dbPTM

ESPL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ESPL1_HUMAN
UniProt AC	Q14674
Protein Name	Separin
Gene Name	ESPL1
Organism	Homo sapiens (Human).
Sequence Length	2120
Subcellular Localization	Cytoplasm. Nucleus.
Protein Description	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..
Protein Sequence	MRSFKRVNFGTLLSSQKEAEELLPALKEFLSNPPAGFPSSRSDAERRQACDAILRACNQQLTAKLACPRHLGSLLELAELACDGYLVSTPQRPPLYLERILFVLLRNAAAQGSPEATLRLAQPLHACLVQCSREAAPQDYEAVARGSFSLLWKGAEALLERRAAFAARLKALSFLVLLEDESTPCEVPHFASPTACRAVAAHQLFDASGHGLNEADADFLDDLLSRHVIRALVGERGSSSGLLSPQRALCLLELTLEHCRRFCWSRHHDKAISAVEKAHSYLRNTNLAPSLQLCQLGVKLLQVGEEGPQAVAKLLIKASAVLSKSMEAPSPPLRALYESCQFFLSGLERGTKRRYRLDAILSLFAFLGGYCSLLQQLRDDGVYGGSSKQQQSFLQMYFQGLHLYTVVVYDFAQGCQIVDLADLTQLVDSCKSTVVWMLEALEGLSGQELTDHMGMTASYTSNLAYSFYSHKLYAEACAISEPLCQHLGLVKPGTYPEVPPEKLHRCFRLQVESLKKLGKQAQGCKMVILWLAALQPCSPEHMAEPVTFWVRVKMDAARAGDKELQLKTLRDSLSGWDPETLALLLREELQAYKAVRADTGQERFNIICDLLELSPEETPAGAWARATHLVELAQVLCYHDFTQQTNCSALDAIREALQLLDSVRPEAQARDQLLDDKAQALLWLYICTLEAKMQEGIERDRRAQAPGNLEEFEVNDLNYEDKLQEDRFLYSNIAFNLAADAAQSKCLDQALALWKELLTKGQAPAVRCLQQTAASLQILAALYQLVAKPMQALEVLLLLRIVSERLKDHSKAAGSSCHITQLLLTLGCPSYAQLHLEEAASSLKHLDQTTDTYLLLSLTCDLLRSQLYWTHQKVTKGVSLLLSVLRDPALQKSSKAWYLLRVQVLQLVAAYLSLPSNNLSHSLWEQLCAQGWQTPEIALIDSHKLLRSIILLLMGSDILSTQKAAVETSFLDYGENLVQKWQVLSEVLSCSEKLVCHLGRLGSVSEAKAFCLEALKLTTKLQIPRQCALFLVLKGELELARNDIDLCQSDLQQVLFLLESCTEFGGVTQHLDSVKKVHLQKGKQQAQVPCPPQLPEEELFLRGPALELVATVAKEPGPIAPSTNSSPVLKTKPQPIPNFLSHSPTCDCSLCASPVLTAVCLRWVLVTAGVRLAMGHQAQGLDLLQVVLKGCPEAAERLTQALQASLNHKTPPSLVPSLLDEILAQAYTLLALEGLNQPSNESLQKVLQSGLKFVAARIPHLEPWRASLLLIWALTKLGGLSCCTTQLFASSWGWQPPLIKSVPGSEPSKTQGQKRSGRGRQKLASAPLRLNNTSQKGLEGRGLPCTPKPPDRIRQAGPHVPFTVFEEVCPTESKPEVPQAPRVQQRVQTRLKVNFSDDSDLEDPVSAEAWLAEEPKRRGTASRGRGRARKGLSLKTDAVVAPGSAPGNPGLNGRSRRAKKVASRHCEERRPQRASDQARPGPEIMRTIPEEELTDNWRKMSFEILRGSDGEDSASGGKTPAPGPEAASGEWELLRLDSSKKKLPSPCPDKESDKDLGPRLRLPSAPVATGLSTLDSICDSLSVAFRGISHCPPSGLYAHLCRFLALCLGHRDPYATAFLVTESVSITCRHQLLTHLHRQLSKAQKHRGSLEIADQLQGLSLQEMPGDVPLARIQRLFSFRALESGHFPQPEKESFQERLALIPSGVTVCVLALATLQPGTVGNTLLLTRLEKDSPPVSVQIPTGQNKLHLRSVLNEFDAIQKAQKENSSCTDKREWWTGRLALDHRMEVLIASLEKSVLGCWKGLLLPSSEEPGPAQEASRLQELLQDCGWKYPDRTLLKIMLSGAGALTPQDIQALAYGLCPTQPERAQELLNEAVGRLQGLTVPSNSHLVLVLDKDLQKLPWESMPSLQALPVTRLPSFRFLLSYSIIKEYGASPVLSQGVDPRSTFYVLNPHNNLSSTEEQFRANFSSEAGWRGVVGEVPRPEQVQEALTKHDLYIYAGHGAGARFLDGQAVLRLSCRAVALLFGCSSAALAVRGNLEGAGIVLKYIMAGCPLFLGNLWDVTDRDIDRYTEALLQGWLGAGPGAPLLYYVNQARQAPRLKYLIGAAPIAYGLPVSLR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MRSFKRVNFG -----CCCCCCCCHH	47.15	-
27	Ubiquitination	EELLPALKEFLSNPP HHHHHHHHHHHHCCC	48.83	-
64	Ubiquitination	CNQQLTAKLACPRHL HHHHHHHHHHCCHHH	31.23	21963094
140	Phosphorylation	REAAPQDYEAVARGS CCCCCCCHHHHHHCC	10.67	27642862
153	Ubiquitination	GSFSLLWKGAEALLE CCHHHHHHHHHHHHH	48.49	-
244	Phosphorylation	GSSSGLLSPQRALCL CCCCCCCCHHHHHHH	24.83	24719451
268	Ubiquitination	RFCWSRHHDKAISAV HHHHHHHHHHHHHHH	36.84	21963094
277	Ubiquitination	KAISAVEKAHSYLRN HHHHHHHHHHHHHHC	44.81	29967540
299	Ubiquitination	QLCQLGVKLLQVGEE HHHHHCCEEEECCCC	41.50	-
313	Ubiquitination	EGPQAVAKLLIKASA CCHHHHHHHHHHHHH	36.91	29967540
324	Ubiquitination	KASAVLSKSMEAPSP HHHHHHHHCCCCCCH	50.05	-
325	Phosphorylation	ASAVLSKSMEAPSPP HHHHHHHCCCCCCHH	20.62	29116813
326	Oxidation	SAVLSKSMEAPSPPL HHHHHHCCCCCCHHH	6.14	17322306
330	Phosphorylation	SKSMEAPSPPLRALY HHCCCCCCHHHHHHH	46.31	23663014
337	Phosphorylation	SPPLRALYESCQFFL CHHHHHHHHHHHHHH	12.57	23663014
339	Phosphorylation	PLRALYESCQFFLSG HHHHHHHHHHHHHHC	10.32	23663014
345	Phosphorylation	ESCQFFLSGLERGTK HHHHHHHHCCCCCCC	35.85	23663014
397	Ubiquitination	QQSFLQMYFQGLHLY HHHHHHHHHCCCCEE	4.64	21963094
397 (in isoform 2)	Ubiquitination	-	4.64	21906983
430	Ubiquitination	LTQLVDSCKSTVVWM HHHHHHHHHHHHHHH	3.32	22817900
435	Ubiquitination	DSCKSTVVWMLEALE HHHHHHHHHHHHHHC	2.23	21963094
491	Ubiquitination	CQHLGLVKPGTYPEV HHHHCCCCCCCCCCC	42.65	29967540
515	Ubiquitination	RLQVESLKKLGKQAQ HHHHHHHHHHHHHHH	56.05	-
562	Acetylation	DAARAGDKELQLKTL HHHHHCCHHHHHHHH	60.45	7462073
562	Ubiquitination	DAARAGDKELQLKTL HHHHHCCHHHHHHHH	60.45	29967540
567	Ubiquitination	GDKELQLKTLRDSLS CCHHHHHHHHHHHHC	32.33	29967540
592	Phosphorylation	LREELQAYKAVRADT HHHHHHHHHHHHCCC	6.11	23403867
593	Ubiquitination	REELQAYKAVRADTG HHHHHHHHHHHCCCC	43.34	21963094
599	Phosphorylation	YKAVRADTGQERFNI HHHHHCCCCCHHHHH	39.52	23403867
683	Ubiquitination	DKAQALLWLYICTLE HHHHHHHHHHHHHHH	6.48	21963094
695	Ubiquitination	TLEAKMQEGIERDRR HHHHHHHHHHHHHHH	59.65	27667366
719	Phosphorylation	FEVNDLNYEDKLQED EEECCCCHHHHHHHC	32.57	29978859
722	Ubiquitination	NDLNYEDKLQEDRFL CCCCHHHHHHHCHHH	39.88	21906983
722 (in isoform 1)	Ubiquitination	-	39.88	21906983
755	Ubiquitination	DQALALWKELLTKGQ HHHHHHHHHHHHCCC	39.06	22817900
760	Ubiquitination	LWKELLTKGQAPAVR HHHHHHHCCCCCHHH	49.33	21963094
810	Phosphorylation	SERLKDHSKAAGSSC HHHHHHHHHHCCCCC	33.84	-
875	Phosphorylation	YWTHQKVTKGVSLLL CCHHHHHHHHHHHHH	29.17	22468782
879	Phosphorylation	QKVTKGVSLLLSVLR HHHHHHHHHHHHHHC	23.20	22468782
883	Phosphorylation	KGVSLLLSVLRDPAL HHHHHHHHHHCCHHH	21.05	24719451
973	Phosphorylation	VETSFLDYGENLVQK HHHHHHCHHHHHHHH	28.61	30576142
1008	Ubiquitination	LGSVSEAKAFCLEAL CCCHHHHHHHHHHHH	37.63	21963094
1016	Ubiquitination	AFCLEALKLTTKLQI HHHHHHHHHHCCCCC	51.33	29967540
1020	Ubiquitination	EALKLTTKLQIPRQC HHHHHHCCCCCHHHH	32.91	27667366
1073	Phosphorylation	GVTQHLDSVKKVHLQ CHHHHHHHCCEEECC	42.04	22817900
1083	Ubiquitination	KVHLQKGKQQAQVPC EEECCCCCCCCCCCC	46.39	-
1111	Phosphorylation	PALELVATVAKEPGP HHHHHHHHHCCCCCC	17.33	24732914
1122	Phosphorylation	EPGPIAPSTNSSPVL CCCCCCCCCCCCCCC	31.06	30266825
1123	Phosphorylation	PGPIAPSTNSSPVLK CCCCCCCCCCCCCCC	37.75	30266825
1125	Phosphorylation	PIAPSTNSSPVLKTK CCCCCCCCCCCCCCC	35.79	30266825
1126	Phosphorylation	IAPSTNSSPVLKTKP CCCCCCCCCCCCCCC	22.54	30266825
1131	Phosphorylation	NSSPVLKTKPQPIPN CCCCCCCCCCCCCCC	43.74	26074081
1153	Phosphorylation	CDCSLCASPVLTAVC CCCHHCCCHHHHHHH	17.97	-
1189	Ubiquitination	DLLQVVLKGCPEAAE CHHHHHHCCCHHHHH	47.02	-
1210	Phosphorylation	QASLNHKTPPSLVPS HHHHCCCCCCCHHHH	32.64	-
1252	Ubiquitination	KVLQSGLKFVAARIP HHHHHCHHHHHHCCC	41.12	-
1301	Phosphorylation	WQPPLIKSVPGSEPS CCCCCEECCCCCCCC	26.93	23927012
1305	Phosphorylation	LIKSVPGSEPSKTQG CEECCCCCCCCCCCC	40.02	23927012
1308	Phosphorylation	SVPGSEPSKTQGQKR CCCCCCCCCCCCCCC	44.26	23927012
1309	Ubiquitination	VPGSEPSKTQGQKRS CCCCCCCCCCCCCCC	56.43	29967540
1316	Phosphorylation	KTQGQKRSGRGRQKL CCCCCCCCCCCHHHH	39.62	-
1322	Ubiquitination	RSGRGRQKLASAPLR CCCCCHHHHHCCCCC	44.66	29967540
1322	Acetylation	RSGRGRQKLASAPLR CCCCCHHHHHCCCCC	44.66	26822725
1325	Phosphorylation	RGRQKLASAPLRLNN CCHHHHHCCCCCCCC	40.64	-
1336	Ubiquitination	RLNNTSQKGLEGRGL CCCCCCCCCCCCCCC	66.29	-
1341	Methylation	SQKGLEGRGLPCTPK CCCCCCCCCCCCCCC	33.81	115916445
1346	Phosphorylation	EGRGLPCTPKPPDRI CCCCCCCCCCCCHHH	32.19	26074081
1363	Phosphorylation	AGPHVPFTVFEEVCP CCCCCCCEEEECCCC	20.44	22817900
1396	Phosphorylation	TRLKVNFSDDSDLED HHEECCCCCCCCCCC	34.99	30175587
1399	Phosphorylation	KVNFSDDSDLEDPVS ECCCCCCCCCCCCCC	49.43	30175587
1406	Phosphorylation	SDLEDPVSAEAWLAE CCCCCCCCHHHHHHC	26.27	30175587
1407 (in isoform 2)	Ubiquitination	-	15.68	21906983
1433	Phosphorylation	GRARKGLSLKTDAVV CCCCCCCCCCCCEEE	36.17	24719451
1444	Phosphorylation	DAVVAPGSAPGNPGL CEEECCCCCCCCCCC	30.17	28555341
1455	Phosphorylation	NPGLNGRSRRAKKVA CCCCCCHHHHHHHHH	27.76	-
1475	Phosphorylation	ERRPQRASDQARPGP HHCCHHHHHCCCCCH	32.23	25159151
1478	Ubiquitination	PQRASDQARPGPEIM CHHHHHCCCCCHHHH	25.32	21963094
1485	Sulfoxidation	ARPGPEIMRTIPEEE CCCCHHHHHCCCHHH	2.70	21406390
1501	Phosphorylation	TDNWRKMSFEILRGS CCCHHHCCEEEHHCC	23.82	23927012
1507	Ubiquitination	MSFEILRGSDGEDSA CCEEEHHCCCCCCCC	27.00	21963094
1508	Phosphorylation	SFEILRGSDGEDSAS CEEEHHCCCCCCCCC	35.69	30266825
1513	Phosphorylation	RGSDGEDSASGGKTP HCCCCCCCCCCCCCC	21.74	30266825
1515	Phosphorylation	SDGEDSASGGKTPAP CCCCCCCCCCCCCCC	52.62	23927012
1518	Ubiquitination	EDSASGGKTPAPGPE CCCCCCCCCCCCCCC	55.66	29967540
1519	Phosphorylation	DSASGGKTPAPGPEA CCCCCCCCCCCCCCC	28.14	21815630
1528	Phosphorylation	APGPEAASGEWELLR CCCCCCCCCCEEEEE	44.27	22199227
1538	Phosphorylation	WELLRLDSSKKKLPS EEEEEECCCCCCCCC	48.96	22199227
1539	Phosphorylation	ELLRLDSSKKKLPSP EEEEECCCCCCCCCC	48.43	22199227
1541	Ubiquitination	LRLDSSKKKLPSPCP EEECCCCCCCCCCCC	62.58	29967540
1542	Ubiquitination	RLDSSKKKLPSPCPD EECCCCCCCCCCCCC	70.17	29967540
1545	Phosphorylation	SSKKKLPSPCPDKES CCCCCCCCCCCCCCC	49.96	25159151
1552	Phosphorylation	SPCPDKESDKDLGPR CCCCCCCCCCCCCCC	56.55	22817900
1576 (in isoform 2)	Ubiquitination	-	28.38	21906983
1614	Phosphorylation	CLGHRDPYATAFLVT HHCCCCCCCCEEEEE	22.37	-
1641	Phosphorylation	THLHRQLSKAQKHRG HHHHHHHHHHHHHCC	20.01	24702127
1649	Phosphorylation	KAQKHRGSLEIADQL HHHHHCCHHHHHHHH	23.84	21712546
1660	Phosphorylation	ADQLQGLSLQEMPGD HHHHCCCCHHCCCCC	34.53	-
1678	Phosphorylation	ARIQRLFSFRALESG HHHHHHHHHHHHHCC	20.58	24719451
1692	Ubiquitination	GHFPQPEKESFQERL CCCCCCCCCCHHHHH	66.40	-
1732	Ubiquitination	LLLTRLEKDSPPVSV EEEEECCCCCCCEEE	69.01	21906983
1732 (in isoform 1)	Ubiquitination	-	69.01	21906983
1747	Ubiquitination	QIPTGQNKLHLRSVL ECCCCCCHHHHHHHH	29.42	29967540
1752	Phosphorylation	QNKLHLRSVLNEFDA CCHHHHHHHHHHHHH	37.00	-
1762	Ubiquitination	NEFDAIQKAQKENSS HHHHHHHHHHHHCCC	46.82	29967540
1768	Phosphorylation	QKAQKENSSCTDKRE HHHHHHCCCCCCCHH	28.07	-
1769	Phosphorylation	KAQKENSSCTDKREW HHHHHCCCCCCCHHH	32.39	-
1771	Phosphorylation	QKENSSCTDKREWWT HHHCCCCCCCHHHHH	46.64	-
1796	Ubiquitination	VLIASLEKSVLGCWK HHHHHHHHHHHHHHC	51.67	-
1803	Ubiquitination	KSVLGCWKGLLLPSS HHHHHHHCCCCCCCC	43.70	21963094
1820	Phosphorylation	PGPAQEASRLQELLQ CCHHHHHHHHHHHHH	32.54	-
1832	Ubiquitination	LLQDCGWKYPDRTLL HHHHCCCCCCCHHHH	31.99	21963094
1884	Phosphorylation	VGRLQGLTVPSNSHL HHHHCCCCCCCCCEE	36.88	20860994
1887	Phosphorylation	LQGLTVPSNSHLVLV HCCCCCCCCCEEEEE	46.78	20860994
1889	Phosphorylation	GLTVPSNSHLVLVLD CCCCCCCCEEEEEEC	23.64	20860994
1901	Ubiquitination	VLDKDLQKLPWESMP EECCCHHHCCHHHCC	64.91	2190698
1901 (in isoform 1)	Ubiquitination	-	64.91	21906983
1928	Phosphorylation	FRFLLSYSIIKEYGA HHHHHHHHHHHHHCC	17.92	24719451
1994	Ubiquitination	QVQEALTKHDLYIYA HHHHHHHHCCCEEEE	35.65	-
1998	Phosphorylation	ALTKHDLYIYAGHGA HHHHCCCEEEECCCC	9.65	29496907
2000	Phosphorylation	TKHDLYIYAGHGAGA HHCCCEEEECCCCCC	7.93	29496907
2103	Ubiquitination	ARQAPRLKYLIGAAP CCCCCCHHHHHCCCC	39.01	-
2104	Phosphorylation	RQAPRLKYLIGAAPI CCCCCHHHHHCCCCC	14.24	-
2118	Phosphorylation	IAYGLPVSLR----- CCCCCCCCCC-----	19.25	-

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
1126	S	Phosphorylation	Kinase	CDK1	P06493	PSP
1126	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
1363	T	Phosphorylation	Kinase	PLK1	P53350	PSP
1399	S	Phosphorylation	Kinase	PLK1	P53350	PSP
1501	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
1501	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
1660	S	Phosphorylation	Kinase	ATM	Q13315	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1126	S	Phosphorylation		11747808
Among them, Ser-1126 phosphorylation is the major site, which conducts to the enzyme inactivation.

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of ESPL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTTG1_HUMAN	PTTG1	physical	24781523
PP2AA_HUMAN	PPP2CA	physical	24781523
2AAA_HUMAN	PPP2R1A	physical	24781523
2A5A_HUMAN	PPP2R5A	physical	24781523
CCNB1_HUMAN	CCNB1	physical	25750436
PTTG1_HUMAN	PTTG1	physical	25750436

Drug and Disease Associations

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

Regulatory Network of ESPL1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1396 AND SER-1399, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1126, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1396; SER-1399 ANDSER-1508, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1508, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Dual inhibition of sister chromatid separation at metaphase."; Stemmann O., Zou H., Gerber S.A., Gygi S.P., Kirschner M.W.; Cell 107:715-726(2001). Cited for: PROTEIN SEQUENCE OF 1117-1130, ENZYME REGULATION, AND PHOSPHORYLATIONAT SER-1126.	11747808 [Abstract]

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