Home

ACSL1 (human)

Overview ACSL1 Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate. Highly expressed in liver, heart, skeletal muscle, kidney and erythroid cells, and to a lesser extent in brain, lung, placenta and pancreas. Belongs to the ATP-dependent AMP-binding enzyme family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB. Protein type: Ligase; Membrane protein, integral; Lipid Metabolism - fatty acid; EC 6.2.1.3 Cellular Component: peroxisomal membrane; endoplasmic reticulum membrane; mitochondrial outer membrane; mitochondrion; plasma membrane; integral to membrane Molecular Function: ATP binding; long-chain-fatty-acid-CoA ligase activity Biological Process: response to drug; response to oleate; unsaturated fatty acid metabolic process; lipid biosynthetic process; linoleic acid metabolic process; triacylglycerol biosynthetic process; cellular lipid metabolic process; long-chain fatty acid metabolic process; response to organic cyclic substance; xenobiotic catabolic process; regulation of fatty acid oxidation; adiponectin-mediated signaling pathway; response to nutrient Reference #:  P33121 (UniProtKB) Alt. Names/Synonyms: ACS1; ACSL1; Acyl-CoA synthetase 1; acyl-CoA synthetase long-chain family member 1; FACL1; FACL2; fatty-acid-Coenzyme A ligase, long-chain 1; fatty-acid-Coenzyme A ligase, long-chain 2; LACS; LACS 1; LACS 2; LACS1; LACS2; lignoceroyl-CoA synthase; Long-chain acyl-CoA synthetase 1; Long-chain acyl-CoA synthetase 2; Long-chain fatty acid-CoA ligase 2; long-chain fatty-acid-coenzyme A ligase 1; Long-chain-fatty-acid--CoA ligase 1; Palmitoyl-CoA ligase 1; Palmitoyl-CoA ligase 2; paltimoyl-CoA ligase 1 Gene Symbols: ACSL1 Molecular weight: 77,943 Da Basal Isoelectric point: 6.81  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below ACSL1

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  ENZYME  |  DISEASE  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  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		K52	ATRPKPLKPPCDLSM
0	1		E80	SALLDSDEPLVYFYD
0	1		Y84	DSDEPLVYFYDDVTT
0	1		S103-p	FQRGIQVsNNGPCLG
0	1		K113	GPCLGSRKPDQPYEW
0	1		Y188-p	LGNEAITyIVNKAEL
0	1		K202	LSLVFVDKPEKAKLL
0	1		K207	VDKPEKAKLLLEGVE
0	1		K216	LLEGVENKLIPGLkI
0	11		K216-u	LLEGVENkLIPGLkI
0	1		K222-u	NkLIPGLkIIVVMDA
0	1		A229	kIIVVMDAYGSELVE
0	1		Y230	IIVVMDAYGSELVER
0	1		R240	ELVERGQRCGVEVTS
0	1		K263-a	RANRRKPkPPAPEDL
0	2		K356-u	RLLMDDLkVLQPTVF
0	22		K386-a	GQANTTLkRWLLDFA
0	1		K386	GQANTTLKRWLLDFA
0	1		S394-p	RWLLDFAskRKEAEL
0	7		K395-a	WLLDFAskRKEAELR
0	3		K395-u	WLLDFAskRKEAELR
0	1		S410	SGIIRNNSLWDRLIF
0	1		R414	RNNSLWDRLIFHkVQ
0	7		K419-u	WDRLIFHkVQSSLGG
0	1		R427	VQSSLGGRVRLMVTG
0	1		T441	GAAPVSATVLTFLRA
0	1		K511	GEGEVCVKGPNVFQG
0	1		Q517	VKGPNVFQGYLKDPA
0	1		K521	NVFQGYLKDPAKTAE
0	2		K532-u	KTAEALDkDGWLHTG
0	5		K543	LHTGDIGKWLPNGTL
0	1		K551	WLPNGTLKIIDRKKH
0	1		K561	DRKKHIFKLAQGEyI
0	18		Y567-p	FKLAQGEyIAPEKIE
0	17		Y577-p	PEKIENIyMRSEPVA
0	2		S620	QKRGFEGSFEELCRN
0	1		K632	CRNKDVKKAILEDMV
0	1		K632	CRNKDVKKAILEDMV
0	1		R640	AILEDMVRLGKDSGL
0	1		K643	EDMVRLGKDSGLKPF
0	1		K654	LKPFEQVKGITLHPE
0	1		K675	GLLTPTMKAKRPELR
0	10		Y693-p	RSQIDDLySTIKV__
0	1		K697	DDLySTIKV______

	mouse
K52-u	ATRPKALkPPCDLSM
K81-u	SAVLEDDkLLVYYYD
Y85	EDDkLLVYYYDDVRT
S104	FQRGIQVSNNGPCLG
K114-u	GPCLGSRkPNQPYEW
Y189	LGADAITYIVNKAEL
K203-u	LSVIFADkPEKAkLL
K208-u	ADkPEKAkLLLEGVE
K217-a	LLEGVENkLTPCLKI
K217-u	LLEGVENkLTPCLKI
K223	NkLTPCLKIIVIMDs
S230-p	KIIVIMDsyGSDLVE
Y231-p	IIVIMDsyGSDLVER
K241-u	DLVERGKkCGVEIIS
K264-a	RVNRVKPkPPEPEDL
K357-u	RLLMDDLkVLQPTIF
K387-a	GQANTSLkRWLLDFA
K387-u	GQANTSLkRWLLDFA
S395	RWLLDFASkRKEAEL
K396-a	WLLDFASkRKEAELR
K396-u	WLLDFASkRKEAELR
S411-p	SGIVRNNsLWDkLIF
K415-u	RNNsLWDkLIFHkIQ
K420-u	WDkLIFHkIQSSLGG
K428-u	IQSSLGGkVRLMITG
T442-p	GAAPVSAtVLTFLRT
K512-u	GEGEVCVkGANVFkG
K518-u	VkGANVFkGYLkDPA
K522-u	NVFkGYLkDPARTAE
K533-u	RTAEALDkDGWLHTG
K544-a	LHTGDIGkWLPNGTL
K552-u	WLPNGTLkIIDRKKH
K562-u	DRKKHIFkLAQGEYI
Y568	FkLAQGEYIAPEKIE
Y578	PEKIENIYLRSEAVA
S621-p	QKRGLQGsFEELCRN
K633	CRNKDINKAILDDLL
K633-u	CRNKDINkAILDDLL
K641-u	AILDDLLkLGkEAGL
K644-u	DDLLkLGkEAGLKPF
K655-u	LKPFEQVkGIAVHPE
K676-u	GLLTPTLkAKRPELR
Y694	RSQIDELYATIkI__
K698-u	DELYATIkI______

	rat
K52	ATRPKALKPPCDLSM
K81	SAVLEDDKLLLyYYD
Y85-p	EDDKLLLyYYDDVRT
S104	FQRGIQVSNDGPCLG
K114	GPCLGSRKPNQPYEW
Y189	LGTDAITYIVNKAEL
K203	LSVIFADKPEKAKLL
K208	ADKPEKAKLLLEGVE
K217	LLEGVENKLTPCLKI
K217	LLEGVENKLTPCLKI
K223	NKLTPCLKIIVIMDS
S230	KIIVIMDSYDNDLVE
Y231	IIVIMDSYDNDLVER
K241	DLVERGQKCGVEIIG
K264	RVNRTKPKPPEPEDL
K357	RLLMDDLKVLQPTIF
K387	GQANTSVKRWLLDFA
K387	GQANTSVKRWLLDFA
S395	RWLLDFASKRKEAEL
K396	WLLDFASKRKEAELR
K396	WLLDFASKRKEAELR
S411	SGIVRNNSLWDKLIF
K415	RNNSLWDKLIFHKIQ
K420	WDKLIFHKIQSSLGG
K428	IQSSLGGKVRLMITG
T442	GAAPVSATVLTFLRA
K512	GEGEVCVKGANVFKG
K518	VKGANVFKGYLKDPA
K522	NVFKGYLKDPARTAE
K533	RTAEALDKDGWLHTG
K544	LHTGDIGKWLPNGTL
K552	WLPNGTLKIIDRKKH
K562	DRKKHIFKLAQGEYI
Y568	FKLAQGEYIAPEKIE
Y578	PEKIENIYLRSEAVA
S621	QKRGFQGSFEELCRN
K633-a	CRNKDINkAILEDMV
K633	CRNKDINKAILEDMV
K641	AILEDMVKLGKNAGL
K644	EDMVKLGKNAGLKPF
K655	LKPFEQVKGIAVHPE
K676	GLLTPTLKAKRPELR
Y694	RSQIDELYSTIKI__
K698	DELYSTIKI______

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.