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Q8BJ56

- PLPL2_MOUSE

UniProt

Q8BJ56 - PLPL2_MOUSE

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Protein
Patatin-like phospholipase domain-containing protein 2
Gene
Pnpla2, Atgl
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. Also has acylglycerol transacylase activity. May act coordinately with LIPE/HLS within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes. May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion.6 Publications

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.1 Publication

Enzyme regulationi

Stimulated by PKA-dependent PLIN phosphorylation.3 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei47 – 471

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. triglyceride lipase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. lipid particle organization Source: MGI
  2. lipid storage Source: UniProtKB
  3. negative regulation of sequestering of triglyceride Source: UniProtKB
  4. positive regulation of triglyceride catabolic process Source: UniProtKB
  5. triglyceride catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_199036. Acyl chain remodeling of DAG and TAG.
UniPathwayiUPA00256.

Names & Taxonomyi

Protein namesi
Recommended name:
Patatin-like phospholipase domain-containing protein 2 (EC:3.1.1.3)
Alternative name(s):
Adipose triglyceride lipase
Desnutrin
Gene namesi
Name:Pnpla2
Synonyms:Atgl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1914103. Pnpla2.

Subcellular locationi

Lipid droplet. Cell membrane; Single-pass type II membrane protein 3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88Cytoplasmic Reviewed prediction
Transmembranei9 – 2921Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini30 – 486457Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cytosol Source: MGI
  2. integral component of membrane Source: UniProtKB-KW
  3. lipid particle Source: UniProtKB
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Lipid droplet, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice show increased adipose mass and triacylglycerol deposition in multiple tissues. They accumulate large amounts of lipid in the heart, causing cardiac dysfunction and premature death.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471S → A: Loss of triacylglycerol hydrolysis activity. 1 Publication
Mutagenesisi396 – 3961S → A: Slightly reduced TG hydrolase activity. 1 Publication
Mutagenesisi406 – 4061S → A: Reduced TG hydrolase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Patatin-like phospholipase domain-containing protein 2
PRO_0000292528Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391N-linked (GlcNAc...) Reviewed prediction
Modified residuei374 – 3741Phosphoserine; in vitro1 Publication
Modified residuei396 – 3961Phosphoserine; by PKA1 Publication
Modified residuei406 – 4061Phosphoserine; by PKA1 Publication
Modified residuei430 – 4301Phosphoserine; in vitro1 Publication
Modified residuei468 – 4681Phosphoserine; in vitro1 Publication

Post-translational modificationi

Phosphorylation at Ser-406 by PKA is increased during fasting and moderate intensity exercise, and moderately increases lipolytic activity.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8BJ56.
PaxDbiQ8BJ56.
PRIDEiQ8BJ56.

PTM databases

PhosphoSiteiQ8BJ56.

Expressioni

Tissue specificityi

Expressed at high levels in white and brown adipose tissue, and to a lesser degree in testis and cardiac muscle. Barely detected in liver, spleen, thymus, kidney, skeletal muscle, and brain. Among the white adipose depots, gonadal fat showed the highest level of expression compared with inguinal and renal white adipose tissues.4 Publications

Developmental stagei

Increased expression when preadipocytes are induced to differentiate to adipocytes. Not detected in proliferating or confluent preadipocytes.4 Publications

Inductioni

Transiently induced during fasting. cAMP and glucagon may not be involved in the induction during fasting. Induced by dexamethasone. Down-regulated by insulin, isoprotenerol and TNF-alfa. Expression is not affected by glucose and by growth hormone. Expression is reduced in fasted leptin deficient mouse (ob/ob), an obese mouse model. Expression is not affected in fed ob/ob mouse.8 Publications

Gene expression databases

ArrayExpressiQ8BJ56.
BgeeiQ8BJ56.
CleanExiMM_PNPLA2.
GenevestigatoriQ8BJ56.

Interactioni

Subunit structurei

Interacts with ABHD5; this association stimulates PNPLA2 triglyceride hydrolase activity. Interacts with SERPINF1; interacts at one site of interaction By similarity. Despite a colocalization in lipid droplets, it probably does not interact with PLIN. Interacts with PLIN5; prevents interaction with ABHD5.4 Publications

Protein-protein interaction databases

BioGridi211763. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8BJ56.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 179170Patatin
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 495GXSXG

Sequence similaritiesi

Contains 1 patatin domain.

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG261571.
GeneTreeiENSGT00390000005295.
HOVERGENiHBG007046.
InParanoidiQ8BJ56.
KOiK16816.
OMAiLVLREMC.
OrthoDBiEOG7J9VQR.
PhylomeDBiQ8BJ56.
TreeFamiTF314272.

Family and domain databases

InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR002641. Patatin/PLipase_A2-rel.
[Graphical view]
PfamiPF01734. Patatin. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BJ56-1) [UniParc]FASTAAdd to Basket

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

MFPRETKWNI SFAGCGFLGV YHIGVASCLR EHAPFLVANA THIYGASAGA    50
LTATALVTGA CLGEAGANII EVSKEARKRF LGPLHPSFNL VKTIRGCLLK 100
TLPADCHERA NGRLGISLTR VSDGENVIIS HFSSKDELIQ ANVCSTFIPV 150
YCGLIPPTLQ GVRYVDGGIS DNLPLYELKN TITVSPFSGE SDICPQDSST 200
NIHELRVTNT SIQFNLRNLY RLSKALFPPE PMVLREMCKQ GYRDGLRFLR 250
RNGLLNQPNP LLALPPVVPQ EEDAEEAAVV EERAGEEDQL QPYRKDRILE 300
HLPARLNEAL LEACVEPKDL MTTLSNMLPV RLATAMMVPY TLPLESAVSF 350
TIRLLEWLPD VPEDIRWMKE QTGSICQYLV MRAKRKLGDH LPSRLSEQVE 400
LRRAQSLPSV PLSCATYSEA LPNWVRNNLS LGDALAKWEE CQRQLLLGLF 450
CTNVAFPPDA LRMRAPASPT AADPATPQDP PGLPPC 486
Length:486
Mass (Da):53,657
Last modified:March 1, 2003 - v1
Checksum:i512FE1931B72FC9C
GO
Isoform 2 (identifier: Q8BJ56-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     253-308: Missing.

Note: No experimental confirmation available.

Show »
Length:430
Mass (Da):47,364
Checksum:i16F03A3A9B559E6A
GO
Isoform 3 (identifier: Q8BJ56-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.
     57-62: VTGACL → MSHACQ

Note: No experimental confirmation available.

Show »
Length:430
Mass (Da):47,877
Checksum:i1A66AF92E3D62A4F
GO

Sequence cautioni

The sequence BAB22643.1 differs from that shown. Reason: Frameshift at positions 301, 317 and 460.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5656Missing in isoform 3.
VSP_026422Add
BLAST
Alternative sequencei57 – 626VTGACL → MSHACQ in isoform 3.
VSP_026423
Alternative sequencei253 – 30856Missing in isoform 2.
VSP_026424Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31P → T in BAB22387. 1 Publication
Sequence conflicti30 – 301R → H in AAU33824. 1 Publication
Sequence conflicti193 – 1931I → V in BAE29364. 1 Publication
Sequence conflicti319 – 3202DL → VG in BAB22643. 1 Publication
Sequence conflicti362 – 3621P → T in BAE29364. 1 Publication
Sequence conflicti385 – 3851R → G in AAC36536. 1 Publication
Sequence conflicti389 – 3891D → G in AAH64747. 1 Publication
Sequence conflicti412 – 4121L → P in AAC36536. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY731699 mRNA. Translation: AAU33824.1.
AY894805 mRNA. Translation: AAW81963.1.
AY510273 mRNA. Translation: AAS48458.1.
AK002826 mRNA. Translation: BAB22387.1.
AK003207 mRNA. Translation: BAB22643.1. Frameshift.
AK031609 mRNA. Translation: BAC27476.1.
AK150184 mRNA. Translation: BAE29364.1.
BC019188 mRNA. Translation: AAH19188.1.
BC044781 mRNA. Translation: AAH44781.1.
BC064747 mRNA. Translation: AAH64747.1.
U89431 mRNA. Translation: AAC36536.1.
CCDSiCCDS22015.1. [Q8BJ56-2]
CCDS52445.1. [Q8BJ56-1]
RefSeqiNP_001157161.1. NM_001163689.1. [Q8BJ56-1]
NP_080078.2. NM_025802.3. [Q8BJ56-2]
UniGeneiMm.29998.

