Q14693 (LPIN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidate phosphatase LPIN1
EC=3.1.3.4

Alternative name(s):
Lipin-1

Gene names

Name:	LPIN1
Synonyms:	KIAA0188

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	890 AA.
Sequence status	Complete.
Protein existence	Evidence 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/PPARA to modulate lipid metabolism gene expression By similarity. Is involved in adipocyte differentiation. May also be involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol 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.
Subunit structure	Interacts (via LXXIL motif) with PPARA By similarity. Interacts with PPARGC1A By similarity. Interaction with PPARA and PPARGC1A leads to the formation of a complex that modulates gene transcription By similarity. Interacts with MEF2C By similarity.
Subcellular location	Nucleus membrane By similarity. Cytoplasm › cytosol By similarity. Endoplasmic reticulum membrane By similarity.
Tissue specificity	Specifically expressed in skeletal muscle. Also abundant in adipose tissue. Lower levels in some portions of the digestive tract. Ref.6 Ref.13
Domain	Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL), a transcriptional binding motif, which mediates interaction with PPARA By similarity. Contains 1 Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif essential for phosphatidate phosphatase activity By similarity.
Post-translational modification	Phosphorylated at multiple sites in response to insulin. Phosphorylation is controlled by the mTOR signaling pathway. Phosphorylation is decreased by epinephrine. Phosphorylation may not directly affect the catalytic activity but may regulate the localization. Dephosphorylated by the CTDNEP1-CNEP1R1 complex By similarity. Sumoylated By similarity.
Involvement in disease	Myoglobinuria, acute recurrent, autosomal recessive (ARARM) [MIM:268200]: Recurrent myoglobinuria is characterized by recurrent attacks of rhabdomyolysis (necrosis or disintegration of skeletal muscle) associated with muscle pain and weakness and followed by excretion of myoglobin in the urine. Renal failure may occasionally occur. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11
Miscellaneous	May represent a candidate gene for human lipodysytropy syndromes.
Sequence similarities	Belongs to the lipin family.
Sequence caution	The sequence BAA11505.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism Transcription Transcription regulation
Cellular component	Cytoplasm Endoplasmic reticulum Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton reorganization Inferred from electronic annotation. Source: Compara cellular response to insulin stimulus Inferred from electronic annotation. Source: Compara fatty acid catabolic process Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial fission Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara organ regeneration Inferred from electronic annotation. Source: Compara phosphatidylcholine biosynthetic process Traceable author statement. Source: Reactome phosphatidylethanolamine biosynthetic process Traceable author statement. Source: Reactome positive regulation of histone deacetylation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara regulation of fat cell differentiation Inferred from electronic annotation. Source: Compara ruffle organization Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW triglyceride biosynthetic process Traceable author statement. Source: Reactome triglyceride mobilization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Traceable author statement. Source: Reactome nuclear membrane Inferred from sequence or structural similarity. Source: UniProtKB transcription factor complex Inferred from electronic annotation. Source: Compara
Molecular_function	phosphatidate phosphatase activity Inferred from electronic annotation. Source: EC transcription coactivator activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q14693-1)

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 2 (identifier: Q14693-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSRVQTM

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 890	890	Phosphatidate phosphatase LPIN1		PRO_0000209879
Regions
	Region	1 – 108	108	N-LIP
	Region	624 – 830	207	C-LIP
	Motif	153 – 158	6	Nuclear localization signal Potential
	Motif	678 – 682	5	DXDXT motif
	Motif	689 – 693	5	LXXIL motif
	Compositional bias	147 – 150	4	Poly-Ser
	Compositional bias	598 – 601	4	Poly-Ser
Amino acid modifications
	Modified residue	106	1	Phosphoserine By similarity
	Modified residue	150	1	Phosphoserine By similarity
	Modified residue	252	1	Phosphoserine By similarity
	Modified residue	254	1	Phosphoserine By similarity
	Modified residue	260	1	Phosphoserine By similarity
	Modified residue	264	1	Phosphothreonine By similarity
	Modified residue	294	1	Phosphoserine By similarity
	Modified residue	434	1	Phosphoserine By similarity
	Modified residue	438	1	Phosphoserine By similarity
	Modified residue	449	1	Phosphoserine By similarity
	Modified residue	600	1	Phosphoserine By similarity
	Modified residue	601	1	Phosphoserine By similarity
	Modified residue	887	1	Phosphoserine By similarity
	Modified residue	889	1	Phosphoserine By similarity
	Cross-link	565		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	595		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	1	1	M → MSRVQTM in isoform 2.		VSP_045533
	Natural variant	56	1	G → E in a colorectal cancer sample; somatic mutation. Ref.10		VAR_035874
	Natural variant	610	1	P → S. Ref.9 Corresponds to variant rs4669781 [ dbSNP | Ensembl ].		VAR_013885
	Natural variant	637	1	S → T. Ref.5 Corresponds to variant rs17852755 [ dbSNP | Ensembl ].		VAR_054878
Experimental info
	Sequence conflict	316	1	D → Y in BAH13844. Ref.2
	Sequence conflict	535	1	K → R in BAH13844. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 10, 2002. Version 2. Checksum: 781761FC47E9CEE7	FASTA	890	98,664
	10 20 30 40 50 60 MNYVGQLAGQ VFVTVKELYK GLNPATLSGC IDIIVIRQPN GNLQCSPFHV RFGKMGVLRS 70 80 90 100 110 120 REKVVDIEIN GESVDLHMKL GDNGEAFFVQ ETDNDQEVIP MHLATSPILS EGASRMECQL 130 140 150 160 170 180 KRGSVDRMRG LDPSTPAQVI APSETPSSSS VVKKRRKRRR KSQLDSLKRD DNMNTSEDED 190 200 210 220 230 240 MFPIEMSSDE AMELLESSRT LPNDIPPFQD DIPEENLSLA VIYPQSASYP NSDREWSPTP 250 260 270 280 290 300 SPSGSRPSTP KSDSELVSKS TERTGQKNPE MLWLWGELPQ AAKSSSPHKM KESSPLSSRK 310 320 330 340 350 360 ICDKSHFQAI HSESSDTFSD QSPTLVGGAL LDQNKPQTEM QFVNEEDLET LGAAAPLLPM 370 380 390 400 410 420 IEELKPPSAS VVQTANKTDS PSRKRDKRSR HLGADGVYLD DLTDMDPEVA ALYFPKNGDP 430 440 450 460 470 480 SGLAKHASDN GARSANQSPQ SVGSSGVDSG VESTSDGLRD LPSIAISLCG GLSDHREITK 490 500 510 520 530 540 DAFLEQAVSY QQFVDNPAII DDPNLVVKIG SKYYNWTTAA PLLLAMQAFQ KPLPKATVES 550 560 570 580 590 600 IMRDKMPKKG GRWWFSWRGR NTTIKEESKP EQCLAGKAHS TGEQPPQLSL ATRVKHESSS 610 620 630 640 650 660 SDEERAAAKP SNAGHLPLLP NVSYKKTLRL TSEQLKSLKL KNGPNDVVFS VTTQYQGTCR 670 680 690 700 710 720 CEGTIYLWNW DDKVIISDID GTITRSDTLG HILPTLGKDW THQGIAKLYH KVSQNGYKFL 730 740 750 760 770 780 YCSARAIGMA DMTRGYLHWV NERGTVLPQG PLLLSPSSLF SALHREVIEK KPEKFKVQCL 790 800 810 820 830 840 TDIKNLFFPN TEPFYAAFGN RPADVYSYKQ VGVSLNRIFT VNPKGELVQE HAKTNISSYV 850 860 870 880 890 RLCEVVDHVF PLLKRSHSSD FPCSDTFSNF TFWREPLPPF ENQDIHSASA
	Isoform 2 [UniParc]. Checksum: CBE905D33C8D62CD	FASTA	896	99,367
	10 20 30 40 50 60 MSRVQTMNYV GQLAGQVFVT VKELYKGLNP ATLSGCIDII VIRQPNGNLQ CSPFHVRFGK 70 80 90 100 110 120 MGVLRSREKV VDIEINGESV DLHMKLGDNG EAFFVQETDN DQEVIPMHLA TSPILSEGAS 130 140 150 160 170 180 RMECQLKRGS VDRMRGLDPS TPAQVIAPSE TPSSSSVVKK RRKRRRKSQL DSLKRDDNMN 190 200 210 220 230 240 TSEDEDMFPI EMSSDEAMEL LESSRTLPND IPPFQDDIPE ENLSLAVIYP QSASYPNSDR 250 260 270 280 290 300 EWSPTPSPSG SRPSTPKSDS ELVSKSTERT GQKNPEMLWL WGELPQAAKS SSPHKMKESS 310 320 330 340 350 360 PLSSRKICDK SHFQAIHSES SDTFSDQSPT LVGGALLDQN KPQTEMQFVN EEDLETLGAA 370 380 390 400 410 420 APLLPMIEEL KPPSASVVQT ANKTDSPSRK RDKRSRHLGA DGVYLDDLTD MDPEVAALYF 430 440 450 460 470 480 PKNGDPSGLA KHASDNGARS ANQSPQSVGS SGVDSGVEST SDGLRDLPSI AISLCGGLSD 490 500 510 520 530 540 HREITKDAFL EQAVSYQQFV DNPAIIDDPN LVVKIGSKYY NWTTAAPLLL AMQAFQKPLP 550 560 570 580 590 600 KATVESIMRD KMPKKGGRWW FSWRGRNTTI KEESKPEQCL AGKAHSTGEQ PPQLSLATRV 610 620 630 640 650 660 KHESSSSDEE RAAAKPSNAG HLPLLPNVSY KKTLRLTSEQ LKSLKLKNGP NDVVFSVTTQ 670 680 690 700 710 720 YQGTCRCEGT IYLWNWDDKV IISDIDGTIT RSDTLGHILP TLGKDWTHQG IAKLYHKVSQ 730 740 750 760 770 780 NGYKFLYCSA RAIGMADMTR GYLHWVNERG TVLPQGPLLL SPSSLFSALH REVIEKKPEK 790 800 810 820 830 840 FKVQCLTDIK NLFFPNTEPF YAAFGNRPAD VYSYKQVGVS LNRIFTVNPK GELVQEHAKT 850 860 870 880 890 NISSYVRLCE VVDHVFPLLK RSHSSDFPCS DTFSNFTFWR EPLPPFENQD IHSASA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N. DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Bone marrow.
[2]	"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] (ISOFORMS 1 AND 2). Tissue: Testis and Thalamus.
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton 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. , 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].
[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] (ISOFORM 1), VARIANT THR-637. Tissue: Uterus.
[6]	"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.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[8]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[9]	"Identification of single-nucleotide polymorphisms in the human LPIN1 gene." Cao H., Hegele R.A. J. Hum. Genet. 47:370-372(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SER-610.
[10]	"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. , 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] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-56.
[11]	"Mutations in LPIN1 cause recurrent acute myoglobinuria in childhood." Zeharia A., Shaag A., Houtkooper R.H., Hindi T., de Lonlay P., Erez G., Hubert L., Saada A., de Keyzer Y., Eshel G., Vaz F.M., Pines O., Elpeleg O. Am. J. Hum. Genet. 83:489-494(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN ARARM.
[12]	Erratum Zeharia A., Shaag A., Houtkooper R.H., Hindi T., de Lonlay P., Erez G., Hubert L., Saada A., de Keyzer Y., Eshel G., Vaz F.M., Pines O., Elpeleg O. Am. J. Hum. Genet. 84:95-95(2008)
[13]	"Nuclear envelope phosphatase-regulatory subunit 1 (formerly TMEM188) is the metazoan SPO7 ortholog and functions in the lipin activation pathway." Han S., Bahmanyar S., Zhang P., Grishin N., Oegema K., Crooke R., Graham M., Reue K., Dixon J.E., Goodman J.M. J. Biol. Chem. 287:3123-3137(2012) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D80010 mRNA. Translation: BAA11505.1. Different initiation. AK290235 mRNA. Translation: BAF82924.1. AK302922 mRNA. Translation: BAH13844.1. AC012456 Genomic DNA. Translation: AAY14695.1. AC106875 Genomic DNA. No translation available. CH471053 Genomic DNA. Translation: EAX00918.1. CH471053 Genomic DNA. Translation: EAX00920.1. BC030537 mRNA. Translation: AAH30537.1.
IPI	IPI00032388. IPI01009658.
RefSeq	NP_001248356.1. NM_001261427.1. NP_001248357.1. NM_001261428.1. NP_001248358.1. NM_001261429.1. NP_663731.1. NM_145693.2.
UniGene	Hs.467740. Hs.739141.
3D structure databases
ProteinModelPortal	Q14693.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14693. 1 interaction.
STRING	9606.ENSP00000256720.
PTM databases
PhosphoSite	Q14693.
Polymorphism databases
DMDM	23831266.
Proteomic databases
PaxDb	Q14693.
PRIDE	Q14693.
Protocols and materials databases
DNASU	23175.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000256720; ENSP00000256720; ENSG00000134324. ENST00000425416; ENSP00000401522; ENSG00000134324.
GeneID	23175.
KEGG	hsa:23175.
UCSC	uc002rbt.3. human.
Organism-specific databases
CTD	23175.
GeneCards	GC02P011864.
HGNC	HGNC:13345. LPIN1.
HPA	HPA038021.
MIM	268200. phenotype. 605518. gene.
neXtProt	NX_Q14693.
Orphanet	99845. Genetic recurrent myoglobinuria.
PharmGKB	PA30436.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5083.
HOVERGEN	HBG052338.
KO	K15728.
PhylomeDB	Q14693.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q14693.
Bgee	Q14693.
CleanEx	HS_LPIN1.
Genevestigator	Q14693.
GermOnline	ENSG00000134324. Homo sapiens.
Family and domain databases
Gene3D	3.40.50.1000. 1 hit.
InterPro	IPR023214. HAD-like_dom. IPR026058. LIPIN. IPR007651. Lipin_N. IPR013209. LNS2. [Graphical view]
PANTHER	PTHR12181. PTHR12181. 1 hit.
Pfam	PF04571. Lipin_N. 1 hit. PF08235. LNS2. 1 hit. [Graphical view]
SMART	SM00775. LNS2. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	LPIN1. human.
GenomeRNAi	23175.
NextBio	44595.
SOURCE	Search...

Entry information

Entry name

LPIN1_HUMAN

Accession

Primary (citable) accession number: Q14693
Secondary accession number(s): B7Z858, D6W506, Q53T25

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	October 10, 2002
Last modified:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.