CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018220
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Isoaspartyl peptidase/L-asparaginase 
Protein Synonyms/Alias
 Asparaginase-like protein 1; Asparaginase-like sperm autoantigen; Beta-aspartyl-peptidase; Glial asparaginase; Isoaspartyl dipeptidase; L-asparagine amidohydrolase; Isoaspartyl peptidase/L-asparaginase alpha chain; Isoaspartyl peptidase/L-asparaginase beta chain 
Gene Name
 Asrgl1 
Gene Synonyms/Alias
 Alp; Gliap; Hiob 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
52LVSEGIAKAATEGYNacetylation[1]
134LARLVMEKTPHCFLTacetylation[1]
147LTGRGAEKFAADMGIacetylation[1]
161IPQTPAEKLITERTKacetylation[1]
173RTKKHLEKEKLEKGAacetylation[1]
187AQKADCPKNSGTVGAacetylation[1]
279TLALDYMKSKLKGLGacetylation[1]
283DYMKSKLKGLGGLILacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 Has both L-asparaginase and beta-aspartyl peptidase activity. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L- Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine (By similarity). May be involved in the production of L- aspartate, which can act as an excitatory neurotransmitter in some brain regions. 
Sequence Annotation
 REGION 219 222 Substrate binding (By similarity).
 REGION 242 245 Substrate binding (By similarity).
 ACT_SITE 191 191 Nucleophile (By similarity).  
Keyword
 Autocatalytic cleavage; Complete proteome; Cytoplasm; Hydrolase; Protease; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 333 AA 
Protein Sequence
MATARPSSCG RDSVPATPRA SIDVSLVVVV HGGGASNISP GRKELVSEGI AKAATEGYNI 60
LKAGGSAVDA VEGAVTMLEN DPEFNAGYGS VLNADGDIEM DASIMDGKDL SAGAVSAVRC 120
IANPVKLARL VMEKTPHCFL TGRGAEKFAA DMGIPQTPAE KLITERTKKH LEKEKLEKGA 180
QKADCPKNSG TVGAVALDCK GNLAYATSTG GIVNKMVGRV GDSPCIGAGG YADNNLGAVS 240
TTGHGESILK VNLARLALFH VEQGKTVDEA ATLALDYMKS KLKGLGGLIL INKTGDWVAK 300
WTSASMPWAA VKNGKLQAGI DLCETKTRNL PTC 333 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0015630; C:microtubule cytoskeleton; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0004067; F:asparaginase activity; IDA:MGI.
 GO:0008798; F:beta-aspartyl-peptidase activity; ISS:UniProtKB.
 GO:0033345; P:asparagine catabolic process via L-aspartate; IDA:UniProtKB.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR000246; Peptidase_T2. 
Pfam
 PF01112; Asparaginase_2 
SMART
  
PROSITE
  
PRINTS