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Protein

Phosphatidate phosphatase LPIN2

Gene

LPIN2

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

Functioni

Plays important roles in controlling the metabolism of fatty acids at differents levels. Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis in the reticulum endoplasmic membrane. Acts also as a nuclear transcriptional coactivator for PPARGC1A to modulate lipid metabolism (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity

Enzyme regulationi

Inhibited by N-ethylmaleimide.By similarity

GO - Molecular functioni

  1. phosphatidate phosphatase activity Source: UniProtKB
  2. transcription coactivator activity Source: UniProtKB

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. dephosphorylation Source: GOC
  3. fatty acid catabolic process Source: GO_Central
  4. glycerophospholipid biosynthetic process Source: Reactome
  5. lipid metabolic process Source: UniProtKB
  6. phosphatidylcholine biosynthetic process Source: Reactome
  7. phosphatidylethanolamine biosynthetic process Source: Reactome
  8. phospholipid metabolic process Source: Reactome
  9. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  10. small molecule metabolic process Source: Reactome
  11. transcription, DNA-templated Source: UniProtKB-KW
  12. triglyceride biosynthetic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_1190. Triglyceride Biosynthesis.
REACT_120919. Synthesis of PE.
REACT_121238. Synthesis of PC.
REACT_200828. Depolymerisation of the Nuclear Lamina.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidate phosphatase LPIN2 (EC:3.1.3.4)
Alternative name(s):
Lipin-2
Gene namesi
Name:LPIN2
Synonyms:KIAA0249
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:14450. LPIN2.

Subcellular locationi

Nucleus By similarity. Cytoplasmcytosol By similarity. Endoplasmic reticulum membrane By similarity
Note: Translocates to endoplasmic reticulum membrane with increasing levels of oleate.By similarity

GO - Cellular componenti

  1. cytosol Source: GO_Central
  2. endoplasmic reticulum membrane Source: GO_Central
  3. nucleus Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Majeed syndrome1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive syndrome characterized by chronic recurrent multifocal osteomyelitis that is of early onset with a lifelong course, congenital dyserythropoietic anemia that presents as hypochromic, microcytic anemia during the first year of life and ranges from mild to transfusion-dependent, and transient inflammatory dermatosis, often manifesting as Sweet syndrome (neutrophilic skin infiltration).

See also OMIM:609628
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti734 – 7341S → L in MAJEEDS. 1 Publication
VAR_023817

Keywords - Diseasei

Congenital dyserythropoietic anemia, Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

MIMi609628. phenotype.
Orphaneti77297. Majeed syndrome.
PharmGKBiPA30437.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 896896Phosphatidate phosphatase LPIN2PRO_0000209881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei186 – 1861PhosphoserineBy similarity
Modified residuei187 – 1871PhosphoserineBy similarity
Modified residuei566 – 5661Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ92539.
PaxDbiQ92539.
PRIDEiQ92539.

PTM databases

DEPODiQ92539.
PhosphoSiteiQ92539.

Expressioni

Tissue specificityi

Expressed in liver, lung, kidney, placenta, spleen, thymus, lymph node, prostate, testes, small intestine, and colon.2 Publications

Gene expression databases

BgeeiQ92539.
CleanExiHS_LPIN2.
ExpressionAtlasiQ92539. baseline and differential.
GenevestigatoriQ92539.

Organism-specific databases

HPAiCAB015223.
HPA017857.
HPA030550.

Interactioni

Protein-protein interaction databases

BioGridi115019. 3 interactions.
IntActiQ92539. 2 interactions.
STRINGi9606.ENSP00000261596.

