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Protein

Glycerol-3-phosphate acyltransferase 2, mitochondrial

Gene

GPAT2

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

Functioni

Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis.By similarity

Catalytic activityi

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.

Pathway:iCDP-diacylglycerol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glycerol-3-phosphate acyltransferase 2, mitochondrial (GPAT2), Glycerol-3-phosphate acyltransferase 4 (AGPAT6), Glycerol-3-phosphate acyltransferase 3 (AGPAT9), Glycerol-3-phosphate acyltransferase 1, mitochondrial (GPAM)
  2. 1-acyl-sn-glycerol-3-phosphate acyltransferase beta (AGPAT2), 1-acyl-sn-glycerol-3-phosphate acyltransferase delta (AGPAT4), 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma (AGPAT3), 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon (AGPAT5), 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (AGPAT1), Lysocardiolipin acyltransferase 1 (LCLAT1)
  3. Phosphatidate cytidylyltransferase 1 (CDS1), Phosphatidate cytidylyltransferase 2 (CDS2), Phosphatidate cytidylyltransferase, mitochondrial (TAMM41), Phosphatidate cytidylyltransferase (CDS1), Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase, Phosphatidate cytidylyltransferase
This subpathway is part of the pathway CDP-diacylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate, the pathway CDP-diacylglycerol biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiREACT_1190. Triglyceride Biosynthesis.
REACT_120906. Synthesis of PA.
UniPathwayiUPA00557; UER00612.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferase 2, mitochondrial (EC:2.3.1.15)
Short name:
GPAT-2
Alternative name(s):
xGPAT1
Gene namesi
Name:GPAT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:27168. GPAT2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 305305CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei306 – 33227HelicalSequence AnalysisAdd
BLAST
Topological domaini333 – 449117Mitochondrial intermembraneSequence AnalysisAdd
BLAST
Transmembranei450 – 47223HelicalSequence AnalysisAdd
BLAST
Topological domaini473 – 795323CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165696677.

Polymorphism and mutation databases

BioMutaiGPAT2.
DMDMi172046129.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 795795Glycerol-3-phosphate acyltransferase 2, mitochondrialPRO_0000325853Add
BLAST

Proteomic databases

PaxDbiQ6NUI2.
PRIDEiQ6NUI2.

PTM databases

PhosphoSiteiQ6NUI2.

Expressioni

Gene expression databases

BgeeiQ6NUI2.
ExpressionAtlasiQ6NUI2. baseline and differential.
GenevisibleiQ6NUI2. HS.

Organism-specific databases

HPAiHPA036841.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000352547.

Structurei

3D structure databases

ProteinModelPortaliQ6NUI2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni180 – 331152AcyltransferaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi205 – 2106HXXXXD motif

Domaini

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.By similarity

Sequence similaritiesi

Belongs to the GPAT/DAPAT family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG134494.
GeneTreeiENSGT00520000055570.
InParanoidiQ6NUI2.
KOiK00629.
OMAiNARSCWG.
OrthoDBiEOG74R1PZ.
PhylomeDBiQ6NUI2.
TreeFamiTF313360.

Family and domain databases

InterProiIPR022284. GPAT/DHAPAT.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6NUI2-1) [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

        10         20         30         40         50
MATMLEGRCQ TQPRSSPSGR EASLWSSGFG MKLEAVTPFL GKYRPFVGRC
60 70 80 90 100
CQTCTPKSWE SLFHRSITDL GFCNVILVKE ENTRFRGWLV RRLCYFLWSL
110 120 130 140 150
EQHIPPCQDV PQKIMESTGV QNLLSGRVPG GTGEGQVPDL VKKEVQRILG
160 170 180 190 200
HIQAPPRPFL VRLFSWALLR FLNCLFLNVQ LHKGQMKMVQ KAAQAGLPLV
210 220 230 240 250
LLSTHKTLLD GILLPFMLLS QGLGVLRVAW DSRACSPALR ALLRKLGGLF
260 270 280 290 300
LPPEASLSLD SSEGLLARAV VQAVIEQLLV SGQPLLIFLE EPPGALGPRL
310 320 330 340 350
SALGQAWVGF VVQAVQVGIV PDALLVPVAV TYDLVPDAPC DIDHASAPLG
360 370 380 390 400
LWTGALAVLR SLWSRWGCSH RICSRVHLAQ PFSLQEYIVS ARSCWGGRQT
410 420 430 440 450
LEQLLQPIVL GQCTAVPDTE KEQEWTPITG PLLALKEEDQ LLVRRLSCHV
460 470 480 490 500
LSASVGSSAV MSTAIMATLL LFKHQKLLGE FSWLTEEILL RGFDVGFSGQ
510 520 530 540 550
LRSLLQHSLS LLRAHVALLR IRQGDLLVVP QPGPGLTHLA QLSAELLPVF
560 570 580 590 600
LSEAVGACAV RGLLAGRVPP QGPWELQGIL LLSQNELYRQ ILLLMHLLPQ
610 620 630 640 650
DLLLLKPCQS SYCYCQEVLD RLIQCGLLVA EETPGSRPAC DTGRQRLSRK
660 670 680 690 700
LLWKPSGDFT DSDSDDFGEA DGRYFRLSQQ SHCPDFFLFL CRLLSPLLKA
710 720 730 740 750
FAQAAAFLRQ GQLPDTELGY TEQLFQFLQA TAQEEGIFEC ADPKLAISAV
760 770 780 790
WTFRDLGVLQ QTPSPAGPRL HLSPTFASLD NQEKLEQFIR QFICS
Length:795
Mass (Da):87,835
Last modified:March 18, 2008 - v2
Checksum:iEE8E387A87A9EE21
GO
Isoform 2 (identifier: Q6NUI2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     633-671: TPGSRPACDT...SDSDDFGEAD → SWATQSSCSS...PSVLSGPSET
     672-795: Missing.

Note: No experimental confirmation available.
Show »
Length:671
Mass (Da):73,521
Checksum:iF44C1200F3AA60A6
GO
Isoform 3 (identifier: Q6NUI2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     476-476: K → KGVFLSQ

Note: No experimental confirmation available.
Show »
Length:801
Mass (Da):88,467
Checksum:i5E29D4F62C9292B0
GO
Isoform 4 (identifier: Q6NUI2-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-216: Missing.
     274-344: Missing.

Note: No experimental confirmation available.
Show »
Length:508
Mass (Da):56,052
Checksum:iD405B71CFA1125F1
GO

Sequence cautioni

The sequence AAH68596.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAD18392.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti336 – 3361P → Q in AAH68596 (PubMed:15489334).Curated
Sequence conflicti689 – 6891F → L in BAC85508 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 216216Missing in isoform 4. 1 PublicationVSP_032450Add
BLAST
Alternative sequencei274 – 34471Missing in isoform 4. 1 PublicationVSP_032451Add
BLAST
Alternative sequencei476 – 4761K → KGVFLSQ in isoform 3. 1 PublicationVSP_032452
Alternative sequencei633 – 67139TPGSR…FGEAD → SWATQSSCSSSCRPPPRKKG SSSVRTQSSPSVLSGPSET in isoform 2. 1 PublicationVSP_032453Add
BLAST
Alternative sequencei672 – 795124Missing in isoform 2. 1 PublicationVSP_032454Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122734 mRNA. Translation: BAC85508.1.
AK131194 mRNA. Translation: BAD18390.1.
AK131197 mRNA. Translation: BAD18392.1. Different initiation.
BC068596 mRNA. Translation: AAH68596.1. Different initiation.
CCDSiCCDS42714.1. [Q6NUI2-1]
RefSeqiNP_997211.2. NM_207328.2. [Q6NUI2-1]
XP_005263941.1. XM_005263884.1. [Q6NUI2-4]
XP_005263945.1. XM_005263888.2. [Q6NUI2-3]
XP_006712378.1. XM_006712315.2. [Q6NUI2-3]
UniGeneiHs.348629.
Hs.679801.

Genome annotation databases

EnsembliENST00000359548; ENSP00000352547; ENSG00000186281.
ENST00000434632; ENSP00000389395; ENSG00000186281.
GeneIDi150763.
KEGGihsa:150763.
UCSCiuc002svd.3. human. [Q6NUI2-4]
uc002svf.3. human. [Q6NUI2-1]
uc002svh.3. human. [Q6NUI2-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122734 mRNA. Translation: BAC85508.1.
AK131194 mRNA. Translation: BAD18390.1.
AK131197 mRNA. Translation: BAD18392.1. Different initiation.
BC068596 mRNA. Translation: AAH68596.1. Different initiation.
CCDSiCCDS42714.1. [Q6NUI2-1]
RefSeqiNP_997211.2. NM_207328.2. [Q6NUI2-1]
XP_005263941.1. XM_005263884.1. [Q6NUI2-4]
XP_005263945.1. XM_005263888.2. [Q6NUI2-3]
XP_006712378.1. XM_006712315.2. [Q6NUI2-3]
UniGeneiHs.348629.
Hs.679801.

3D structure databases

ProteinModelPortaliQ6NUI2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000352547.

PTM databases

PhosphoSiteiQ6NUI2.

Polymorphism and mutation databases

BioMutaiGPAT2.
DMDMi172046129.

Proteomic databases

PaxDbiQ6NUI2.
PRIDEiQ6NUI2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359548; ENSP00000352547; ENSG00000186281.
ENST00000434632; ENSP00000389395; ENSG00000186281.
GeneIDi150763.
KEGGihsa:150763.
UCSCiuc002svd.3. human. [Q6NUI2-4]
uc002svf.3. human. [Q6NUI2-1]
uc002svh.3. human. [Q6NUI2-3]

Organism-specific databases

CTDi150763.
GeneCardsiGC02M096687.
HGNCiHGNC:27168. GPAT2.
HPAiHPA036841.
neXtProtiNX_Q6NUI2.
PharmGKBiPA165696677.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG134494.
GeneTreeiENSGT00520000055570.
InParanoidiQ6NUI2.
KOiK00629.
OMAiNARSCWG.
OrthoDBiEOG74R1PZ.
PhylomeDBiQ6NUI2.
TreeFamiTF313360.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00612.
ReactomeiREACT_1190. Triglyceride Biosynthesis.
REACT_120906. Synthesis of PA.

Miscellaneous databases

GenomeRNAii150763.
NextBioi86529.
PROiQ6NUI2.

Gene expression databases

BgeeiQ6NUI2.
ExpressionAtlasiQ6NUI2. baseline and differential.
GenevisibleiQ6NUI2. HS.

Family and domain databases

InterProiIPR022284. GPAT/DHAPAT.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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 2 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-795 (ISOFORM 3).
    Tissue: Brain, Heart and Testis.
  2. "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).
    Tissue: Testis.

Entry informationi

Entry nameiGPAT2_HUMAN
AccessioniPrimary (citable) accession number: Q6NUI2
Secondary accession number(s): Q6P2E4
, Q6ZNI3, Q6ZNI5, Q6ZWJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: July 22, 2015
This is version 92 of the entry and version 2 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.