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Reviewed, UniProtKB/Swiss-Prot O14939 (PLD2_HUMAN)

Last modified June 16, 2009. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phospholipase D2
      Short name=PLD 2
      Short name=hPLD2
    EC=3.1.4.4
Alternative name(s):
    Choline phosphatase 2
    Phosphatidylcholine-hydrolyzing phospholipase D2
    PLD1C
Gene names
Name: PLD2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length933 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May have a role in signal-induced cytoskeletal regulation and/or endocytosis By similarity.

Catalytic activity

A phosphatidylcholine + H2O = choline + a phosphatidate.

Enzyme regulation

Stimulated by phosphatidylinositol 4,5-bisphosphate and activated by the ADP-ribosylation factor-1 (ARF-1).

Subunit structure

Interacts with EGFR By similarity. Interacts with PIP5K1A.

Subcellular location

Membrane; Peripheral membrane protein By similarity.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the phospholipase D family.

Contains 1 PH domain.

Contains 2 PLD phosphodiesterase domains.

Contains 1 PX (phox homology) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GRB2P629932EBI-1053996,EBI-401755

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform PLD2A (identifier: O14939-1)

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.
Isoform PLD2B (identifier: O14939-2)

The sequence of this isoform differs from the canonical sequence as follows:
     810-820: Missing.
Isoform PLD2C (identifier: O14939-3)

The sequence of this isoform differs from the canonical sequence as follows:
     337-933: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 933933Phospholipase D2
PRO_0000218805

Regions

Domain65 – 195131PX
Domain203 – 311109PH
Domain437 – 46428PLD phosphodiesterase 1
Domain751 – 77828PLD phosphodiesterase 2
Region441 – 788348Catalytic

Natural variations

Alternative sequence337 – 933597Missing in isoform PLD2C.
VSP_005027
Alternative sequence810 – 82011Missing in isoform PLD2B.
VSP_005028
Natural variant1721R → C: dbSNP rs2286672. Ref.1 Ref.4
VAR_051704
Natural variant5771T → I: dbSNP rs1052748. Ref.4 Ref.2
VAR_051705
Natural variant8041A → T: dbSNP rs11545163.
VAR_051706
Natural variant8071Q → E in a breast cancer sample; somatic mutation. Ref.6
VAR_036503
Natural variant8211G → R: dbSNP rs3764897.
VAR_051707

Experimental info

Sequence conflict161D → G in AAB96656. Ref.3
Sequence conflict1651Y → C in AAB96656. Ref.3
Sequence conflict2121R → C in AAB96656. Ref.3
Sequence conflict2681Q → R in AAB96655. Ref.3
Sequence conflict3251S → R in AAB96656. Ref.3
Sequence conflict4451L → P in AAB96656. Ref.3
Sequence conflict5101D → G in AAB96656. Ref.3
Sequence conflict5661T → I in AAB96655. Ref.3
Sequence conflict6321E → G in AAB96656. Ref.3
Sequence conflict7841D → G in AAB96656. Ref.3
Sequence conflict801 – 8022MN → ID in AAC24498. Ref.2
Sequence conflict8211G → S in AAB96655. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform PLD2A [UniParc].

Last modified February 21, 2001. Version 2.
Checksum: F25F6B73B45F57ED

FASTA933105,987
        10         20         30         40         50         60 
MTATPESLFP TGDELDSSQL QMESDEVDTL KEGEDPADRM HPFLAIYELQ SLKVHPLVFA 

        70         80         90        100        110        120 
PGVPVTAQVV GTERYTSGSK VGTCTLYSVR LTHGDFSWTT KKKYRHFQEL HRDLLRHKVL 

       130        140        150        160        170        180 
MSLLPLARFA VAYSPARDAG NREMPSLPRA GPEGSTRHAA SKQKYLENYL NRLLTMSFYR 

       190        200        210        220        230        240 
NYHAMTEFLE VSQLSFIPDL GRKGLEGMIR KRSGGHRVPG LTCCGRDQVC YRWSKRWLVV 

       250        260        270        280        290        300 
KDSFLLYMCL ETGAISFVQL FDPGFEVQVG KRSTEARHGV RIDTSHRSLI LKCSSYRQAR 

       310        320        330        340        350        360 
WWAQEITELA QGPGRDFLQL HRHDSYAPPR PGTLARWFVN GAGYFAAVAD AILRAQEEIF 

       370        380        390        400        410        420 
ITDWWLSPEV YLKRPAHSDD WRLDIMLKRK AEEGVRVSIL LFKEVELALG INSGYSKRAL 

       430        440        450        460        470        480 
MLLHPNIKVM RHPDQVTLWA HHEKLLVVDQ VVAFLGGLDL AYGRWDDLHY RLTDLGDSSE 

       490        500        510        520        530        540 
SAASQPPTPR PDSPATPDLS HNQFFWLGKD YSNLITKDWV QLDRPFEDFI DRETTPRMPW 

       550        560        570        580        590        600 
RDVGVVVHGL PARDLARHFI QRWNFTKTTK AKYKTPTYPY LLPKSTSTAN QLPFTLPGGQ 

       610        620        630        640        650        660 
CTTVQVLRSV DRWSAGTLEN SILNAYLHTI RESQHFLYIE NQFFISCSDG RTVLNKVGDE 