Genome annotation databases

EnsembliENSMUST00000064151; ENSMUSP00000065116; ENSMUSG00000025509. [Q8BJ56-2]
ENSMUST00000164016; ENSMUSP00000127149; ENSMUSG00000025509. [Q8BJ56-1]
GeneIDi66853.
KEGGimmu:66853.
UCSCiuc009klg.2. mouse. [Q8BJ56-2]
uc009klh.2. mouse. [Q8BJ56-3]
uc009kli.2. mouse. [Q8BJ56-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY731699 mRNA. Translation: AAU33824.1 .
AY894805 mRNA. Translation: AAW81963.1 .
AY510273 mRNA. Translation: AAS48458.1 .
AK002826 mRNA. Translation: BAB22387.1 .
AK003207 mRNA. Translation: BAB22643.1 . Frameshift.
AK031609 mRNA. Translation: BAC27476.1 .
AK150184 mRNA. Translation: BAE29364.1 .
BC019188 mRNA. Translation: AAH19188.1 .
BC044781 mRNA. Translation: AAH44781.1 .
BC064747 mRNA. Translation: AAH64747.1 .
U89431 mRNA. Translation: AAC36536.1 .
CCDSi CCDS22015.1. [Q8BJ56-2 ]
CCDS52445.1. [Q8BJ56-1 ]
RefSeqi NP_001157161.1. NM_001163689.1. [Q8BJ56-1 ]
NP_080078.2. NM_025802.3. [Q8BJ56-2 ]
UniGenei Mm.29998.

3D structure databases

ProteinModelPortali Q8BJ56.
ModBasei Search...

Protein-protein interaction databases

BioGridi 211763. 4 interactions.

PTM databases

PhosphoSitei Q8BJ56.

Proteomic databases

MaxQBi Q8BJ56.
PaxDbi Q8BJ56.
PRIDEi Q8BJ56.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000064151 ; ENSMUSP00000065116 ; ENSMUSG00000025509 . [Q8BJ56-2 ]
ENSMUST00000164016 ; ENSMUSP00000127149 ; ENSMUSG00000025509 . [Q8BJ56-1 ]
GeneIDi 66853.
KEGGi mmu:66853.
UCSCi uc009klg.2. mouse. [Q8BJ56-2 ]
uc009klh.2. mouse. [Q8BJ56-3 ]
uc009kli.2. mouse. [Q8BJ56-1 ]

Organism-specific databases

CTDi 57104.
MGIi MGI:1914103. Pnpla2.

Phylogenomic databases

eggNOGi NOG261571.
GeneTreei ENSGT00390000005295.
HOVERGENi HBG007046.
InParanoidi Q8BJ56.
KOi K16816.
OMAi LVLREMC.
OrthoDBi EOG7J9VQR.
PhylomeDBi Q8BJ56.
TreeFami TF314272.

Enzyme and pathway databases

UniPathwayi UPA00256 .
Reactomei REACT_199036. Acyl chain remodeling of DAG and TAG.

Miscellaneous databases

ChiTaRSi PNPLA2. mouse.
NextBioi 322819.
PROi Q8BJ56.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8BJ56.
Bgeei Q8BJ56.
CleanExi MM_PNPLA2.
Genevestigatori Q8BJ56.

