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AGPAT2 (human)

Overview AGPAT2 Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Defects in AGPAT2 are the cause of congenital generalized lipodystrophy type 1 (CGL1); also known as Berardinelli-Seip congenital lipodystrophy type 1 (BSCL1) or Berardinelli-Seip syndrome. CGL1 is an autosomal recessive disorder characterized by marked paucity of adipose tissue, extreme insulin resistance, hypertriglyceridemia, hepatic steatosis and early onset of diabetes. Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB. Protein type: Membrane protein, integral; EC 2.3.1.51; Lipid Metabolism - glycerolipid; Transferase; Lipid Metabolism - ether lipid; Lipid Metabolism - glycerophospholipid Cellular Component: endoplasmic reticulum membrane; endoplasmic reticulum; integral to membrane Molecular Function: 1-acylglycerol-3-phosphate O-acyltransferase activity Biological Process: positive regulation of cytokine production; epidermis development; phospholipid metabolic process; glycerophospholipid biosynthetic process; phosphatidic acid biosynthetic process; triacylglycerol biosynthetic process; cellular lipid metabolic process; CDP-diacylglycerol biosynthetic process; positive regulation of cytokine and chemokine mediated signaling pathway Reference #:  O15120 (UniProtKB) Alt. Names/Synonyms: 1-acyl-sn-glycerol-3-phosphate acyltransferase beta; 1-acylglycerol-3-phosphate O-acyltransferase 2; 1-acylglycerol-3-phosphate O-acyltransferase 2 (lysophosphatidic acid acyltransferase, beta); 1-acylglycerol-3-phosphate O-acyltransferase 2 (lysophosphatidic acid acyltransferase-beta); 1-AGP acyltransferase 2; 1-AGPAT 2; 1-AGPAT2; AGPAT2; BSCL; BSCL1; LPAAB; LPAAT-beta; Lysophosphatidic acid acyltransferase beta; lysophosphatidic acid acyltransferase-beta; PLCB Gene Symbols: AGPAT2 Molecular weight: 30,914 Da Basal Isoelectric point: 9.21  Predict pI for various phosphorylation states

Select Structure to View Below AGPAT2

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  ENZYME  |  DISEASE 603100 608594  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		Y72-p	WFVRSFKyFyGLRFE
0	1		Y74-p	VRSFKyFyGLRFEVR
0	4		R84	RFEVRDPRRLQEARP
0	2		R85	FEVRDPRRLQEARPC
0	6		K120	ERCVQIAKRELLFLG
0	3		K166-u	RMVRENLkVWIYPEG
0	6		K185	NGDLLPFKKGAFYLA
0	1		K185-u	NGDLLPFkKGAFYLA
0	1		K216	SFYNTKKKFFTsGTV
0	1		S220-p	TKKKFFTsGTVTVQV
0	1		T233-p	QVLEAIPtsGLtAAD
0	1		S234-p	VLEAIPtsGLtAADV
0	1		T237-p	AIPtsGLtAADVPAL
0	1		H249	PALVDTCHRAMRTTF
0	1		T255	CHRAMRTTFLHISkt
0	1		S260	RTTFLHISktPQENG
0	1		K261-u	TTFLHISktPQENGA
0	1		T262-p	TFLHISktPQENGAT
0	1		A270	PQENGATAGsGVQPA
0	1		S272-p	ENGATAGsGVQPAQ_

	mouse
Y72	WFVRSFKYVYGLRFE
Y74	VRSFKYVYGLRFEVS
K84-a	RFEVSGQkkLEVDGP
K85-a	FEVSGQkkLEVDGPC
K120-a	KRCVQIAkRELMFTG
K166-u	LMVKENLkVWIYPEG
K185-a	NGDLLPFkKGAFYLA
K185	NGDLLPFKKGAFYLA
K216-u	SFYNVKTkLFTSGTI
S220	VKTkLFTSGTIKVQV
T233	QVLDAVPTNGLTDAD
N234	VLDAVPTNGLTDADV
T237	AVPTNGLTDADVTKL
Y249-p	TKLVDTCyQSMRAtF
T255-p	CyQSMRAtFLQIsQI
S260-p	RAtFLQIsQIPQENS
Q261	AtFLQIsQIPQENSA
I262	tFLQIsQIPQENSAI
K270-u	PQENSAIkEPGVLPA
P272	ENSAIkEPGVLPAQ_

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