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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 2

Gene

Enpp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids (PubMed:17208043, PubMed:28414242, PubMed:27780639). Major substrate is lysophosphatidylcholine (PubMed:17208043, PubMed:27780639). Also can act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP (PubMed:18175805). 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 (By similarity). Possible involvement in cell proliferation and adipose tissue development (Probable). Tumor cell motility-stimulating factor.By similarity1 Publication5 Publications

Catalytic activityi

1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine.5 Publications

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P) (By similarity). Inhibited by EDTA and EGTA.By similarity1 Publication

Kineticsi

  1. KM=12.9 mM for pNppp (isoform 1)1 Publication
  2. KM=4.4 mM for pNppp (isoform 2)1 Publication
  3. KM=11.8 mM for pNppp (isoform 3)1 Publication
  1. Vmax=1.9 nmol/min/µg enzyme with pNppp as substrate (isoform 1)1 Publication
  2. Vmax=0.35 nmol/min/µg enzyme with pNppp as substrate (isoform 2)1 Publication
  3. Vmax=1.8 nmol/min/µg enzyme with pNppp as substrate (isoform 3)1 Publication

pH dependencei

Optimum pH is 8.0 for isoforms 1, 2 and 3.1 Publication

Temperature dependencei

Isoforms 1 and 3 have maximum activity from 45 to 55 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi171Zinc 1; catalyticCombined sources2 Publications1
Active sitei209Nucleophile1 Publication1
Metal bindingi209Zinc 1; catalyticCombined sources2 Publications1
Binding sitei230SubstrateCombined sources1 Publication1
Binding sitei306SubstrateCombined sources1 Publication1
Metal bindingi311Zinc 2; catalyticCombined sources2 Publications1
Metal bindingi315Zinc 2; via tele nitrogen; catalyticCombined sources2 Publications1
Metal bindingi358Zinc 1; catalyticCombined sources2 Publications1
Metal bindingi359Zinc 1; via tele nitrogen; catalyticCombined sources2 Publications1
Metal bindingi474Zinc 2; via tele nitrogen; catalyticCombined sources2 Publications1
Metal bindingi739CalciumCombined sources3 Publications1
Metal bindingi741CalciumCombined sources3 Publications1
Metal bindingi743CalciumCombined sources3 Publications1
Metal bindingi745Calcium; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi747CalciumCombined sources3 Publications1
Sitei852Essential for catalytic activity1 Publication1

GO - Molecular functioni

  • alkylglycerophosphoethanolamine phosphodiesterase activity Source: MGI
  • calcium ion binding Source: UniProtKB
  • lysophospholipase activity Source: UniProtKB
  • nucleic acid binding Source: InterPro
  • nucleotide diphosphatase activity Source: MGI
  • phosphodiesterase I activity Source: MGI
  • polysaccharide binding Source: InterPro
  • scavenger receptor activity Source: InterPro
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processChemotaxis, Lipid degradation, Lipid metabolism
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.1.4.39 3474
SABIO-RKiQ9R1E6

Names & Taxonomyi

Protein namesi
Recommended name:
Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 (EC:3.1.4.395 Publications)
Short name:
E-NPP 2
Alternative name(s):
Autotaxin1 Publication
Extracellular lysophospholipase D
Short name:
LysoPLD
Gene namesi
Name:Enpp2
Synonyms:Npps2, Pdnp21 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1321390 Enpp2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