Family and domain databases

InterProi IPR016035. Acyl_Trfase/lysoPLipase.
IPR002641. Patatin/PLipase_A2-rel.
[Graphical view ]
Pfami PF01734. Patatin. 1 hit.
[Graphical view ]
SUPFAMi SSF52151. SSF52151. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Desnutrin, an adipocyte gene encoding a novel patatin domain-containing protein, is induced by fasting and glucocorticoids: ectopic expression of desnutrin increases triglyceride hydrolysis."
    Villena J.A., Roy S., Sarkadi-Nagy E., Kim K.-H., Sul H.S.
    J. Biol. Chem. 279:47066-47075(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
    Strain: C57BL/6.
    Tissue: White adipose tissue.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
    Strain: C57BL/6.
  3. "The adipose tissue triglyceride lipase ATGL/PNPLA2 is downregulated by insulin and TNF-alpha in 3T3-L1 adipocytes and is a target for transactivation by PPARgamma."
    Kim J.Y., Tillison K., Lee J.-H., Rearick D.A., Smas C.M.
    Am. J. Physiol. 291:E115-E127(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
    Strain: C57BL/6.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Bone marrow, Kidney and Testis.
  5. "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] (ISOFORMS 1 AND 3).
    Strain: FVB/N.
    Tissue: Trophoblast stem cell.
  6. "Expressed genes in interleukin-4 treated B cells identified by cDNA representational difference analysis."
    Chu C.C., Paul W.E.
    Mol. Immunol. 35:487-502(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 296-473.
    Strain: BALB/c.
    Tissue: Spleen.
  7. "Expression, regulation, and triglyceride hydrolase activity of Adiponutrin family members."
    Lake A.C., Sun Y., Li J.-L., Kim J.E., Johnson J.W., Li D., Revett T., Shih H.H., Liu W., Paulsen J.E., Gimeno R.E.
    J. Lipid Res. 46:2477-2487(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
  8. "Isoproterenol, TNFalpha, and insulin downregulate adipose triglyceride lipase in 3T3-L1 adipocytes."
    Kralisch S., Klein J., Lossner U., Bluher M., Paschke R., Stumvoll M., Fasshauer M.
    Mol. Cell. Endocrinol. 240:43-49(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is activated by CGI-58 and defective in Chanarin-Dorfman Syndrome."
    Lass A., Zimmermann R., Haemmerle G., Riederer M., Schoiswohl G., Schweiger M., Kienesberger P., Strauss J.G., Gorkiewicz G., Zechner R.
    Cell Metab. 3:309-319(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ABHD5, MUTAGENESIS OF SER-47.
  10. "Adipose triglyceride lipase: function, regulation by insulin, and comparison with adiponutrin."
    Kershaw E.E., Hamm J.K., Verhagen L.A.W., Peroni O., Katic M., Flier J.S.
    Diabetes 55:148-157(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "Adipose triglyceride lipase and hormone-sensitive lipase are the major enzymes in adipose tissue triacylglycerol catabolism."
    Schweiger M., Schreiber R., Haemmerle G., Lass A., Fledelius C., Jacobsen P., Tornqvist H., Zechner R., Zimmermann R.
    J. Biol. Chem. 281:40236-40241(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  12. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  13. "Control of adipose triglyceride lipase action by serine 517 of perilipin A globally regulates protein kinase A-stimulated lipolysis in adipocytes."
    Miyoshi H., Perfield J.W. II, Souza S.C., Shen W.-J., Zhang H.-H., Stancheva Z.S., Kraemer F.B., Obin M.S., Greenberg A.S.
    J. Biol. Chem. 282:996-1002(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  14. "Analysis of lipolytic protein trafficking and interactions in adipocytes."
    Granneman J.G., Moore H.-P.H., Granneman R.L., Greenberg A.S., Obin M.S., Zhu Z.
    J. Biol. Chem. 282:5726-5735(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ABHD5, LACK OF INTERACTION WITH PLIN.
  15. "Interactions of perilipin-5 (Plin5) with adipose triglyceride lipase."
    Granneman J.G., Moore H.P., Mottillo E.P., Zhu Z., Zhou L.
    J. Biol. Chem. 286:5126-5135(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLIN5, EXCLUSION OF INTERACTION WITH ABHD5.
  16. "Unique regulation of adipose triglyceride lipase (ATGL) by perilipin 5, a lipid droplet-associated protein."
    Wang H., Bell M., Sreenivasan U., Sreenevasan U., Hu H., Liu J., Dalen K., Londos C., Yamaguchi T., Rizzo M.A., Coleman R., Gong D., Brasaemle D., Sztalryd C.
    J. Biol. Chem. 286:15707-15715(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLIN5.
  17. "Identification and functional characterization of protein kinase A phosphorylation sites in the major lipolytic protein, adipose triglyceride lipase."
    Pagnon J., Matzaris M., Stark R., Meex R.C., Macaulay S.L., Brown W., O'Brien P.E., Tiganis T., Watt M.J.
    Endocrinology 153:4278-4289(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-374; SER-396; SER-406; SER-430 AND SER-468, MUTAGENESIS OF SER-396 AND SER-406.

Entry informationi

Entry nameiPLPL2_MOUSE
AccessioniPrimary (citable) accession number: Q8BJ56
Secondary accession number(s): O89080
, Q05BJ0, Q3UD97, Q643S0, Q6P234, Q9D1Q9, Q9DCF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi