SwissPalm

P35555 FBN1_HUMAN

General info Cross-references Sequences Orthologs Ortholog sequences Predictions Palmitoyl-proteomes References

Palmitoyl-proteomes

2/22 articles for human
0 ortholog

Palmitoyl-proteome experiments

Validation experiments

0 experiment
0 ortholog

Curated sites & Enzymes

0 site from validation experiments^*
0 site from palmitoyl-proteomes^*
No PAT known
No APT known
^*In main isoform only

Predictions

Predicted

14 cysteines in main isoform

Predictions

Protein general information from UniProt

Protein names

Fibrillin-1 [Cleaved into: Asprosin ]

Subcellular location

Secreted (By similarity); extracellular space (Probable); extracellular matrix (Probable); Extracellular space (Probable); Extracellular matrix (Probable)

Isoforms & protein length

Isoform 1 (main): 2871 aa; Isoform 1 (main): 2871 aa

Known functions

The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Asprosin: Mutations specifically affect Asprosin, a hormone peptide present at the C-terminus of Fibrillin-1 chain, which is cleaved from Fibrillin-1 following secretion (PubMed:27087445). Asprosin: Was named after the Greek word for white, because of the reduction in subcutaneous white adipose tissue that is displayed by asprosin-deficient patients. Belongs to the fibrillin family. Fibrillin-1: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues (PubMed:1860873, PubMed:15062093). Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles. Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components (PubMed:27026396). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (By similarity). Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11. This leads to disruption of TNFSF11-induced Ca(2+) signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232). Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1 (PubMed:12807887, PubMed:17158881). Binds heparin and this interaction has an important role in the assembly of microfibrils (PubMed:11461921). Asprosin: Hormone that targets the liver to increase plasma glucose levels. Secreted by white adipose tissue and circulates in the plasma. Acts in response to fasting and promotes blood glucose elevation by binding to the surface of hepatocytes. Promotes hepatocyte glucose release by activating the protein kinase A activity in the liver, resulting in rapid glucose release into the circulation. Interacts with COL16A1 (PubMed:15165854). Interacts with integrin alpha-V/beta-3 (PubMed:15062093). Interacts with ADAMTS10; this interaction promotes microfibril assembly (PubMed:21402694). Interacts with THSD4; this interaction promotes fibril formation (By similarity). Interacts (via N-terminal domain) with FBLN2, FBLN4 and FBLN5 (PubMed:15790312, PubMed:17255108). Interacts with ELN (PubMed:15790312). Forms a ternary complex with ELN and FBLN2 or FBLN5 and a significant interaction with ELN seen only in the presence of FBLN2 or FBLN5 (PubMed:17255108). Interacts (via N-terminal domain) with LTBP2 (via C-terminal domain) in a Ca(+2)-dependent manner (PubMed:17293099). Interacts (via N-terminal domain) with LTBP1 (via C-terminal domain) (PubMed:17293099). Interacts with integrins ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6 (PubMed:17158881, PubMed:12807887). Interacts (via N-terminal domain) with BMP2, BMP4, BMP7, BMP10 and GDF5 (PubMed:18339631). Interacts (via N-terminal domain) with MFAP2 and MFAP5 (PubMed:15131124). Interacts with ADAMTSL5 (PubMed:23010571). Interacts with MFAP4 (PubMed:26601954). Interacts (via N-terminal domain) with TNFSF11 in a Ca(+2)-dependent manner (PubMed:24039232). Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin (PubMed:24982166). Secreted into the plasma. Fibrillin-1: Cleavage of N- and C-terminus by furin is required for incorporation into the extracellular matrix and assembly into microfibrils (PubMed:27026396). The C-terminus, which corresponds to the Asprosin chain, was initially thought to constitute a propeptide (PubMed:24982166). Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin, an essential step for incorporation of Fibrillin-1 into the nascent microfibrils (PubMed:24982166). Fibrillin-1: Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils. The disease is caused by mutations affecting the gene represented in this entry. The majority of the more than thousand mutations in FBN1 currently known are point mutations, the rest are frameshifts and splice site mutations. Marfan syndrome has been suggested in at least 2 historical figures, Abraham Lincoln and Paganini. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues (PubMed:1860873, PubMed:15062093). Fibrillin-1-containing microfibrils provide long-term force bearing structural support (PubMed:27026396). In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin (PubMed:27026396). In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles (PubMed:27026396). Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components (PubMed:27026396). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (By similarity). Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11 (PubMed:24039232). This leads to disruption of TNFSF11-induced Ca(2+) signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232). Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1 (PubMed:12807887, PubMed:17158881). Binds heparin and this interaction has an important role in the assembly of microfibrils (PubMed:11461921). Adipokine secreted by white adipose tissue that plays an important regulatory role in the glucose metabolism of liver, muscle and pancreas (PubMed:27087445, PubMed:30853600). Hormone that targets the liver in response to fasting to increase plasma glucose levels (PubMed:27087445). Binds the olfactory receptor OR4M1 at the surface of hepatocytes and promotes hepatocyte glucose release by activating the protein kinase A activity in the liver, resulting in rapid glucose release into the circulation (PubMed:27087445, PubMed:31230984). May act as a regulator of adaptive thermogenesis by inhibiting browning and energy consumption, while increasing lipid deposition in white adipose tissue (By similarity). Also acts as an orexigenic hormone that increases appetite: crosses the blood brain barrier and exerts effects on the hypothalamus (By similarity). In the arcuate nucleus of the hypothalamus, asprosin directly activates orexigenic AgRP neurons and indirectly inhibits anorexigenic POMC neurons, resulting in appetite stimulation (By similarity). Activates orexigenic AgRP neurons via binding to the olfactory receptor OR4M1 (By similarity). May also play a role in sperm motility in testis via interaction with OR4M1 receptor (By similarity). Interacts with COL16A1 (PubMed:15165854). Interacts with integrin alpha-V/beta-3 (PubMed:15062093). Interacts with ADAMTS10; this interaction promotes microfibril assembly (PubMed:21402694). Interacts with THSD4; this interaction promotes fibril formation (By similarity). Interacts (via N-terminal domain) with FBLN2 and FBLN5 (PubMed:15790312, PubMed:17255108). Interacts with ELN (PubMed:15790312). Forms a ternary complex with ELN and FBLN2 or FBLN5 and a significant interaction with ELN seen only in the presence of FBLN2 or FBLN5 (PubMed:17255108). Interacts (via N-terminal domain) with LTBP2 (via C-terminal domain) in a Ca(+2)-dependent manner (PubMed:17293099). Interacts (via N-terminal domain) with LTBP1 (via C-terminal domain) (PubMed:17293099). Interacts with integrins ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6 (PubMed:17158881, PubMed:12807887). Interacts (via N-terminal domain) with BMP2, BMP4, BMP7, BMP10 and GDF5 (PubMed:18339631). Interacts (via N-terminal domain) with MFAP2 and MFAP5 (PubMed:15131124). Interacts with ADAMTSL5 (PubMed:23010571). Interacts with MFAP4 (PubMed:26601954). Interacts (via N-terminal domain) with TNFSF11 in a Ca(+2)-dependent manner (PubMed:24039232). Interacts (via N-terminal domain) with EFEMP2; this interaction inhibits EFEMP2 binding to LOX and ELN (PubMed:17255108, PubMed:19349279, PubMed:19570982). Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin (PubMed:24982166). Secreted by white adipose tissue and circulates in the plasma. Asprosin levels are elevated in patients with type II diabetes and metabolic syndrome (at protein level). Cleavage of N- and C-terminus by furin is required for incorporation into the extracellular matrix and assembly into microfibrils (PubMed:27026396). The C-terminus, which corresponds to the Asprosin chain, was initially thought to constitute a propeptide (PubMed:24982166). Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin, an essential step for incorporation of Fibrillin-1 into the nascent microfibrils (PubMed:24982166). Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils. O-glycosylated on serine residues by POGLUT2 and POGLUT3 which is necessary for efficient protein secretion. The disease is caused by variants affecting the gene represented in this entry. The majority of the more than a thousand mutations in FBN1 currently known are point mutations, the rest are frameshifts and splice site mutations. Marfan syndrome has been suggested in at least 2 historical figures, Abraham Lincoln and Paganini. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Attractive therapeutic target for type II diabetes and metabolic syndrome. Was named after the Greek word for white, because of the reduction in subcutaneous white adipose tissue that is displayed by asprosin-deficient patients. Belongs to the fibrillin family. Fibrillin-1: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues (PubMed:1860873, PubMed:15062093). Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles. Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components (PubMed:27026396). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (By similarity). Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11. This leads to disruption of TNFSF11-induced Ca2+ signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232). Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1 (PubMed:12807887, PubMed:17158881). Binds heparin and this interaction has an important role in the assembly of microfibrils (PubMed:11461921). Asprosin: Hormone that targets the liver to increase plasma glucose levels. Secreted by white adipose tissue and circulates in the plasma. Acts in response to fasting and promotes blood glucose elevation by binding to the surface of hepatocytes. Promotes hepatocyte glucose release by activating the protein kinase A activity in the liver, resulting in rapid glucose release into the circulation. Interacts with COL16A1 (PubMed:15165854). Interacts with integrin alpha-V/beta-3 (PubMed:15062093). Interacts with ADAMTS10; this interaction promotes microfibril assembly (PubMed:21402694). Interacts with THSD4; this interaction promotes fibril formation (By similarity). Interacts (via N-terminal domain) with FBLN2, FBLN4 and FBLN5 (PubMed:15790312, PubMed:17255108). Interacts with ELN (PubMed:15790312). Forms a ternary complex with ELN and FBLN2 or FBLN5 and a significant interaction with ELN seen only in the presence of FBLN2 or FBLN5 (PubMed:17255108). Interacts (via N-terminal domain) with LTBP2 (via C-terminal domain) in a Ca(+2)-dependent manner (PubMed:17293099). Interacts (via N-terminal domain) with LTBP1 (via C-terminal domain) (PubMed:17293099). Interacts with integrins ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6 (PubMed:17158881, PubMed:12807887). Interacts (via N-terminal domain) with BMP2, BMP4, BMP7, BMP10 and GDF5 (PubMed:18339631). Interacts (via N-terminal domain) with MFAP2 and MFAP5 (PubMed:15131124). Interacts with ADAMTSL5 (PubMed:23010571). Interacts with MFAP4 (PubMed:26601954). Interacts (via N-terminal domain) with TNFSF11 in a Ca(+2)-dependent manner (PubMed:24039232). Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin (PubMed:24982166). Secreted into the plasma. Fibrillin-1: Cleavage of N- and C-terminus by furin is required for incorporation into the extracellular matrix and assembly into microfibrils (PubMed:27026396). The C-terminus, which corresponds to the Asprosin chain, was initially thought to constitute a propeptide (PubMed:24982166). Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin, an essential step for incorporation of Fibrillin-1 into the nascent microfibrils (PubMed:24982166). Fibrillin-1: Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils. The disease is caused by mutations affecting the gene represented in this entry. The majority of the more than thousand mutations in FBN1 currently known are point mutations, the rest are frameshifts and splice site mutations. Marfan syndrome has been suggested in at least 2 historical figures, Abraham Lincoln and Paganini. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Asprosin: Mutations specifically affect Asprosin, a hormone peptide present at the C-terminus of Fibrillin-1 chain, which is cleaved from Fibrillin-1 following secretion (PubMed:27087445). Asprosin: Was named after the Greek word for white, because of the reduction in subcutaneous white adipose tissue that is displayed by asprosin-deficient patients. Belongs to the fibrillin family. The disease is caused by mutations affecting the gene represented in this entry.