Structurei

3D structure databases

ProteinModelPortaliQ92539.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 108108N-LIPAdd
BLAST
Regioni635 – 837203C-LIPAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi153 – 1586Nuclear localization signalSequence Analysis
Motifi689 – 6935DXDXT motif
Motifi700 – 7045LXXIL motif

Domaini

Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, a motif known to be a transcriptional binding motif.By similarity

Sequence similaritiesi

Belongs to the lipin family.Curated

Phylogenomic databases

eggNOGiCOG5083.
GeneTreeiENSGT00390000011286.
HOGENOMiHOG000230954.
HOVERGENiHBG052338.
InParanoidiQ92539.
KOiK15728.
OMAiMEDTVCT.
OrthoDBiEOG7QZG8X.
PhylomeDBiQ92539.
TreeFamiTF314095.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR007651. Lipin_N.
IPR013209. LNS2.
IPR026744. LPIN2.
[Graphical view]
PANTHERiPTHR12181:SF11. PTHR12181:SF11. 1 hit.
PfamiPF04571. Lipin_N. 1 hit.
PF08235. LNS2. 1 hit.
[Graphical view]
SMARTiSM00775. LNS2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.

Sequencei

Sequence statusi: Complete.

Q92539-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYVGQLAGQ VIVTVKELYK GINQATLSGC IDVIVVQQQD GSYQCSPFHV
60 70 80 90 100
RFGKLGVLRS KEKVIDIEIN GSAVDLHMKL GDNGEAFFVE ETEEEYEKLP
110 120 130 140 150
AYLATSPIPT EDQFFKDIDT PLVKSGGDET PSQSSDISHV LETETIFTPS
160 170 180 190 200
SVKKKKRRRK KYKQDSKKEE QAASAAAEDT CDVGVSSDDD KGAQAARGSS
210 220 230 240 250
NASLKEEECK EPLLFHSGDH YPLSDGDWSP LETTYPQTAC PKSDSELEVK
260 270 280 290 300
PAESLLRSES HMEWTWGGFP ESTKVSKRER SDHHPRTATI TPSENTHFRV
310 320 330 340 350
IPSEDNLISE VEKDASMEDT VCTIVKPKPR ALGTQMSDPT SVAELLEPPL
360 370 380 390 400
ESTQISSMLD ADHLPNAALA EAPSESKPAA KVDSPSKKKG VHKRSQHQGP
410 420 430 440 450
DDIYLDDLKG LEPEVAALYF PKSESEPGSR QWPESDTLSG SQSPQSVGSA
460 470 480 490 500
AADSGTECLS DSAMDLPDVT LSLCGGLSEN GEISKEKFME HIITYHEFAE
510 520 530 540 550
NPGLIDNPNL VIRIYNRYYN WALAAPMILS LQVFQKSLPK ATVESWVKDK
560 570 580 590 600
MPKKSGRWWF WRKRESMTKQ LPESKEGKSE APPASDLPSS SKEPAGARPA
610 620 630 640 650
ENDSSSDEGS QELEESITVD PIPTEPLSHG STTSYKKSLR LSSDQIAKLK
660 670 680 690 700
LHDGPNDVVF SITTQYQGTC RCAGTIYLWN WNDKIIISDI DGTITKSDAL
710 720 730 740 750
GQILPQLGKD WTHQGIAKLY HSINENGYKF LYCSARAIGM ADMTRGYLHW
760 770 780 790 800
VNDKGTILPR GPLMLSPSSL FSAFHREVIE KKPEKFKIEC LNDIKNLFAP
810 820 830 840 850
SKQPFYAAFG NRPNDVYAYT QVGVPDCRIF TVNPKGELIQ ERTKGNKSSY
860 870 880 890
HRLSELVEHV FPLLSKEQNS AFPCPEFSSF CYWRDPIPEV DLDDLS
Length:896
Mass (Da):99,399
Last modified:February 1, 1997 - v1
Checksum:i080113FCCA533272
GO

Sequence cautioni

The sequence BAA13380.2 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti734 – 7341S → L in MAJEEDS. 1 Publication
VAR_023817

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87436 mRNA. Translation: BAA13380.2. Different initiation.
CH471113 Genomic DNA. Translation: EAX01686.1.
CH471113 Genomic DNA. Translation: EAX01687.1.
BC152448 mRNA. Translation: AAI52449.1.
CCDSiCCDS11829.1.
RefSeqiNP_055461.1. NM_014646.2.
XP_005258235.1. XM_005258178.1.
XP_005258236.1. XM_005258179.2.
XP_006722431.1. XM_006722368.1.
UniGeneiHs.132342.