May contribute to obesity (PubMed:15700135).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi12 – 27Missing : Complete inhibition of secretion. 1 PublicationAdd BLAST16
Mutagenesisi12 – 22Missing : Complete inhibition of secretion. 1 PublicationAdd BLAST11
Mutagenesisi23 – 27Missing : No effect on secretion. 1 Publication5
Mutagenesisi23Missing : No effect on secretion. 1
Mutagenesisi25Missing : No effect on secretion. 1 Publication1
Mutagenesisi27 – 35Missing : No effect on secretion nor lysophospholipase activity. 1 Publication9
Mutagenesisi27 – 30Missing : No effect on secretion. 1 Publication4
Mutagenesisi27Missing : No effect on secretion. 1 Publication1
Mutagenesisi30 – 41Missing : No effect on secretion nor lysophospholipase activity. 1 PublicationAdd BLAST12
Mutagenesisi30 – 33Missing : No effect on secretion nor lysophospholipase activity. 1 Publication4
Mutagenesisi32 – 35Missing : No effect on secretion nor lysophospholipase activity. 1 Publication4
Mutagenesisi36 – 40Missing : No effect on secretion nor lysophospholipase activity. 1 Publication5
Mutagenesisi53Missing : No effect on secretion; slightly decreases lysophospholipase activity. Almost complete loss of lysophospholipase activity; when associated with N-410 del. 1 Publication1
Mutagenesisi210F → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi213L → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi230N → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi243L → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi247E → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi249F → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi410Missing : No effect on secretion; greatly inhibits lysoPLD activity. Inhibits secretion. Almost complete loss of lysoPLD activity; when associated with N-53 del. 1 Publication1
Mutagenesisi512M → A: Reduced lysophospholipase activity. 1
Mutagenesisi851 – 853LKT → AAA, RRR or SSS: No catalytic activity. 1 Publication3
Mutagenesisi851L → A: No effect. 1 Publication1
Mutagenesisi852K → A or R: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi853T → A: No effect. 1 Publication1

Keywords - Diseasei

Obesity

Chemistry databases

ChEMBLiCHEMBL3826871
GuidetoPHARMACOLOGYi2901

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27By similarityAdd BLAST27
PropeptideiPRO_000028165028 – 35Removed by furin8
ChainiPRO_000018856836 – 862Ectonucleotide pyrophosphatase/phosphodiesterase family member 2Add BLAST827

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi53N-linked (GlcNAc...) asparagineCombined sources2 Publications1
Disulfide bondi58 ↔ 75Combined sources4 Publications
Disulfide bondi62 ↔ 93Combined sources4 Publications
Disulfide bondi73 ↔ 86Combined sources4 Publications
Disulfide bondi79 ↔ 85Combined sources4 Publications
Disulfide bondi102 ↔ 119Combined sources4 Publications
Disulfide bondi107 ↔ 137Combined sources4 Publications
Disulfide bondi117 ↔ 130Combined sources4 Publications
Disulfide bondi123 ↔ 129Combined sources4 Publications
Disulfide bondi148 ↔ 194Combined sources4 Publications
Disulfide bondi156 ↔ 350Combined sources3 Publications
Disulfide bondi366 ↔ 468Combined sources3 Publications
Glycosylationi410N-linked (GlcNAc...) asparagineCombined sources3 Publications1
Disulfide bondi413 ↔ 805Combined sources4 Publications
Glycosylationi524N-linked (GlcNAc...) asparagineCombined sources3 Publications1
Disulfide bondi566 ↔ 666Combined sources4 Publications
Disulfide bondi568 ↔ 651Combined sources4 Publications
Disulfide bondi774 ↔ 784Combined sources4 Publications
Glycosylationi806N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

N-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity. Secretion requires simultaneous glycosylation on Asn-53 and Asn-410, while probable glycosylation of Asn-410 has a preferential role on lysoPLD activity. Not O-glycosylated.3 Publications
The interdomain disulfide bond between Cys-413 and Cys-805 is essential for catalytic activity.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PeptideAtlasiQ9R1E6
PRIDEiQ9R1E6

PTM databases

iPTMnetiQ9R1E6
PhosphoSitePlusiQ9R1E6

Expressioni

Tissue specificityi

Expressed in brain and adipose tissue.1 Publication

Inductioni

Up-regulated in adipocytes of obese-diabetic db/db mice.1 Publication

Gene expression databases

BgeeiENSMUSG00000022425
ExpressionAtlasiQ9R1E6 baseline and differential
GenevisibleiQ9R1E6 MM

