ESF1_HUMAN - dbPTM
ESF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ESF1_HUMAN
UniProt AC Q9H501
Protein Name ESF1 homolog
Gene Name ESF1
Organism Homo sapiens (Human).
Sequence Length 851
Subcellular Localization Nucleus, nucleolus. Nucleus, nucleoplasm.
Protein Description May constitute a novel regulatory system for basal transcription. Negatively regulates ABT1 (By similarity)..
Protein Sequence MSSKQEIMSDQRFRRVAKDPRFWEMPEKDRKVKIDKRFRAMFHDKKFKLNYAVDKRGRPISHSTTEDLKRFYDLSDSDSNLSGEDSKALSQKKIKKKKTQTKKEIDSKNLVEKKKETKKANHKGSENKTDLDNSIGIKKMKTSCKFKIDSNISPKKDSKEFTQKNKKEKKNIVQHTTDSSLEEKQRTLDSGTSEIVKSPRIECSKTRREMQSVVQLIMTRDSDGYENSTDGEMCDKDALEEDSESVSEIGSDEESENEITSVGRASGDDDGSEDDEEEDEDEEEDEDEDSEDDDKSDSGPDLARGKGNIETSSEDEDDTADLFPEESGFEHAWRELDKDAPRADEITRRLAVCNMDWDRLKAKDLLALFNSFKPKGGVIFSVKIYPSEFGKERMKEEQVQGPVELLSIPEDAPEKDWTSREKLRDYQFKRLKYYYAVVDCDSPETASKIYEDCDGLEFESSCSFIDLRFIPDDITFDDEPKDVASEVNLTAYKPKYFTSAAMGTSTVEITWDETDHERITMLNRKFKKEELLDMDFQAYLASSSEDEEEIEEELQGDDGVNVEEDGKTKKSQKDDEEQIAKYRQLLQVIQEKEKKGKENDMEMEIKWVPGLKESAEEMVKNKLEGKDKLTPWEQFLEKKKEKKRLKRKQKALAEEASEEELPSDVDLNDPYFAEEVKQIGINKKSVKSAKDGTSPEEEIEIERQKAEMALLMMDEDEDSKKHFNYNKIVEHQNLSKKKKKQLMKKKELIEDDFEVNVNDARFQAMYTSHLFNLDPSDPNFKKTKAMEKILEEKARQRERKEQELTQAIKKKESEIEKESQRKSIDPALSMLIKSIKTKTEQFQARKKQKVK
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
2Acetylation------MSSKQEIMS
------CCCHHHHHC
46.3622814378
2Phosphorylation------MSSKQEIMS
------CCCHHHHHC
46.3622964224
4Sumoylation----MSSKQEIMSDQ
----CCCHHHHHCCH
44.64-
4Acetylation----MSSKQEIMSDQ
----CCCHHHHHCCH
44.6422424773
4Sumoylation----MSSKQEIMSDQ
----CCCHHHHHCCH
44.64-
4Ubiquitination----MSSKQEIMSDQ
----CCCHHHHHCCH
44.6422505724
9PhosphorylationSSKQEIMSDQRFRRV
CCHHHHHCCHHHHHH
35.9323401153
28UbiquitinationRFWEMPEKDRKVKID
CHHCCCCCCCCCHHC
57.89-
51PhosphorylationDKKFKLNYAVDKRGR
CCCCEEEEEECCCCC
20.59-
552-HydroxyisobutyrylationKLNYAVDKRGRPISH
EEEEEECCCCCCCCC
50.59-
55UbiquitinationKLNYAVDKRGRPISH
EEEEEECCCCCCCCC
50.5921906983
61PhosphorylationDKRGRPISHSTTEDL
CCCCCCCCCCCHHHH
17.6728555341
63PhosphorylationRGRPISHSTTEDLKR
CCCCCCCCCHHHHHH
30.1828555341
69UbiquitinationHSTTEDLKRFYDLSD
CCCHHHHHHHHCCCC
53.4321906983
72PhosphorylationTEDLKRFYDLSDSDS
HHHHHHHHCCCCCCC
21.7330108239
75PhosphorylationLKRFYDLSDSDSNLS
HHHHHCCCCCCCCCC
31.9726503892
77PhosphorylationRFYDLSDSDSNLSGE
HHHCCCCCCCCCCHH
39.2926503892
79PhosphorylationYDLSDSDSNLSGEDS
HCCCCCCCCCCHHHH
43.5526503892
82PhosphorylationSDSDSNLSGEDSKAL
CCCCCCCCHHHHHHH
44.3726503892
86PhosphorylationSNLSGEDSKALSQKK
CCCCHHHHHHHHHHH
18.6122115753
90PhosphorylationGEDSKALSQKKIKKK
HHHHHHHHHHHHHHC
44.8318669648
108SumoylationTKKEIDSKNLVEKKK
CHHHHHHHHHHHHHH
51.02-
108SumoylationTKKEIDSKNLVEKKK
CHHHHHHHHHHHHHH
51.02-
108UbiquitinationTKKEIDSKNLVEKKK
CHHHHHHHHHHHHHH
51.02-
123UbiquitinationETKKANHKGSENKTD
HHHHCCCCCCCCCCC
65.0322817900
125PhosphorylationKKANHKGSENKTDLD
HHCCCCCCCCCCCCC
42.6823186163
128AcetylationNHKGSENKTDLDNSI
CCCCCCCCCCCCCCC
39.0921339330
128UbiquitinationNHKGSENKTDLDNSI
CCCCCCCCCCCCCCC
39.0922817900
134PhosphorylationNKTDLDNSIGIKKMK
CCCCCCCCCCHHCCC
23.1225159151
138AcetylationLDNSIGIKKMKTSCK
CCCCCCHHCCCCCCE
41.4225953088
138UbiquitinationLDNSIGIKKMKTSCK
CCCCCCHHCCCCCCE
41.42-
139AcetylationDNSIGIKKMKTSCKF
CCCCCHHCCCCCCEE
43.6511924517
150PhosphorylationSCKFKIDSNISPKKD
CCEEEECCCCCCCCC
39.2723927012
153PhosphorylationFKIDSNISPKKDSKE
EEECCCCCCCCCHHH
34.6129255136
158PhosphorylationNISPKKDSKEFTQKN
CCCCCCCHHHHHHHH
42.8626074081
166UbiquitinationKEFTQKNKKEKKNIV
HHHHHHHHHHHHHHH
70.1522817900
167UbiquitinationEFTQKNKKEKKNIVQ
HHHHHHHHHHHHHHH
81.7022817900
169UbiquitinationTQKNKKEKKNIVQHT
HHHHHHHHHHHHHHC
61.0622817900
170SumoylationQKNKKEKKNIVQHTT
HHHHHHHHHHHHHCC
53.66-
170SumoylationQKNKKEKKNIVQHTT
HHHHHHHHHHHHHCC
53.66-
170UbiquitinationQKNKKEKKNIVQHTT
HHHHHHHHHHHHHCC
53.6621906983
176PhosphorylationKKNIVQHTTDSSLEE
HHHHHHHCCCCCHHH
18.4025159151
177PhosphorylationKNIVQHTTDSSLEEK
HHHHHHCCCCCHHHH
31.5929255136
179PhosphorylationIVQHTTDSSLEEKQR
HHHHCCCCCHHHHHH
34.4329255136
180PhosphorylationVQHTTDSSLEEKQRT
HHHCCCCCHHHHHHH
42.4829255136
184AcetylationTDSSLEEKQRTLDSG
CCCCHHHHHHHCCCC
35.3920167786
184UbiquitinationTDSSLEEKQRTLDSG
CCCCHHHHHHHCCCC
35.3921906983
187PhosphorylationSLEEKQRTLDSGTSE
CHHHHHHHCCCCCCH
32.2123927012
190PhosphorylationEKQRTLDSGTSEIVK
HHHHHCCCCCCHHHC
47.2723927012
192PhosphorylationQRTLDSGTSEIVKSP
HHHCCCCCCHHHCCC
27.4330278072
193PhosphorylationRTLDSGTSEIVKSPR
HHCCCCCCHHHCCCC
28.9330278072
197AcetylationSGTSEIVKSPRIECS
CCCCHHHCCCCCCCC
61.4726051181
197UbiquitinationSGTSEIVKSPRIECS
CCCCHHHCCCCCCCC
61.4721906983
198PhosphorylationGTSEIVKSPRIECSK
CCCHHHCCCCCCCCH
14.4429255136
204PhosphorylationKSPRIECSKTRREMQ
CCCCCCCCHHHHHHH
25.0326074081
212PhosphorylationKTRREMQSVVQLIMT
HHHHHHHHHHHHHHC
23.97-
219PhosphorylationSVVQLIMTRDSDGYE
