ENPP2

Functionⁱ

Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids (PubMed:15769751, PubMed:26371182, PubMed:27754931). Major substrate is lysophosphatidylcholine (PubMed:12176993, PubMed:27754931). 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:15769751, PubMed:12176993). 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 (PubMed:11559573). Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein (PubMed:1733949). May have a role in induction of parturition (PubMed:12176993). Possible involvement in cell proliferation and adipose tissue development (Probable). Tumor cell motility-stimulating factor (PubMed:1733949, PubMed:11559573).1 Publication7 Publications

Catalytic activityⁱ

1-alkyl-sn-glycero-3-phosphoethanolamine + H₂O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine.6 Publications

Cofactorⁱ

Protein has several cofactor binding sites:

Activity regulationⁱ

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

Kineticsⁱ

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 key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	172	Zinc 1; catalyticCombined sources2 Publications	1
Active siteⁱ	210	NucleophileBy similarity	1
Metal bindingⁱ	210	Zinc 1; catalyticCombined sources2 Publications	1
Binding siteⁱ	231	SubstrateCombined sources1 Publication	1
Binding siteⁱ	307	SubstrateBy similarity	1
Metal bindingⁱ	312	Zinc 2; catalyticCombined sources1 Publication	1
Metal bindingⁱ	316	Zinc 2; via tele nitrogen; catalyticCombined sources1 Publication	1
Metal bindingⁱ	359	Zinc 1; catalyticCombined sources2 Publications	1
Metal bindingⁱ	360	Zinc 1; via tele nitrogen; catalyticCombined sources2 Publications	1
Metal bindingⁱ	475	Zinc 2; via tele nitrogen; catalyticCombined sources1 Publication	1
Metal bindingⁱ	740	CalciumCombined sources2 Publications	1
Metal bindingⁱ	742	CalciumCombined sources2 Publications	1
Metal bindingⁱ	744	CalciumCombined sources1 Publication	1
Metal bindingⁱ	746	Calcium; via carbonyl oxygenCombined sources2 Publications	1
Metal bindingⁱ	748	CalciumCombined sources2 Publications	1
Siteⁱ	853	Essential for catalytic activityBy similarity	1

GO - Molecular functionⁱ

alkylglycerophosphoethanolamine phosphodiesterase activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
calcium ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 26371182
hydrolase activity
Source: UniProtKB
Traceable author statementⁱ
- 7982964
lysophospholipase activity
Source: UniProtKB
Inferred from direct assayⁱ
nucleic acid binding Source: InterPro
nucleotide diphosphatase activity Source: InterPro
phosphodiesterase I activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
polysaccharide binding Source: InterPro
scavenger receptor activity Source: InterPro
transcription factor binding
Source: ProtInc
Traceable author statementⁱ
- 8586446
zinc ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 26371182

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell chemotaxis
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cell motility
Source: UniProtKB
Traceable author statementⁱ
- 1733949
cellular response to cadmium ion
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cellular response to estradiol stimulus
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
chemotaxis
Source: UniProtKB
Non-traceable author statementⁱ
- 7982964
diencephalon development
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
forebrain development
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
immune response Source: InterPro
midbrain development
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
negative regulation of cell-matrix adhesion
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
phosphatidylcholine catabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 21240271
phospholipid catabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 15280042
- 26371182
positive regulation of cell proliferation
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
positive regulation of epithelial cell migration
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 18054784
positive regulation of focal adhesion assembly
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
positive regulation of lamellipodium morphogenesis
Source: UniProtKB
Inferred from genetic interactionⁱ
- 18054784
positive regulation of oligodendrocyte differentiation
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
positive regulation of peptidyl-tyrosine phosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 18054784
positive regulation of substrate adhesion-dependent cell spreading
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
regulation of angiogenesis Source: InterPro
regulation of cell migration
Source: UniProtKB
Inferred from direct assayⁱ
- 1733949
response to polycyclic arene
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase
Biological process	Chemotaxis, Lipid degradation, Lipid metabolism
Ligand	Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS06258-MONOMER
BRENDAⁱ	3.1.4.39 2681
Reactomeⁱ	R-HSA-199220 Vitamin B5 (pantothenate) metabolism
SABIO-RKⁱ	Q13822

Chemistry databases

SwissLipidsⁱ	SLP:000000393 SLP:000000641 [Q13822-1]

SwissLipidsⁱ

SLP:000000393
SLP:000000641 [Q13822-1]

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): Autotaxin2 Publications Extracellular lysophospholipase D Short name: LysoPLD1 Publication
Gene namesⁱ	Name:ENPP2 Synonyms:ATX2 Publications, PDNP21 Publication
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 8

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000136960.12
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:3357 ENPP2
MIMⁱ	601060 gene
neXtProtⁱ	NX_Q13822

Keywords - Cellular componentⁱ

Secreted

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	170	S → E: Reduces lysophospholipase activity by about 70%.	1
Mutagenesisⁱ	210	T → A: Loss of lysophospholipase activity. 1 Publication	1
Mutagenesisⁱ	211	F → Y: Reduces lysophospholipase activity by about 70%. 1 Publication	1
Mutagenesisⁱ	218	A → V: Reduces lysophospholipase activity by about 50%. 1 Publication	1
Mutagenesisⁱ	231	N → A: Strongly reduced lysophospholipase activity. 1 Publication	1
Mutagenesisⁱ	307	Y → Q: Reduces lysophospholipase activity by about 70%. 1 Publication	1

Keywords - Diseaseⁱ

Obesity

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5168
Open Targets More...OpenTargetsⁱ	ENSG00000136960
PharmGKBⁱ	PA27792

Chemistry databases

ChEMBLⁱ	CHEMBL3691
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2901

Polymorphism and mutation databases

BioMutaⁱ	ENPP2
DMDMⁱ	290457674

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Signal peptideⁱ	1 – 27	By similarityAdd BLAST	27
PropeptideⁱPRO_0000281649	28 – 35	Removed by furin2 Publications	8
ChainⁱPRO_0000188567	36 – 863	Ectonucleotide pyrophosphatase/phosphodiesterase family member 2Add BLAST	828

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	54	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	59 ↔ 76	PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondⁱ	63 ↔ 94	PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondⁱ	74 ↔ 87	PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondⁱ	80 ↔ 86	PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondⁱ	103 ↔ 120	PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondⁱ	108 ↔ 138	PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondⁱ	118 ↔ 131	PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondⁱ	124 ↔ 130	PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondⁱ	149 ↔ 195	PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondⁱ	157 ↔ 351	PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondⁱ	367 ↔ 469	PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationⁱ	411	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	414 ↔ 806	PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationⁱ	525	N-linked (GlcNAc...) asparagineCombined sources1 Publication	1
Disulfide bondⁱ	567 ↔ 667	PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondⁱ	569 ↔ 652	PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondⁱ	775 ↔ 785	PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationⁱ	807	N-linked (GlcNAc...) asparagineSequence analysis	1

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

PeptideAtlas More...PeptideAtlasⁱ	Q13822
PRIDEⁱ	Q13822
ProteomicsDBⁱ	59692 59693 [Q13822-2] 59694 [Q13822-3]

PTM databases

GlyConnectⁱ	1197
iPTMnetⁱ	Q13822
PhosphoSitePlusⁱ	Q13822

Expressionⁱ

Tissue specificityⁱ

Detected in blood plasma (at protein level) (PubMed:12176993, PubMed:26371182). 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.5 Publications

Inductionⁱ

Up-regulated in massively obese subjects with glucose intolerance, and during adipogenesis.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000136960 Expressed in 235 organ(s), highest expression level in pigmented layer of retina
CleanExⁱ	HS_ENPP2
ExpressionAtlasⁱ	Q13822 baseline and differential
Genevisibleⁱ	Q13822 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA023700 HPA053652

HPAⁱ

HPA023700
HPA053652

Interactionⁱ

GO - Molecular functionⁱ

transcription factor binding
Source: ProtInc
Traceable author statementⁱ
- 8586446

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	111194, 3 interactors
IntActⁱ	Q13822, 2 interactors
Molecular INTeraction database More...MINTⁱ	Q13822

Chemistry databases

BindingDBⁱ

Q13822

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	60 – 64	Combined sources	5
Helixⁱ	80 – 83	Combined sources	4
Helixⁱ	90 – 94	Combined sources	5
Turnⁱ	99 – 101	Combined sources	3
Helixⁱ	105 – 107	Combined sources	3
Beta strandⁱ	116 – 119	Combined sources	4
Beta strandⁱ	121 – 123	Combined sources	3
Helixⁱ	124 – 127	Combined sources	4
Helixⁱ	134 – 138	Combined sources	5
Helixⁱ	144 – 146	Combined sources	3
Beta strandⁱ	166 – 172	Combined sources	7
Helixⁱ	176 – 181	Combined sources	6
Helixⁱ	182 – 185	Combined sources	4
Helixⁱ	187 – 195	Combined sources	9
Beta strandⁱ	196 – 198	Combined sources	3
Helixⁱ	210 – 219	Combined sources	10
Helixⁱ	223 – 226	Combined sources	4
Beta strandⁱ	230 – 235	Combined sources	6
Turnⁱ	236 – 239	Combined sources	4
Beta strandⁱ	240 – 242	Combined sources	3
Beta strandⁱ	244 – 247	Combined sources	4
Helixⁱ	248 – 250	Combined sources	3
Helixⁱ	252 – 254	Combined sources	3
Beta strandⁱ	255 – 257	Combined sources	3
Helixⁱ	260 – 266	Combined sources	7
Beta strandⁱ	278 – 280	Combined sources	3
Helixⁱ	282 – 292	Combined sources	11
Turnⁱ	297 – 299	Combined sources	3
Beta strandⁱ	302 – 311	Combined sources	10
Helixⁱ	312 – 318	Combined sources	7
Helixⁱ	323 – 325	Combined sources	3
Helixⁱ	326 – 345	Combined sources	20
Turnⁱ	349 – 351	Combined sources	3
Beta strandⁱ	353 – 359	Combined sources	7
Beta strandⁱ	369 – 372	Combined sources	4
Helixⁱ	373 – 375	Combined sources	3
Helixⁱ	380 – 382	Combined sources	3
Beta strandⁱ	383 – 386	Combined sources	4
Beta strandⁱ	388 – 399	Combined sources	12
Helixⁱ	405 – 412	Combined sources	8
Beta strandⁱ	413 – 416	Combined sources	4
Beta strandⁱ	420 – 425	Combined sources	6
Helixⁱ	426 – 428	Combined sources	3
Helixⁱ	431 – 433	Combined sources	3
Beta strandⁱ	443 – 448	Combined sources	6
Beta strandⁱ	453 – 457	Combined sources	5
Beta strandⁱ	472 – 474	Combined sources	3
Helixⁱ	482 – 484	Combined sources	3
Beta strandⁱ	488 – 492	Combined sources	5
Beta strandⁱ	497 – 500	Combined sources	4
Helixⁱ	506 – 508	Combined sources	3
Helixⁱ	509 – 516	Combined sources	8
Turnⁱ	528 – 531	Combined sources	4
Helixⁱ	532 – 534	Combined sources	3
Beta strandⁱ	535 – 537	Combined sources	3
Helixⁱ	560 – 562	Combined sources	3
Helixⁱ	593 – 596	Combined sources	4
Beta strandⁱ	610 – 614	Combined sources	5
Beta strandⁱ	619 – 623	Combined sources	5
Turnⁱ	624 – 627	Combined sources	4
Beta strandⁱ	628 – 636	Combined sources	9
Helixⁱ	647 – 649	Combined sources	3
Helixⁱ	661 – 663	Combined sources	3
Helixⁱ	667 – 672	Combined sources	6
Beta strandⁱ	677 – 682	Combined sources	6
Helixⁱ	684 – 686	Combined sources	3
Turnⁱ	690 – 692	Combined sources	3
Helixⁱ	693 – 696	Combined sources	4
Helixⁱ	699 – 701	Combined sources	3
Beta strandⁱ	702 – 705	Combined sources	4
Helixⁱ	707 – 718	Combined sources	12
Helixⁱ	720 – 728	Combined sources	9
Beta strandⁱ	730 – 738	Combined sources	9
Beta strandⁱ	744 – 746	Combined sources	3
Helixⁱ	750 – 752	Combined sources	3
Beta strandⁱ	766 – 777	Combined sources	12
Helixⁱ	782 – 784	Combined sources	3
Beta strandⁱ	789 – 797	Combined sources	9
Turnⁱ	806 – 809	Combined sources	4
Helixⁱ	812 – 814	Combined sources	3
Helixⁱ	816 – 822	Combined sources	7
Helixⁱ	827 – 834	Combined sources	8
Beta strandⁱ	841 – 844	Combined sources	4
Helixⁱ	846 – 854	Combined sources	9

Show more details

3D structure databases

ProteinModelPortalⁱ	Q13822
SMRⁱ	Q13822
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	55 – 98	SMB 1PROSITE-ProRule annotationAdd BLAST		44
Domainⁱ	99 – 143	SMB 2PROSITE-ProRule annotationAdd BLAST		45

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	211 – 214	Substrate bindingBy similarity	4
Regionⁱ	244 – 255	Substrate bindingBy similarityAdd BLAST	12
Regionⁱ	830 – 851	Required for secretionBy similarityAdd BLAST	22

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	127 – 129	Cell attachment siteSequence analysis		3

Sequence similaritiesⁱ

Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.Curated

Keywords - Domainⁱ

Repeat, Signal

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000119157
HOVERGENⁱ	HBG051484
InParanoidⁱ	Q13822
KEGG Orthology (KO) More...KOⁱ	K01122
OMAⁱ	DGLHDTQ
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G017X
PhylomeDBⁱ	Q13822
TreeFamⁱ	TF330032

Family and domain databases

Gene3Dⁱ	3.40.720.10, 1 hit
InterProⁱ	View 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
PANTHERⁱ	PTHR10151:SF21 PTHR10151:SF21, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01223 Endonuclease_NS, 1 hit PF01663 Phosphodiest, 1 hit PF01033 Somatomedin_B, 2 hits
PRINTSⁱ	PR00022 SOMATOMEDINB
SMARTⁱ	View protein in SMART SM00892 Endonuclease_NS, 1 hit SM00477 NUC, 1 hit SM00201 SO, 2 hits
SUPFAMⁱ	SSF53649 SSF53649, 1 hit SSF90188 SSF90188, 2 hits
PROSITEⁱ	View 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. Align Add to basket

This entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q13822-1) [UniParc]FASTA Add 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]FASTA Add to basket

Also known as: ATXmel, Alpha

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

« 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 FGPEESSYGS PFTPAKRPKR KVAPKRRQER 
       360        370        380        390        400
PVAPPKKRRR KIHRMDHYAA ETRQDKMTNP LREIDKIVGQ LMDGLKQLKL 
       410        420        430        440        450
HRCVNVIFVG DHGMEDVTCD RTEFLSNYLT NVDDITLVPG TLGRIRSKFS 
       460        470        480        490        500
NNAKYDPKAI IANLTCKKPD QHFKPYLKQH LPKRLHYANN RRIEDIHLLV 
       510        520        530        540        550
ERRWHVARKP LDVYKKPSGK CFFQGDHGFD NKVNSMQTVF VGYGSTFKYK 
       560        570        580        590        600
TKVPPFENIE LYNVMCDLLG LKPAPNNGTH GSLNHLLRTN TFRPTMPEEV 
       610        620        630        640        650
TRPNYPGIMY LQSDFDLGCT CDDKVEPKNK LDELNKRLHT KGSTEERHLL 
       660        670        680        690        700
YGRPAVLYRT RYDILYHTDF ESGYSEIFLM PLWTSYTVSK QAEVSSVPDH 
       710        720        730        740        750
LTSCVRPDVR VSPSFSQNCL AYKNDKQMSY GFLFPPYLSS SPEAKYDAFL 
       760        770        780        790        800
VTNMVPMYPA FKRVWNYFQR VLVKKYASER NGVNVISGPI FDYDYDGLHD 
       810        820        830        840        850
TEDKIKQYVE GSSIPVPTHY YSIITSCLDF TQPADKCDGP LSVSSFILPH 
       860        870        880        890        900
RPDNEESCNS SEDESKWVEE LMKMHTARVR DIEHLTSLDF FRKTSRSYPE 
       910 
ILTLKTYLHT YESEI

Show »

