CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022415
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Endoplasmic reticulum aminopeptidase 1 
Protein Synonyms/Alias
 ARTS-1; Adipocyte-derived leucine aminopeptidase; A-LAP; Aminopeptidase PILS; Puromycin-insensitive leucyl-specific aminopeptidase; PILS-AP; Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator 
Gene Name
 ERAP1 
Gene Synonyms/Alias
 APPILS; ARTS1; KIAA0525; UNQ584/PRO1154 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
440FDDVSYDKGACILNMubiquitination[1]
458YLSADAFKSGIVQYLubiquitination[1]
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] 
Functional Description
 Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney. 
Sequence Annotation
 REGION 317 321 Substrate binding (By similarity).
 ACT_SITE 354 354 Proton acceptor (By similarity).
 METAL 353 353 Zinc; catalytic.
 METAL 357 357 Zinc; catalytic.
 METAL 376 376 Zinc; catalytic.
 BINDING 183 183 Substrate (By similarity).
 CARBOHYD 70 70 N-linked (GlcNAc...).
 CARBOHYD 154 154 N-linked (GlcNAc...).
 CARBOHYD 414 414 N-linked (GlcNAc...).
 CARBOHYD 760 760 N-linked (GlcNAc...).
 CARBOHYD 901 901 N-linked (GlcNAc...) (Potential).
 DISULFID 404 443
 DISULFID 736 743  
Keyword
 3D-structure; Adaptive immunity; Alternative splicing; Aminopeptidase; Complete proteome; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Immunity; Membrane; Metal-binding; Metalloprotease; Polymorphism; Protease; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 941 AA 
Protein Sequence
MVFLPLKWSL ATMSFLLSSL LALLTVSTPS WCQSTEASPK RSDGTPFPWN KIRLPEYVIP 60
VHYDLLIHAN LTTLTFWGTT KVEITASQPT STIILHSHHL QISRATLRKG AGERLSEEPL 120
QVLEHPRQEQ IALLAPEPLL VGLPYTVVIH YAGNLSETFH GFYKSTYRTK EGELRILAST 180
QFEPTAARMA FPCFDEPAFK ASFSIKIRRE PRHLAISNMP LVKSVTVAEG LIEDHFDVTV 240
KMSTYLVAFI ISDFESVSKI TKSGVKVSVY AVPDKINQAD YALDAAVTLL EFYEDYFSIP 300
YPLPKQDLAA IPDFQSGAME NWGLTTYRES ALLFDAEKSS ASSKLGITMT VAHELAHQWF 360
GNLVTMEWWN DLWLNEGFAK FMEFVSVSVT HPELKVGDYF FGKCFDAMEV DALNSSHPVS 420
TPVENPAQIR EMFDDVSYDK GACILNMLRE YLSADAFKSG IVQYLQKHSY KNTKNEDLWD 480
SMASICPTDG VKGMDGFCSR SQHSSSSSHW HQEGVDVKTM MNTWTLQKGF PLITITVRGR 540
NVHMKQEHYM KGSDGAPDTG YLWHVPLTFI TSKSDMVHRF LLKTKTDVLI LPEEVEWIKF 600
NVGMNGYYIV HYEDDGWDSL TGLLKGTHTA VSSNDRASLI NNAFQLVSIG KLSIEKALDL 660
SLYLKHETEI MPVFQGLNEL IPMYKLMEKR DMNEVETQFK AFLIRLLRDL IDKQTWTDEG 720
SVSERMLRSQ LLLLACVHNY QPCVQRAEGY FRKWKESNGN LSLPVDVTLA VFAVGAQSTE 780
GWDFLYSKYQ FSLSSTEKSQ IEFALCRTQN KEKLQWLLDE SFKGDKIKTQ EFPQILTLIG 840
RNPVGYPLAW QFLRKNWNKL VQKFELGSSS IAHMVMGTTN QFSTRTRLEE VKGFFSSLKE 900
NGSQLRCVQQ TIETIEENIG WMDKNFDKIR VWLQSEKLEH DPEADATG 948 
Gene Ontology
 GO:0005829; C:cytosol; NAS:UniProtKB.
 GO:0005788; C:endoplasmic reticulum lumen; TAS:HGNC.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0005576; C:extracellular region; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; NAS:UniProtKB.
 GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
 GO:0005151; F:interleukin-1, Type II receptor binding; TAS:HGNC.
 GO:0008235; F:metalloexopeptidase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; NAS:UniProtKB.
 GO:0001525; P:angiogenesis; TAS:HGNC.
 GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; NAS:UniProtKB.
 GO:0045444; P:fat cell differentiation; NAS:UniProtKB.
 GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
 GO:0045766; P:positive regulation of angiogenesis; IEA:Compara.
 GO:0008217; P:regulation of blood pressure; NAS:UniProtKB.
 GO:0045088; P:regulation of innate immune response; NAS:UniProtKB.
 GO:0009617; P:response to bacterium; IEP:BHF-UCL. 
Interpro
 IPR024571; DUF3358.
 IPR001930; Peptidase_M1.
 IPR014782; Peptidase_M1_N. 
Pfam
 PF11838; DUF3358
 PF01433; Peptidase_M1 
SMART
  
PROSITE
 PS00142; ZINC_PROTEASE 
PRINTS
 PR00756; ALADIPTASE.