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O14495

- LPP3_HUMAN

UniProt

O14495 - LPP3_HUMAN

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Protein

Lipid phosphate phosphohydrolase 3

Gene

PPAP2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA = PA > C-1-P > S-1-P. May be involved in cell adhesion and in cell-cell interactions.

Catalytic activityi

A 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.

Enzyme regulationi

Inhibited by sphingosine, zinc ions and propanolol. Not inhibited by N-ethylmaleimide treatment.

GO - Molecular functioni

  1. lipid phosphatase activity Source: Ensembl
  2. phosphatidate phosphatase activity Source: UniProtKB-EC
  3. phosphoprotein phosphatase activity Source: ProtInc
  4. sphingosine-1-phosphate phosphatase activity Source: Ensembl

GO - Biological processi

  1. Bergmann glial cell differentiation Source: Ensembl
  2. blood vessel development Source: Ensembl
  3. canonical Wnt signaling pathway involved in positive regulation of cell-cell adhesion Source: BHF-UCL
  4. canonical Wnt signaling pathway involved in positive regulation of endothelial cell migration Source: BHF-UCL
  5. canonical Wnt signaling pathway involved in positive regulation of wound healing Source: BHF-UCL
  6. dephosphorylation Source: GOC
  7. gastrulation with mouth forming second Source: Ensembl
  8. germ cell migration Source: ProtInc
  9. homotypic cell-cell adhesion Source: BHF-UCL
  10. lipid metabolic process Source: ProtInc
  11. negative regulation of protein phosphorylation Source: BHF-UCL
  12. phospholipid metabolic process Source: Ensembl
  13. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  14. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  15. protein stabilization Source: BHF-UCL
  16. regulation of sphingolipid mediated signaling pathway Source: Ensembl
  17. regulation of Wnt signaling pathway Source: Ensembl
  18. small molecule metabolic process Source: Reactome
  19. sphingolipid biosynthetic process Source: Reactome
  20. sphingolipid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.
SignaLinkiO14495.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipid phosphate phosphohydrolase 3 (EC:3.1.3.4)
Alternative name(s):
PAP2-beta
Phosphatidate phosphohydrolase type 2b
Phosphatidic acid phosphatase 2b
Short name:
PAP-2b
Short name:
PAP2b
Vascular endothelial growth factor and type I collagen-inducible protein
Short name:
VCIP
Gene namesi
Name:PPAP2B
Synonyms:LPP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9229. PPAP2B.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3333CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei34 – 5421HelicalSequence AnalysisAdd
BLAST
Topological domaini55 – 8531LumenalSequence AnalysisAdd
BLAST
Transmembranei86 – 10621HelicalSequence AnalysisAdd
BLAST
Topological domaini107 – 12216CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei123 – 14321HelicalSequence AnalysisAdd
BLAST
Topological domaini144 – 19350LumenalSequence AnalysisAdd
BLAST
Transmembranei194 – 21421HelicalSequence AnalysisAdd
BLAST
Topological domaini215 – 22713CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei228 – 24821HelicalSequence AnalysisAdd
BLAST
Topological domaini249 – 2579LumenalSequence Analysis
Transmembranei258 – 27821HelicalSequence AnalysisAdd
BLAST
Topological domaini279 – 31133CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. adherens junction Source: BHF-UCL
  2. extracellular vesicular exosome Source: UniProt
  3. Golgi apparatus Source: UniProtKB-KW
  4. integral component of membrane Source: UniProtKB-KW
  5. membrane Source: ProtInc
  6. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33553.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 311311Lipid phosphate phosphohydrolase 3PRO_0000220912Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphoserine2 Publications
Glycosylationi170 – 1701N-linked (GlcNAc...)Sequence Analysis
Modified residuei297 – 2971Phosphoserine1 Publication

Post-translational modificationi

N-glycosylated. Contains high-mannose oligosaccharides.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO14495.
PaxDbiO14495.
PRIDEiO14495.

PTM databases

PhosphoSiteiO14495.

Expressioni

Tissue specificityi

Ubiquitously expressed. Highly expressed in heart and placenta.

Inductioni

By EGF, VEGF, FGF2 and phorbol myristate acetate (PMA).1 Publication

Gene expression databases

BgeeiO14495.
CleanExiHS_PPAP2B.
GenevestigatoriO14495.

Organism-specific databases

HPAiHPA028892.

Interactioni

Subunit structurei

Homodimer. This complex seems not to be involved in substrate recognition, it may confer only structural or functional stability.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNND1O607169EBI-766232,EBI-701927

Protein-protein interaction databases

BioGridi114171. 3 interactions.
IntActiO14495. 4 interactions.
MINTiMINT-4648964.
STRINGi9606.ENSP00000294390.

Structurei

3D structure databases

ProteinModelPortaliO14495.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0671.
GeneTreeiENSGT00620000087654.
HOGENOMiHOG000041307.
HOVERGENiHBG002048.
InParanoidiO14495.
KOiK01080.
OMAiNNNCKDH.
OrthoDBiEOG7C5M9Q.
PhylomeDBiO14495.
TreeFamiTF316040.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR028675. LPP3.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PANTHERiPTHR10165:SF79. PTHR10165:SF79. 1 hit.
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.

Sequencei

Sequence statusi: Complete.

O14495-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQNYKYDKAI VPESKNGGSP ALNNNPRRSG SKRVLLICLD LFCLFMAGLP
60 70 80 90 100
FLIIETSTIK PYHRGFYCND ESIKYPLKTG ETINDAVLCA VGIVIAILAI
110 120 130 140 150
ITGEFYRIYY LKKSRSTIQN PYVAALYKQV GCFLFGCAIS QSFTDIAKVS
160 170 180 190 200
IGRLRPHFLS VCNPDFSQIN CSEGYIQNYR CRGDDSKVQE ARKSFFSGHA
210 220 230 240 250
SFSMYTMLYL VLYLQARFTW RGARLLRPLL QFTLIMMAFY TGLSRVSDHK
260 270 280 290 300
HHPSDVLAGF AQGALVACCI VFFVSDLFKT KTTLSLPAPA IRKEILSPVD
310
IIDRNNHHNM M
Length:311
Mass (Da):35,116
Last modified:January 1, 1998 - v1
Checksum:iCB3F60189044DA31
GO

Sequence cautioni

The sequence AAB50222.1 differs from that shown. Reason: Frameshift at position 225. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321K → M in AAV38396. 1 PublicationCurated
Sequence conflicti282 – 2821T → M in AAH09196. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000889 mRNA. Translation: BAA22594.1.
AF017786 mRNA. Translation: AAC63433.1.
AF480883 mRNA. Translation: AAO84481.1.
AF043329 mRNA. Translation: AAD02271.1.
U79294 mRNA. Translation: AAB50222.1. Frameshift.
AK312439 mRNA. Translation: BAG35348.1.
BT019589 mRNA. Translation: AAV38396.1.
CH471059 Genomic DNA. Translation: EAX06651.1.
CH471059 Genomic DNA. Translation: EAX06652.1.
CH471059 Genomic DNA. Translation: EAX06653.1.
BC009196 mRNA. Translation: AAH09196.1.
CCDSiCCDS604.1.
RefSeqiNP_003704.3. NM_003713.4.
UniGeneiHs.405156.
Hs.619002.

Genome annotation databases

EnsembliENST00000371250; ENSP00000360296; ENSG00000162407.
GeneIDi8613.
KEGGihsa:8613.
UCSCiuc001cyj.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000889 mRNA. Translation: BAA22594.1 .
AF017786 mRNA. Translation: AAC63433.1 .
AF480883 mRNA. Translation: AAO84481.1 .
AF043329 mRNA. Translation: AAD02271.1 .
U79294 mRNA. Translation: AAB50222.1 . Frameshift.
AK312439 mRNA. Translation: BAG35348.1 .
BT019589 mRNA. Translation: AAV38396.1 .
CH471059 Genomic DNA. Translation: EAX06651.1 .
CH471059 Genomic DNA. Translation: EAX06652.1 .
CH471059 Genomic DNA. Translation: EAX06653.1 .
BC009196 mRNA. Translation: AAH09196.1 .
CCDSi CCDS604.1.
RefSeqi NP_003704.3. NM_003713.4.
UniGenei Hs.405156.
Hs.619002.

3D structure databases

ProteinModelPortali O14495.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114171. 3 interactions.
IntActi O14495. 4 interactions.
MINTi MINT-4648964.
STRINGi 9606.ENSP00000294390.

PTM databases

PhosphoSitei O14495.

Proteomic databases

MaxQBi O14495.
PaxDbi O14495.
PRIDEi O14495.

Protocols and materials databases

DNASUi 8613.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371250 ; ENSP00000360296 ; ENSG00000162407 .
GeneIDi 8613.
KEGGi hsa:8613.
UCSCi uc001cyj.2. human.

Organism-specific databases

CTDi 8613.
GeneCardsi GC01M056879.
HGNCi HGNC:9229. PPAP2B.
HPAi HPA028892.
MIMi 607125. gene.
neXtProti NX_O14495.
PharmGKBi PA33553.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0671.
GeneTreei ENSGT00620000087654.
HOGENOMi HOG000041307.
HOVERGENi HBG002048.
InParanoidi O14495.
KOi K01080.
OMAi NNNCKDH.
OrthoDBi EOG7C5M9Q.
PhylomeDBi O14495.
TreeFami TF316040.

Enzyme and pathway databases

Reactomei REACT_115810. Sphingolipid de novo biosynthesis.
SignaLinki O14495.

Miscellaneous databases

ChiTaRSi PPAP2B. human.
GeneWikii PPAP2B.
GenomeRNAii 8613.
NextBioi 32277.
PROi O14495.
SOURCEi Search...

Gene expression databases

Bgeei O14495.
CleanExi HS_PPAP2B.
Genevestigatori O14495.

Family and domain databases

Gene3Di 1.20.144.10. 1 hit.
InterProi IPR028675. LPP3.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view ]
PANTHERi PTHR10165:SF79. PTHR10165:SF79. 1 hit.
Pfami PF01569. PAP2. 1 hit.
[Graphical view ]
SMARTi SM00014. acidPPc. 1 hit.
[Graphical view ]
SUPFAMi SSF48317. SSF48317. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase."
    Kai M., Wada I., Imai S., Sakane F., Kanoh H.
    J. Biol. Chem. 272:24572-24578(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INDUCTION.
  2. "Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform."
    Roberts R., Sciorra V.A., Morris A.J.
    J. Biol. Chem. 273:22059-22067(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
  3. "Regulation of cell-cell interactions by phosphatidic acid phosphatase 2b/VCIP."
    Humtsoe J.O., Feng S., Thakker G.D., Yang J., Hong J., Wary K.K.
    EMBO J. 22:1539-1554(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Molecular cloning of and expression of an isoform of human phosphatidic acid phosphatase cDNA."
    Leung D.W., Tompkins C.K.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Large-scale concatenation cDNA sequencing."
    Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
    Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  10. "Lipid phosphate phosphatases dimerise, but this interaction is not required for in vivo activity."
    Burnett C., Makridou P., Hewlett L., Howard K.
    BMC Biochem. 5:2-2(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLPP3_HUMAN
AccessioniPrimary (citable) accession number: O14495
Secondary accession number(s): B2R651
, D3DQ52, Q5U0F7, Q96GW0, Q99782
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 126 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3