Cross-references

Source	Identifiers
UniProt gene names	FBN1, FBN
UniProt secondary AC	B2RUU0, D2JYH6, Q15972, Q75N87
Refseq protein ID	NP_000129.3
IPI ID	IPI00328113, IPI00784458, IPI00471957, IPI00292703, IPI00177701

Source	Identifiers
Ensembl protein	ENSP00000325527
Ensembl gene	ENSG00000166147

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Isoform sequence alignment

Tip: Hover over an amino acid to display its position!

Orthologs

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UniProt AC	UniProt ID	Orthology source	Organism	Gene names	Protein name	Palmitome articles	Predicted
Q61554	FBN1_MOUSE	InParanoid, OMA, MetaPhors	M. musculus	Fbn1, Fbn-1	Fibrillin-1 [Cleaved into: Asprosin ]	0/23	Yes
F1PIA3	F1PIA3_CANLF	InParanoid	C. familiaris	FBN1	Fibrillin 1	0/1	Yes
Q9SY59	NFXL1_ARATH	MetaPhors	A. thaliana	NFXL1, At1g10170, F14N23.5	NF-X1-type zinc finger protein NFXL1, AtNFXL1, EC 2.3.2.-	0/1	Yes
A0A178UUR8	A0A178UUR8_ARATH	MetaPhors	A. thaliana	AXX17_At4g17050, C24_LOCUS18006	Uncharacterized protein	0/1	No
Q61555	FBN2_MOUSE	OrthoDB	M. musculus	Fbn2, Fbn-2	Fibrillin-2 [Cleaved into: Placensin ]	0/23	Yes
P98133	FBN1_BOVIN	OMA, InParanoid, MetaPhors	B. taurus	FBN1	Fibrillin-1	0/2	Yes
G3V9M6	G3V9M6_RAT	InParanoid, MetaPhors	R. norvegicus	Fbn1, rCG_27283	Fibrillin 1	0/3	Yes

Ortholog sequence alignment (CLUSTALW)

Cysteine summary and predictions

Pos in alignment	59	67	68	80	85	89	94	100	102	111	119	123	129	134
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	coil	strand	coil	strand	coil	coil	coil	strand	coil	coil	coil	coil	strand	strand
UniProt secondary structure	strand	NA	NA	NA	NA	NA	strand	strand	NA	NA	coil	NA	strand	strand
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys⁵⁹	Cys⁶⁷	Cys⁶⁸ MC	Cys⁸⁰	Cys⁸⁵	Cys⁸⁹	Cys⁹⁴	Cys¹⁰⁰	Cys¹⁰²	Cys¹¹¹	Cys¹¹⁹	Cys¹²³ MC	Cys¹²⁹	Cys¹³⁴

Pos in alignment	136	145	150	154	160	166	168	177	186	195	204	209	210	221
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	no	no	no	no	no	no
PSIPRED v.4.02 prediction	coil	coil	coil	coil	strand	strand	coil	coil	coil	strand	strand	strand	strand	coil
UniProt secondary structure	NA	coil	NA	NA	strand	strand	NA	NA	strand	NA	NA	helix	helix	coil
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys¹³⁶	Cys¹⁴⁵	Cys¹⁵⁰	Cys¹⁵⁴	Cys¹⁶⁰	Cys¹⁶⁶	Cys¹⁶⁸	Cys¹⁷⁷	Cys¹⁸⁶	Cys¹⁹⁵	Cys²⁰⁴	Cys²⁰⁹ HC	Cys²¹⁰ HC	Cys²²¹

Pos in alignment	224	231	244	250	257	262	271	273	286	292	299	304	313	315
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	no	no	no	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	coil	coil	strand	helix	coil	strand	strand	coil	strand	helix	coil	strand	strand	coil
UniProt secondary structure	NA	strand	strand	helix	NA	strand	strand	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys²²⁴	Cys²³¹	Cys²⁴⁴	Cys²⁵⁰	Cys²⁵⁷	Cys²⁶²	Cys²⁷¹	Cys²⁷³	Cys²⁸⁶	Cys²⁹²	Cys²⁹⁹	Cys³⁰⁴	Cys³¹³	Cys³¹⁵

Pos in alignment	328	336	345	358	359	360	365	377	389	453	460	465	474	476
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	no	no	no	no	no	no	no	no	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	strand	coil	strand	strand	strand	strand	strand	coil	coil	helix	coil	strand	strand	strand
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys³²⁸	Cys³³⁶	Cys³⁴⁵	Cys³⁵⁸ HC	Cys³⁵⁹ HC	Cys³⁶⁰ LC	Cys³⁶⁵	Cys³⁷⁷	Cys³⁸⁹	Cys⁴⁵³	Cys⁴⁶⁰	Cys⁴⁶⁵	Cys⁴⁷⁴	Cys⁴⁷⁶

Pos in alignment	488	494	499	504	513	515	528	534	541	546	555	557	570	576
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	strand	coil	coil	strand	strand	strand	strand	helix	coil	strand	strand	strand	strand	coil
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys⁴⁸⁸	Cys⁴⁹⁴	Cys⁴⁹⁹	Cys⁵⁰⁴	Cys⁵¹³	Cys⁵¹⁵	Cys⁵²⁸	Cys⁵³⁴	Cys⁵⁴¹	Cys⁵⁴⁶	Cys⁵⁵⁵	Cys⁵⁵⁷	Cys⁵⁷⁰	Cys⁵⁷⁶

Pos in alignment	582	587	596	598	611	617	623	628	637	639	652	661	670	683
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	no	no	no
PSIPRED v.4.02 prediction	coil	strand	strand	strand	strand	helix	coil	strand	strand	strand	strand	coil	strand	coil
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys⁵⁸²	Cys⁵⁸⁷	Cys⁵⁹⁶ MC	Cys⁵⁹⁸	Cys⁶¹¹	Cys⁶¹⁷ MC	Cys⁶²³	Cys⁶²⁸	Cys⁶³⁷	Cys⁶³⁹	Cys⁶⁵²	Cys⁶⁶¹	Cys⁶⁷⁰	Cys⁶⁸³ HC

Pos in alignment	684	685	696	699	711	727	734	739	748	750	763	769	776	781
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	no	no	no	no	no	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	coil	coil	coil	coil	coil	helix	coil	strand	strand	strand	strand	helix	coil	strand
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys⁶⁸⁴ HC	Cys⁶⁸⁵ HC	Cys⁶⁹⁶	Cys⁶⁹⁹	Cys⁷¹¹	Cys⁷²⁷	Cys⁷³⁴	Cys⁷³⁹	Cys⁷⁴⁸	Cys⁷⁵⁰	Cys⁷⁶³	Cys⁷⁶⁹	Cys⁷⁷⁶	Cys⁷⁸¹

Pos in alignment	790	792	805	811	816	821	830	832	845	853	862	875	876	887
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	strand	coil	strand	helix	coil	strand	strand	strand	strand	coil	strand	coil	coil	coil
UniProt secondary structure	NA	NA	NA	helix	NA	strand	strand	NA	strand	strand	strand	helix	helix	coil
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys⁷⁹⁰	Cys⁷⁹²	Cys⁸⁰⁵	Cys⁸¹¹	Cys⁸¹⁶	Cys⁸²¹	Cys⁸³⁰	Cys⁸³²	Cys⁸⁴⁵	Cys⁸⁵³	Cys⁸⁶²	Cys⁸⁷⁵	Cys⁸⁷⁶	Cys⁸⁸⁷

Pos in alignment	890	896	908	914	921	926	935	937	950	958	967	980	981	982
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	no	no	no	no	no
PSIPRED v.4.02 prediction	coil	coil	strand	coil	coil	strand	strand	coil	strand	coil	coil	coil	coil	coil
UniProt secondary structure	NA	coil	strand	helix	strand	strand	strand	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys⁸⁹⁰	Cys⁸⁹⁶	Cys⁹⁰⁸	Cys⁹¹⁴	Cys⁹²¹	Cys⁹²⁶	Cys⁹³⁵	Cys⁹³⁷	Cys⁹⁵⁰	Cys⁹⁵⁸	Cys⁹⁶⁷	Cys⁹⁸⁰ HC	Cys⁹⁸¹ HC	Cys⁹⁸²

Pos in alignment	993	996	1008	1032	1039	1044	1053	1055	1068	1074	1081	1086	1095	1097
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	no	no	no	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	coil	coil	coil	helix	coil	strand	strand	strand	strand	helix	coil	strand	strand	strand
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	coil	coil	strand	strand	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys⁹⁹³	Cys⁹⁹⁶	Cys¹⁰⁰⁸	Cys¹⁰³² LC	Cys¹⁰³⁹	Cys¹⁰⁴⁴	Cys¹⁰⁵³	Cys¹⁰⁵⁵	Cys¹⁰⁶⁸	Cys¹⁰⁷⁴ LC	Cys¹⁰⁸¹	Cys¹⁰⁸⁶	Cys¹⁰⁹⁵	Cys¹⁰⁹⁷

Pos in alignment	1111	1117	1124	1129	1138	1140	1153	1159	1166	1171	1180	1182	1195	1201
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	strand	helix	coil	strand	strand	coil	strand	helix	coil	strand	strand	coil	strand	coil
UniProt secondary structure	strand	helix	coil	strand	strand	strand	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys¹¹¹¹	Cys¹¹¹⁷	Cys¹¹²⁴	Cys¹¹²⁹	Cys¹¹³⁸	Cys¹¹⁴⁰	Cys¹¹⁵³	Cys¹¹⁵⁹ MC	Cys¹¹⁶⁶	Cys¹¹⁷¹	Cys¹¹⁸⁰	Cys¹¹⁸²	Cys¹¹⁹⁵	Cys¹²⁰¹

Pos in alignment	1208	1212	1221	1223	1236	1242	1249	1254	1263	1265	1278	1284	1291	1296
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	coil	strand	strand	coil	strand	helix	coil	strand	strand	coil	strand	helix	coil	strand
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys¹²⁰⁸	Cys¹²¹²	Cys¹²²¹	Cys¹²²³	Cys¹²³⁶	Cys¹²⁴²	Cys¹²⁴⁹	Cys¹²⁵⁴	Cys¹²⁶³	Cys¹²⁶⁵	Cys¹²⁷⁸	Cys¹²⁸⁴ LC	Cys¹²⁹¹	Cys¹²⁹⁶

Pos in alignment	1305	1307	1320	1326	1333	1339	1348	1350	1361	1367	1374	1380	1389	1391
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	strand	strand	coil	coil	coil	strand	strand	strand	strand	coil	coil	strand	strand	strand
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys¹³⁰⁵	Cys¹³⁰⁷	Cys¹³²⁰	Cys¹³²⁶	Cys¹³³³	Cys¹³³⁹	Cys¹³⁴⁸	Cys¹³⁵⁰	Cys¹³⁶¹	Cys¹³⁶⁷	Cys¹³⁷⁴	Cys¹³⁸⁰	Cys¹³⁸⁹	Cys¹³⁹¹ HC

Pos in alignment	1402	1408	1415	1420	1429	1431	1444	1450	1456	1461	1470	1472	1485	1491
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	strand	coil	coil	strand	strand	strand	strand	coil	coil	strand	strand	strand	strand	coil
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	helix
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys¹⁴⁰²	Cys¹⁴⁰⁸	Cys¹⁴¹⁵	Cys¹⁴²⁰	Cys¹⁴²⁹	Cys¹⁴³¹	Cys¹⁴⁴⁴	Cys¹⁴⁵⁰	Cys¹⁴⁵⁶	Cys¹⁴⁶¹	Cys¹⁴⁷⁰	Cys¹⁴⁷²	Cys¹⁴⁸⁵	Cys¹⁴⁹¹

Pos in alignment	1497	1502	1511	1513	1526	1534	1549	1562	1563	1564	1574	1577	1589	1610
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	coil	strand	strand	coil	coil	coil	coil	strand	strand	strand	coil	coil	coil	helix
UniProt secondary structure	strand	strand	strand	NA	strand	strand	NA	helix	helix	coil	coil	NA	NA	helix
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys¹⁴⁹⁷	Cys¹⁵⁰²	Cys¹⁵¹¹	Cys¹⁵¹³	Cys¹⁵²⁶	Cys¹⁵³⁴	Cys¹⁵⁴⁹	Cys¹⁵⁶² HC	Cys¹⁵⁶³ HC	Cys¹⁵⁶⁴ MC	Cys¹⁵⁷⁴ HC	Cys¹⁵⁷⁷ MC	Cys¹⁵⁸⁹	Cys¹⁶¹⁰

Pos in alignment	1617	1622	1631	1633	1646	1652	1658	1663	1672	1674	1687	1695	1706	1719
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	no	no	no
PSIPRED v.4.02 prediction	coil	strand	strand	coil	strand	coil	coil	strand	strand	coil	strand	coil	coil	strand
UniProt secondary structure	helix	strand	strand	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys¹⁶¹⁷	Cys¹⁶²²	Cys¹⁶³¹	Cys¹⁶³³	Cys¹⁶⁴⁶	Cys¹⁶⁵²	Cys¹⁶⁵⁸	Cys¹⁶⁶³	Cys¹⁶⁷²	Cys¹⁶⁷⁴	Cys¹⁶⁸⁷	Cys¹⁶⁹⁵	Cys¹⁷⁰⁶	Cys¹⁷¹⁹ HC

Pos in alignment	1720	1721	1733	1736	1748	1770	1777	1782	1791	1793	1806	1812	1818	1824
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	no	no	no	no	no	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	coil	coil	coil	coil	coil	helix	coil	strand	strand	coil	strand	helix	coil	strand
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys¹⁷²⁰ HC	Cys¹⁷²¹ HC	Cys¹⁷³³	Cys¹⁷³⁶	Cys¹⁷⁴⁸	Cys¹⁷⁷⁰	Cys¹⁷⁷⁷	Cys¹⁷⁸²	Cys¹⁷⁹¹	Cys¹⁷⁹³	Cys¹⁸⁰⁶	Cys¹⁸¹²	Cys¹⁸¹⁸	Cys¹⁸²⁴

Pos in alignment	1833	1835	1847	1853	1860	1865	1874	1876	1889	1895	1900	1905	1914	1916
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	strand	coil	strand	helix	coil	strand	strand	strand	strand	helix	coil	strand	strand	strand
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys¹⁸³³	Cys¹⁸³⁵ LC	Cys¹⁸⁴⁷	Cys¹⁸⁵³	Cys¹⁸⁶⁰	Cys¹⁸⁶⁵	Cys¹⁸⁷⁴	Cys¹⁸⁷⁶	Cys¹⁸⁸⁹	Cys¹⁸⁹⁵	Cys¹⁹⁰⁰	Cys¹⁹⁰⁵	Cys¹⁹¹⁴	Cys¹⁹¹⁶

Pos in alignment	1928	1934	1942	1947	1956	1958	1971	1977	1984	1989	1998	2000	2011	2017
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	strand	coil	coil	strand	strand	strand	strand	helix	coil	strand	strand	coil	strand	helix
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys¹⁹²⁸	Cys¹⁹³⁴	Cys¹⁹⁴²	Cys¹⁹⁴⁷	Cys¹⁹⁵⁶	Cys¹⁹⁵⁸	Cys¹⁹⁷¹	Cys¹⁹⁷⁷	Cys¹⁹⁸⁴	Cys¹⁹⁸⁹	Cys¹⁹⁹⁸	Cys²⁰⁰⁰	Cys²⁰¹¹	Cys²⁰¹⁷

Pos in alignment	2024	2029	2038	2040	2053	2061	2070	2083	2084	2085	2096	2099	2111	2131
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	coil	strand	strand	coil	strand	coil	strand	coil	coil	coil	coil	coil	coil	coil
UniProt secondary structure	NA	NA	NA	NA	NA	strand	strand	helix	helix	NA	coil	NA	NA	strand
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys²⁰²⁴	Cys²⁰²⁹	Cys²⁰³⁸	Cys²⁰⁴⁰	Cys²⁰⁵³	Cys²⁰⁶¹	Cys²⁰⁷⁰	Cys²⁰⁸³ HC	Cys²⁰⁸⁴ HC	Cys²⁰⁸⁵ HC	Cys²⁰⁹⁶	Cys²⁰⁹⁹	Cys²¹¹¹	Cys²¹³¹

Pos in alignment	2137	2142	2151	2153	2164	2170	2176	2181	2190	2192	2204	2210	2217	2221
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	coil	strand	strand	strand	strand	coil	coil	strand	strand	strand	strand	helix	coil	strand
UniProt secondary structure	NA	strand	NA	NA	strand	helix	NA	strand	strand	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys²¹³⁷	Cys²¹⁴²	Cys²¹⁵¹	Cys²¹⁵³	Cys²¹⁶⁴	Cys²¹⁷⁰	Cys²¹⁷⁶	Cys²¹⁸¹	Cys²¹⁹⁰	Cys²¹⁹²	Cys²²⁰⁴	Cys²²¹⁰	Cys²²¹⁷	Cys²²²¹

Pos in alignment	2230	2232	2245	2251	2258	2265	2274	2276	2289	2295	2302	2307	2316	2318
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	strand	coil	strand	helix	coil	strand	strand	coil	coil	helix	coil	strand	strand	strand
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys²²³⁰ LC	Cys²²³²	Cys²²⁴⁵	Cys²²⁵¹	Cys²²⁵⁸	Cys²²⁶⁵	Cys²²⁷⁴	Cys²²⁷⁶	Cys²²⁸⁹	Cys²²⁹⁵	Cys²³⁰²	Cys²³⁰⁷	Cys²³¹⁶	Cys²³¹⁸

