CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001552
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Luc7-like protein 3 
Protein Synonyms/Alias
 Cisplatin resistance-associated-overexpressed protein; Luc7A; Okadaic acid-inducible phosphoprotein OA48-18; cAMP regulatory element-associated protein 1; CRE-associated protein 1; CREAP-1 
Gene Name
 LUC7L3 
Gene Synonyms/Alias
 CREAP1; CROP; O48 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
23RNLAPDEKRSNVRWDubiquitination[1]
78EKSSRFMKVGYERDFacetylation[2]
124GAAGPTGKNEEKIQVubiquitination[3]
166MKLVEQLKEERELLRacetylation[2]
231KATVEELKEKLRKRTacetylation[2]
231KATVEELKEKLRKRTubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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
Functional Description
 Binds cAMP regulatory element DNA sequence. May play a role in RNA splicing. 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 3 3 Phosphoserine.
 MOD_RES 110 110 Phosphoserine.
 MOD_RES 231 231 N6-acetyllysine.
 MOD_RES 420 420 Phosphoserine.
 MOD_RES 425 425 Phosphoserine.
 MOD_RES 431 431 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Coiled coil; Complete proteome; DNA-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 432 AA 
Protein Sequence
MISAAQLLDE LMGRDRNLAP DEKRSNVRWD HESVCKYYLC GFCPAELFTN TRSDLGPCEK 60
IHDENLRKQY EKSSRFMKVG YERDFLRYLQ SLLAEVERRI RRGHARLALS QNQQSSGAAG 120
PTGKNEEKIQ VLTDKIDVLL QQIEELGSEG KVEEAQGMMK LVEQLKEERE LLRSTTSTIE 180
SFAAQEKQME VCEVCGAFLI VGDAQSRVDD HLMGKQHMGY AKIKATVEEL KEKLRKRTEE 240
PDRDERLKKE KQEREEREKE REREREERER KRRREEEERE KERARDRERR KRSRSRSRHS 300
SRTSDRRCSR SRDHKRSRSR ERRRSRSRDR RRSRSHDRSE RKHRSRSRDR RRSKSRDRKS 360
YKHRSKSRDR EQDRKSKEKE KRGSDDKKSS VKSGSREKQS EDTNTESKES DTKNEVNGTS 420
EDIKSEGDTQ SN 432 
Gene Ontology
 GO:0005925; C:focal adhesion; IDA:HPA.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003729; F:mRNA binding; IMP:UniProtKB.
 GO:0006915; P:apoptotic process; IMP:UniProtKB.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0006950; P:response to stress; IMP:UniProtKB.
 GO:0008380; P:RNA splicing; IMP:UniProtKB. 
Interpro
 IPR004882; LUC7-rel. 
Pfam
 PF03194; LUC7 
SMART
  
PROSITE
  
PRINTS