CPLM-005072

Genbank Nucleotide ID

Non-specific lipid-transfer protein

Protein Synonyms/Alias

NSL-TP; Propanoyl-CoA C-acyltransferase; SCP-chi; SCPX; Sterol carrier protein 2; SCP-2; Sterol carrier protein X; SCP-X

Homo sapiens (Human)

Position	Peptide	Type	References
132	SKGSLGIKFSDRTIP	acetylation	[1]
183	TKIEHFAKIGWKNHK	acetylation	[1]
183	TKIEHFAKIGWKNHK	ubiquitination	[2]
282	MVGFDMSKEAARKCY	ubiquitination	[2]
438	FKANLVFKEIEKKLE	acetylation	[1, 3]
438	FKANLVFKEIEKKLE	ubiquitination	[2]
443	VFKEIEKKLEEEGEQ	ubiquitination	[2, 4]
453	EEGEQFVKKIGGIFA	acetylation	[1]
453	EEGEQFVKKIGGIFA	ubiquitination	[2, 4, 5]
454	EGEQFVKKIGGIFAF	ubiquitination	[2]
462	IGGIFAFKVKDGPGG	ubiquitination	[2, 4, 5, 6, 7]
470	VKDGPGGKEATWVVD	acetylation	[1]
522	QSAFFQGKLKITGNM	acetylation	[8, 9]
546	QLQPGNAKL******	acetylation	[8, 9]

[1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[3] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[9] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]

Functional Description

Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis.

DOMAIN 433 543 SCP2.
MOTIF 545 547 Microbody targeting signal (Potential).
MOD_RES 142 142 N6-acetyllysine (By similarity).
MOD_RES 173 173 N6-acetyllysine (By similarity).
MOD_RES 183 183 N6-acetyllysine.
MOD_RES 282 282 N6-acetyllysine (By similarity).
MOD_RES 341 341 N6-acetyllysine (By similarity).
MOD_RES 425 425 Phosphoserine (By similarity).
MOD_RES 438 438 N6-acetyllysine.
MOD_RES 453 453 N6-acetyllysine (By similarity).
MOD_RES 470 470 N6-acetyllysine.

3D-structure; Acetylation; Acyltransferase; Alternative initiation; Alternative promoter usage; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Lipid transport; Lipid-binding; Mitochondrion; Peroxisome; Phosphoprotein; Polymorphism; Reference proteome; Transferase; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO:0005634; C:nucleus; IDA:HPA.
GO:0005782; C:peroxisomal matrix; TAS:Reactome.
GO:0043234; C:protein complex; IDA:UniProtKB.
GO:0015485; F:cholesterol binding; IDA:UniProtKB.
GO:0036042; F:long-chain fatty acyl-CoA binding; IDA:UniProtKB.
GO:0070538; F:oleic acid binding; IDA:UniProtKB.
GO:0008526; F:phosphatidylinositol transporter activity; IDA:UniProtKB.
GO:0033814; F:propanoyl-CoA C-acyltransferase activity; IEA:EC.
GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
GO:0032959; P:inositol trisphosphate biosynthetic process; IDA:UniProtKB.
GO:1901373; P:lipid hydroperoxide transport; IDA:UniProtKB.
GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
GO:0007031; P:peroxisome organization; IEA:Compara.
GO:0032385; P:positive regulation of intracellular cholesterol transport; IDA:UniProtKB.
GO:0045940; P:positive regulation of steroid metabolic process; IDA:UniProtKB.
GO:0006701; P:progesterone biosynthetic process; IDA:UniProtKB.
GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.

IPR003033; SCP2_sterol-bd_dom.
IPR016039; Thiolase-like.
IPR016038; Thiolase-like_subgr.
IPR020615; Thiolase_acyl_enz_int_AS.
IPR020617; Thiolase_C.
IPR020613; Thiolase_CS.
IPR020616; Thiolase_N.

PF02036; SCP2
PF02803; Thiolase_C
PF00108; Thiolase_N

PS00098; THIOLASE_1
PS00737; THIOLASE_2
PS00099; THIOLASE_3