ERAP2
entrez
64167
canonical
uniprot
Q6P179
canonical
ensembl
ENSG00000164308
resolver
ensp
ENSP00000369235
resolver
ensp
ENSP00000400376
resolver
ensp
ENSP00000421175
resolver
ensp
ENSP00000425758
resolver
ensp
ENSP00000519508
resolver
enst
ENST00000714228
resolver
genesymbol
ERAP2
resolver
genesymbol_syn
LRAP
resolver
hgnc
HGNC:29499
resolver
uniprot
A0AAQ5BHS6
resolver
uniprot
B2R769
resolver
uniprot
Q7Z5K1
resolver
uniprot
Q8TD32
resolver
uniprot
Q8WVJ4
resolver
uniprot
Q9HBX2
resolver
uniprot_entry
A0AAQ5BHS6_HUMAN
resolver
uniprot_entry
B2R769_HUMAN
resolver
uniprot_entry
ERAP2_HUMAN
resolver
uniprot_sec
Q7Z5K1
resolver
uniprot_sec
Q8TD32
resolver
uniprot_sec
Q8WVJ4
resolver
uniprot_sec
Q9HBX2
resolver
amino_acid_sequence
MFHSSAMVNSHRKPMFNIHRGFYCLTAILPQICICSQFSVPSSYHFTEDPGAFPVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSNATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVPEKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHFETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQASLKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDPKTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLKEGFAKYMELIAVNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEVSYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNSCLESDFTSGGVCHSDPKMTSNMLAFLGENAEVKEMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGVFQEDPEWRALQERYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSNGYYIVHYEGHGWDQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKALDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISENLKRYLLQYFKPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMESSGKLNIPTDVLKIVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYALSTSKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENWTHLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDIFQTVLETITKNIKWLEKNLPTLRTWLMVNT
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. Preferentially hydrolyzes the basic residues Arg and Lys. {ECO:0000269|PubMed:12799365, ECO:0000269|PubMed:15908954, ECO:0000269|PubMed:16286653}.
uniprot
proteins
mass_dalton
110462
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:12799365, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22106953}.
uniprot
proteins
protein_family
Peptidase M1 family
uniprot
proteins
pubmed
12799365
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15691326
uniprot
proteins
pubmed
15908954
uniprot
proteins
pubmed
16286653
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16585582
uniprot
proteins
pubmed
17332242
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22106953
uniprot
proteins
pubmed
41882355
uniprot
proteins
sequence_length
960
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12799365}; Single-pass type II membrane protein {ECO:0000269|PubMed:12799365}.
uniprot
proteins
transmembrane_region
TRANSMEM 21..40; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins