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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi172 – 1721Zinc 1; catalyticBy similarity
Active sitei210 – 2101NucleophileBy similarity
Metal bindingi210 – 2101Zinc 1; catalyticBy similarity
Binding sitei231 – 2311SubstrateBy similarity
Binding sitei307 – 3071SubstrateBy similarity
Metal bindingi312 – 3121Zinc 2; catalyticBy similarity
Metal bindingi316 – 3161Zinc 2; catalyticBy similarity
Metal bindingi316 – 3161Zinc 2; via tele nitrogen; catalyticBy similarity
Metal bindingi359 – 3591Zinc 1; catalyticBy similarity
Metal bindingi360 – 3601Zinc 1; catalyticBy similarity
Metal bindingi360 – 3601Zinc 1; via tele nitrogen; catalyticBy similarity
Metal bindingi475 – 4751Zinc 2; catalyticBy similarity
Metal bindingi475 – 4751Zinc 2; via tele nitrogen; catalyticBy similarity
Metal bindingi740 – 7401CalciumBy similarity
Metal bindingi744 – 7441CalciumBy similarity
Metal bindingi746 – 7461Calcium; via carbonyl oxygenBy similarity
Metal bindingi748 – 7481CalciumBy similarity
Sitei853 – 8531Essential for catalytic activityBy similarity

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

BRENDAi3.1.4.39. 2681.
SABIO-RKQ13822.

Chemistry

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)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.

Chemistry

ChEMBLiCHEMBL3691.

Polymorphism and mutation databases

BioMutaiENPP2.
DMDMi290457674.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727By similarityAdd
BLAST
Propeptidei28 – 358Removed by furin2 PublicationsPRO_0000281649
Chaini36 – 863828Ectonucleotide pyrophosphatase/phosphodiesterase family member 2PRO_0000188567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi54 – 541N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi411 – 4111N-linked (GlcNAc...)Sequence analysis
Disulfide bondi414 ↔ 806PROSITE-ProRule annotation
Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence analysis
Disulfide bondi567 ↔ 667PROSITE-ProRule annotation
Disulfide bondi569 ↔ 652PROSITE-ProRule annotation
Disulfide bondi775 ↔ 785PROSITE-ProRule annotation
Glycosylationi807 – 8071N-linked (GlcNAc...)Sequence analysis

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.
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.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 interactions.
IntActiQ13822. 2 interactions.
MINTiMINT-7969086.

Chemistry

BindingDBiQ13822.

Structurei

Secondary structure

1
863
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni60 – 645Combined sources
Helixi80 – 834Combined sources
Helixi90 – 945Combined sources
Turni99 – 1013Combined sources
Helixi105 – 1073Combined sources
Beta strandi116 – 1194Combined sources
Beta strandi121 – 1233Combined sources
Helixi124 – 1274Combined sources
Helixi134 – 1385Combined sources
Helixi144 – 1463Combined sources
Beta strandi166 – 1727Combined sources
Helixi176 – 1816Combined sources
Helixi182 – 1854Combined sources
Helixi187 – 1959Combined sources
Beta strandi196 – 1983Combined sources
Helixi210 – 21910Combined sources
Helixi223 – 2264Combined sources
Beta strandi230 – 2356Combined sources
Turni236 – 2394Combined sources
Beta strandi240 – 2423Combined sources
Beta strandi244 – 2474Combined sources
Helixi248 – 2503Combined sources
Helixi252 – 2543Combined sources
Beta strandi255 – 2573Combined sources
Helixi260 – 2667Combined sources
Beta strandi278 – 2803Combined sources
Helixi282 – 29211Combined sources
Turni297 – 2993Combined sources
Beta strandi302 – 31110Combined sources
Helixi312 – 3187Combined sources
Helixi323 – 3253Combined sources
Helixi326 – 34520Combined sources
Turni349 – 3513Combined sources
Beta strandi353 – 3597Combined sources
Beta strandi369 – 3724Combined sources
Helixi373 – 3753Combined sources
Helixi380 – 3823Combined sources
Beta strandi383 – 3864Combined sources
Beta strandi388 – 39912Combined sources
Helixi405 – 4128Combined sources
Beta strandi420 – 4256Combined sources
Helixi426 – 4283Combined sources
Helixi431 – 4333Combined sources
Beta strandi443 – 4486Combined sources
Beta strandi453 – 4575Combined sources
Beta strandi472 – 4743Combined sources
Helixi482 – 4843Combined sources
Beta strandi488 – 4925Combined sources
Beta strandi497 – 5004Combined sources
Helixi506 – 5083Combined sources
Helixi509 – 5168Combined sources
Turni528 – 5314Combined sources
Helixi532 – 5343Combined sources
Beta strandi535 – 5373Combined sources
Helixi560 – 5623Combined sources
Helixi593 – 5964Combined sources
Beta strandi610 – 6145Combined sources
Beta strandi619 – 6235Combined sources
Turni624 – 6274Combined sources
Beta strandi628 – 6369Combined sources
Helixi647 – 6493Combined sources
Helixi661 – 6633Combined sources
Helixi667 – 6726Combined sources
Beta strandi677 – 6826Combined sources
Helixi684 – 6863Combined sources
Turni690 – 6923Combined sources
Helixi693 – 6964Combined sources
Helixi699 – 7013Combined sources
Beta strandi702 – 7054Combined sources
Helixi707 – 71812Combined sources
Helixi720 – 7289Combined sources
Beta strandi730 – 7389Combined sources
Beta strandi744 – 7463Combined sources
Helixi750 – 7523Combined sources
Beta strandi766 – 77712Combined sources
Helixi782 – 7843Combined sources
Beta strandi789 – 7979Combined sources
Turni806 – 8094Combined sources
Helixi812 – 8143Combined sources
Helixi816 – 8227Combined sources
Helixi827 – 8348Combined sources
Beta strandi841 – 8444Combined sources
Helixi846 – 8549Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZG6X-ray1.80A/B17-863[»]
4ZG7X-ray1.75A55-860[»]
4ZG9X-ray2.95A/B1-863[»]
4ZGAX-ray2.60A1-863[»]
ProteinModelPortaliQ13822.
SMRiQ13822. Positions 52-860.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 9844SMB 1PROSITE-ProRule annotationAdd
BLAST
Domaini99 – 14345SMB 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni211 – 2144Substrate bindingBy similarity
Regioni244 – 25512Substrate bindingBy similarityAdd
BLAST
Regioni830 – 85122Required for secretionBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi127 – 1293Cell attachment siteSequence analysis

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231N → S in AAA64785 (PubMed:7982964).Curated
Sequence conflicti23 – 231N → S in ABW38316 (PubMed:18175805).Curated
Sequence conflicti73 – 731D → H in BAA08260 (PubMed:8586446).Curated
Sequence conflicti100 – 1001G → A in AAB00855 (PubMed:8579579).Curated
Sequence conflicti291 – 2911Q → R in AAA64785 (PubMed:7982964).Curated
Sequence conflicti291 – 2911Q → R in ABW38316 (PubMed:18175805).Curated
Sequence conflicti349 – 3491H → R in AAA64785 (PubMed:7982964).Curated
Sequence conflicti349 – 3491H → R in ABW38316 (PubMed:18175805).Curated
Sequence conflicti457 – 4571K → P AA sequence (PubMed:1733949).Curated
Sequence conflicti501 – 5011V → S AA sequence (PubMed:1733949).Curated
Sequence conflicti508 – 5081E → N AA sequence (PubMed:1733949).Curated
Sequence conflicti554 – 5541P → L AA sequence (PubMed:1733949).Curated
Sequence conflicti629 – 6291P → L in AAA64785 (PubMed:7982964).Curated
Sequence conflicti629 – 6291P → L in ABW38316 (PubMed:18175805).Curated
Sequence conflicti644 – 6441S → R in BAA08260 (PubMed:8586446).Curated
Sequence conflicti703 – 7031V → A in BAA08260 (PubMed:8586446).Curated
Sequence conflicti769 – 7691Y → H in BAA08260 (PubMed:8586446).Curated
Isoform 3 (identifier: Q13822-3)
Sequence conflicti23 – 231N → S in ABW38316 (PubMed:18175805).Curated
Sequence conflicti291 – 2911Q → R in ABW38316 (PubMed:18175805).Curated
Sequence conflicti349 – 3491H → R in ABW38316 (PubMed:18175805).Curated
Sequence conflicti493 – 4931S → P in ABW38316 (PubMed:18175805).Curated
Sequence conflicti599 – 5991F → Y in ABW38316 (PubMed:18175805).Curated
Sequence conflicti602 – 6021S → T in ABW38316 (PubMed:18175805).Curated
Sequence conflicti654 – 6541P → L in ABW38316 (PubMed:18175805).Curated

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. 2 PublicationsVSP_006750
Alternative sequencei593 – 5931E → EAETRKFRGSRNENKENING NFEPRK in isoform 3. 1 PublicationVSP_036398

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZG6X-ray1.80A/B17-863[»]
4ZG7X-ray1.75A55-860[»]
4ZG9X-ray2.95A/B1-863[»]
4ZGAX-ray2.60A1-863[»]
ProteinModelPortaliQ13822.
SMRiQ13822. Positions 52-860.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

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

PTM databases

iPTMnetiQ13822.
PhosphoSiteiQ13822.

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

Phylogenomic databases

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

Enzyme and pathway databases

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: September 7, 2016
This is version 155 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.