CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001314
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SEC14-like protein 2 
Protein Synonyms/Alias
 Alpha-tocopherol-associated protein; TAP; hTAP; Squalene transfer protein; Supernatant protein factor; SPF 
Gene Name
 SEC14L2 
Gene Synonyms/Alias
 C22orf6; KIAA1186; KIAA1658 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
196LFVVKAPKLFPVAYNubiquitination[1, 2]
225MVLGANWKEVLLKHIubiquitination[3]
255PDGNPKCKSKINYGGubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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
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. 
Sequence Annotation
 DOMAIN 76 249 CRAL-TRIO.
 DOMAIN 275 383 GOLD.  
Keyword
 3D-structure; Activator; Alternative splicing; Complete proteome; Cytoplasm; Lipid-binding; Nucleus; Polymorphism; Reference proteome; Transcription; Transcription regulation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 403 AA 
Protein Sequence
MSGRVGDLSP RQKEALAKFR ENVQDVLPAL PNPDDYFLLR WLRARSFDLQ KSEAMLRKHV 60
EFRKQKDIDN IISWQPPEVI QQYLSGGMCG YDLDGCPVWY DIIGPLDAKG LLFSASKQDL 120
LRTKMRECEL LLQECAHQTT KLGRKVETIT IIYDCEGLGL KHLWKPAVEA YGEFLCMFEE 180
NYPETLKRLF VVKAPKLFPV AYNLIKPFLS EDTRKKIMVL GANWKEVLLK HISPDQVPVE 240
YGGTMTDPDG NPKCKSKINY GGDIPRKYYV RDQVKQQYEH SVQISRGSSH QVEYEILFPG 300
CVLRWQFMSD GADVGFGIFL KTKMGERQRA GEMTEVLPNQ RYNSHLVPED GTLTCSDPGI 360
YVLRFDNTYS FIHAKKVNFT VEVLLPDKAS EEKMKQLGAG TPK 403 
Gene Ontology
 GO:0005737; C:cytoplasm; NAS:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:InterPro.
 GO:0005634; C:nucleus; NAS:UniProtKB.
 GO:0005543; F:phospholipid binding; NAS:UniProtKB.
 GO:0005215; F:transporter activity; IEA:InterPro.
 GO:0008431; F:vitamin E binding; NAS:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; NAS:UniProtKB.
 GO:0045540; P:regulation of cholesterol biosynthetic process; NAS:UniProtKB.
 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.