Interactioni

Chemistry databases

BindingDBiQ9R1E6

Structurei

Secondary structure

1862
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni59 – 63Combined sources5
Helixi77 – 79Combined sources3
Turni80 – 83Combined sources4
Helixi89 – 93Combined sources5
Turni98 – 100Combined sources3
Helixi104 – 106Combined sources3
Beta strandi115 – 118Combined sources4
Helixi123 – 126Combined sources4
Helixi133 – 138Combined sources6
Helixi143 – 145Combined sources3
Beta strandi165 – 171Combined sources7
Helixi175 – 183Combined sources9
Helixi186 – 194Combined sources9
Beta strandi195 – 197Combined sources3
Helixi209 – 218Combined sources10
Helixi222 – 225Combined sources4
Beta strandi229 – 234Combined sources6
Turni235 – 238Combined sources4
Beta strandi239 – 241Combined sources3
Beta strandi243 – 246Combined sources4
Helixi247 – 249Combined sources3
Helixi251 – 253Combined sources3
Helixi259 – 265Combined sources7
Helixi281 – 292Combined sources12
Turni296 – 298Combined sources3
Beta strandi301 – 310Combined sources10
Helixi311 – 317Combined sources7
Helixi322 – 324Combined sources3
Helixi325 – 344Combined sources20
Turni348 – 350Combined sources3
Beta strandi352 – 358Combined sources7
Beta strandi368 – 371Combined sources4
Helixi372 – 374Combined sources3
Helixi379 – 381Combined sources3
Beta strandi382 – 385Combined sources4
Beta strandi387 – 396Combined sources10
Helixi404 – 411Combined sources8
Beta strandi419 – 424Combined sources6
Helixi425 – 427Combined sources3
Helixi430 – 432Combined sources3
Beta strandi442 – 447Combined sources6
Beta strandi452 – 456Combined sources5
Helixi457 – 459Combined sources3
Beta strandi471 – 473Combined sources3
Helixi481 – 483Combined sources3
Beta strandi487 – 494Combined sources8
Beta strandi496 – 499Combined sources4
Helixi505 – 507Combined sources3
Helixi508 – 515Combined sources8
Turni527 – 530Combined sources4
Helixi531 – 533Combined sources3
Beta strandi534 – 536Combined sources3
Helixi559 – 561Combined sources3
Helixi579 – 581Combined sources3
Turni583 – 586Combined sources4
Turni593 – 595Combined sources3
Beta strandi609 – 613Combined sources5
Beta strandi618 – 622Combined sources5
Turni623 – 626Combined sources4
Beta strandi627 – 635Combined sources9
Helixi646 – 648Combined sources3
Helixi660 – 662Combined sources3
Helixi666 – 671Combined sources6
Beta strandi676 – 681Combined sources6
Helixi683 – 685Combined sources3
Helixi689 – 695Combined sources7
Helixi698 – 700Combined sources3
Beta strandi701 – 704Combined sources4
Helixi706 – 717Combined sources12
Helixi719 – 727Combined sources9
Beta strandi729 – 737Combined sources9
Beta strandi743 – 745Combined sources3
Helixi749 – 751Combined sources3
Beta strandi765 – 776Combined sources12
Helixi781 – 783Combined sources3
Beta strandi788 – 796Combined sources9
Turni805 – 808Combined sources4
Helixi811 – 813Combined sources3
Helixi815 – 821Combined sources7
Helixi826 – 833Combined sources8
Beta strandi834 – 836Combined sources3
Helixi845 – 853Combined sources9

3D structure databases

ProteinModelPortaliQ9R1E6
SMRiQ9R1E6
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9R1E6

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini54 – 97SMB 1PROSITE-ProRule annotationAdd BLAST44
Domaini98 – 142SMB 2PROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni144 – 501PhosphodiesteraseAdd BLAST358
Regioni210 – 213Substrate bindingCombined sources1 Publication4
Regioni243 – 254Substrate binding1 PublicationAdd BLAST12
Regioni597 – 862NucleaseAdd BLAST266
Regioni829 – 850Required for secretionAdd BLAST22

