ESCO2_HUMAN - dbPTM
ESCO2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ESCO2_HUMAN
UniProt AC Q56NI9
Protein Name N-acetyltransferase ESCO2
Gene Name ESCO2
Organism Homo sapiens (Human).
Sequence Length 601
Subcellular Localization Nucleus . Chromosome . Nuclear in interphase cells, excluded from chromosomes during metaphase but reassociates with chromosomes in telophase.
Protein Description Acetyltransferase required for the establishment of sister chromatid cohesion. [PubMed: 15821733]
Protein Sequence MAALTPRKRKQDSLKCDSLLHFTENLFPSPNKKHCFYQNSDKNEENLHCSQQEHFVLSALKTTEINRLPSANQGSPFKSALSTVSFYNQNKWYLNPLERKLIKESRSTCLKTNDEDKSFPIVTEKMQGKPVCSKKNNKKPQKSLTAKYQPKYRHIKPVSRNSRNSKQNRVIYKPIVEKENNCHSAENNSNAPRVLSQKIKPQVTLQGGAAFFVRKKSSLRKSSLENEPSLGRTQKSKSEVIEDSDVETVSEKKTFATRQVPKCLVLEEKLKIGLLSASSKNKEKLIKDSSDDRVSSKEHKVDKNEAFSSEDSLGENKTISPKSTVYPIFSASSVNSKRSLGEEQFSVGSVNFMKQTNIQKNTNTRDTSKKTKDQLIIDAGQKHFGATVCKSCGMIYTASNPEDEMQHVQHHHRFLEGIKYVGWKKERVVAEFWDGKIVLVLPHDPSFAIKKVEDVQELVDNELGFQQVVPKCPNKIKTFLFISDEKRVVGCLIAEPIKQAFRVLSEPIGPESPSSTECPRAWQCSDVPEPAVCGISRIWVFRLKRRKRIARRLVDTLRNCFMFGCFLSTDEIAFSDPTPDGKLFATKYCNTPNFLVYNFNS
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 Orthologous
Protein Cluster
5Phosphorylation---MAALTPRKRKQD
---CCCCCCCCCCCC		19.1325056879
13PhosphorylationPRKRKQDSLKCDSLL
CCCCCCCCCCCCHHH		27.5123312004
18PhosphorylationQDSLKCDSLLHFTEN
CCCCCCCHHHHHHHC		42.1523186163
23PhosphorylationCDSLLHFTENLFPSP
CCHHHHHHHCCCCCC		17.1420068231
29PhosphorylationFTENLFPSPNKKHCF
HHHCCCCCCCCCCCE		33.5023401153
33UbiquitinationLFPSPNKKHCFYQNS
CCCCCCCCCCEEECC		52.8529967540
37PhosphorylationPNKKHCFYQNSDKNE
CCCCCCEEECCCCCC		16.5126074081
40PhosphorylationKHCFYQNSDKNEENL
CCCEEECCCCCCCCC		34.1426074081
42UbiquitinationCFYQNSDKNEENLHC
CEEECCCCCCCCCCH		67.1129967540
50PhosphorylationNEENLHCSQQEHFVL
CCCCCCHHHHHHHHH		24.9320873877
58PhosphorylationQQEHFVLSALKTTEI
HHHHHHHHHHHHHHH		26.6720873877
61UbiquitinationHFVLSALKTTEINRL
HHHHHHHHHHHHHCC		53.7929967540
62PhosphorylationFVLSALKTTEINRLP
HHHHHHHHHHHHCCC		30.4328176443
63PhosphorylationVLSALKTTEINRLPS
HHHHHHHHHHHCCCC		33.0328176443
70PhosphorylationTEINRLPSANQGSPF
HHHHCCCCCCCCCCC		44.4325159151
75PhosphorylationLPSANQGSPFKSALS
CCCCCCCCCCCCHHH		19.8729255136
93PhosphorylationFYNQNKWYLNPLERK
ECCCCCEECCHHHHH		9.75-
111SumoylationESRSTCLKTNDEDKS
HHHHHHCCCCCCCCC		47.64-
111SumoylationESRSTCLKTNDEDKS
HHHHHHCCCCCCCCC		47.64-
111UbiquitinationESRSTCLKTNDEDKS
