CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012851
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peroxisomal leader peptide-processing protease 
Protein Synonyms/Alias
 Trypsin domain-containing protein 1; Peroxisomal leader peptide-processing protease, 15 kDa form; Peroxisomal leader peptide-processing protease, 45 kDa form 
Gene Name
 TYSND1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
389LVRSTTPKSVAIWGRubiquitination[1, 2]
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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Peroxisomal protease that mediates both the removal of the leader peptide from proteins containing a PTS2 target sequence and processes several PTS1-containing proteins. Catalyzes the processing of PTS1-proteins involved in the peroxisomal beta- oxidation of fatty acids. 
Sequence Annotation
 REGION 319 531 Serine protease.
 ACT_SITE 372 372 Charge relay system (By similarity).
 ACT_SITE 408 408 Charge relay system (By similarity).
 ACT_SITE 481 481 Charge relay system (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Hydrolase; Peroxisome; Polymorphism; Protease; Reference proteome; Serine protease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 566 AA 
Protein Sequence
MRRQWGSAMR AAEQAGCMVS ASRAGQPEAG PWSCSGVILS RSPGLVLCHG GIFVPFLRAG 60
SEVLTAAGAV FLPGDSCRDD LRLHVQWAPT AAGPGGGAER GRPGLCTPQC ASLEPGPPAP 120
SRGRPLQPRL PAELLLLLSC PAFWAHFARL FGDEAAEQWR FSSAARDDEV SEDEEADQLR 180
ALGWFALLGV RLGQEEVEEE RGPAMAVSPL GAVPKGAPLL VCGSPFGAFC PDIFLNTLSC 240
GVLSNVAGPL LLTDARCLPG TEGGGVFTAR PAGALVALVV APLCWKAGEW VGFTLLCAAA 300
PLFRAARDAL HRLPHSTAAL AALLPPEVGV PWGLPLRDSG PLWAAAAVLV ECGTVWGSGV 360
AVAPRLVVTC RHVSPREAAR VLVRSTTPKS VAIWGRVVFA TQETCPYDIA VVSLEEDLDD 420
VPIPVPAEHF HEGEAVSVVG FGVFGQSCGP SVTSGILSAV VQVNGTPVML QTTCAVHSGS 480
SGGPLFSNHS GNLLGIITSN TRDNNTGATY PHLNFSIPIT VLQPALQQYS QTQDLGGLRE 540
LDRAAEPVRV VWRLQRPLAE APRSKL 566 
Gene Ontology
 GO:0005777; C:peroxisome; IDA:UniProtKB.
 GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
 GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
 GO:0016485; P:protein processing; IMP:UniProtKB.
 GO:0006508; P:proteolysis; IMP:UniProtKB.
 GO:0031998; P:regulation of fatty acid beta-oxidation; IMP:UniProtKB. 
Interpro
 IPR017345; Pept_S1A_Tysnd1.
 IPR001254; Peptidase_S1.
 IPR009003; Trypsin-like_Pept_dom. 
Pfam
  
SMART
 SM00020; Tryp_SPc 
PROSITE
  
PRINTS