Pos in alignment	2331	2339	2348	2363	2364	2365	2375	2378	2390	2406	2413	2418	2427	2429
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	no	no	no	no	no	no	no	no	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	strand	strand	coil	strand	coil	coil	coil	coil	coil	helix	coil	strand	strand	coil
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys²³³¹	Cys²³³⁹	Cys²³⁴⁸	Cys²³⁶³ HC	Cys²³⁶⁴ HC	Cys²³⁶⁵	Cys²³⁷⁵ MC	Cys²³⁷⁸	Cys²³⁹⁰	Cys²⁴⁰⁶	Cys²⁴¹³	Cys²⁴¹⁸	Cys²⁴²⁷	Cys²⁴²⁹ MC

Pos in alignment	2442	2448	2455	2459	2468	2470	2483	2489	2496	2500	2509	2511	2522	2528
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	strand	helix	coil	strand	strand	coil	strand	helix	coil	strand	strand	coil	strand	coil
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys²⁴⁴²	Cys²⁴⁴⁸	Cys²⁴⁵⁵	Cys²⁴⁵⁹	Cys²⁴⁶⁸	Cys²⁴⁷⁰	Cys²⁴⁸³	Cys²⁴⁸⁹	Cys²⁴⁹⁶	Cys²⁵⁰⁰	Cys²⁵⁰⁹	Cys²⁵¹¹	Cys²⁵²²	Cys²⁵²⁸

Pos in alignment	2535	2541	2550	2552	2565	2571	2577	2581	2590	2592	2605	2611	2617	2622
Subcell. location	E	E	E	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes	yes
PSIPRED v.4.02 prediction	coil	strand	strand	strand	coil	coil	coil	coil	strand	coil	strand	helix	coil	strand
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys²⁵³⁵	Cys²⁵⁴¹	Cys²⁵⁵⁰	Cys²⁵⁵²	Cys²⁵⁶⁵	Cys²⁵⁷¹	Cys²⁵⁷⁷	Cys²⁵⁸¹	Cys²⁵⁹⁰	Cys²⁵⁹²	Cys²⁶⁰⁵	Cys²⁶¹¹	Cys²⁶¹⁷	Cys²⁶²²

Pos in alignment	2631	2633	2646	2652	2659	2663	2672	2674	2686	2715	2718
Subcell. location	E	E	E	E	E	E	E	E	E	E	E
Disulfide	yes	yes	yes	yes	yes	yes	yes	yes	yes	no	no
PSIPRED v.4.02 prediction	strand	coil	strand	coil	coil	strand	strand	coil	strand	coil	coil
UniProt secondary structure	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys²⁶³¹	Cys²⁶³³ HC	Cys²⁶⁴⁶	Cys²⁶⁵²	Cys²⁶⁵⁹	Cys²⁶⁶³	Cys²⁶⁷² LC	Cys²⁶⁷⁴	Cys²⁶⁸⁶	Cys²⁷¹⁵	Cys²⁷¹⁸

Legend

Subcell. location

U Undefined E Extracellular/Lumenal T Transmembrane C Cytosolic/Nuclear

Prediction confidence

Cysteine position: Predicted (high confidence prediction with CSS-Palm or/and PalmPred) and validated (in terms of disulfide bonds and cellular location) / Predicted but not validated (in terms of disulfide bond and cellular location) / Not predicted
CSS-Palm 4.0: High confidence, Medium confidence, Low confidence, Not predicted.
PalmPred: High confidence (score > 0.4), Medium confidence (0.1 < score < 0.4), Low confidence (score < 0.1), Not predicted.

Palmitoyl-proteome experiments

List of palmitoyl-proteomes

Tip: Keep CTRL key pressed down while clicking on column headers to do multiple sorting. This applies to any sortable table on this site.

ID of the experiment	Reference	Year	Organism	Cell type	Subcellular location	Technique(s)	Found?	In list	All lists
SPalmE:14	Roth AF et al.	2006	Saccharomyces cerevisiae	Isogenic LRB759	Total membrane	ABE	x		HC HC: 48 hits
SPalmE:13	Kang R et al.	2008	Rattus norvegicus	Cortical neuron	Synaptosomal membrane	ABE	x		HC: 107 hits LC: 308 hits
SPalmE:6	Martin BR et al.	2009	Homo sapiens	Jurkat	Total membrane	Click chemistry	x		HC: 127 hits LC: 188 hits List: 0 hits
SPalmE:1	Yang W et al.	2010	Homo sapiens	DU145	Total membrane	ABE	x		HC: 162 hits LC: 218 hits
SPalmE:10	Yount JS et al.	2010	Mus musculus	Dendritic cell	Total cell lysate	Click chemistry	x		HC: 59 hits LC: 105 hits
SPalmE:578	Yang W et al.	2010	Homo sapiens	DU145	Lipid raft	ABE	x		HC: 102 hits LC: 73 hits
SPalmE:577	Yang W et al.	2010	Homo sapiens	DU145	Non-lipid raft	ABE	x		HC: 63 hits LC: 147 hits
SPalmE:12	Martin BR et al.	2011	Mus musculus	BW5147-derived mouse T-cell hybridoma cell	Total membrane	Click chemistry	x		HC HC: 352 hits LC LC: 8 hits
SPalmE:2	Dowal L et al.	2011	Homo sapiens	Platelet	Total membrane	ABE	x		List: 214 hits
SPalmE:8	Merrick BA et al.	2011	Mus musculus	Macrophage Raw 264.7	Total membrane	ABE	x		List: 69 hits
SPalmE:511	Emmer BT et al.	2011	Trypanosoma brucei brucei	NA	Total cell lysate	ABE	x		List: 126 hits
SPalmE:5	Forrester MT et al.	2011	Homo sapiens	HEK293	Total membrane	ARAC	x		List: 69 hits
SPalmE:7	Wilson JP et al.	2011	Homo sapiens	Jurkat	Total cell lysate	Click chemistry	x		HC: 164 hits LC: 178 hits
SPalmE:3	Ivaldi C et al.	2012	Homo sapiens	B-cell	Total membrane	ABE	x		HC HC: 93 hits
SPalmE:580	Jones ML et al.	2012	Plasmodium falciparum	Whole organism	Total cell lysate	Click chemistry, SILAC	x		HC: 79 hits LC: 89 hits
SPalmE:162	Jones ML et al.	2012	Plasmodium falciparum	Whole organism	Total cell lysate	ABE	x		HC: 100 hits LC: 217 hits
SPalmE:11	Li Y et al.	2012	Mus musculus	Neural stem cell	Total cell lysate	Click chemistry	x		HC HC: 254 hits
SPalmE:4	Marin EP et al.	2012	Homo sapiens	Umbilical vein blood	NA	ABE	x		List: 154 hits
SPalmE:9	Ren W et al.	2013	Mus musculus	3T3-L1 and epididymal fat pads	Total membrane	ARAC	x		List: 664 hits
SPalmE:15	Hemsley PA et al.	2013	Arabidopsis thaliana	Heyn Col-4 ecotype root cell suspension	Microsomal membrane	ABE	x		HC: 122 hits MC: 94 hits LC: 366 hits
SPalmE:119	Wan J et al.	2013	Mus musculus	Brain	Total cell lysate	ABE	x		List: 378 hits
SPalmE:160	Zhang MM et al.	2013	Schizosaccharomyces pombe	Whole organism	Total cell lysate	Click chemistry	x		List: 238 hits
SPalmE:507	Chesarino NM et al.	2014	Mus musculus	DC2.4	Total cell lysate	Click chemistry	x		List: 246 hits
SPalmE:508	Chesarino NM et al.	2014	Mus musculus	MEF	Total cell lysate	Click chemistry	x		List: 436 hits
SPalmE:184	Wei X et al.	2014	Homo sapiens	HUVEC	Total cell lysate	ABE	x		Palm decreased: 40 hits Palm increased: 33 hits List: 367 hits
SPalmE:619	Peng T et al.	2015	Homo sapiens	HEK293	Total cell lysate	Alk16 Labeling	x		List: 354 hits
SPalmE:504	Serwa RA et al.	2015	Homo sapiens	RPE-1	Total cell lysate	SILAC, 16-HDYA labeling	x		List: 1348 hits
SPalmE:620	Peng T et al.	2015	Homo sapiens	HEK293	Total cell lysate	Photo cleavable x-alk16 labeling	x		List: 354 hits
SPalmE:506	Morrison E et al.	2015	Homo sapiens	Jurkat	Total cell lysate	Click chemistry, SILAC	x		List: 226 hits
SPalmE:540	Gould NS et al.	2015	Mus musculus	Liver	Total cell lysate	APE	x		List: 780 hits
SPalmE:529	Colquhoun DR et al.	2015	Homo sapiens	174 x CEM.T1	Total cell lysate	Click-IT Palmitic Acid labeling	x		List: 113 hits
SPalmE:510	Santiago-Tirado FH et al.	2015	Cryptococcus neoformans	NA	Total cell lysate	Click chemistry	x		List: 354 hits
SPalmE:509	Santiago-Tirado FH et al.	2015	Cryptococcus neoformans	NA	Total cell lysate	Click chemistry	x		List: 426 hits
SPalmE:505	Morrison E et al.	2015	Homo sapiens	Primary CD4 + T cells	Total cell lysate	ABE, In gel SILAC labeling	x		List: 274 hits
SPalmE:536	Foe IT et al.	2015	Toxoplasma gondii	NA	Total membrane	Click chemistry	x		HC: 210 hits MC: 72 hits
SPalmE:902	Caballero MC et al.	2016	Toxoplasma gondii	whole parasite lysates	NA	ABE	x		HC: 164 hits
SPalmE:829	Upadhyay S et al.	2016	Aspergillus fumigatus	Conidia	NA	ABE	x		List: 133 hits
SPalmE:724	Fang C et al.	2016	Homo sapiens	SW480	NA	ARAC	x		List: 100 hits
SPalmE:909	Thinon E et al.	2016	Mus musculus	Macrophage Raw 264.7	Total cell lysate	Alk16 Labeling	x		HC: 197 hits MC: 143 hits LC: 302 hits
SPalmE:723	Hernandez JL et al.	2016	Homo sapiens	MCF7	Total cell lysate	Alk16 Labeling	x		List: 1353 hits
SPalmE:698	Pinner AL et al.	2016	Homo sapiens	Brain	Total cell lysate	ABE	x		List: 216 hits
SPalmE:993	Shen LF et al.	2017	Mus musculus	Liver	Total membrane	ARAC	x		ZDHHC13 substrates: 16 hits
SPalmE:903	Collins MO et al.	2017	Mus musculus	Forebrain	NA	ABE	x		HC: 1079 hits
SPalmE:907	Edmonds MJ et al.	2017	Rattus norvegicus	Brain	NA	ARAC	x		List: 95 hits
SPalmE:906	Edmonds MJ et al.	2017	Rattus norvegicus	Brain	NA	ABE	x		List: 193 hits
SPalmE:855	Shen LF et al.	2017	Mus musculus	Liver	Total membrane	ARAC	x		List: 865 hits
SPalmE:1183	Thinon E et al.	2018	Homo sapiens	HeLa	Total cell lysate	NH2OH cleavage of thioester bond, Alk16 Labeling	x		HC: 132 hits MC: 138 hits LC: 110 hits
SPalmE:1184	Thinon E et al.	2018	Homo sapiens	HeLa	Total cell lysate	ARAC	Found	in LC	HC: 545 hits MC: 415 hits LC: 219 hits
SPalmE:1182	Thinon E et al.	2018	Mus musculus	Macrophage Raw 264.7	Total cell lysate	ARAC	x		HC: 198 hits MC: 143 hits LC: 120 hits
SPalmE:1186	Thinon E et al.	2018	Mus musculus	Macrophage Raw 264.7	Total cell lysate	NH2OH cleavage of thioester bond, Alk16 Labeling	x		HC: 177 hits MC: 162 hits LC: 123 hits
SPalmE:1181	Thinon E et al.	2018	Mus musculus	Macrophage Raw 264.7	Total cell lysate	NH2OH cleavage of thioester bond, Alk16 Labeling	x		HC: 244 hits MC: 187 hits LC: 120 hits
SPalmE:1191	Won SJ et al.	2018	Homo sapiens	HEK293T	Total cell lysate	Click chemistry	x		List: 195 hits
SPalmE:1192	Won SJ et al.	2018	Homo sapiens	HAP1	Total cell lysate	Click chemistry	x		List: 984 hits
SPalmE:1193	Won SJ et al.	2018	Homo sapiens	HAP1	Total cell lysate	ARAC	x		List: 1394 hits
SPalmE:1194	Won SJ et al.	2018	Homo sapiens	HAP1	Total cell lysate	ARAC,	x		List: 1404 hits
SPalmE:1203	Zhang X et al.	2018	Mus musculus	Brain	Total membrane	Enrichment by magnetic nanoparticles	x		HC: 917 hits MC: 352 hits LC: 15 hits
SPalmE:1259	Dumoulin A et al.	2018	Mus musculus	F11	Total membrane	ABE, NH2OH cleavage of thioester bond, LC-MS	x		HC: 1 hits MC: 10 hits LC: 4 hits
SPalmE:1260	Wang Z et al.	2018	Bos taurus	Lens fiber cell	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS	x		List: 52 hits
SPalmE:920	Sobocińska J et al.	2018	Mus musculus	Macrophage Raw 264.7	Total cell lysate	Click chemistry	x		LPS treatment: 646 hits
SPalmE:919	Sobocińska J et al.	2018	Mus musculus	Macrophage Raw 264.7	Total cell lysate	Click chemistry	x		List: 646 hits
SPalmE:908	Sobocińska J et al.	2018	Mus musculus	Macrophage Raw 264.7	Total cell lysate	Click chemistry	x		Palm. up with LPS: 156 hits Palm. down with LPS: 189 hits
SPalmE:1185	Thinon E et al.	2018	Homo sapiens	HeLa	Total cell lysate	NH2OH cleavage of thioester bond, LC-MS, Alk16 Labeling	x		Chymotrypsin: 286 hits Trypsin: 1291 hits
SPalmE:1187	Thinon E et al.	2018	Mus musculus	Macrophage Raw 264.7	Total cell lysate	ARAC	x		HC: 281 hits MC: 139 hits LC: 113 hits
SPalmE:1303	Zaręba-Kozioł M et al.	2019	Mus musculus	Brain	Postsynaptic density fraction	ABE, NH2OH cleavage of thioester bond, LC-MS	x
SPalmE:1270	Strassburger K et al.	2019	Drosophila melanogaster	Circa 160 L2 larvae	Total cell lysate	ABE, NH2OH cleavage of thioester bond, PAT KO, MS	x		List: 13 hits
SPalmE:1266	Strassburger K et al.	2019	Drosophila melanogaster	Circa 160 L2 larvae	Total cell lysate	ABE, NH2OH cleavage of thioester bond, PAT KO, MS	x		List: 157 hits
SPalmE:1265	Wang J et al.	2019	Mus musculus	3T3-L1	Total membrane	MS, BioID	x		List: 9 hits
SPalmE:1333	Zaręba-Kozioł M et al.	2019	Mus musculus	Brain	Postsynaptic density fraction	ABE, NH2OH cleavage of thioester bond, LC-MS	x
SPalmE:1433	Zhou B et al.	2019	Homo sapiens	LNCaP	Total cell lysate	NH2OH cleavage of thioester bond, LC-MS, LB-ABE, ABE	x		List: 2929 hits
SPalmE:1432	Zhou B et al.	2019	Homo sapiens	LNCaP	Total cell lysate	ABE, SILAC, NH2OH cleavage of thioester bond, LC-MS	x		List: 590 hits
SPalmE:1434	Wegleiter T et al.	2019	Mus musculus	Neural stem cell	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS	x		List: 370 hits
SPalmE:1438	Mariscal J et al.	2020	Homo sapiens	PC3	Total membrane	ARAC, NH2OH cleavage of thioester bond, LC-MS, LB-ABE	x		HC: 1837 hits
SPalmE:1439	Mariscal J et al.	2020	Homo sapiens	PC3	Large Extracellular Vesicles	ARAC, NH2OH cleavage of thioester bond, LC-MS, LB-ABE	x		HC: 1350 hits
SPalmE:1440	Mariscal J et al.	2020	Homo sapiens	PC3	Small Extracellular Vesicles	ARAC, NH2OH cleavage of thioester bond, LC-MS, LB-ABE	x		HC: 600 hits
SPalmE:1435	Morrison E et al.	2020	Homo sapiens	Jurkat	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS, SILAC	x		Unstimulated: 37 hits
SPalmE:1436	Morrison E et al.	2020	Homo sapiens	Jurkat	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS, SILAC	x		List: 185 hits
SPalmE:1458	Morrison E et al.	2020	Homo sapiens	Jurkat	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS, SILAC	x		Stimulated: 148 hits
SPalmE:1437	Mariscal J et al.	2020	Homo sapiens	PC3	Total cell lysate	ARAC, NH2OH cleavage of thioester bond, LC-MS, LB-ABE	x		HC: 1869 hits
SPalmE:1450	Zaręba-Kozioł M et al.	2021	Mus musculus	Brain	Synaptoneurosomal fraction	ABE, NH2OH cleavage of thioester bond, LC-MS	x		List: 1093 hits
SPalmE:1444	Miles MR et al.	2021	Homo sapiens	Heart	Total cell lysate	ARAC, NH2OH cleavage of thioester bond, LC-MS	x		List: 687 hits
SPalmE:1447	Pradhan AJ et al.	2021	Homo sapiens	HT-29	Total cell lysate	Labeling of substrate with C20 AlkFA (Alk-18), LC-MS	x		List: 1173 hits
SPalmE:1448	Pradhan AJ et al.	2021	Homo sapiens	HT-29	Total cell lysate	Labeling of substrate with C20 AlkFA (Alk-18), LC-MS	Found	in List	List: 770 hits
SPalmE:1449	Ripamonti M et al.	2021	Mus musculus	NIH-3T3	Total cell lysate	ARAC, NH2OH cleavage of thioester bond, LC-MS	x		List: 199 hits
SPalmE:1445	Miles MR et al.	2021	Rattus norvegicus	Heart	Total cell lysate	ARAC, NH2OH cleavage of thioester bond, LC-MS	x		List: 399 hits
SPalmE:1451	Zaręba-Kozioł M et al.	2021	Mus musculus	Brain	Synaptoneurosomal fraction	ABE, NH2OH cleavage of thioester bond, LC-MS	x		List: 1048 hits
SPalmE:1452	Zaręba-Kozioł M et al.	2021	Mus musculus	Brain	Synaptoneurosomal fraction	ABE, NH2OH cleavage of thioester bond, LC-MS	x		List: 1112 hits
SPalmE:1453	Zaręba-Kozioł M et al.	2021	Mus musculus	Brain	Synaptoneurosomal fraction	ABE, NH2OH cleavage of thioester bond, LC-MS	x		List: 1040 hits
SPalmE:1455	Ziemlińska E et al.	2021	Mus musculus	Liver	Total membrane	ABE, NH2OH cleavage of thioester bond, LC-MS	x		HC: 850 hits MC: 303 hits LC: 21 hits
SPalmE:1446	Miles MR et al.	2021	Canis familiaris	Heart	Total cell lysate	ARAC, NH2OH cleavage of thioester bond, LC-MS	x		List: 464 hits
SPalmE:1454	Ziemlińska E et al.	2021	Mus musculus	Liver	Total membrane	ABE, NH2OH cleavage of thioester bond, LC-MS	x		HC: 675 hits MC: 360 hits LC: 27 hits
SPalmE:1443	Uzbekova S et al.	2021	Bos taurus	Bovine follicular cells	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS	x		List: 80 hits
SPalmE:1456	Gao J et al.	2022	Mus musculus	Testis	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS	x		HC: 4107 hits
SPalmE:1442	Gorenberg EL et al.	2022	Mus musculus	Brain	Total cell lysate	ARAC, NH2OH cleavage of thioester bond, LC-MS	x		List: 1597 hits
SPalmE:1441	Gorenberg EL et al.	2022	Mus musculus	Brain	Synaptic fraction	ARAC, NH2OH cleavage of thioester bond, LC-MS	x		List: 1378 hits
SPalmE:1457	Gao J et al.	2022	Mus musculus	Testis	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS	x		HC: 3870 hits

