ESP1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ESP1_ARATH
• UniProt AC: Q5IBC5
• Protein Name: Separase
• Gene Name: ESP1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 2180
• Protein Description: Cleaves SYN1, releasing sister chromatid cohesion. Required for the release of cohesin at anaphase I and anaphase II, whereas the release of cohesin during diplotene and diakinesis occurs in a separase-independent process. Essential for embryo and endosperm development. May play a role in centromeric heterochromatin structure/formation during early meiosis, non-homologous centromere association and radial microtubule system (RMS) formation. May regulate the mitosis-specific cyclin CYCB1-1..
• Protein Sequence: MASSGDDLRLLSLIDVGDNVFSSFSDYLKPFSTLSTSRKKQDRATTIRALAKQFLPFLNKSISLLPKRLSVANSDKEARESALDLFRAYELCLDCLELVSAQLACKPHTVQSQRLRMIHCLDVWGLYENVYTEAFKVLEKLRGSDSKSRKSRLLPEVQDGDAEMALVVVDAVAAIFRAVAMSQQLDDKRYRKVLLLLEEVGGWLRVLDAKVYEKLHRAMVTSMGKCAVSLVREAERFNGDLVISFCDLTVKEHYKSALSKDRVYKFAREVLSVLFGFKDRKMSVTIDISMSVLRSLSCQFEDESNENLMEFFDLVDYCAHKFRAAGDMYCAKVSKKLNEMAAIFVEAIPQLNLVLRLYSTGLSITVCNSKLGEIKLEDSTDDWKIQAMFDDDARWQSLVSLLGMVDSYSGDEGNQTGSSSIGGHRNYNNKTHDSCKDRNKITCWPQYVDALKFLCQPLADFIYSVKRKIVLETEMSCASAHLITIHDAFLQFCDGCLFLQRCTSDKGDREIANNKAFLNAAMGAFIVSLRTQLKLEISAHLVEDVIGSPWIQSQELKYLIATLYNIGIVLYRNKELNKACEALKLCSKVSWRCVELHCHMFVNQSSSSDNDLSEDAIMDFVGEACNRCAFYLDILQKCSRRKIRQNIVHILENWLSAEHLIRRLPGPEAIVKQWVKIERECHTDLDAAGSCTTLYSLLSSSQKKSKRGIGKILEQELLAYDRVLPLRSNLGQQTRIKIADILLKDVYVTEDMHIERARILIWKARMTRTSGTEHITECICFLSEAISILGELHHGPNEEGSPSSHMLPIAYCLRAFCTQEADPNSKKVFQDISTSLNLWLRILSLDDSGDSLPTENIIPLLYNMIDLMSVKGCTELHHHIYQLIFRLFKWKNVKLEVCLAMLWECRRLSHALCPSPISDAFIQTLSENCADKSTCIDFWMDCLKDSKAKLIGFQQNFHDLHNKDEGPFQSDITIDDIKDAASELISSASLSGNSSFAAAYLYYDLCERLISFGKLSEALSYAKEAYRIRTLIFQDKFKYTAEKHIEKHNEDGKISEIRTFSIKNFQVYRLLATDFWPCGNFLWDINRCYLSPWSVLQCYLESTLQVGILNELIGNGLEAETILSWGKAFSCSQSLFPFVVAFSSALGNLYHKKQCLDLAEKELQNAKEILIANQRDFSCVKCKLKLEVTLDKQLGDISRKQIDRVSQTDGFLHAESLFSAALGKFCCSAWKSCIRSHGEEIAEEIVIDRNGGEGLGHNSSKTKLSIKEPPGNRGSRRGGRANKTCLSKDQDLISEPTSRLTRSMRHSLREQCQNRSNVPEVVSKKPNLCDRSVGSRGERVLLDTSNALPGFCICYKEKRQQCLSEEVTESGSLNNLVSLKWELCHRKLASSILVSLGKCLGDSGRIHLAHEALLHSISVLFKSTWSSHNQPSVSQLLEFIGKEVTRDVFAVDRAIILYNLCWLNLRNYHCRKSRSICCDLFHIPFTKLVSWLMLAFVLSGEVPILFQKVSRLLASLYLLSSSNSEFTFESDGNELSASHWVSFFHQASLGTHLSYHFISNLSQKHKSQCLSDKECTEATCSSCMVPEDLDLPRLAPDRTQDLVQFAKEFFINLPSSTIICISLLGGALNQLLQELMHIRSPVCAWVLISRLNPESQPVATLLPVDSIVEDMSDDSANLSSTEATQVKSLKGPWLCPWGTTVVDEVAPAFKSILEESHSSSSTTEEDTIESRGLWWKKRKKLNHRLGIFLRNLEASWLGPWRCLLLGEWSNYKLPDSAQKKLVNDLKSKCKMEVNEMLLKVILGGGTDNFKGEACVAQLSLRNGCYVGRGGYLYEEDSCKTPTAASNISESRHELALKLIHDAASKLGQQDGHENREPIILVLDPEVQMLPWENIPILRKQEVYRMPSVGCISAVLKKRSLQGEPAKSHVASFPLIDPLDSFYLLNPGGDLTDTQVTFESWFRDQNFEGKAGSEPSAIELTEALETHDLFLYFGHGSGAQYIPRREIEKLDNCSATFLMGCSSGSLWLKGCYIPQGVPLSYLLGGSPAIVATLWDVTDRDIDRFGKALLEAWLQERSDSSSEGGCSQCESLANDLAAMTLKGTKRSRKPSSRNKPAQSDVDGSGKIECNHKHRRKIGSFIAAARDACNLQYLIGAAPVCYGVPTGITRKKGIDALLPSSSR

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
45	Phosphorylation	RKKQDRATTIRALAK CCHHHHHHHHHHHHH		24894044
46	Phosphorylation	KKQDRATTIRALAKQ CHHHHHHHHHHHHHH		24894044
363	Phosphorylation	RLYSTGLSITVCNSK HHHHCCCEEEEECCC		28011693
365	Phosphorylation	YSTGLSITVCNSKLG HHCCCEEEEECCCCC		28011693
1395	Phosphorylation	LASSILVSLGKCLGD HHHHHHHHHHHHHCC		24894044

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ESP1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ESP1_ARATH !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ESP1_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of ESP1_ARATH !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.