CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010796
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alpha-1-antitrypsin 1-5 
Protein Synonyms/Alias
 Alpha-1 protease inhibitor 5; Serine protease inhibitor 1-5; Serine protease inhibitor A1e; Serpin A1e 
Gene Name
 Serpina1e 
Gene Synonyms/Alias
 Dom5; Spi1-5 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
213ILFKGKWKKPFDPENubiquitination[1]
214LFKGKWKKPFDPENTubiquitination[1]
222PFDPENTKQAEFHVDubiquitination[1]
292LNKELISKFLLNRRRacetylation[2, 3]
292LNKELISKFLLNRRRubiquitination[1]
347TEENAPLKLSQAVHKubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [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
Functional Description
 Does not inhibit elastase or chymotrypsin. No target protease has been identified to date. 
Sequence Annotation
 REGION 368 387 RCL.
 CARBOHYD 64 64 N-linked (GlcNAc...).
 CARBOHYD 101 101 N-linked (GlcNAc...) (Potential).
 CARBOHYD 265 265 N-linked (GlcNAc...) (Potential).  
Keyword
 Complete proteome; Glycoprotein; Protease inhibitor; Reference proteome; Secreted; Serine protease inhibitor; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 413 AA 
Protein Sequence
MTPSISWCLL LLAGLCCLVP SFLAEDVQET DTSQKDQSPA SHEIATNLGD FAISLYRELV 60
HQSNTSNIFF SPVSIATAFA MLSLGSKGDT HTQILEGLQF NLTQTSEADI HNSFQHLLQT 120
LNRPDSELQL STGNGLFVNN DLKLVEKFLE EAKNHYQAEV FSVNFAESEE AKKVINDFVE 180
KGTQGKIVEA VKKLEQDTVF VLANYILFKG KWKKPFDPEN TKQAEFHVDE STTVKVPMMT 240
LSGMLDVHHC STLSSWVLLM DYAGNATAVF LLPDDGKMQH LEQTLNKELI SKFLLNRRRR 300
LAQIHIPRLS ISGNYNLETL MSPLGITRIF NSGADLSGIT EENAPLKLSQ AVHKAVLTID 360
ETGTEAAAAT VLQGGFLSMP PILHFNRPFL FIIFEEHSQS PLFVGKVVDP THK 413 
Gene Ontology
 GO:0005576; C:extracellular region; IBA:RefGenome.
 GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:RefGenome.
 GO:0030162; P:regulation of proteolysis; IBA:RefGenome.
 GO:0034097; P:response to cytokine stimulus; IDA:MGI.
 GO:0043434; P:response to peptide hormone stimulus; IDA:MGI. 
Interpro
 IPR023795; Protease_inhib_I4_serpin_CS.
 IPR023796; Serpin_dom.
 IPR000215; Serpin_fam. 
Pfam
 PF00079; Serpin 
SMART
 SM00093; SERPIN 
PROSITE
 PS00284; SERPIN 
PRINTS