       670        680        690        700        710        720 
IVDRILKAHK QGWCYRVYVL LPLLPGFEGD ISTGGGNSIQ AILHFTYRTL CRGEYSILHR 

       730        740        750        760        770        780 
LKAAMGTAWR DYISICGLRT HGELGGHPVS ELIYIHSKVL IADDRTVIIG SANINDRSLL 

       790        800        810        820        830        840 
GKRDSELAVL IEDTETEPSL MNGAEYQAGR FALSLRKHCF GVILGANTRP DLDLRDPICD 

       850        860        870        880        890        900 
DFFQLWQDMA ESNANIYEQI FRCLPSNATR SLRTLREYVA VEPLATVSPP LARSELTQVQ 

       910        920        930 
GHLVHFPLKF LEDESLLPPL GSKEGMIPLE VWT 

« Hide

Isoform PLD2B.

Checksum: 6E0D388D73E222AF
Show »

FASTA922104,627
Isoform PLD2C.

Checksum: B88330C3765169E3
Show »

FASTA33638,252

References

« Hide 'large scale' references
[1]"Characterization of human PLD2 and the analysis of PLD isoform splice variants."
Steed P.M., Clark K.L., Boyar W.C., Lasala D.J.
FASEB J. 12:1309-1317(1998) [PubMed: 9761774] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD2A; PLD2B AND PLD2C), CHARACTERIZATION, VARIANT CYS-172.
Tissue: Brain.
[2]"Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2."
Lopez I., Arnold R.S., Lambeth J.D.
J. Biol. Chem. 273:12846-12852(1998) [PubMed: 9582313] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PLD2A), CHARACTERIZATION, VARIANT ILE-577.
Tissue: B-cell.
[3]Saqib K.M., Clark J.M., Byrd P.J., Armstrong S.J., Wakelam M.J.O.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD2A AND PLD2B).
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PLD2A), VARIANTS CYS-172 AND ILE-577.
Tissue: Uterus.
[5]"Interaction of the type Ialpha PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4, 5-bisphosphate in the regulation of PLD2 activity."
Divecha N., Roefs M., Halstead J.R., D'Andrea S., Fernandez-Borga M., Oomen L., Saqib K.M., Wakelam M.J.O., D'Santos C.
EMBO J. 19:5440-5449(2000) [PubMed: 11032811] [Abstract]
Cited for: INTERACTION WITH PIP5K1A.
[6]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-807.
+Additional computationally mapped references.

Web resources

Wikipedia

Phospholipase D entry

Cross-references

Sequence databases

AF033850 mRNA. Translation: AAD04197.1.
AF035483 mRNA. Translation: AAC24498.1.
AF038440 mRNA. Translation: AAB96655.1.
AF038441 mRNA. Translation: AAB96656.1.
BC015033 mRNA. Translation: AAH15033.1.
IPIIPI00024727.
IPI00216566.
IPI00216567.
RefSeqNP_002654.3.
UniGeneHs.104519

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActO14939. 6 interactions.

PTM databases

PhosphoSiteO14939.

Proteomic databases

PRIDEO14939.

Genome annotation databases

EnsemblENSG00000129219. Homo sapiens. [Contig view]
GeneID5338.
KEGGhsa:5338.

Organism-specific databases

GeneCardsGC17P004657.
H-InvDBHIX0013451.
HGNCHGNC:9068. PLD2.
HPAHPA013397.
MIM602384. gene.
PharmGKBPA142672077.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO14939.
HOVERGENO14939.
OMAO14939. WRLDKIL.

Enzyme and pathway databases

BRENDA3.1.4.4. 247.
Pathway_Interaction_DBalphasynuclein_pathway. Alpha-synuclein signaling.
angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
arf_3pathway. Arf1 pathway.
arf6downstreampathway. Arf6 downstream pathway.
arf6_traffickingpathway. Arf6 trafficking events.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
lysophospholipid_pathway. LPA receptor mediated events.

Gene expression databases

ArrayExpressO14939.
BgeeO14939.
CleanExHS_PLD2.
GermOnlineENSG00000129219. Homo sapiens.

Family and domain databases

InterProIPR015679. Phospholipase_D.
IPR001849. Pleckstrin_homology.
IPR001736. PLipase_D/transphosphatidylase.
IPR016555. PLipase_D_euk.
IPR001683. PX.
[Graphical view]
Gene3DG3DSA:3.30.1520.10. PX. 1 hit.
PANTHERPTHR18896. Phospholipase_D. 1 hit.
PfamPF00169. PH. 1 hit.
PF00614. PLDc. 2 hits.
PF00787. PX. 1 hit.
[Graphical view]
PIRSFPIRSF009376. Phospholipase_D_euk. 1 hit.
SMARTSM00233. PH. 1 hit.
SM00155. PLDc. 2 hits.
SM00312. PX. 1 hit.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. False negative.
PS50035. PLD. 2 hits.
PS50195. PX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00122. Choline.
NextBio20676.
SOURCESearch...

Entry information

Entry namePLD2_HUMAN
AccessionPrimary (citable) accession number: O14939
Secondary accession number(s): O43540 expand/collapse secondary AC list , O43579, O43580, Q96BY3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: February 21, 2001
Last modified: June 16, 2009
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents