CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005594
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carboxypeptidase S 
Protein Synonyms/Alias
 GLY-X carboxypeptidase; YSCS 
Gene Name
 CPS1 
Gene Synonyms/Alias
 CPS; YJL172W; J0510 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
8MIALPVEKAPRKSLWubiquitination[1, 2, 3]
374FCPRRKDKLVEYISNacetylation[4]
442YAKKIAEKYGYGLSKacetylation[4]
Reference
 [1] A perturbed ubiquitin landscape distinguishes between ubiquitin in trafficking and in proteolysis.
 Ziv I, Matiuhin Y, Kirkpatrick DS, Erpapazoglou Z, Leon S, Pantazopoulou M, Kim W, Gygi SP, Haguenauer-Tsapis R, Reis N, Glickman MH, Kleifeld O.
 Mol Cell Proteomics. 2011 May;10(5):M111.009753. [PMID: 21427232]
 [2] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [3] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [4] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 Necessary for use of certain peptides as sole nitrogen source. May also cleave intracellularly generated peptides to recycle amino acids for protein synthesis. 
Sequence Annotation
 ACT_SITE 170 170 By similarity.
 ACT_SITE 239 239 Proton acceptor (By similarity).
 METAL 168 168 Zinc 2 (By similarity).
 METAL 205 205 Zinc 1 (By similarity).
 METAL 205 205 Zinc 2 (By similarity).
 METAL 240 240 Zinc 1 (By similarity).
 METAL 268 268 Zinc 2 (By similarity).
 METAL 547 547 Zinc 1 (By similarity).
 CARBOHYD 88 88 N-linked (GlcNAc...) (Potential).
 CARBOHYD 176 176 N-linked (GlcNAc...) (Potential).
 CARBOHYD 228 228 N-linked (GlcNAc...) (Potential).
 CARBOHYD 381 381 N-linked (GlcNAc...) (Potential).
 CARBOHYD 525 525 N-linked (GlcNAc...) (Potential).  
Keyword
 Carboxypeptidase; Complete proteome; Glycoprotein; Hydrolase; Membrane; Metal-binding; Protease; Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation; Vacuole; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 576 AA 
Protein Sequence
MIALPVEKAP RKSLWQRHRA FISGIVALII IGTFFLTSGL HPAPPHEAKR PHHGKGPMHS 60
PKCEKIEPLS PSFKHSVDTI LHDPAFRNSS IEKLSNAVRI PTVVQDKNPN PADDPDFYKH 120
FYELHDYFEK TFPNIHKHLK LEKVNELGLL YTWEGSDPDL KPLLLMAHQD VVPVNNETLS 180
SWKFPPFSGH YDPETDFVWG RGSNDCKNLL IAEFEAIEQL LIDGFKPNRT IVMSLGFDEE 240
ASGTLGAASL ASFLHERYGD DGIYSIIDEG EGIMEVDKDV FVATPINAEK GYVDFEVSIL 300
GHGGHSSVPP DHTTIGIASE LITEFEANPF DYEFEFDNPI YGLLTCAAEH SKSLSKDVKK 360
TILGAPFCPR RKDKLVEYIS NQSHLRSLIR TTQAVDIING GVKANALPET TRFLINHRIN 420
LHSSVAEVFE RNIEYAKKIA EKYGYGLSKN GDDYIIPETE LGHIDITLLR ELEPAPLSPS 480
SGPVWDILAG TIQDVFENGV LQNNEEFYVT TGLFSGNTDT KYYWNLSKNI YRFVGSIIDI 540
DLLKTLHSVN EHVDVPGHLS AIAFVYEYIV NVNEYA 576 
Gene Ontology
 GO:0000328; C:fungal-type vacuole lumen; IDA:SGD.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
 GO:0004180; F:carboxypeptidase activity; IMP:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
 GO:0006807; P:nitrogen compound metabolic process; IMP:SGD.
 GO:0051603; P:proteolysis involved in cellular protein catabolic process; IMP:SGD. 
Interpro
 IPR001261; ArgE/DapE_CS.
 IPR017141; Pept_M20_carboxypep.
 IPR002933; Peptidase_M20.
 IPR011650; Peptidase_M20_dimer. 
Pfam
 PF07687; M20_dimer
 PF01546; Peptidase_M20 
SMART
  
PROSITE
 PS00758; ARGE_DAPE_CPG2_1
 PS00759; ARGE_DAPE_CPG2_2 
PRINTS