CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019833
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SEC14-like protein 2 
Protein Synonyms/Alias
 Alpha-tocopherol-associated protein; TAP 
Gene Name
 Sec14l2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
11RVGDLSPKQEEALAKacetylation[1, 2, 3, 4, 5]
11RVGDLSPKQEEALAKsuccinylation[4]
11RVGDLSPKQEEALAKubiquitination[6]
18KQEEALAKFRENVQDubiquitination[6]
51ARSFDLQKSEAMLRKacetylation[1, 4]
51ARSFDLQKSEAMLRKsuccinylation[4]
51ARSFDLQKSEAMLRKubiquitination[6]
66HVEFRKQKDIDKIISacetylation[2]
117GLLFSASKQDLLRTKacetylation[1]
117GLLFSASKQDLLRTKubiquitination[6]
193LKRLFVVKAPKLFPVacetylation[7]
193LKRLFVVKAPKLFPVubiquitination[6]
196LFVVKAPKLFPVAYNubiquitination[6]
225MVLGANWKEVLLKHIubiquitination[6]
230NWKEVLLKHISPDQLacetylation[1, 2]
230NWKEVLLKHISPDQLubiquitination[6]
253TDPDGNPKCKSKINYacetylation[4]
253TDPDGNPKCKSKINYsuccinylation[4]
253TDPDGNPKCKSKINYubiquitination[6]
257GNPKCKSKINYGGDIacetylation[4]
257GNPKCKSKINYGGDIsuccinylation[4]
257GNPKCKSKINYGGDIubiquitination[6]
266NYGGDIPKQYYVRDQubiquitination[6]
275YYVRDQVKQQYEHTVubiquitination[6]
375TYSFIHAKKVSFTVEubiquitination[6]
393PDKAAEEKMNQQGADacetylation[4]
393PDKAAEEKMNQQGADsuccinylation[4]
393PDKAAEEKMNQQGADubiquitination[6]
Reference
 [1] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [6] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [7] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
Functional Description
 Carrier protein. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds with high affinity to alpha-tocopherol. Also binds with a weaker affinity to other tocopherols and to tocotrienols. May have a transcriptional activatory activity via its association with alpha-tocopherol. Probably recognizes and binds some squalene structure, suggesting that it may regulate cholesterol biosynthesis by increasing the transfer of squalene to a metabolic active pool in the cell (By similarity). 
Sequence Annotation
 DOMAIN 76 249 CRAL-TRIO.
 DOMAIN 275 383 GOLD.  
Keyword
 Activator; Complete proteome; Cytoplasm; Lipid-binding; Nucleus; Reference proteome; Transcription; Transcription regulation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 403 AA 
Protein Sequence
MSGRVGDLSP KQEEALAKFR ENVQDVLPTL PNPDDYFLLR WLRARSFDLQ KSEAMLRKHV 60
EFRKQKDIDK IISWQPPEVI QQYLSGGRCG YDLDGCPVWY DIIGPLDAKG LLFSASKQDL 120
LRTKMRDCEL LLQECIQQTT KLGKKIETIT MIYDCEGLGL KHLWKPAVEA YGEFLTMFEE 180
NYPETLKRLF VVKAPKLFPV AYNLIKPFLS EDTRRKIMVL GANWKEVLLK HISPDQLPVE 240
YGGTMTDPDG NPKCKSKINY GGDIPKQYYV RDQVKQQYEH TVQVSRGSSH QVEYEILFPG 300
CVLRWQFMSE GSDVGFGIFL KTKMGERQRA GEMTEVLPNQ RYNSHMVPED GTLTCSEPGI 360
YVLRFDNTYS FIHAKKVSFT VEVLLPDKAA EEKMNQQGAD TPK 403 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:InterPro.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
 GO:0005215; F:transporter activity; IEA:InterPro.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001071; CRAL-bd_toc_tran.
 IPR001251; CRAL-TRIO_dom.
 IPR011074; CRAL/TRIO_N_dom.
 IPR009038; GOLD. 
Pfam
 PF00650; CRAL_TRIO
 PF03765; CRAL_TRIO_N 
SMART
 SM01100; CRAL_TRIO_N
 SM00516; SEC14 
PROSITE
 PS50191; CRAL_TRIO
 PS50866; GOLD 
PRINTS
 PR00180; CRETINALDHBP.