Summary table by organism

Organism	Total number of palmitoyl-proteome articles	Total number of palmitoyl-proteomes	Number of palmitoyl-proteomes containing this protein or an ortholog	% of palmitoyl-proteomes containing this protein or an ortholog	Orthologs
S. cerevisiae S288c	1	1	0	0.0	NA
R. norvegicus	3	4	0	0.0	NA
H. sapiens	22	38	2	5.3	NA
M. musculus	23	37	0	0.0	NA
T. brucei brucei	1	1	0	0.0	NA
P. falciparum	1	2	0	0.0	NA
A. thaliana	1	1	0	0.0	NA
S. pombe	1	1	0	0.0	NA
C. neoformans var. grubii serotype A strain H99	1	2	0	0.0	NA
T. gondii	2	2	0	0.0	NA
A. fumigatus	1	1	0	0.0	NA
B. taurus	2	2	0	0.0	NA
D. melanogaster	1	2	0	0.0	NA
C. familiaris	1	1	0	0.0	NA

References

Authors	Year	Reference title	PMID
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Ren W et al.	2013	Proteomic analysis of protein palmitoylation in adipocytes.	23599907
Marin EP et al.	2012	Endothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferases.	22496122
Li Y et al.	2012	DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells.	22081607
Martin BR et al.	2011	Global profiling of dynamic protein palmitoylation.	22056678
Dowal L et al.	2011	Proteomic analysis of palmitoylated platelet proteins.	21813449
Merrick BA et al.	2011	Proteomic profiling of S-acylated macrophage proteins identifies a role for palmitoylation in mitochondrial targeting of phospholipid scramblase 3.	21785166
Wilson JP et al.	2011	Proteomic analysis of fatty-acylated proteins in mammalian cells with chemical reporters reveals S-acylation of histone H3 variants.	21076176
Forrester MT et al.	2011	Site-specific analysis of protein S-acylation by resin-assisted capture.	21044946
Yount JS et al.	2010	Palmitoylome profiling reveals S-palmitoylation-dependent antiviral activity of IFITM3.	20601941
Yang W et al.	2010	Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes.	19801377
Martin BR et al.	2009	Large-scale profiling of protein palmitoylation in mammalian cells.	19137006
Roth AF et al.	2006	Global analysis of protein palmitoylation in yeast.	16751107
Hemsley PA et al.	2013	A proteomic approach identifies many novel palmitoylated proteins in Arabidopsis.	23252521
Ivaldi C et al.	2012	Proteomic analysis of S-acylated proteins in human B cells reveals palmitoylation of the immune regulators CD20 and CD23.	22615937
Wan J et al.	2013	Tracking brain palmitoylation change: predominance of glial change in a mouse model of Huntington's disease.	24211138
Zhang MM et al.	2013	Quantitative control of protein S-palmitoylation regulates meiotic entry in fission yeast.	23843742
Jones ML et al.	2012	Analysis of protein palmitoylation reveals a pervasive role in Plasmodium development and pathogenesis.	22901544
Wei X et al.	2014	Insulin-regulated protein palmitoylation impacts endothelial cell function.	24357059
Serwa RA et al.	2015	Systems Analysis of Protein Fatty Acylation in Herpes Simplex Virus-Infected Cells Using Chemical Proteomics.	26256475
Morrison E et al.	2015	Quantitative analysis of the human T cell palmitome.	26111759
Chesarino NM et al.	2014	Chemoproteomics reveals Toll-like receptor fatty acylation.	25371237
Santiago-Tirado FH et al.	2015	A Single Protein S-acyl Transferase Acts through Diverse Substrates to Determine Cryptococcal Morphology, Stress Tolerance, and Pathogenic Outcome.	25970403
Emmer BT et al.	2011	Global analysis of protein palmitoylation in African trypanosomes.	21193548
Colquhoun DR et al.	2015	Bioorthogonal mimetics of palmitoyl-CoA and myristoyl-CoA and their subsequent isolation by click chemistry and characterization by mass spectrometry reveal novel acylated host-proteins modified by HIV-1 infection.	25914232
Foe IT et al.	2015	Global Analysis of Palmitoylated Proteins in Toxoplasma gondii.	26468752
Gould NS et al.	2015	Site-Specific Proteomic Mapping Identifies Selectively Modified Regulatory Cysteine Residues in Functionally Distinct Protein Networks.	26165157
Peng T et al.	2015	Bifunctional fatty acid chemical reporter for analyzing S-palmitoylated membrane protein-protein interactions in mammalian cells.	25575299
Pinner AL et al.	2016	Decreased protein S-palmitoylation in dorsolateral prefrontal cortex in schizophrenia.	26876311
Hernandez JL et al.	2016	Correlated S-palmitoylation profiling of Snail-induced epithelial to mesenchymal transition.	27030425
Fang C et al.	2016	Identification of Palmitoylated Transitional Endoplasmic Reticulum ATPase by Proteomic Technique and Pan Antipalmitoylation Antibody.	26865113
Caballero MC et al.	2016	Identification of new palmitoylated proteins in Toxoplasma gondii.	26825284
Upadhyay S et al.	2016	Interactions between Melanin Enzymes and Their Atypical Recruitment to the Secretory Pathway by Palmitoylation.	27879337
Edmonds MJ et al.	2017	Analysis of the brain palmitoyl-proteome using both acyl-biotin exchange and acyl-resin-assisted capture methods.	28607426
Shen LF et al.	2017	Role of S-Palmitoylation by ZDHHC13 in Mitochondrial function and Metabolism in Liver.	28526873
Sobocińska J et al.	2018	Lipopolysaccharide Upregulates Palmitoylated Enzymes of the Phosphatidylinositol Cycle: An Insight from Proteomic Studies.	29217618
Collins MO et al.	2017	Global, site-specific analysis of neuronal protein S-acylation.	28680068
Thinon E et al.	2016	Bioorthogonal Chemical Reporters for Monitoring Unsaturated Fatty-Acylated Proteins.	27350074
Thinon E et al.	2018	Selective Enrichment and Direct Analysis of Protein S-Palmitoylation Sites.	29575903
Zhang X et al.	2018	Ultradeep Palmitoylomics Enabled by Dithiodipyridine-Functionalized Magnetic Nanoparticles.	29660268
Won SJ et al.	2018	Temporal Profiling Establishes a Dynamic S-Palmitoylation Cycle.	29733200
Dumoulin A et al.	2018	S-palmitoylation Is Required for the Control of Growth Cone Morphology of DRG Neurons by CNP-Induced cGMP Signaling.	30319353
Wang Z et al.	2018	Proteomic Analysis of S-Palmitoylated Proteins in Ocular Lens Reveals Palmitoylation of AQP5 and MP20.	30489624
Wang J et al.	2019	DHHC4 and DHHC5 Facilitate Fatty Acid Uptake by Palmitoylating and Targeting CD36 to the Plasma Membrane.	30605677
Strassburger K et al.	2019	Drosophila ZDHHC8 palmitoylates scribble and Ras64B and controls growth and viability.	30735487
Zhou B et al.	2019	Low-background Acyl-biotinyl Exchange Largely Eliminates the Co-isolation of Non-S-acylated Proteins and Enables Deep S-acylproteomic Analysis.	31251020
Zaręba-Kozioł M et al.	2019	Stress-induced changes in the S-palmitoylation and S-nitrosylation of synaptic proteins.	31311849
Wegleiter T et al.	2019	Palmitoylation of BMPR1a regulates neural stem cell fate.	31772009
Morrison E et al.	2020	Dynamic palmitoylation events following T-cell receptor signaling.	32651440
Mariscal J et al.	2020	Comprehensive palmitoyl-proteomic analysis identifies distinct protein signatures for large and small cancer-derived extracellular vesicles.	32944167
Gorenberg EL et al.	2022	Identification of substrates of palmitoyl protein thioesterase 1 highlights roles of depalmitoylation in disulfide bond formation and synaptic function.	35358180
Uzbekova S et al.	2021	Protein Palmitoylation in Bovine Ovarian Follicle.	34769186
Miles MR et al.	2021	Global identification of S-palmitoylated proteins and detection of palmitoylating (DHHC) enzymes in heart.	33636221
Pradhan AJ et al.	2021	Protein acylation by saturated very long chain fatty acids and endocytosis are involved in necroptosis.	33848465
Ripamonti M et al.	2021	Structural and functional analysis of LIM domain-dependent recruitment of paxillin to αvβ3 integrin-positive focal adhesions.	33782527
Zaręba-Kozioł M et al.	2021	S-Palmitoylation of Synaptic Proteins as a Novel Mechanism Underlying Sex-Dependent Differences in Neuronal Plasticity.	34200797
Ziemlińska E et al.	2021	Palm Oil-Rich Diet Affects Murine Liver Proteome and <i>S</i>-Palmitoylome.	34884899
Gao J et al.	2022	Proteome-wide identification of palmitoylated proteins in mouse testis.	35477839