Genome annotation databases

EnsembliENST00000261596; ENSP00000261596; ENSG00000101577.
GeneIDi9663.
KEGGihsa:9663.
UCSCiuc002klo.3. human.

Polymorphism databases

DMDMi2495724.

Cross-referencesi

Web resourcesi

INFEVERS

Repertory of FMF and hereditary autoinflammatory disorders mutations

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87436 mRNA. Translation: BAA13380.2. Different initiation.
CH471113 Genomic DNA. Translation: EAX01686.1.
CH471113 Genomic DNA. Translation: EAX01687.1.
BC152448 mRNA. Translation: AAI52449.1.
CCDSiCCDS11829.1.
RefSeqiNP_055461.1. NM_014646.2.
XP_005258235.1. XM_005258178.1.
XP_005258236.1. XM_005258179.2.
XP_006722431.1. XM_006722368.1.
UniGeneiHs.132342.

3D structure databases

ProteinModelPortaliQ92539.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115019. 3 interactions.
IntActiQ92539. 2 interactions.
STRINGi9606.ENSP00000261596.

PTM databases

DEPODiQ92539.
PhosphoSiteiQ92539.

Polymorphism databases

DMDMi2495724.

Proteomic databases

MaxQBiQ92539.
PaxDbiQ92539.
PRIDEiQ92539.

Protocols and materials databases

DNASUi9663.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261596; ENSP00000261596; ENSG00000101577.
GeneIDi9663.
KEGGihsa:9663.
UCSCiuc002klo.3. human.

Organism-specific databases

CTDi9663.
GeneCardsiGC18M002906.
GeneReviewsiLPIN2.
HGNCiHGNC:14450. LPIN2.
HPAiCAB015223.
HPA017857.
HPA030550.
MIMi605519. gene.
609628. phenotype.
neXtProtiNX_Q92539.
Orphaneti77297. Majeed syndrome.
PharmGKBiPA30437.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5083.
GeneTreeiENSGT00390000011286.
HOGENOMiHOG000230954.
HOVERGENiHBG052338.
InParanoidiQ92539.
KOiK15728.
OMAiMEDTVCT.
OrthoDBiEOG7QZG8X.
PhylomeDBiQ92539.
TreeFamiTF314095.

Enzyme and pathway databases

ReactomeiREACT_1190. Triglyceride Biosynthesis.
REACT_120919. Synthesis of PE.
REACT_121238. Synthesis of PC.
REACT_200828. Depolymerisation of the Nuclear Lamina.

Miscellaneous databases

GenomeRNAii9663.
NextBioi36287.
PROiQ92539.
SOURCEiSearch...

Gene expression databases

BgeeiQ92539.
CleanExiHS_LPIN2.
ExpressionAtlasiQ92539. baseline and differential.
GenevestigatoriQ92539.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR007651. Lipin_N.
IPR013209. LNS2.
IPR026744. LPIN2.
[Graphical view]
PANTHERiPTHR12181:SF11. PTHR12181:SF11. 1 hit.
PfamiPF04571. Lipin_N. 1 hit.
PF08235. LNS2. 1 hit.
[Graphical view]
SMARTiSM00775. LNS2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
    Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
    DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
  4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns."
    Donkor J., Sariahmetoglu M., Dewald J., Brindley D.N., Reue K.
    J. Biol. Chem. 282:3450-3457(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Homozygous mutations in LPIN2 are responsible for the syndrome of chronic recurrent multifocal osteomyelitis and congenital dyserythropoietic anaemia (Majeed syndrome)."
    Ferguson P.J., Chen S., Tayeh M.K., Ochoa L., Leal S.M., Pelet A., Munnich A., Lyonnet S., Majeed H.A., El-Shanti H.
    J. Med. Genet. 42:551-557(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MAJEEDS LEU-734, TISSUE SPECIFICITY.

Entry informationi

Entry nameiLPIN2_HUMAN
AccessioniPrimary (citable) accession number: Q92539
Secondary accession number(s): A7MD25, D3DUH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: March 4, 2015
This is version 113 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 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.