CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006125
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aminopeptidase 2, mitochondrial 
Protein Synonyms/Alias
 AP-II; Aminopeptidase II; YscII 
Gene Name
 APE2 
Gene Synonyms/Alias
 LAP1; YKL157W; YKL158W; YKL611; YKL612 
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
320YATPGNEKHGQFAADacetylation[1]
338KTLAFFEKTFGIQYPubiquitination[2]
379VVDLLLDKDNSTLDRacetylation[1]
494SLLRMISKWLGEETFubiquitination[2]
511GVSQYLNKFKYGNAKacetylation[1]
605VVLSERSKTIELEDPubiquitination[2]
799GGAENYEKVYKIYLDacetylation[1]
Reference
 [1] 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]
 [2] 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, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 Involved in the cellular supply of leucine from externally offered leucine-containing dipeptide substrates. 
Sequence Annotation
 REGION 360 364 Substrate binding (By similarity).
 ACT_SITE 397 397 Proton acceptor (By similarity).
 METAL 396 396 Zinc; catalytic (By similarity).
 METAL 400 400 Zinc; catalytic (By similarity).
 METAL 419 419 Zinc; catalytic (By similarity).
 BINDING 228 228 Substrate (By similarity).
 CARBOHYD 381 381 N-linked (GlcNAc...) (Potential).
 CARBOHYD 713 713 N-linked (GlcNAc...) (Potential).  
Keyword
 Aminopeptidase; Complete proteome; Cytoplasm; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Periplasm; Protease; Reference proteome; Transit peptide; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 952 AA 
Protein Sequence
MPIVRWLLLK SAVRGSSLIG KAHPCLRSIA AHPRYLSNVY SPPAGVSRSL RINVMWKQSK 60
LTPPRFVKIM NRRPLFTETS HACAKCQKTS QLLNKTPNRE ILPDNVVPLH YDLTVEPDFK 120
TFKFEGSVKI ELKINNPAID TVTLNTVDTD IHSAKIGDVT SSEIISEEEQ QVTTFAFPKG 180
TMSSFKGNAF LDIKFTGILN DNMAGFYRAK YEDKLTGETK YMATTQMEPT DARRAFPCFD 240
EPNLKASFAI TLVSDPSLTH LSNMDVKNEY VKDGKKVTLF NTTPKMSTYL VAFIVAELKY 300
VESKNFRIPV RVYATPGNEK HGQFAADLTA KTLAFFEKTF GIQYPLPKMD NVAVHEFSAG 360
AMENWGLVTY RVVDLLLDKD NSTLDRIQRV AEVVQHELAH QWFGNLVTMD WWEGLWLNEG 420
FATWMSWYSC NEFQPEWKVW EQYVTDTLQH ALSLDSLRSS HPIEVPVKKA DEINQIFDAI 480
SYSKGASLLR MISKWLGEET FIKGVSQYLN KFKYGNAKTE DLWDALADAS GKDVRSVMNI 540
WTKKVGFPVI SVSEDGNGKI TFRQNRYLST ADVKPDEDKT IYPVFLALKT KNGVDSSVVL 600
SERSKTIELE DPTFFKVNSE QSGIYITSYT DERWAKLGQQ ADLLSVEDRV GLVADVKTLS 660
ASGYTSTTNF LNLVSKWNNE KSFVVWDQII NSISSMKSTW LFEPKETQDA LDNFTKQLIS 720
GMTHHLGWEF KSSDSFSTQR LKVTMFGAAC AARDADVEKA ALKMFTDYCS GNKEAIPALI 780
KPIVFNTVAR VGGAENYEKV YKIYLDPISN DEKLAALRSL GRFKEPKLLE RTLGYLFDGT 840
VLNQDIYIPM QGMRAHQEGV EALWNWVKKN WDELVKRLPP GLSMLGSVVT LGTSGFTSMQ 900
KIDEIKKFFA TKSTKGFDQS LAQSLDTITS KAQWVNRDRD VVNKYLKENG YY 952 
Gene Ontology
 GO:0030287; C:cell wall-bounded periplasmic space; IDA:SGD.
 GO:0005576; C:extracellular region; IDA:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0070006; F:metalloaminopeptidase activity; IDA:SGD.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0043171; P:peptide catabolic process; IDA:SGD.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR024571; DUF3358.
 IPR001930; Peptidase_M1.
 IPR014782; Peptidase_M1_N. 
Pfam
 PF11838; DUF3358
 PF01433; Peptidase_M1 
SMART
  
PROSITE
 PS00142; ZINC_PROTEASE 
PRINTS
 PR00756; ALADIPTASE.