Length:915

Mass (Da):105,201

Checksum:ⁱ30C7CB1E60101B75

GO

Isoform 3 (identifier: Q13822-3) [UniParc]FASTA Add to basket

Also known as: Gamma

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

« 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 STEAETRKFR 
       610        620        630        640        650
GSRNENKENI NGNFEPRKER HLLYGRPAVL YRTRYDILYH TDFESGYSEI 
       660        670        680        690        700
FLMPLWTSYT VSKQAEVSSV PDHLTSCVRP DVRVSPSFSQ NCLAYKNDKQ 
       710        720        730        740        750
MSYGFLFPPY LSSSPEAKYD AFLVTNMVPM YPAFKRVWNY FQRVLVKKYA 
       760        770        780        790        800
SERNGVNVIS GPIFDYDYDG LHDTEDKIKQ YVEGSSIPVP THYYSIITSC 
       810        820        830        840        850
LDFTQPADKC DGPLSVSSFI LPHRPDNEES CNSSEDESKW VEELMKMHTA 
       860        870        880 
RVRDIEHLTS LDFFRKTSRS YPEILTLKTY LHTYESEI

Show »

Length:888

Mass (Da):101,968

Checksum:ⁱ17A8986783028C4D

GO

Computationally mapped potential isoform sequencesⁱ

There are 4 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

E5RIB9	E5RIB9_HUMAN	Ectonucleotide pyrophosphatase/phos... Ectonucleotide pyrophosphatase/phosphodiesterase family member 2	ENPP2	162	Annotation score:
E5RJ49	E5RJ49_HUMAN	Ectonucleotide pyrophosphatase/phos... Ectonucleotide pyrophosphatase/phosphodiesterase family member 2	ENPP2	245	Annotation score:
E7EUF1	E7EUF1_HUMAN	Ectonucleotide pyrophosphatase/phos... Ectonucleotide pyrophosphatase/phosphodiesterase family member 2	ENPP2	884	Annotation score:
E5RIA2	E5RIA2_HUMAN	Ectonucleotide pyrophosphatase/phos... Ectonucleotide pyrophosphatase/phosphodiesterase family member 2	ENPP2	498	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	23	N → S in AAA64785 (PubMed:7982964).Curated	1
Sequence conflictⁱ	23	N → S in ABW38316 (PubMed:18175805).Curated	1
Sequence conflictⁱ	73	D → H in BAA08260 (PubMed:8586446).Curated	1
Sequence conflictⁱ	100	G → A in AAB00855 (PubMed:8579579).Curated	1
Sequence conflictⁱ	291	Q → R in AAA64785 (PubMed:7982964).Curated	1
Sequence conflictⁱ	291	Q → R in ABW38316 (PubMed:18175805).Curated	1
Sequence conflictⁱ	349	H → R in AAA64785 (PubMed:7982964).Curated	1
Sequence conflictⁱ	349	H → R in ABW38316 (PubMed:18175805).Curated	1
Sequence conflictⁱ	457	K → P AA sequence (PubMed:1733949).Curated	1
Sequence conflictⁱ	501	V → S AA sequence (PubMed:1733949).Curated	1
Sequence conflictⁱ	508	E → N AA sequence (PubMed:1733949).Curated	1
Sequence conflictⁱ	554	P → L AA sequence (PubMed:1733949).Curated	1
Sequence conflictⁱ	629	P → L in AAA64785 (PubMed:7982964).Curated	1
Sequence conflictⁱ	629	P → L in ABW38316 (PubMed:18175805).Curated	1
Sequence conflictⁱ	644	S → R in BAA08260 (PubMed:8586446).Curated	1
Sequence conflictⁱ	703	V → A in BAA08260 (PubMed:8586446).Curated	1
Sequence conflictⁱ	769	Y → H in BAA08260 (PubMed:8586446).Curated	1
Isoform 3 (identifier: Q13822-3)
Sequence conflictⁱ	23	N → S in ABW38316 (PubMed:18175805).	1
Sequence conflictⁱ	291	Q → R in ABW38316 (PubMed:18175805).	1
Sequence conflictⁱ	349	H → R in ABW38316 (PubMed:18175805).	1
Sequence conflictⁱ	493	S → P in ABW38316 (PubMed:18175805).	1
Sequence conflictⁱ	599	F → Y in ABW38316 (PubMed:18175805).	1
Sequence conflictⁱ	602	S → T in ABW38316 (PubMed:18175805).	1
Sequence conflictⁱ	654	P → L in ABW38316 (PubMed:18175805).	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_060469	493	S → P7 PublicationsCorresponds to variant dbSNP:rs10283100Ensembl.	1
Natural variantⁱVAR_057472	577	N → S. Corresponds to variant dbSNP:rs2289886Ensembl.	1
Natural variantⁱVAR_057473	726	S → L. Corresponds to variant dbSNP:rs16892767Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_006750	324	E → EESSYGSPFTPAKRPKRKVA PKRRQERPVAPPKKRRRKIH RMDHYAAETRQDK in isoform 2. 2 Publications		1
Alternative sequenceⁱVSP_036398	593	E → EAETRKFRGSRNENKENING NFEPRK in isoform 3. 1 Publication		1

