ESPL1
entrez
9700
canonical
uniprot
Q14674
canonical
ensembl
ENSG00000135476
resolver
ensp
ENSP00000257934
resolver
ensp
ENSP00000753241
resolver
genesymbol
ESPL1
resolver
genesymbol_syn
ESP1
resolver
genesymbol_syn
KIAA0165
resolver
hgnc
HGNC:16856
resolver
uniprot_entry
ESPL1_HUMAN
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by at least two independent mechanisms. First, it is inactivated via its interaction with securin/PTTG1, which probably covers its active site. The association with PTTG1 is not only inhibitory, since PTTG1 is also required for activating it, the enzyme being inactive in cells in which PTTG1 is absent. PTTG1 degradation at anaphase, liberates it and triggers RAD21 cleavage. Second, phosphorylation at Ser-1126 inactivates it. The complete phosphorylation during mitosis, is removed when cells undergo anaphase. Activation of the enzyme at the metaphase-anaphase transition probably requires the removal of both securin and inhibitory phosphate. {ECO:0000269|PubMed:11747808, ECO:0000269|PubMed:12194817, ECO:0000269|PubMed:12297314}.
uniprot
proteins
amino_acid_sequence
MRSFKRVNFGTLLSSQKEAEELLPALKEFLSNPPAGFPSSRSDAERRQACDAILRACNQQLTAKLACPRHLGSLLELAELACDGYLVSTPQRPPLYLERILFVLLRNAAAQGSPEATLRLAQPLHACLVQCSREAAPQDYEAVARGSFSLLWKGAEALLERRAAFAARLKALSFLVLLEDESTPCEVPHFASPTACRAVAAHQLFDASGHGLNEADADFLDDLLSRHVIRALVGERGSSSGLLSPQRALCLLELTLEHCRRFCWSRHHDKAISAVEKAHSYLRNTNLAPSLQLCQLGVKLLQVGEEGPQAVAKLLIKASAVLSKSMEAPSPPLRALYESCQFFLSGLERGTKRRYRLDAILSLFAFLGGYCSLLQQLRDDGVYGGSSKQQQSFLQMYFQGLHLYTVVVYDFAQGCQIVDLADLTQLVDSCKSTVVWMLEALEGLSGQELTDHMGMTASYTSNLAYSFYSHKLYAEACAISEPLCQHLGLVKPGTYPEVPPEKLHRCFRLQVESLKKLGKQAQGCKMVILWLAALQPCSPEHMAEPVTFWVRVKMDAARAGDKELQLKTLRDSLSGWDPETLALLLREELQAYKAVRADTGQERFNIICDLLELSPEETPAGAWARATHLVELAQVLCYHDFTQQTNCSALDAIREALQLLDSVRPEAQARDQLLDDKAQALLWLYICTLEAKMQEGIERDRRAQAPGNLEEFEVNDLNYEDKLQEDRFLYSNIAFNLAADAAQSKCLDQALALWKELLTKGQAPAVRCLQQTAASLQILAALYQLVAKPMQALEVLLLLRIVSERLKDHSKAAGSSCHITQLLLTLGCPSYAQLHLEEAASSLKHLDQTTDTYLLLSLTCDLLRSQLYWTHQKVTKGVSLLLSVLRDPALQKSSKAWYLLRVQVLQLVAAYLSLPSNNLSHSLWEQLCAQGWQTPEIALIDSHKLLRSIILLLMGSDILSTQKAAVETSFLDYGENLVQKWQVLSEVLSCSEKLVCHLGRLGSVSEAKAFCLEALKLTTKLQIPRQCALFLVLKGELELARNDIDLCQSDLQQVLFLLESCTEFGGVTQHLDSVKKVHLQKGKQQAQVPCPPQLPEEELFLRGPALELVATVAKEPGPIAPSTNSSPVLKTKPQPIPNFLSHSPTCDCSLCASPVLTAVCLRWVLVTAGVRLAMGHQAQGLDLLQVVLKGCPEAAERLTQALQASLNHKTPPSLVPSLLDEILAQAYTLLALEGLNQPSNESLQKVLQSGLKFVAARIPHLEPWRASLLLIWALTKLGGLSCCTTQLFASSWGWQPPLIKSVPGSEPSKTQGQKRSGRGRQKLASAPLRLNNTSQKGLEGRGLPCTPKPPDRIRQAGPHVPFTVFEEVCPTESKPEVPQAPRVQQRVQTRLKVNFSDDSDLEDPVSAEAWLAEEPKRRGTASRGRGRARKGLSLKTDAVVAPGSAPGNPGLNGRSRRAKKVASRHCEERRPQRASDQARPGPEIMRTIPEEELTDNWRKMSFEILRGSDGEDSASGGKTPAPGPEAASGEWELLRLDSSKKKLPSPCPDKESDKDLGPRLRLPSAPVATGLSTLDSICDSLSVAFRGISHCPPSGLYAHLCRFLALCLGHRDPYATAFLVTESVSITCRHQLLTHLHRQLSKAQKHRGSLEIADQLQGLSLQEMPGDVPLARIQRLFSFRALESGHFPQPEKESFQERLALIPSGVTVCVLALATLQPGTVGNTLLLTRLEKDSPPVSVQIPTGQNKLHLRSVLNEFDAIQKAQKENSSCTDKREWWTGRLALDHRMEVLIASLEKSVLGCWKGLLLPSSEEPGPAQEASRLQELLQDCGWKYPDRTLLKIMLSGAGALTPQDIQALAYGLCPTQPERAQELLNEAVGRLQGLTVPSNSHLVLVLDKDLQKLPWESMPSLQALPVTRLPSFRFLLSYSIIKEYGASPVLSQGVDPRSTFYVLNPHNNLSSTEEQFRANFSSEAGWRGVVGEVPRPEQVQEALTKHDLYIYAGHGAGARFLDGQAVLRLSCRAVALLFGCSSAALAVRGNLEGAGIVLKYIMAGCPLFLGNLWDVTDRDIDRYTEALLQGWLGAGPGAPLLYYVNQARQAPRLKYLIGAAPIAYGLPVSLR
uniprot
proteins
ec_number
3.4.22.49
uniprot
proteins
function
FUNCTION: Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the SCC1/RAD21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by different mechanisms. {ECO:0000269|PubMed:10411507, ECO:0000269|PubMed:11509732}.
uniprot
proteins
mass_dalton
233175
uniprot
proteins
mutagenesis
MUTAGEN 1126; /note="S->A: Abolishes phosphorylation at this site, as well as the negative regulation due to phosphorylation."; MUTAGEN 1483..1486; /note="EIMR->RIME: Abolishes autocleavage; when associated with R-1178; E-1181; R-1207 and E-1210. Does not affect the protease function."; /evidence="ECO:0000269|PubMed:12194817"; MUTAGEN 1486; /note="R->A: Abolishes autocleavage; when associated with A-1181 and A-1210."; /evidence="ECO:0000269|PubMed:12297314"; MUTAGEN 1503..1506; /note="EILR->RILE: Does not affect autocleavage. Does not affect the protease function."; /evidence="ECO:0000269|PubMed:12194817"; MUTAGEN 1506; /note="R->A: Abolishes autocleavage; when associated with A-1161 and A-1210."; /evidence="ECO:0000269|PubMed:12297314"; MUTAGEN 1532..1535; /note="ELLR->RLLE: Strongly reduces autocleavage at this site, but enhances autocleavage at site 1. Does not affect the protease function."; /evidence="ECO:0000269|PubMed:12194817"; MUTAGEN 1535; /note="R->A: Abolishes autocleavage; when associated with A-1161 and A-1281."; /evidence="ECO:0000269|PubMed:12297314"; MUTAGEN 2029; /note="C->A: Abolishes protease activity."; /evidence="ECO:0000269|PubMed:12194817
uniprot
proteins
post_translational_modification
PTM: Autocleaves. This function, which is not essential for its protease activity, is unknown.; PTM: Phosphorylated by CDK1. There are 8 Ser/Thr phosphorylation sites. Among them, Ser-1126 phosphorylation is the major site, which conducts to the enzyme inactivation. {ECO:0000269|PubMed:11747808}.
uniprot
proteins
pubmed
10411507
uniprot
proteins
pubmed
11509732
uniprot
proteins
pubmed
11747808
uniprot
proteins
pubmed
12194817
uniprot
proteins
pubmed
12297314
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
8724849
uniprot
proteins
sequence_length
2120
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
uniprot
proteins