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Q92539 (LPIN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidate phosphatase LPIN2

EC=3.1.3.4
Alternative name(s):
Lipin-2
Gene names
Name:LPIN2
Synonyms:KIAA0249
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length896 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

Mg2+ By similarity.

Enzyme regulation

Inhibited by N-ethylmaleimide By similarity.

Subcellular location

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

Tissue specificity

Expressed in liver, lung, kidney, placenta, spleen, thymus, lymph node, prostate, testes, small intestine, and colon. Ref.5 Ref.10

Domain

Contains 1 Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif known to be essential for phosphatidate phosphatase activity By similarity.

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

Involvement in disease

Majeed syndrome (MAJEEDS) [MIM:609628]: An 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).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Sequence similarities

Belongs to the lipin family.

Sequence caution

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

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
Transcription
Transcription regulation
   Cellular componentCytoplasm
Endoplasmic reticulum
Membrane
Nucleus
   DiseaseCongenital dyserythropoietic anemia
Disease mutation
Hereditary hemolytic anemia
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular lipid metabolic process

Traceable author statement. Source: Reactome

dephosphorylation

Inferred from sequence or structural similarity. Source: GOC

fatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

lipid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylcholine biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylethanolamine biosynthetic process

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

triglyceride biosynthetic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphatidate phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 896896Phosphatidate phosphatase LPIN2
PRO_0000209881

Regions

Region1 – 108108N-LIP
Region635 – 837203C-LIP
Motif153 – 1586Nuclear localization signal Potential
Motif689 – 6935DXDXT motif
Motif700 – 7045LXXIL motif

Amino acid modifications

Modified residue1061Phosphoserine By similarity
Modified residue1861Phosphoserine By similarity
Modified residue1871Phosphoserine By similarity

Natural variations

Natural variant7341S → L in MAJEEDS. Ref.10
VAR_023817

Sequences

Sequence LengthMass (Da)Tools
Q92539 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 080113FCCA533272

FASTA89699,399
        10         20         30         40         50         60 
MNYVGQLAGQ VIVTVKELYK GINQATLSGC IDVIVVQQQD GSYQCSPFHV RFGKLGVLRS 

        70         80         90        100        110        120 
KEKVIDIEIN GSAVDLHMKL GDNGEAFFVE ETEEEYEKLP AYLATSPIPT EDQFFKDIDT 

       130        140        150        160        170        180 
PLVKSGGDET PSQSSDISHV LETETIFTPS SVKKKKRRRK KYKQDSKKEE QAASAAAEDT 

       190        200        210        220        230        240 
CDVGVSSDDD KGAQAARGSS NASLKEEECK EPLLFHSGDH YPLSDGDWSP LETTYPQTAC 

       250        260        270        280        290        300 
PKSDSELEVK PAESLLRSES HMEWTWGGFP ESTKVSKRER SDHHPRTATI TPSENTHFRV 

       310        320        330        340        350        360 
IPSEDNLISE VEKDASMEDT VCTIVKPKPR ALGTQMSDPT SVAELLEPPL ESTQISSMLD 

       370        380        390        400        410        420 
ADHLPNAALA EAPSESKPAA KVDSPSKKKG VHKRSQHQGP DDIYLDDLKG LEPEVAALYF 

       430        440        450        460        470        480 
PKSESEPGSR QWPESDTLSG SQSPQSVGSA AADSGTECLS DSAMDLPDVT LSLCGGLSEN 

       490        500        510        520        530        540 
GEISKEKFME HIITYHEFAE NPGLIDNPNL VIRIYNRYYN WALAAPMILS LQVFQKSLPK 

       550        560        570        580        590        600 
ATVESWVKDK MPKKSGRWWF WRKRESMTKQ LPESKEGKSE APPASDLPSS SKEPAGARPA 

       610        620        630        640        650        660 
ENDSSSDEGS QELEESITVD PIPTEPLSHG STTSYKKSLR LSSDQIAKLK LHDGPNDVVF 

       670        680        690        700        710        720 
SITTQYQGTC RCAGTIYLWN WNDKIIISDI DGTITKSDAL GQILPQLGKD WTHQGIAKLY 

       730        740        750        760        770        780 
HSINENGYKF LYCSARAIGM ADMTRGYLHW VNDKGTILPR GPLMLSPSSL FSAFHREVIE 

       790        800        810        820        830        840 
KKPEKFKIEC LNDIKNLFAP SKQPFYAAFG NRPNDVYAYT QVGVPDCRIF TVNPKGELIQ 

       850        860        870        880        890 
ERTKGNKSSY HRLSELVEHV FPLLSKEQNS AFPCPEFSSF CYWRDPIPEV DLDDLS 

« Hide

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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]"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.
+Additional computationally mapped references.

Web resources

INFEVERS

Repertory of FMF and hereditary autoinflammatory disorders mutations

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D87436 mRNA. Translation: BAA13380.2. Different initiation.
CH471113 Genomic DNA. Translation: EAX01686.1.
CH471113 Genomic DNA. Translation: EAX01687.1.
BC152448 mRNA. Translation: AAI52449.1.
RefSeqNP_055461.1. NM_014646.2.
XP_005258235.1. XM_005258178.1.
XP_005258236.1. XM_005258179.2.
UniGeneHs.132342.

3D structure databases

ProteinModelPortalQ92539.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115019. 2 interactions.
IntActQ92539. 2 interactions.
STRING9606.ENSP00000261596.

PTM databases

PhosphoSiteQ92539.

Polymorphism databases

DMDM2495724.

Proteomic databases

PaxDbQ92539.
PRIDEQ92539.

Protocols and materials databases

DNASU9663.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261596; ENSP00000261596; ENSG00000101577.
GeneID9663.
KEGGhsa:9663.
UCSCuc002klo.3. human.

Organism-specific databases

CTD9663.
GeneCardsGC18M002906.
HGNCHGNC:14450. LPIN2.
HPACAB015223.
HPA017857.
HPA030550.
MIM605519. gene.
609628. phenotype.
neXtProtNX_Q92539.
Orphanet77297. Majeed syndrome.
PharmGKBPA30437.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5083.
HOGENOMHOG000230954.
HOVERGENHBG052338.
InParanoidQ92539.
KOK15728.
OMAEDTVCTI.
OrthoDBEOG7QZG8X.
PhylomeDBQ92539.
TreeFamTF314095.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ92539.
BgeeQ92539.
CleanExHS_LPIN2.
GenevestigatorQ92539.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
InterProIPR023214. HAD-like_dom.
IPR007651. Lipin_N.
IPR013209. LNS2.
IPR026744. LPIN2.
[Graphical view]
PANTHERPTHR12181:SF11. PTHR12181:SF11. 1 hit.
PfamPF04571. Lipin_N. 1 hit.
PF08235. LNS2. 1 hit.
[Graphical view]
SMARTSM00775. LNS2. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi9663.
NextBio36287.
PROQ92539.
SOURCESearch...

Entry information

Entry nameLPIN2_HUMAN
AccessionPrimary (citable) accession number: Q92539
Secondary accession number(s): A7MD25, D3DUH3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM