Gene name:
ERAP1 (UNQ584/PRO1154;APPILS;ARTS1;KIAA0525) ;
Protein name:
Endoplasmic reticulum aminopeptidase 1 ;
Alternative:
Adipocyte-derived leucine aminopeptidase (A-LAP) ;ARTS-1 ;Puromycin-insensitive leucyl-specific aminopeptidase (PILS-AP) ;Aminopeptidase PILS ;Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator ;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Monomer. May also exist as a heterodimer; with ERAP2. Interacts with RBMX.
Function:
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.
Subcellular Location:
Endoplasmic reticulum membrane
Single-pass type II membrane protein
Protein Attributes:
50:
MVFLPLKWSL | ATMSFLLSSL | LALLTVSTPS | WCQSTEASPK | RSDGTPFPWN |
100:
KIRLPEYVIP | VHYDLLIHAN | LTTLTFWGTT | KVEITASQPT | STIILHSHHL |
150:
QISRATLRKG | AGERLSEEPL | QVLEHPRQEQ | IALLAPEPLL | VGLPYTVVIH |
200:
YAGNLSETFH | GFYKSTYRTK | EGELRILAST | QFEPTAARMA | FPCFDEPAFK |
250:
ASFSIKIRRE | PRHLAISNMP | LVKSVTVAEG | LIEDHFDVTV | KMSTYLVAFI |
300:
ISDFESVSKI | TKSGVKVSVY | AVPDKINQAD | YALDAAVTLL | EFYEDYFSIP |
350:
YPLPKQDLAA | IPDFQSGAME | NWGLTTYRES | ALLFDAEKSS | ASSKLGITMT |
400:
VAHELAHQWF | GNLVTMEWWN | DLWLNEGFAK | FMEFVSVSVT | HPELKVGDYF |
450:
FGKCFDAMEV | DALNSSHPVS | TPVENPAQIR | EMFDDVSYDK | GACILNMLRE |
500:
YLSADAFKSG | IVQYLQKHSY | KNTKNEDLWD | SMASICPTDG | VKGMDGFCSR |
550:
SQHSSSSSHW | HQEGVDVKTM | MNTWTLQKGF | PLITITVRGR | NVHMKQEHYM |
600:
KGSDGAPDTG | YLWHVPLTFI | TSKSDMVHRF | LLKTKTDVLI | LPEEVEWIKF |
650:
NVGMNGYYIV | HYEDDGWDSL | TGLLKGTHTA | VSSNDRASLI | NNAFQLVSIG |
700:
KLSIEKALDL | SLYLKHETEI | MPVFQGLNEL | IPMYKLMEKR | DMNEVETQFK |
750:
AFLIRLLRDL | IDKQTWTDEG | SVSERMLRSQ | LLLLACVHNY | QPCVQRAEGY |
800:
FRKWKESNGN | LSLPVDVTLA | VFAVGAQSTE | GWDFLYSKYQ | FSLSSTEKSQ |
850:
IEFALCRTQN | KEKLQWLLDE | SFKGDKIKTQ | EFPQILTLIG | RNPVGYPLAW |
900:
QFLRKNWNKL | VQKFELGSSS | IAHMVMGTTN | QFSTRTRLEE | VKGFFSSLKE |
941:
NGSQLRCVQQ | TIETIEENIG | WMDKNFDKIR | VWLQSEKLER | M
Vaild Sequence:
Related Databases
Uniprot:
ELISA Kit
CLIA Kit
Polyclonal Antibody
Monoclonal Antibody
Protein
FOR
Human
Rat
Mouse
ELISA Kit for Human Endoplasmic reticulum aminopeptidase 1
ELISA Kit for Human Endoplasmic reticulum aminopeptidase 1
ELISA Kit for Human Endoplasmic reticulum aminopeptidase 1
CLIA Kit for Human Endoplasmic reticulum aminopeptidase 1
CLIA Kit for Human Endoplasmic reticulum aminopeptidase 1
CLIA Kit for Human Endoplasmic reticulum aminopeptidase 1
Polyclonal Antibody for Human Endoplasmic reticulum aminopeptidase 1
Polyclonal Antibody for Human Endoplasmic reticulum aminopeptidase 1
Polyclonal Antibody for Human Endoplasmic reticulum aminopeptidase 1
Monoclonal Antibody for Human Endoplasmic reticulum aminopeptidase 1
Monoclonal Antibody for Human Endoplasmic reticulum aminopeptidase 1
Monoclonal Antibody for Human Endoplasmic reticulum aminopeptidase 1
Protein for Human Endoplasmic reticulum aminopeptidase 1
Protein for Human Endoplasmic reticulum aminopeptidase 1
Protein for Human Endoplasmic reticulum aminopeptidase 1
R&D Technical Data
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Precision
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Recovery
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Linearity
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References
1.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);VARIANT PRO-127
tissue :
White adipose tissue .
2.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2);VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730
tissue :
Leukocyte .
3.
"Molecular characterization of human aminopeptidase PILS."
Schomburg L.
Submitted (1999-09) to the EMBL/GenBank/DDBJ databases
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);VARIANTS ASP-346; ARG-528 AND GLU-730
4.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
5.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2);VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730
tissue :
Brain .
6.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : SEQUENCE REVISION
7.
"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
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Xie M.-H.
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Yansura D.G.
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Yi S.
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Yu G.
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Yuan J.
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Zhang M.
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Zhang Z.
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Goddard A.D.
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Wood W.I.
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Godowski P.J.
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more...
Genome Res.13:2265-2270(2003)
[
PubMed ]
[
Europe PMC ]
[
Abstract ]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1);VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730
8.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
tissue :
Testis .
9.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : PROTEIN SEQUENCE OF 37-49;CHARACTERIZATION
10.
"Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum."
Saveanu L.
,
Carroll O.
,
Lindo V.
,
Del Val M.
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Lopez D.
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Lepelletier Y.
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Nat. Immunol.6:689-697(2005)
[
PubMed ]
[
Europe PMC ]
[
Abstract ]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION;SUBCELLULAR LOCATION;SUBUNIT;INDUCTION BY IFNG
11.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION
12.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : INTERACTION WITH RBMX
13.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-414
tissue :
Liver .
14.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
15.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 46-940 IN COMPLEX WITH ZINC IONS;DISULFIDE BONDS;GLYCOSYLATION AT ASN-70; ASN-154 AND ASN-414
16.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 37-939 IN COMPLEX WITH ZINC IONS AND BESTATIN;FUNCTION;DISULFIDE BONDS;GLYCOSYLATION AT ASN-70; ASN-154 AND ASN-760;ACTIVE SITE;CATALYTIC ACTIVITY;SUBUNIT;MUTAGENESIS OF TYR-438