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS34936.1 [Q13822-1] CCDS47914.1 [Q13822-3] CCDS6329.1 [Q13822-2]
PIRⁱ	A55144
NCBI Reference Sequences More...RefSeqⁱ	NP_001035181.1, NM_001040092.2 [Q13822-1] NP_001124335.1, NM_001130863.2 [Q13822-3] NP_006200.3, NM_006209.4 [Q13822-2]
UniGeneⁱ	Hs.190977

Genome annotation databases

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

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q13822	Ectonucleotide pyrophosphatase/phosphodiesterase family member 2	)	MOUSE		862	UniRef90_Q9R1E6
Uncharacterized protein		PAPAN		957
Uncharacterized protein		RHIBE		957
Uncharacterized protein		MACNE		957
ectonucleotide pyrophosphatase/phosphodiesterase family member 2 isoform X3		DELLE		930
+175
Q13822-2	Isoform 2 of Ectonucleotide pyrophosphatase/phosphodiesterase family member 2		MOUSE		914	UniRef90_Q9R1E6-2
Uncharacterized protein		PIG		981
Uncharacterized protein		CALJA		918
ectonucleotide pyrophosphatase/phosphodiesterase family member 2 isoform X1		ERIEU		915
ectonucleotide pyrophosphatase/phosphodiesterase family member 2 isoform X4		TURTR		915
+127
Q13822-3	Isoform 3 of Ectonucleotide pyrophosphatase/phosphodiesterase family member 2		MOUSE		887	UniRef90_Q9R1E6-3
Ectonucleotide pyrophosphatase/phosphodiesterase family member 2		BOVIN		888
Ectonucleotide pyrophosphatase/phosphodiesterase family member 2	)	RAT		887
Uncharacterized protein		PAPAN		982
Uncharacterized protein		MACFA		884
+179

Protein	Similar proteins		Species	Score	Length	Source
Q13822	Ectonucleotide pyrophosphatase/phosphodiesterase family member 2	)	MOUSE		862	UniRef50_Q9R1E6
Uncharacterized protein		PAPAN		957
Uncharacterized protein		RHIBE		957
Uncharacterized protein		MACNE		957
ectonucleotide pyrophosphatase/phosphodiesterase family member 2 isoform X3		DELLE		930
+746
Q13822-3	Isoform 3 of Ectonucleotide pyrophosphatase/phosphodiesterase family member 2		MOUSE		887	UniRef50_Q9R1E6-3
Ectonucleotide pyrophosphatase/phosphodiesterase family member 2		BOVIN		888
Ectonucleotide pyrophosphatase/phosphodiesterase family member 2	)	RAT		887
Uncharacterized protein		PAPAN		982
Uncharacterized protein		MACFA		884
+371

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
CCDSⁱ	CCDS34936.1 [Q13822-1] CCDS47914.1 [Q13822-3] CCDS6329.1 [Q13822-2]
PIRⁱ	A55144
RefSeqⁱ	NP_001035181.1, NM_001040092.2 [Q13822-1] NP_001124335.1, NM_001130863.2 [Q13822-3] NP_006200.3, NM_006209.4 [Q13822-2]
UniGeneⁱ	Hs.190977