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi126 – 128Cell attachment siteSequence analysis3

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

GeneTreeiENSGT00760000119157
HOGENOMiHOG000037439
HOVERGENiHBG051484
InParanoidiQ9R1E6
KOiK01122
OMAiKLHRCVN
OrthoDBiEOG091G017X
PhylomeDBiQ9R1E6
TreeFamiTF330032

Family and domain databases

Gene3Di3.40.720.10, 1 hit
InterProiView protein in InterPro
IPR017849 Alkaline_Pase-like_a/b/a
IPR017850 Alkaline_phosphatase_core_sf
IPR001604 DNA/RNA_non-sp_Endonuclease
IPR029881 ENPP2
IPR020821 Extracellular_endonuc_su_A
IPR002591 Phosphodiest/P_Trfase
IPR036024 Somatomedin_B-like_dom_sf
IPR020436 Somatomedin_B_chordata
IPR001212 Somatomedin_B_dom
PANTHERiPTHR10151:SF21 PTHR10151:SF21, 1 hit
PfamiView protein in Pfam
PF01223 Endonuclease_NS, 1 hit
PF01663 Phosphodiest, 1 hit
PF01033 Somatomedin_B, 2 hits
PRINTSiPR00022 SOMATOMEDINB
SMARTiView protein in SMART
SM00892 Endonuclease_NS, 1 hit
SM00477 NUC, 1 hit
SM00201 SO, 2 hits
SUPFAMiSSF53649 SSF53649, 1 hit
SSF90188 SSF90188, 2 hits
PROSITEiView protein in PROSITE
PS00524 SMB_1, 2 hits
PS50958 SMB_2, 2 hits

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: Q9R1E6-1) [UniParc]FASTAAdd to basket
Also known as: 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
MARQGCFGSY QVISLFTFAI GVNLCLGFTA SRIKRAEWDE GPPTVLSDSP
60 70 80 90 100
WTNTSGSCKG RCFELQEVGP PDCRCDNLCK SYSSCCHDFD ELCLKTARGW
110 120 130 140 150
ECTKDRCGEV RNEENACHCS EDCLSRGDCC TNYQVVCKGE SHWVDDDCEE
160 170 180 190 200
IRVPECPAGF VRPPLIIFSV DGFRASYMKK GSKVMPNIEK LRSCGTHAPY
210 220 230 240 250
MRPVYPTKTF PNLYTLATGL YPESHGIVGN SMYDPVFDAT FHLRGREKFN
260 270 280 290 300
HRWWGGQPLW ITATKQGVRA GTFFWSVSIP HERRILTILQ WLSLPDNERP
310 320 330 340 350
SVYAFYSEQP DFSGHKYGPF GPEMTNPLRE IDKTVGQLMD GLKQLKLHRC
360 370 380 390 400
VNVIFVGDHG MEDVTCDRTE FLSNYLTNVD DITLVPGTLG RIRPKIPNNL
410 420 430 440 450
KYDPKAIIAN LTCKKPDQHF KPYMKQHLPK RLHYANNRRI EDLHLLVERR
460 470 480 490 500
WHVARKPLDV YKKPSGKCFF QGDHGFDNKV NSMQTVFVGY GPTFKYRTKV
510 520 530 540 550
PPFENIELYN VMCDLLGLKP APNNGTHGSL NHLLRTNTFR PTLPEEVSRP
560 570 580 590 600
NYPGIMYLQS DFDLGCTCDD KVEPKNKLEE LNKRLHTKGS TEERHLLYGR
610 620 630 640 650
PAVLYRTSYD ILYHTDFESG YSEIFLMPLW TSYTISKQAE VSSIPEHLTN
660 670 680 690 700
CVRPDVRVSP GFSQNCLAYK NDKQMSYGFL FPPYLSSSPE AKYDAFLVTN
710 720 730 740 750
MVPMYPAFKR VWTYFQRVLV KKYASERNGV NVISGPIFDY NYNGLRDIED
760 770 780 790 800
EIKQYVEGSS IPVPTHYYSI ITSCLDFTQP ADKCDGPLSV SSFILPHRPD
810 820 830 840 850
NDESCNSSED ESKWVEELMK MHTARVRDIE HLTGLDFYRK TSRSYSEILT
860
LKTYLHTYES EI
Length:862
Mass (Da):98,885
Last modified:February 10, 2009 - v3
Checksum:i343D44DEAA8FA352
GO
Isoform 2 (identifier: Q9R1E6-2) [UniParc]FASTAAdd to basket
Also known as: Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     323-323: E → EESSYGSPLTPAKRPKRKVAPKRRQERPVAPPKKRRRKLHRMDHYTAETRQDK

Show »
Length:914
Mass (Da):105,089
Checksum:iE36A577AB858AF02
GO
Isoform 3 (identifier: Q9R1E6-3) [UniParc]FASTAAdd to basket
Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     592-592: E → EAETGKFRGSKHENKKSLNGNVEPRK

Show »
Length:887
Mass (Da):101,680
Checksum:i599952429BBFBD6B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti103T → I in ACD12866 (Ref. 3) Curated1
Sequence conflicti517G → S in AAD46480 (PubMed:10702660).Curated1
Sequence conflicti550P → T in AAD46480 (PubMed:10702660).Curated1
Sequence conflicti573E → K in AAD46480 (PubMed:10702660).Curated1
Sequence conflicti743N → D in ACD12866 (Ref. 3) Curated1
Sequence conflicti743N → D in AAH03264 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_036396323E → EESSYGSPLTPAKRPKRKVA PKRRQERPVAPPKKRRRKLH RMDHYTAETRQDK in isoform 2. 1 Publication1
Alternative sequenceiVSP_036397592E → EAETGKFRGSKHENKKSLNG NVEPRK in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF123542 mRNA Translation: AAD46480.1
EU131009 mRNA Translation: ABW38314.1
EU131010 mRNA Translation: ABW38315.1
EU677474 Genomic DNA Translation: ACD12865.1
EU677475 Genomic DNA Translation: ACD12866.1
AK161144 mRNA Translation: BAE36214.1
CH466545 Genomic DNA Translation: EDL29265.1
BC003264 mRNA Translation: AAH03264.1
BC058759 mRNA Translation: AAH58759.1
CCDSiCCDS27472.1 [Q9R1E6-1]
CCDS49607.1 [Q9R1E6-2]
CCDS70628.1 [Q9R1E6-3]
RefSeqiNP_001129549.1, NM_001136077.3 [Q9R1E6-2]
NP_001272923.1, NM_001285994.2 [Q9R1E6-3]
NP_001272924.1, NM_001285995.2
NP_056559.2, NM_015744.4 [Q9R1E6-1]
UniGeneiMm.250256

Genome annotation databases

EnsembliENSMUST00000041591; ENSMUSP00000036180; ENSMUSG00000022425 [Q9R1E6-1]
ENSMUST00000167541; ENSMUSP00000132640; ENSMUSG00000022425 [Q9R1E6-3]
ENSMUST00000171545; ENSMUSP00000128941; ENSMUSG00000022425 [Q9R1E6-2]
GeneIDi18606
KEGGimmu:18606
UCSCiuc007vro.3 mouse [Q9R1E6-1]
uc007vrq.3 mouse [Q9R1E6-3]
uc011zsx.2 mouse [Q9R1E6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiENPP2_MOUSE
AccessioniPrimary (citable) accession number: Q9R1E6
Secondary accession number(s): A8UH85
, A8UH93, B2ZP54, Q6PDE0, Q99LG9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: February 10, 2009
Last modified: July 18, 2018
This is version 164 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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