HHHHHHCCCCCCCCC		47.6433845483
111AcetylationESRSTCLKTNDEDKS
HHHHHHCCCCCCCCC		47.6420167786
135AcetylationGKPVCSKKNNKKPQK
CCCCCCCCCCCCCCC		49.8424846217
138AcetylationVCSKKNNKKPQKSLT
CCCCCCCCCCCCHHC		75.1924846225
142AcetylationKNNKKPQKSLTAKYQ
CCCCCCCCHHCCCCC		56.8319814929
146UbiquitinationKPQKSLTAKYQPKYR
CCCCHHCCCCCCCCC		17.53-
147AcetylationPQKSLTAKYQPKYRH
CCCHHCCCCCCCCCC		38.9019814937
147SumoylationPQKSLTAKYQPKYRH
CCCHHCCCCCCCCCC		38.90-
147UbiquitinationPQKSLTAKYQPKYRH
CCCHHCCCCCCCCCC		38.9029967540
147SumoylationPQKSLTAKYQPKYRH
CCCHHCCCCCCCCCC		38.90-
152PhosphorylationTAKYQPKYRHIKPVS
CCCCCCCCCCCCCCC		17.69-
156SumoylationQPKYRHIKPVSRNSR
CCCCCCCCCCCCCCC		32.99-
156UbiquitinationQPKYRHIKPVSRNSR
CCCCCCCCCCCCCCC		32.9929967540
156SumoylationQPKYRHIKPVSRNSR
CCCCCCCCCCCCCCC		32.99-
159PhosphorylationYRHIKPVSRNSRNSK
CCCCCCCCCCCCCCC		33.9820068231
172PhosphorylationSKQNRVIYKPIVEKE
CCCCCEEEECCEECC		14.0927642862
173AcetylationKQNRVIYKPIVEKEN
CCCCEEEECCEECCC		19.6925953088
173SumoylationKQNRVIYKPIVEKEN
CCCCEEEECCEECCC		19.69-
173UbiquitinationKQNRVIYKPIVEKEN
CCCCEEEECCEECCC		19.6929967540
173SumoylationKQNRVIYKPIVEKEN
CCCCEEEECCEECCC		19.69-
222PhosphorylationKKSSLRKSSLENEPS
EHHHCCCHHCCCCCC		33.4525159151
223PhosphorylationKSSLRKSSLENEPSL
HHHCCCHHCCCCCCC		42.6225159151
236PhosphorylationSLGRTQKSKSEVIED
CCCCCCCCHHHEECC		31.4326074081
237UbiquitinationLGRTQKSKSEVIEDS
CCCCCCCHHHEECCC		58.64-
238PhosphorylationGRTQKSKSEVIEDSD
CCCCCCHHHEECCCC		44.1626074081
244PhosphorylationKSEVIEDSDVETVSE
HHHEECCCCCCCHHH		30.6623401153
248PhosphorylationIEDSDVETVSEKKTF
ECCCCCCCHHHCCCC		29.2227794612
250PhosphorylationDSDVETVSEKKTFAT
CCCCCCHHHCCCCCC		51.6326074081
252UbiquitinationDVETVSEKKTFATRQ
CCCCHHHCCCCCCCC		50.0021906983
253SumoylationVETVSEKKTFATRQV
CCCHHHCCCCCCCCC		44.84-
253SumoylationVETVSEKKTFATRQV
CCCHHHCCCCCCCCC		44.84-
253UbiquitinationVETVSEKKTFATRQV
CCCHHHCCCCCCCCC		44.8422817900
278PhosphorylationKIGLLSASSKNKEKL
HHCCCCCCCCCHHHH		38.1723186163
279PhosphorylationIGLLSASSKNKEKLI
HCCCCCCCCCHHHHH		39.7123186163
280UbiquitinationGLLSASSKNKEKLIK
CCCCCCCCCHHHHHC		70.3329967540
282UbiquitinationLSASSKNKEKLIKDS
CCCCCCCHHHHHCCC		61.02-
284UbiquitinationASSKNKEKLIKDSSD
CCCCCHHHHHCCCCC		58.06-
290PhosphorylationEKLIKDSSDDRVSSK
HHHHCCCCCCCCCCC		54.3824719451
300UbiquitinationRVSSKEHKVDKNEAF
CCCCCCCCCCHHHCC		53.9022817900
303UbiquitinationSKEHKVDKNEAFSSE
CCCCCCCHHHCCCCC		60.7221906983
308PhosphorylationVDKNEAFSSEDSLGE
CCHHHCCCCCCCCCC		39.6129978859
309PhosphorylationDKNEAFSSEDSLGEN
CHHHCCCCCCCCCCC		38.6828985074
312PhosphorylationEAFSSEDSLGENKTI
HCCCCCCCCCCCCCC		33.9323401153
317UbiquitinationEDSLGENKTISPKST
CCCCCCCCCCCCCCC		42.8229967540
318PhosphorylationDSLGENKTISPKSTV
CCCCCCCCCCCCCCC		37.9623312004
320PhosphorylationLGENKTISPKSTVYP
CCCCCCCCCCCCCEE		31.3523401153
330PhosphorylationSTVYPIFSASSVNSK
CCCEEEEECHHCCCC		28.1428555341
333PhosphorylationYPIFSASSVNSKRSL
EEEEECHHCCCCCCC		25.6528555341
337SumoylationSASSVNSKRSLGEEQ
ECHHCCCCCCCCCCC		40.58-
337MethylationSASSVNSKRSLGEEQ
ECHHCCCCCCCCCCC		40.58-
337SumoylationSASSVNSKRSLGEEQ
ECHHCCCCCCCCCCC		40.58-
346PhosphorylationSLGEEQFSVGSVNFM
CCCCCCCCHHHEEHH		25.8424719451
349PhosphorylationEEQFSVGSVNFMKQT
CCCCCHHHEEHHHHC		16.2524719451
360AcetylationMKQTNIQKNTNTRDT
HHHCCCCCCCCCCCC		63.0425953088
360UbiquitinationMKQTNIQKNTNTRDT
HHHCCCCCCCCCCCC		63.0429967540
372SumoylationRDTSKKTKDQLIIDA
CCCCHHHHCEEEEEC		52.97-
372SumoylationRDTSKKTKDQLIIDA
CCCCHHHHCEEEEEC		52.97-
372UbiquitinationRDTSKKTKDQLIIDA
CCCCHHHHCEEEEEC		52.9729967540
451SumoylationDPSFAIKKVEDVQEL
CCCHHCEEHHHHHHH		44.75-
451SumoylationDPSFAIKKVEDVQEL
CCCHHCEEHHHHHHH		44.75-
451UbiquitinationDPSFAIKKVEDVQEL
CCCHHCEEHHHHHHH		44.7529967540
487MethylationLFISDEKRVVGCLIA
EEECCCCCEEEEEEC		26.72-
498UbiquitinationCLIAEPIKQAFRVLS
EEECHHHHHHHHHHC		46.41-
505PhosphorylationKQAFRVLSEPIGPES
HHHHHHHCCCCCCCC		38.1727987026
512PhosphorylationSEPIGPESPSSTECP
CCCCCCCCCCCCCCC		32.9629255136
514PhosphorylationPIGPESPSSTECPRA
CCCCCCCCCCCCCCC		60.2030266825
515PhosphorylationIGPESPSSTECPRAW
CCCCCCCCCCCCCCC		31.4530266825
516PhosphorylationGPESPSSTECPRAWQ
CCCCCCCCCCCCCCC		46.0423401153
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 ESCO2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ESCO2_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 ESCO2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RCOR1_HUMANRCOR1physical
18501190
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
268300Roberts syndrome (RBS)
269000SC phocomelia syndrome (SCPS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ESCO2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-312, AND MASSSPECTROMETRY.
"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-75 AND SER-244, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASSSPECTROMETRY.

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