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4ZG6	X-ray	1.80	A/B	17-863	[»]
	4ZG7	X-ray	1.75	A	55-860	[»]
	4ZG9	X-ray	2.95	A/B	1-863	[»]
	4ZGA	X-ray	2.60	A	1-863	[»]
	5KXA	X-ray	2.59	A	1-863	[»]
	5M7M	X-ray	2.70	A	1-863	[»]
	5MHP	X-ray	2.43	A	1-863	[»]
ProteinModelPortalⁱ	Q13822
SMRⁱ	Q13822
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	111194, 3 interactors
IntActⁱ	Q13822, 2 interactors
MINTⁱ	Q13822

Chemistry databases

BindingDBⁱ	Q13822
ChEMBLⁱ	CHEMBL3691
GuidetoPHARMACOLOGYⁱ	2901
SwissLipidsⁱ	SLP:000000393 SLP:000000641 [Q13822-1]

PTM databases

GlyConnectⁱ	1197
iPTMnetⁱ	Q13822
PhosphoSitePlusⁱ	Q13822

Polymorphism and mutation databases

BioMutaⁱ	ENPP2
DMDMⁱ	290457674

Proteomic databases

PeptideAtlasⁱ	Q13822
PRIDEⁱ	Q13822
ProteomicsDBⁱ	59692 59693 [Q13822-2] 59694 [Q13822-3]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	5168
Structural Biology Knowledgebase	Search...

Genome annotation databases

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

Organism-specific databases

CTDⁱ	5168
DisGeNETⁱ	5168
EuPathDBⁱ	HostDB:ENSG00000136960.12
GeneCardsⁱ	ENPP2
H-InvDBⁱ	HIX0025550
HGNCⁱ	HGNC:3357 ENPP2
HPAⁱ	HPA023700 HPA053652
MIMⁱ	601060 gene
neXtProtⁱ	NX_Q13822
OpenTargetsⁱ	ENSG00000136960
PharmGKBⁱ	PA27792
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

GeneTreeⁱ	ENSGT00760000119157
HOVERGENⁱ	HBG051484
InParanoidⁱ	Q13822
KOⁱ	K01122
OMAⁱ	DGLHDTQ
OrthoDBⁱ	EOG091G017X
PhylomeDBⁱ	Q13822
TreeFamⁱ	TF330032

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS06258-MONOMER
BRENDAⁱ	3.1.4.39 2681
Reactomeⁱ	R-HSA-199220 Vitamin B5 (pantothenate) metabolism
SABIO-RKⁱ	Q13822

Miscellaneous databases

ChiTaRSⁱ	ENPP2 human
GeneWikiⁱ	Autotaxin
GenomeRNAiⁱ	5168
Protein Ontology More...PROⁱ	PR:Q13822
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000136960 Expressed in 235 organ(s), highest expression level in pigmented layer of retina
CleanExⁱ	HS_ENPP2
ExpressionAtlasⁱ	Q13822 baseline and differential
Genevisibleⁱ	Q13822 HS

Family and domain databases

Gene3Dⁱ	3.40.720.10, 1 hit
InterProⁱ	View 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
PANTHERⁱ	PTHR10151:SF21 PTHR10151:SF21, 1 hit
Pfamⁱ	View protein in Pfam PF01223 Endonuclease_NS, 1 hit PF01663 Phosphodiest, 1 hit PF01033 Somatomedin_B, 2 hits
PRINTSⁱ	PR00022 SOMATOMEDINB
SMARTⁱ	View protein in SMART SM00892 Endonuclease_NS, 1 hit SM00477 NUC, 1 hit SM00201 SO, 2 hits
SUPFAMⁱ	SSF53649 SSF53649, 1 hit SSF90188 SSF90188, 2 hits
PROSITEⁱ	View protein in PROSITE PS00524 SMB_1, 2 hits PS50958 SMB_2, 2 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ENPP2_HUMAN
Accessionⁱ	Q13822Primary (citable) accession number: Q13822 Secondary accession number(s): A8UHA1 Q9UCR4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
	Last sequence update:	March 2, 2010
	Last modified:	November 7, 2018
	This is version 172 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 8
Human chromosome 8: entries, gene names and cross-references to MIM

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UniProtKB - Q13822 (ENPP2_HUMAN)

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Ectonucleotide pyrophosphatase/phosphodiesterase family member 2

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

pH dependencei

Temperature dependencei

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Chemistry databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted

Extracellular region or secreted

Golgi apparatus

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

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Functionⁱ

Kineticsⁱ

pH dependenceⁱ

Temperature dependenceⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