ERAP1
entrez
51752
canonical
uniprot
Q9NZ08
canonical
ensembl
ENSG00000164307
resolver
ensp
ENSP00000296754
resolver
ensp
ENSP00000406304
resolver
ensp
ENSP00000723782
resolver
ensp
ENSP00000723784
resolver
ensp
ENSP00000777749
resolver
ensp
ENSP00000777750
resolver
genesymbol
ERAP1
resolver
genesymbol_syn
APPILS
resolver
genesymbol_syn
ARTS1
resolver
genesymbol_syn
KIAA0525
resolver
hgnc
HGNC:18173
resolver
uniprot
A0A075BTL2
resolver
uniprot
O60278
resolver
uniprot
Q6UWY6
resolver
uniprot
Q8NEL4
resolver
uniprot
Q8TAD0
resolver
uniprot
Q9UHF8
resolver
uniprot
Q9UKY2
resolver
uniprot_entry
A0A075BTL2_HUMAN
resolver
uniprot_entry
ERAP1_HUMAN
resolver
uniprot_sec
O60278
resolver
uniprot_sec
Q6UWY6
resolver
uniprot_sec
Q8NEL4
resolver
uniprot_sec
Q8TAD0
resolver
uniprot_sec
Q9UHF8
resolver
uniprot_sec
Q9UKY2
resolver
amino_acid_sequence
MVFLPLKWSLATMSFLLSSLLALLTVSTPSWCQSTEASPKRSDGTPFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMASICPTDGVKGMDGFCSRSQHSSSSSHWHQEGVDVKTMMNTWTLQKGFPLITITVRGRNVHMKQEHYMKGSDGAPDTGYLWHVPLTFITSKSDMVHRFLLKTKTDVLILPEEVEWIKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYLKHETEIMPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPCVQRAEGYFRKWKESNGNLSLPVDVTLAVFAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQEFPQILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQLRCVQQTIETIEENIGWMDKNFDKIRVWLQSEKLERM
uniprot
proteins
ec_number
3.4.11.-
uniprot
proteins
function
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 (PubMed:16286653, PubMed:26224046). Rapidly degrades 13-mer to a 9-mer and then stops (PubMed:16286653). 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. {ECO:0000269|PubMed:15908954, ECO:0000269|PubMed:16286653, ECO:0000269|PubMed:21478864, ECO:0000269|PubMed:26224046}.
uniprot
proteins
mass_dalton
107235
uniprot
proteins
mutagenesis
MUTAGEN 438; /note="Y->F: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:21478864
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:21478864, ECO:0000269|Ref.16}.
uniprot
proteins
protein_family
Peptidase M1 family
uniprot
proteins
pubmed
10220586
uniprot
proteins
pubmed
11056387
uniprot
proteins
pubmed
11481040
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15908954
uniprot
proteins
pubmed
16286653
uniprot
proteins
pubmed
18445477
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21478864
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26224046
uniprot
proteins
pubmed
41882355
uniprot
proteins
pubmed
9628581
uniprot
proteins
sequence_length
941
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:15908954}; Single-pass type II membrane protein {ECO:0000305|PubMed:15908954}.
uniprot
proteins
transmembrane_region
TRANSMEM 2..21; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins