ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9NUQ2


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PLCE_HUMAN
Primary accession number Q9NUQ2
Secondary accession numbers Q8IZ47 Q9BQG4
Integrated into Swiss-Prot on January 23, 2002
Sequence was last modified on May 16, 2003 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 57)
Name and origin of the protein
Protein name 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
Synonyms EC 2.3.1.51
1-AGP acyltransferase 5
1-AGPAT 5
Lysophosphatidic acid acyltransferase epsilon
LPAAT-epsilon
1-acylglycerol-3-phosphate O-acyltransferase 5
Gene name
Name: AGPAT5
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Leung D.W.;
"Cloning and expression of LPAAT-epsilon.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala;
DOI=10.1101/gr.GR1547R; PubMed=11230166 [NCBI, ExPASy, EBI, Israel, Japan]
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF375789; AAK54809.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136587; CAB66522.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK002072; BAA92069.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC023550; AAH23550.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC080537; AAH80537.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_060831.2; -.
UniGene Hs.624002
3D structure databases
ModBase Q9NUQ2.
PTM databases
PhosphoSite Q9NUQ2; -.
Enzyme and pathway databases
Reactome REACT_602; Lipid and lipoprotein metabolism.
Organism-specific databases
HGNC HGNC:20886; AGPAT5.
GenAtlas AGPAT5.
HPA HPA010644; -.
HPA010950; -.
PharmGKB PA134952751; -.
GeneCards Q9NUQ2.
Gene expression databases
ArrayExpress Q9NUQ2; -.
CleanEx HS_AGPAT5; -.
GermOnline ENSG00000155189; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from LIFEdb).
GO:0003841; Molecular function: 1-acylglycerol-3-phosphate O-acyltransferase activity (non-traceable author statement from UniProtKB).
GO:0046027; Molecular function: phospholipid:diacylglycerol acyltransferase activity (inferred from experiment from Reactome).
GO:0008654; Biological process: phospholipid biosynthetic process (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002123; Acyltransferase.
Graphical view of domain structure.
Pfam PF01553; Acyltransferase; 1.
Pfam graphical view of domain structure.
SMART SM00563; PlsC; 1.
SMART graphical view of domain structure.
ProtoNet Q9NUQ2.
Proteomic databases
PeptideAtlas Q9NUQ2; -.
Genome annotation databases
Ensembl ENSG00000155189; Homo sapiens. [Contig view]
GeneID 55326; -.
KEGG hsa:55326; -.
Phylogenomic databases
HOGENOM Q9NUQ2; -.
HOVERGEN Q9NUQ2; -.
Other
LinkHub Q9NUQ2; -.
NextBio 59600; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acyltransferase; Membrane; Phospholipid biosynthesis; Polymorphism; Transferase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   364  364     1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon. PRO_0000208200
TRANSMEM   15    35  21     Potential. 
TRANSMEM   61    81  21     Potential. 
TRANSMEM   344   364  21     Potential. 
MOTIF   93    98  6     HXXXXD motif. 
VARIANT   77    77  1     Y -> C (in dbSNP:rs17077958 [NCBI]). VAR_022696 
CONFLICT   156   156        L -> V (in Ref. 2; BAA92069). 
Sequence information
Length: 364 AA [This is the length of the unprocessed precursor] Molecular weight: 42072 Da [This is the MW of the unprocessed precursor] CRC64: 90A0F87FC7C78081 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLLSLVLHTY SMRYLLPSVV LLGTAPTYVL AWGVWRLLSA FLPARFYQAL DDRLYCVYQS 

        70         80         90        100        110        120 
MVLFFFENYT GVQILLYGDL PKNKENIIYL ANHQSTVDWI VADILAIRQN ALGHVRYVLK 

       130        140        150        160        170        180 
EGLKWLPLYG CYFAQHGGIY VKRSAKFNEK EMRNKLQSYV DAGTPMYLVI FPEGTRYNPE 

       190        200        210        220        230        240 
QTKVLSASQA FAAQRGLAVL KHVLTPRIKA THVAFDCMKN YLDAIYDVTV VYEGKDDGGQ 

       250        260        270        280        290        300 
RRESPTMTEF LCKECPKIHI HIDRIDKKDV PEEQEHMRRW LHERFEIKDK MLIEFYESPD 

       310        320        330        340        350        360 
PERRKRFPGK SVNSKLSIKK TLPSMLILSG LTAGMLMTDA GRKLYVNTWI YGTLLGCLWV 


TIKA 

Q9NUQ2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!