ADAMTS1
entrez
9510
canonical
uniprot
Q9UHI8
canonical
ensembl
ENSG00000154734
resolver
ensp
ENSP00000284984
resolver
enst
ENST00000284984
resolver
genesymbol
ADAMTS1
resolver
genesymbol_syn
KIAA1346
resolver
genesymbol_syn
METH1
resolver
hgnc
HGNC:217
resolver
uniprot
B2RB33
resolver
uniprot
D3DSD5
resolver
uniprot
Q9NSJ8
resolver
uniprot
Q9P2K0
resolver
uniprot
Q9UH83
resolver
uniprot
Q9UP80
resolver
uniprot_entry
ATS1_HUMAN
resolver
uniprot_entry
B2RB33_HUMAN
resolver
uniprot_sec
D3DSD5
resolver
uniprot_sec
Q9NSJ8
resolver
uniprot_sec
Q9P2K0
resolver
uniprot_sec
Q9UH83
resolver
uniprot_sec
Q9UP80
resolver
amino_acid_sequence
MQRAVPEGFGRRKLGSDMGNAERAPGSRSFGPVPTLLLLAAALLAVSDALGRPSEEDEELVVPELERAPGHGTTRLRLHAFDQQLDLELRPDSSFLAPGFTLQNVGRKSGSETPLPETDLAHCFYSGTVNGDPSSAAALSLCEGVRGAFYLLGEAYFIQPLPAASERLATAAPGEKPPAPLQFHLLRRNRQGDVGGTCGVVDDEPRPTGKAETEDEDEGTEGEDEGAQWSPQDPALQGVGQPTGTGSIRKKRFVSSHRYVETMLVADQSMAEFHGSGLKHYLLTLFSVAARLYKHPSIRNSVSLVVVKILVIHDEQKGPEVTSNAALTLRNFCNWQKQHNPPSDRDAEHYDTAILFTRQDLCGSQTCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDAKQCASLNGVNQDSHMMASMLSNLDHSQPWSPCSAYMITSFLDNGHGECLMDKPQNPIQLPGDLPGTSYDANRQCQFTFGEDSKHCPDAASTCSTLWCTGTSGGVLVCQTKHFPWADGTSCGEGKWCINGKCVNKTDRKHFDTPFHGSWGMWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNLEDCPDNNGKTFREEQCEAHNEFSKASFGSGPAVEWIPKYAGVSPKDRCKLICQAKGIGYFFVLQPKVVDGTPCSPDSTSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGGNGSTCKKISGSVTSAKPGYHDIITIPTGATNIEVKQRNQRGSRNNGSFLAIKAADGTYILNGDYTLSTLEQDIMYKGVVLRYSGSSAALERIRSFSPLKEPLTIQVLTVGNALRPKIKYTYFVKKKKESFNAIPTFSAWVIEEWGECSKSCELGWQRRLVECRDINGQPASECAKEVKPASTRPCADHPCPQWQLGEWSSCSKTCGKGYKKRSLKCLSHDGGVLSHESCDPLKKPKHFIDFCTMAECS
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Metalloprotease which cleaves aggrecan, a cartilage proteoglycan, at the '1938-Glu-|-Leu-1939' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover (By similarity). Also cleaves COMP (PubMed:39672391). Has angiogenic inhibitor activity (PubMed:10438512). May play a critical role in follicular rupture (By similarity). {ECO:0000250|UniProtKB:P97857, ECO:0000269|PubMed:10438512, ECO:0000269|PubMed:39672391}.
uniprot
proteins
mass_dalton
105358
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
10438512
uniprot
proteins
pubmed
10718198
uniprot
proteins
pubmed
10785405
uniprot
proteins
pubmed
10830953
uniprot
proteins
pubmed
17897672
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
39672391
uniprot
proteins
sequence_length
967
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
uniprot
proteins