Espl1
entrez
105988
canonical
uniprot
P60330
canonical
ensembl
ENSMUSG00000058290
resolver
ensp
ENSMUSP00000064465
resolver
ensp
ENSMUSP00000155304
resolver
ensp
ENSMUSP00000232002
resolver
enst
ENSMUST00000064924
resolver
enst
ENSMUST00000229050
resolver
genesymbol
Espl1
resolver
genesymbol_syn
Esp1
resolver
genesymbol_syn
Kiaa0165
resolver
uniprot
A6H6E3
resolver
uniprot_entry
ESPL1_MOUSE
resolver
uniprot_sec
A6H6E3
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-1121 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 (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MRNFKGVNFATLLCSKEETQQLLPDLKEFLSRSRTDFPSSRTDAERRQICDTILRACTQQLTAKLDCPGHLRSILDLAELACDGYLLSTPQRPPLYLERILFILLRNGSTQGSPDTVLRLAQPLHACLVQNSGEAAPQDYEAVTRGSFSLFWKGAEALLERRAAFSTRLNALSFLVLLEDGSVPCEVPHFASPTACRLVAAYQLYDATGQGLDEADADFLYEVLSRHLIRVLVGEGGSSPGPLSPQRALCLLEITLEHCRRLCWNHHHRQAARAVERARNHLEKTSVAPSLQLCQMGVELLEAVEERPGAVAQLLRKAAAVLINSIEAPSPPLRALYDSCQFFLSGLERGIRRHCGLDAILSLFAFLGGYSSLVRHLREVSEASSKQQQCLLQMHFQGFHLFTGIVYDFAQGCQATELAQLVDGCRSAAVWMLEALEGLSGGELADYLSMTASYTSNLAYSFFSQKLYEEACVISEPVCQHLGSATSGACPEVPPEKLHRCFRLHVESLKKLGKQAQGCKMVTLWLAALKPYSLEHMVEPVTFWVRVKMDASRAGDKELQLQTLRDSLSCWDPETQSLLLREELRAYKSVRADTGQERFNIICDLLELSPEETAAGAWARATYLVELAQVLCYHNFTQQTNCSALDAVQEALQLLESVSPEAQEQDRLLDDKAQALLWLYICTLEAKMQEGIERDRRAQAPSNLEEFEVNDLNYEDKLQEDRFLYSSIAFNLAADAAQSKCLDQALTLWKEVLTKGRAPAVRCLQQTAASLQILAAVYQLVAKPLQALETLLLLQIVSKRLQDHAKAASSSCQLTQLLLNLGCPSYAQLYLEEAESSLRSLDQTSDACQLLSLTCALLGSQLCWACQKVTAGVSLLLSVLRDPALQKSSKAWYLLRVQALQVLAFYLSLSSNLLSSALREQLWDQGWQTPETALIDAHKLLRSIIILLMGSDVLSIQKAATESPFLDYGENLVQKWQVLTEVLTCSERLVGRLGRLGNVSEAKAFCLEALKLTTKLQIPRQCALFLVLKGELELARGDIDLCQSDLQQVLFLLESSTEFGVVTQHPDSVKKVHTQKGKHKAQGPCFPPLSEEEPFLKGPALELVDTVLNEPGPIQSSVNSSPVLKTKPPPNPGFLSHLPSCDCLLCASPALSAVCLRWVLVTAGVRLATGHKAQGLDLLQAVLTRCPAATKRFTQSLQASLNHRTTPSCVPSLFDEIMAQVYTHLALEFLNQTSEKSLGKVLASGLKFVATRIQSLEIWRAHLLLVQALAKLAHFSCCTSELFASSWGWHPPLVKSLPVLEPAKIRRQKCSGRGRRRIASVPPPLHNSSQKGLEEEGPPCTPKPPGRARQAGPRVPFTIFEEVHPTKSKLQVPLAPRVHRRAQTRLKVIFSDDSDLEDLVSADTQLVEEPKRRGTASRTRGQTRKGRSLKTDAVVAIESTPGHSSVSGRTRRARKVASRNCEEESPKAPLCVWASQGPEIMRSIPEEEPVDNHLEKSFEILRGSDGEDSASGEKAAAADTGLPVGECEVLRRDSSKAERPVLYSDTEANSDPSPWLPPFSVPAPIDLSTLDSISDSLSIAFRGVSHCPPSGLYAHLCRFLALCLGHRDPYATAFLVAESISITCRHQLLTHLHRQLSKAQKQQESPELAEHLQRLDLKERPGGVPLARIQRLFSFKALGSGCFPQAEKESFQERLALIPSGVTVCVLALATLQPGTLSNTLLLTRLEKDNPPITVKIPTAQNKLPLSAVLKEFDAIQKDQKENSSCTEKRVWWTGRLALDQRMEALITALEEQVLGCWRGLLLPCSADPSLAQEASKLQELLRECGWEYPDSTLLKVILSGARILTSQDVQALACGLCPAQPDRAQVLLSEAVGQVQSQEAPRSQHLVLVLDKDLQKLPWESTPILQAQPVTRLPSFRFLLSYTVTKEAGASSVLSQGVDPQNTFYVLNPHSNLSSTEERFRASFSSETGWKGVIGEVPSLDQVQAALTERDLYIYAGHGAGARFLDGQAVLRLSCRAVALLFGCSSAALAVHGNLEGAGIVLKYIMAGCPLFLGNLWDVTDRDIDRYTEALLQGWLGAGPGAPFLYYASQARQAPRLKYLIGAAPVAYGLPISLQTP
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 (By similarity). {ECO:0000250}.
uniprot
proteins
mass_dalton
233035
uniprot
proteins
post_translational_modification
PTM: Autocleaves. This function, which is not essential for its protease activity, is unknown (By similarity). {ECO:0000250}.; PTM: Phosphorylated by CDK1. There is 8 Ser/Thr phosphorylation sites. Among them, only Ser-1121 phosphorylation is the major site, which conducts to the enzyme inactivation (By similarity). {ECO:0000250}.
uniprot
proteins
pubmed
14621295
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
2118
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
uniprot
proteins