CTSE
entrez
1510
canonical
uniprot
P14091
canonical
ensembl
ENSG00000196188
resolver
ensp
ENSP00000350911
resolver
ensp
ENSP00000353350
resolver
ensp
ENSP00000504305
resolver
ensp
ENSP00000694543
resolver
enst
ENST00000360218
resolver
genesymbol
CTSE
resolver
hgnc
HGNC:2530
resolver
uniprot
A0A7P0MPN9
resolver
uniprot
B4DNU8
resolver
uniprot
Q5TZ01
resolver
uniprot
Q5TZ02
resolver
uniprot
Q9NY58
resolver
uniprot
Q9UCE3
resolver
uniprot
Q9UCE4
resolver
uniprot_entry
A0A7P0MPN9_HUMAN
resolver
uniprot_entry
B4DNU8_HUMAN
resolver
uniprot_entry
CATE_HUMAN
resolver
uniprot_sec
Q5TZ01
resolver
uniprot_sec
Q5TZ02
resolver
uniprot_sec
Q9NY58
resolver
uniprot_sec
Q9UCE3
resolver
uniprot_sec
Q9UCE4
resolver
amino_acid_sequence
MKTLLLLLLVLLELGEAQGSLHRVPLRRHPSLKKKLRARSQLSEFWKSHNLDMIQFTESCSMDQSAKEPLINYLDMEYFGTISIGSPPQNFTVIFDTGSSNLWVPSVYCTSPACKTHSRFQPSQSSTYSQPGQSFSIQYGTGSLSGIIGADQVSVEGLTVVGQQFGESVTEPGQTFVDAEFDGILGLGYPSLAVGGVTPVFDNMMAQNLVDLPMFSVYMSSNPEGGAGSELIFGGYDHSHFSGSLNWVPVTKQAYWQIALDNIQVGGTVMFCSEGCQAIVDTGTSLITGPSDKIKQLQNAIGAAPVDGEYAVECANLNVMPDVTFTINGVPYTLSPTAYTLLDFVDGMQFCSSGFQGLDIHPPAGPLWILGDVFIRQFYSVFDRGNNRVGLAPAVP
uniprot
proteins
ec_number
3.4.23.34
uniprot
proteins
function
FUNCTION: May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain. {ECO:0000269|PubMed:8765029}.
uniprot
proteins
mass_dalton
42794
uniprot
proteins
mutagenesis
MUTAGEN 60; /note="C->A: Abolishes homodimerization."; /evidence="ECO:0000269|PubMed:7789521
uniprot
proteins
post_translational_modification
PTM: Glycosylated. The nature of the carbohydrate chain varies between cell types. In fibroblasts, the proenzyme contains a high mannose-type oligosaccharide, while the mature enzyme contains a complex-type oligosaccharide. In erythrocyte membranes, both the proenzyme and mature enzyme contain a complex-type oligosaccharide. {ECO:0000269|PubMed:2334440, ECO:0000269|PubMed:7983070, ECO:0000269|PubMed:8346912}.; PTM: Two forms are produced by autocatalytic cleavage, form I begins at Ile-54, form II begins at Thr-57.
uniprot
proteins
protein_family
Peptidase A1 family
uniprot
proteins
pubmed
11322887
uniprot
proteins
pubmed
12531480
uniprot
proteins
pubmed
1370478
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
2334440
uniprot
proteins
pubmed
2674141
uniprot
proteins
pubmed
7789521
uniprot
proteins
pubmed
7983070
uniprot
proteins
pubmed
8346912
uniprot
proteins
pubmed
8765029
uniprot
proteins
sequence_length
396
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:7983070}. Note=The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome.
uniprot
proteins