ADAMTS14
entrez
140766
canonical
uniprot
Q8WXS8
canonical
ensembl
ENSG00000138316
resolver
ensp
ENSP00000362303
resolver
ensp
ENSP00000362304
resolver
genesymbol
ADAMTS14
resolver
hgnc
HGNC:14899
resolver
uniprot
Q5T4G0
resolver
uniprot
Q5T4G1
resolver
uniprot
Q8TE55
resolver
uniprot
Q8TEY8
resolver
uniprot_entry
ATS14_HUMAN
resolver
uniprot_sec
Q5T4G0
resolver
uniprot_sec
Q5T4G1
resolver
uniprot_sec
Q8TE55
resolver
uniprot_sec
Q8TEY8
resolver
amino_acid_sequence
MAPLRALLSYLLPLHCALCAAAGSRTPELHLSGKLSDYGVTVPCSTDFRGRFLSHVVSGPAAASAGSMVVDTPPTLPRHSSHLRVARSPLHPGGTLWPGRVGRHSLYFNVTVFGKELHLRLRPNRRLVVPGSSVEWQEDFRELFRQPLRQECVYTGGVTGMPGAAVAISNCDGLAGLIRTDSTDFFIEPLERGQQEKEASGRTHVVYRREAVQQEWAEPDGDLHNEAFGLGDLPNLLGLVGDQLGDTERKRRHAKPGSYSIEVLLVVDDSVVRFHGKEHVQNYVLTLMNIVDEIYHDESLGVHINIALVRLIMVGYRQSLSLIERGNPSRSLEQVCRWAHSQQRQDPSHAEHHDHVVFLTRQDFGPSGYAPVTGMCHPLRSCALNHEDGFSSAFVIAHETGHVLGMEHDGQGNGCADETSLGSVMAPLVQAAFHRFHWSRCSKLELSRYLPSYDCLLDDPFDPAWPQPPELPGINYSMDEQCRFDFGSGYQTCLAFRTFEPCKQLWCSHPDNPYFCKTKKGPPLDGTECAPGKWCFKGHCIWKSPEQTYGQDGGWSSWTKFGSCSRSCGGGVRSRSRSCNNPSPAYGGRLCLGPMFEYQVCNSEECPGTYEDFRAQQCAKRNSYYVHQNAKHSWVPYEPDDDAQKCELICQSADTGDVVFMNQVVHDGTRCSYRDPYSVCARGECVPVGCDKEVGSMKADDKCGVCGGDNSHCRTVKGTLGKASKQAGALKLVQIPAGARHIQIEALEKSPHRIVVKNQVTGSFILNPKGKEATSRTFTAMGLEWEDAVEDAKESLKTSGPLPEAIAILALPPTEGGPRSSLAYKYVIHEDLLPLIGSNNVLLEEMDTYEWALKSWAPCSKACGGGIQFTKYGCRRRRDHHMVQRHLCDHKKRPKPIRRRCNQHPCSQPVWVTEEWGACSRSCGKLGVQTRGIQCLLPLSNGTHKVMPAKACAGDRPEARRPCLRVPCPAQWRLGAWSQCSATCGEGIQQRQVVCRTNANSLGHCEGDRPDTVQVCSLPACGGNHQNSTVRADVWELGTPEGQWVPQSEPLHPINKISSTEPCTGDRSVFCQMEVLDRYCSIPGYHRLCCVSCIKKASGPNPGPDPGPTSLPPFSTPGSPLPGPQDPADAAEPPGKPTGSEDHQHGRATQLPGALDTSSPGTQHPFAPETPIPGASWSISPTTPGGLPWGWTQTPTPVPEDKGQPGEDLRHPGTSLPAASPVT
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Has aminoprocollagen type I processing activity in the absence of ADAMTS2 (PubMed:11741898). Seems to be synthesized as a latent enzyme that requires activation to display aminoprocollagen peptidase activity (PubMed:11741898). Cleaves lysyl oxidase LOX at a site downstream of its propeptide cleavage site to produce a short LOX form (PubMed:31152061). {ECO:0000269|PubMed:11741898, ECO:0000269|PubMed:31152061}.
uniprot
proteins
mass_dalton
133888
uniprot
proteins
post_translational_modification
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Can also be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}.
uniprot
proteins
pubmed
11741898
uniprot
proteins
pubmed
11779638
uniprot
proteins
pubmed
11867212
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
31152061
uniprot
proteins
sequence_length
1223
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
uniprot
proteins