Publication1
Mutagenesisi307Y → Q: Reduces lysophospholipase activity by about 70%. 1 Publication1

Keywords - Diseasei

Obesity

Organism-specific databases

DisGeNETi5168.
OpenTargetsiENSG00000136960.
PharmGKBiPA27792.

Chemistry databases

ChEMBLiCHEMBL3691.
GuidetoPHARMACOLOGYi2901.

Polymorphism and mutation databases

BioMutaiENPP2.
DMDMi290457674.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27By similarityAdd BLAST27
PropeptideiPRO_000028164928 – 35Removed by furin2 Publications8
ChainiPRO_000018856736 – 863Ectonucleotide pyrophosphatase/phosphodiesterase family member 2Add BLAST828

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi54N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi59 ↔ 76PROSITE-ProRule annotation
Disulfide bondi63 ↔ 94PROSITE-ProRule annotation
Disulfide bondi74 ↔ 87PROSITE-ProRule annotation
Disulfide bondi80 ↔ 86PROSITE-ProRule annotation
Disulfide bondi103 ↔ 120PROSITE-ProRule annotation
Disulfide bondi108 ↔ 138PROSITE-ProRule annotation
Disulfide bondi118 ↔ 131PROSITE-ProRule annotation
Disulfide bondi124 ↔ 130PROSITE-ProRule annotation
Disulfide bondi149 ↔ 195PROSITE-ProRule annotation
Disulfide bondi157 ↔ 351PROSITE-ProRule annotation
Disulfide bondi367 ↔ 469PROSITE-ProRule annotation
Glycosylationi411N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi414 ↔ 806PROSITE-ProRule annotation
Glycosylationi525N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi567 ↔ 667PROSITE-ProRule annotation
Disulfide bondi569 ↔ 652PROSITE-ProRule annotation
Disulfide bondi775 ↔ 785PROSITE-ProRule annotation
Glycosylationi807N-linked (GlcNAc...)Sequence analysis1

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

EPDiQ13822.
PeptideAtlasiQ13822.
PRIDEiQ13822.

PTM databases

iPTMnetiQ13822.
PhosphoSitePlusiQ13822.

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.1 Publication

Gene expression databases

BgeeiENSG00000136960.
CleanExiHS_ENPP2.
ExpressionAtlasiQ13822. baseline and differential.
GenevisibleiQ13822. HS.

Organism-specific databases

HPAiHPA023700.
HPA053652.

Interactioni

GO - Molecular functioni

  • transcription factor binding Source: ProtInc

Protein-protein interaction databases

BioGridi111194. 4 interactors.
IntActiQ13822. 2 interactors.
MINTiMINT-7969086.

Chemistry databases

BindingDBiQ13822.

Structurei

Secondary structure

1863
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni60 – 64Combined sources5
Helixi80 – 83Combined sources4
Helixi90 – 94Combined sources5
Turni99 – 101Combined sources3
Helixi105 – 107Combined sources3
Beta strandi116 – 119Combined sources4
Beta strandi121 – 123Combined sources3
Helixi124 – 127Combined sources4
Helixi134 – 138Combined sources5
Helixi144 – 146Combined sources3
Beta strandi166 – 172Combined sources7
Helixi176 – 181Combined sources6
Helixi182 – 185Combined sources4
Helixi187 – 195Combined sources9
Beta strandi196 – 198Combined sources3
Helixi210 – 219Combined sources10
Helixi223 – 226Combined sources4
Beta strandi230 – 235Combined sources6
Turni236 – 239Combined sources4
Beta strandi240 – 242Combined sources3
Beta strandi244 – 247Combined sources4
Helixi248 – 250Combined sources3
Helixi252 – 254Combined sources3
Beta strandi255 – 257Combined sources3
Helixi260 – 266Combined sources7
Beta strandi278 – 280Combined sources3
Helixi282 – 292Combined sources11
Turni297 – 299Combined sources3
Beta strandi302 – 311Combined sources10
Helixi312 – 318Combined sources7
Helixi323 – 325Combined sources3
Helixi326 – 345Combined sources20
Turni349 – 351Combined sources3
Beta strandi353 – 359Combined sources7
Beta strandi369 – 372Combined sources4
Helixi373 – 375Combined sources3
Helixi380 – 382Combined sources3
Beta strandi383 – 386Combined sources4
Beta strandi388 – 399Combined sources12
Helixi405 – 412Combined sources8
Beta strandi420 – 425Combined sources6
Helixi426 – 428Combined sources3
Helixi431 – 433Combined sources3
Beta strandi443 – 448Combined sources6
Beta strandi453 – 457Combined sources5
Beta strandi472 – 474Combined sources3
Helixi482 – 484Combined sources3
Beta strandi488 – 492Combined sources5
Beta strandi497 – 500Combined sources4
Helixi506 – 508Combined sources3
Helixi509 – 516Combined sources8
Turni528 – 531Combined sources4
Helixi532 – 534Combined sources3
Beta strandi535 – 537Combined sources3
Helixi560 – 562Combined sources3
Helixi593 – 596Combined sources4
Beta strandi610 – 614Combined sources5
Beta strandi619 – 623Combined sources5
Turni624 – 627Combined sources4
Beta strandi628 – 636Combined sources9
Helixi647 – 649Combined sources3
Helixi661 – 663Combined sources3
Helixi667 – 672Combined sources6
Beta strandi677 – 682Combined sources6
Helixi684 – 686Combined sources3
Turni690 – 692Combined sources3
Helixi693 – 696Combined sources4
Helixi699 – 701Combined sources3
Beta strandi702 – 705Combined sources4
Helixi707 – 718Combined sources12
Helixi720 – 728Combined sources9
Beta strandi730 – 738Combined sources9
Beta strandi744 – 746Combined sources3
Helixi750 – 752Combined sources3
Beta strandi766 – 777Combined sources12
Helixi782 – 784Combined sources3
Beta strandi789 – 797Combined sources9
Turni806 – 809Combined sources4
Helixi812 – 814Combined sources3
Helixi816 – 822Combined sources7
Helixi827 – 834Combined sources8
Beta strandi841 – 844Combined sources4
Helixi846 – 854Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZG6X-ray1.80A/B17-863[»]
4ZG7X-ray1.75A55-860[»]
4ZG9X-ray2.95A/B1-863[»]
4ZGAX-ray2.60A1-863[»]
ProteinModelPortaliQ13822.
SMRiQ13822.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 98SMB 1PROSITE-ProRule annotationAdd BLAST44
Domaini99 – 143SMB 2PROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni211 – 214Substrate bindingBy similarity4
Regioni244 – 255Substrate bindingBy similarityAdd BLAST12
Regioni830 – 851Required for secretionBy similarityAdd BLAST22

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi127 – 129Cell attachment siteSequence analysis3

Sequence similaritiesi

Contains 2 SMB (somatomedin-B) domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

GeneTreeiENSGT00760000119157.
HOVERGENiHBG051484.
InParanoidiQ13822.
KOiK01122.
OMAiGMEDVTC.
OrthoDBiEOG091G017X.
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.
IPR029881. ENPP2.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PTHR10151:SF21. PTHR10151:SF21. 1 hit.
PfamiPF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
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.
SSF90188. SSF90188. 2 hits.
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. AlignAdd to basket

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

        10         20         30         40         50
MARRSSFQSC QIISLFTFAV GVNICLGFTA HRIKRAEGWE EGPPTVLSDS
60 70 80 90 100
PWTNISGSCK GRCFELQEAG PPDCRCDNLC KSYTSCCHDF DELCLKTARG
110 120 130 140 150
WECTKDRCGE VRNEENACHC SEDCLARGDC CTNYQVVCKG ESHWVDDDCE
160 170 180 190 200
EIKAAECPAG FVRPPLIIFS VDGFRASYMK KGSKVMPNIE KLRSCGTHSP
210 220 230 240 250
YMRPVYPTKT FPNLYTLATG LYPESHGIVG NSMYDPVFDA TFHLRGREKF
260 270 280 290 300
NHRWWGGQPL WITATKQGVK AGTFFWSVVI PHERRILTIL QWLTLPDHER
310 320 330 340 350
PSVYAFYSEQ PDFSGHKYGP FGPEMTNPLR EIDKIVGQLM DGLKQLKLHR
360 370 380 390 400
CVNVIFVGDH GMEDVTCDRT EFLSNYLTNV DDITLVPGTL GRIRSKFSNN
410 420 430 440 450
AKYDPKAIIA NLTCKKPDQH FKPYLKQHLP KRLHYANNRR IEDIHLLVER
460 470 480 490 500
RWHVARKPLD VYKKPSGKCF FQGDHGFDNK VNSMQTVFVG YGSTFKYKTK
510 520 530 540 550
VPPFENIELY NVMCDLLGLK PAPNNGTHGS LNHLLRTNTF RPTMPEEVTR
560 570 580 590 600
PNYPGIMYLQ SDFDLGCTCD DKVEPKNKLD ELNKRLHTKG STEERHLLYG
610 620 630 640 650
RPAVLYRTRY DILYHTDFES GYSEIFLMPL WTSYTVSKQA EVSSVPDHLT
660 670 680 690 700
SCVRPDVRVS PSFSQNCLAY KNDKQMSYGF LFPPYLSSSP EAKYDAFLVT
710 720 730 740 750
NMVPMYPAFK RVWNYFQRVL VKKYASERNG VNVISGPIFD YDYDGLHDTE
760 770 780 790 800
DKIKQYVEGS SIPVPTHYYS IITSCLDFTQ PADKCDGPLS VSSFILPHRP
810 820 830 840 850
DNEESCNSSE DESKWVEELM KMHTARVRDI EHLTSLDFFR KTSRSYPEIL
860
TLKTYLHTYE SEI
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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23N → S in AAA64785 (PubMed:7982964).Curated1
Sequence conflicti23N → S in ABW38316 (PubMed:18175805).Curated1
Sequence conflicti73D → H in BAA08260 (PubMed:8586446).Curated1
Sequence conflicti100G → A in AAB00855 (PubMed:8579579).Curated1
Sequence conflicti291Q → R in AAA64785 (PubMed:7982964).Curated1
Sequence conflicti291Q → R in ABW38316 (PubMed:18175805).Curated1
Sequence conflicti349H → R in AAA64785 (PubMed:7982964).Curated1
Sequence conflicti349H → R in ABW38316 (PubMed:18175805).Curated1
Sequence conflicti457K → P AA sequence (PubMed:1733949).Curated1
Sequence conflicti501V → S AA sequence (PubMed:1733949).Curated1
Sequence conflicti508E → N AA sequence (PubMed:1733949).Curated1
Sequence conflicti554P → L AA sequence (PubMed:1733949).Curated1
Sequence conflicti629P → L in AAA64785 (PubMed:7982964).Curated1
Sequence conflicti629P → L in ABW38316 (PubMed:18175805).Curated1
Sequence conflicti644S → R in BAA08260 (PubMed:8586446).Curated1
Sequence conflicti703V → A in BAA08260 (PubMed:8586446).Curated1
Sequence conflicti769Y → H in BAA08260 (PubMed:8586446).Curated1
Isoform 3 (identifier: Q13822-3)
Sequence conflicti23N → S in ABW38316 (PubMed:18175805).Curated1
Sequence conflicti291Q → R in ABW38316 (PubMed:18175805).Curated1
Sequence conflicti349H → R in ABW38316 (PubMed:18175805).Curated1
Sequence conflicti493S → P in ABW38316 (PubMed:18175805).Curated1
Sequence conflicti599F → Y in ABW38316 (PubMed:18175805).Curated1
Sequence conflicti602S → T in ABW38316 (PubMed:18175805).Curated1
Sequence conflicti654P → L in ABW38316 (PubMed:18175805).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_060469493S → P.7 PublicationsCorresponds to variant rs10283100dbSNPEnsembl.1
Natural variantiVAR_057472577N → S.Corresponds to variant rs2289886dbSNPEnsembl.1
Natural variantiVAR_057473726S → L.Corresponds to variant rs16892767dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_006750324E → EESSYGSPFTPAKRPKRKVA PKRRQERPVAPPKKRRRKIH RMDHYAAETRQDK in isoform 2. 2 Publications1
Alternative sequenceiVSP_036398593E → EAETRKFRGSRNENKENING NFEPRK in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.3. human. [Q13822-1]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZG6X-ray1.80A/B17-863[»]
4ZG7X-ray1.75A55-860[»]
4ZG9X-ray2.95A/B1-863[»]
4ZGAX-ray2.60A1-863[»]
ProteinModelPortaliQ13822.
SMRiQ13822.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111194. 4 interactors.
IntActiQ13822. 2 interactors.
MINTiMINT-7969086.

Chemistry databases

BindingDBiQ13822.
ChEMBLiCHEMBL3691.
GuidetoPHARMACOLOGYi2901.
SwissLipidsiSLP:000000393.
SLP:000000641. [Q13822-1]

PTM databases

iPTMnetiQ13822.
PhosphoSitePlusiQ13822.

Polymorphism and mutation databases

BioMutaiENPP2.
DMDMi290457674.

Proteomic databases

EPDiQ13822.
PeptideAtlasiQ13822.
PRIDEiQ13822.

Protocols and materials databases

DNASUi5168.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5168.
DisGeNETi5168.
GeneCardsiENPP2.
H-InvDBHIX0025550.
HGNCiHGNC:3357. ENPP2.
HPAiHPA023700.
HPA053652.
MIMi601060. gene.
neXtProtiNX_Q13822.
OpenTargetsiENSG00000136960.
PharmGKBiPA27792.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000119157.
HOVERGENiHBG051484.
InParanoidiQ13822.
KOiK01122.
OMAiGMEDVTC.
OrthoDBiEOG091G017X.
PhylomeDBiQ13822.
TreeFamiTF330032.

Enzyme and pathway databases

BioCyciMetaCyc:HS06258-MONOMER.
ZFISH:HS06258-MONOMER.
BRENDAi3.1.4.39. 2681.
SABIO-RKQ13822.

Miscellaneous databases

ChiTaRSiENPP2. human.
GeneWikiiAutotaxin.
GenomeRNAii5168.
PROiQ13822.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000136960.
CleanExiHS_ENPP2.
ExpressionAtlasiQ13822. baseline and differential.
GenevisibleiQ13822. HS.

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.
IPR029881. ENPP2.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PTHR10151:SF21. PTHR10151:SF21. 1 hit.
PfamiPF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
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.
SSF90188. SSF90188. 2 hits.
PROSITEiPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 157 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.