dbPTM

ESCO1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ESCO1_HUMAN
UniProt AC	Q5FWF5
Protein Name	N-acetyltransferase ESCO1
Gene Name	ESCO1
Organism	Homo sapiens (Human).
Sequence Length	840
Subcellular Localization	Nucleus . Chromosome . Nuclear at interphase, associated with chromosomes during mitosis.
Protein Description	Acetyltransferase required for the establishment of sister chromatid cohesion. [PubMed: 15958495]
Protein Sequence	MMSIQEKSKENSSKVTKKSDDKNSETEIQDSQKNLAKKSGPKETIKSQAKSSSESKINQPELETRMSTRSSKAASNDKATKSINKNTVTVRGYSQESTKKKLSQKKLVHENPKANEQLNRRSQRLQQLTEVSRRSLRSREIQGQVQAVKQSLPPTKKEQCSSTQSKSNKTSQKHVKRKVLEVKSDSKEDENLVINEVINSPKGKKRKVEHQTACACSSQCTQGSEKCPQKTTRRDETKPVPVTSEVKRSKMATSVVPKKNEMKKSVHTQVNTNTTLPKSPQPSVPEQSDNELEQAGKSKRGSILQLCEEIAGEIESDNVEVKKESSQMESVKEEKPTEIKLEETSVERQILHQKETNQDVQCNRFFPSRKTKPVKCILNGINSSAKKNSNWTKIKLSKFNSVQHNKLDSQVSPKLGLLRTSFSPPALEMHHPVTQSTFLGTKLHDRNITCQQEKMKEINSEEVKINDITVEINKTTERAPENCHLANEIKPSDPPLDNQMKHSFDSASNKNFSQCLESKLENSPVENVTAASTLLSQAKIDTGENKFPGSAPQQHSILSNQTSKSSDNRETPRNHSLPKCNSHLEITIPKDLKLKEAEKTDEKQLIIDAGQKRFGAVSCNVCGMLYTASNPEDETQHLLFHNQFISAVKYVGWKKERILAEYPDGRIIMVLPEDPKYALKKVDEIREMVDNDLGFQQAPLMCYSRTKTLLFISNDKKVVGCLIAEHIQWGYRVIEEKLPVIRSEEEKVRFERQKAWCCSTLPEPAICGISRIWVFSMMRRKKIASRMIECLRSNFIYGSYLSKEEIAFSDPTPDGKLFATQYCGTGQFLVYNFINGQNST

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MMSIQEKSKE -----CCCHHHHCCC	21.59	23401153
8	Phosphorylation	MMSIQEKSKENSSKV CCCHHHHCCCCCCCC	44.44	23401153
9	Acetylation	MSIQEKSKENSSKVT CCHHHHCCCCCCCCC	72.48	7695277
17	Acetylation	ENSSKVTKKSDDKNS CCCCCCCCCCCCCCC	53.95	7695287
24	Phosphorylation	KKSDDKNSETEIQDS CCCCCCCCHHHHHHH	52.19	25159151
26	Phosphorylation	SDDKNSETEIQDSQK CCCCCCHHHHHHHHH	37.90	28985074
31	Phosphorylation	SETEIQDSQKNLAKK CHHHHHHHHHHHHHH	27.03	17525332
33	Acetylation	TEIQDSQKNLAKKSG HHHHHHHHHHHHHHC	58.86	26051181
53	Phosphorylation	KSQAKSSSESKINQP HHHHHCCCCCCCCCH	53.64	22468782
55	Phosphorylation	QAKSSSESKINQPEL HHHCCCCCCCCCHHH	40.56	22468782
55	O-linked_Glycosylation	QAKSSSESKINQPEL HHHCCCCCCCCCHHH	40.56	30379171
56	Ubiquitination	AKSSSESKINQPELE HHCCCCCCCCCHHHH	41.44	-
68	Phosphorylation	ELETRMSTRSSKAAS HHHHHHHHHCHHHHC	25.81	-
70	Phosphorylation	ETRMSTRSSKAASND HHHHHHHCHHHHCCC	35.96	-
71	Phosphorylation	TRMSTRSSKAASNDK HHHHHHCHHHHCCCC	24.03	22210691
75	Phosphorylation	TRSSKAASNDKATKS HHCHHHHCCCCCCHH	50.88	22210691
89	Phosphorylation	SINKNTVTVRGYSQE HHCCCCEEEEEECHH	11.49	-
135	Phosphorylation	LTEVSRRSLRSREIQ HHHHHHHHHHHHHHH	27.33	20068231
138	Phosphorylation	VSRRSLRSREIQGQV HHHHHHHHHHHHHHH	39.29	20068231
151	Phosphorylation	QVQAVKQSLPPTKKE HHHHHHHCCCCCCHH	36.81	18452278
161	Phosphorylation	PTKKEQCSSTQSKSN CCCHHHCCCCCCCCC	35.79	25627689
162	Phosphorylation	TKKEQCSSTQSKSNK CCHHHCCCCCCCCCH	37.78	25627689
163	Phosphorylation	KKEQCSSTQSKSNKT CHHHCCCCCCCCCHH	22.14	25627689
165	Phosphorylation	EQCSSTQSKSNKTSQ HHCCCCCCCCCHHHH	37.83	25627689
170	O-linked_Glycosylation	TQSKSNKTSQKHVKR CCCCCCHHHHHHHHH	40.41	30379171
184	Phosphorylation	RKVLEVKSDSKEDEN HHEEEECCCCCCCCC	52.90	25072903
186	Phosphorylation	VLEVKSDSKEDENLV EEEECCCCCCCCCCH	45.06	25072903
200	Phosphorylation	VINEVINSPKGKKRK HHHHHHCCCCCCCCC	19.50	30266825
218	Phosphorylation	QTACACSSQCTQGSE CEECHHCHHCCCCCC	29.20	-
243	Phosphorylation	ETKPVPVTSEVKRSK CCCCCCCCHHHHHHH	17.07	28555341
265	Phosphorylation	KKNEMKKSVHTQVNT CCCCCCCCEEEEECC	17.39	22468782
268	Phosphorylation	EMKKSVHTQVNTNTT CCCCCEEEEECCCCC	31.86	29978859
268	O-linked_Glycosylation	EMKKSVHTQVNTNTT CCCCCEEEEECCCCC	31.86	30379171
272	Phosphorylation	SVHTQVNTNTTLPKS CEEEEECCCCCCCCC	34.78	29978859
274	Phosphorylation	HTQVNTNTTLPKSPQ EEEECCCCCCCCCCC	27.89	29978859
275	Phosphorylation	TQVNTNTTLPKSPQP EEECCCCCCCCCCCC	43.03	29978859
279	Phosphorylation	TNTTLPKSPQPSVPE CCCCCCCCCCCCCCC	27.16	30266825
283	Phosphorylation	LPKSPQPSVPEQSDN CCCCCCCCCCCCCHH	45.09	30266825
288	Phosphorylation	QPSVPEQSDNELEQA CCCCCCCCHHHHHHH	40.52	25262027
297	Acetylation	NELEQAGKSKRGSIL HHHHHHHHCCCHHHH	56.68	25953088
332	Sumoylation	SSQMESVKEEKPTEI HHHCCHHCCCCCCCC	70.23	25772364
344	Phosphorylation	TEIKLEETSVERQIL CCCCCCCHHHHHHHH	28.79	29449344
345	Phosphorylation	EIKLEETSVERQILH CCCCCCHHHHHHHHH	25.84	29449344
354	Ubiquitination	ERQILHQKETNQDVQ HHHHHHHHHCCCCCC	56.62	-
383	Phosphorylation	CILNGINSSAKKNSN EEECCCCCCCCCCCC	29.74	25627689
384	Phosphorylation	ILNGINSSAKKNSNW EECCCCCCCCCCCCC	39.35	28555341
393	Acetylation	KKNSNWTKIKLSKFN CCCCCCCEEEHHHCC	29.47	26051181
398	Ubiquitination	WTKIKLSKFNSVQHN CCEEEHHHCCCCCCC	60.03	-
406	Ubiquitination	FNSVQHNKLDSQVSP CCCCCCCCCCCCCCC	52.09	-
409	Phosphorylation	VQHNKLDSQVSPKLG CCCCCCCCCCCCCCC	42.81	20068231
412	Phosphorylation	NKLDSQVSPKLGLLR CCCCCCCCCCCCCCC	14.53	30278072
423	Phosphorylation	GLLRTSFSPPALEMH CCCCCCCCCCCCCCC	29.73	25159151
469	Phosphorylation	EVKINDITVEINKTT CEEECEEEEEEECCC	18.23	24114839
513	Phosphorylation	SASNKNFSQCLESKL HCCCCCHHHHHHHHH	29.40	26714015
523	Phosphorylation	LESKLENSPVENVTA HHHHHHCCCCCCHHH	22.43	29255136
529	Phosphorylation	NSPVENVTAASTLLS CCCCCCHHHHHHHHH	28.25	29978859
546	Acetylation	KIDTGENKFPGSAPQ CCCCCCCCCCCCCHH	48.94	26051181
582	Phosphorylation	HSLPKCNSHLEITIP CCCCCCCCCEEEECC	38.63	28348404
590	Acetylation	HLEITIPKDLKLKEA CEEEECCCCCCCCCC	72.36	25953088
612	Acetylation	LIIDAGQKRFGAVSC EEEECCHHHCCEEEE	49.10	25953088
706	Phosphorylation	PLMCYSRTKTLLFIS CEEEECCCCEEEEEC	23.57	-
747	Acetylation	VIRSEEEKVRFERQK CCCCHHHHHHHHHHH	41.83	25953088

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
Oops, there are no upstream regulatory protein records of ESCO1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ESCO1_HUMAN !!

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 ESCO1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
H31_HUMAN	HIST1H3A	physical	20331966

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 ESCO1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-200, AND MASSSPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASSSPECTROMETRY.	17525332 [Abstract]