HHHHHHHCCCCCCCC
25.0828102081
222PhosphorylationQLIMTRDSDGYENST
HHHHCCCCCCCCCCC
29.6423663014
225PhosphorylationMTRDSDGYENSTDGE
HCCCCCCCCCCCCCC
19.5428985074
228PhosphorylationDSDGYENSTDGEMCD
CCCCCCCCCCCCCCC
18.8823927012
229PhosphorylationSDGYENSTDGEMCDK
CCCCCCCCCCCCCCH
60.6523927012
272PhosphorylationASGDDDGSEDDEEED
CCCCCCCCCCCCCCC
44.8628290473
290PhosphorylationEEDEDEDSEDDDKSD
CCCCCCCCCCCCCCC
40.6628290473
296PhosphorylationDSEDDDKSDSGPDLA
CCCCCCCCCCCCCHH
43.9625159151
298PhosphorylationEDDDKSDSGPDLARG
CCCCCCCCCCCHHCC
60.3520164059
311PhosphorylationRGKGNIETSSEDEDD
CCCCCCCCCCCCCCC
33.4826503892
312PhosphorylationGKGNIETSSEDEDDT
CCCCCCCCCCCCCCH
20.9526503892
313PhosphorylationKGNIETSSEDEDDTA
CCCCCCCCCCCCCHH
57.3926503892
319PhosphorylationSSEDEDDTADLFPEE
CCCCCCCHHHCCCCC
34.1022115753
327PhosphorylationADLFPEESGFEHAWR
HHCCCCCCCHHHHHH
47.3120873877
381PhosphorylationPKGGVIFSVKIYPSE
CCCCEEEEEEECHHH
16.0420068231
387PhosphorylationFSVKIYPSEFGKERM
EEEEECHHHHCHHHH
28.6920068231
391UbiquitinationIYPSEFGKERMKEEQ
ECHHHHCHHHHHHHH
47.6822817900
395UbiquitinationEFGKERMKEEQVQGP
HHCHHHHHHHHHCCC
65.4122817900
407PhosphorylationQGPVELLSIPEDAPE
CCCEEHHCCCCCCCC
49.0430576142
415UbiquitinationIPEDAPEKDWTSREK
CCCCCCCCCCCCHHH
58.4621906983
432AcetylationDYQFKRLKYYYAVVD
HHHHHCCEEEEEEEE
34.9326051181
442PhosphorylationYAVVDCDSPETASKI
EEEEECCCHHHHHHH
30.8525627689
445PhosphorylationVDCDSPETASKIYED
EECCCHHHHHHHHHC
39.3530576142
461PhosphorylationDGLEFESSCSFIDLR
CCCEEECCCEEEEEE
13.4430576142
463PhosphorylationLEFESSCSFIDLRFI
CEEECCCEEEEEEEC
27.4730576142
485PhosphorylationDEPKDVASEVNLTAY
CCCCCHHHHCCCCEE
41.7620873877
490PhosphorylationVASEVNLTAYKPKYF
HHHHCCCCEECCCCE
23.8020860994
492PhosphorylationSEVNLTAYKPKYFTS
HHCCCCEECCCCEEC
23.6920860994
493AcetylationEVNLTAYKPKYFTSA
HCCCCEECCCCEECC
32.3525953088
493UbiquitinationEVNLTAYKPKYFTSA
HCCCCEECCCCEECC
32.3529967540
569UbiquitinationVEEDGKTKKSQKDDE
CCCCCCCCCCCCCHH
54.6422817900
570UbiquitinationEEDGKTKKSQKDDEE
CCCCCCCCCCCCHHH
64.4522817900
573UbiquitinationGKTKKSQKDDEEQIA
CCCCCCCCCHHHHHH
74.3922817900
581AcetylationDDEEQIAKYRQLLQV
CHHHHHHHHHHHHHH
42.4626051181
581UbiquitinationDDEEQIAKYRQLLQV
CHHHHHHHHHHHHHH
42.4621906983
592UbiquitinationLLQVIQEKEKKGKEN
HHHHHHHHHHCCCCC
59.4629967540
597UbiquitinationQEKEKKGKENDMEME
HHHHHCCCCCCCHHH
63.32-
612UbiquitinationIKWVPGLKESAEEMV
EEECCCCHHHHHHHH
56.38-
614PhosphorylationWVPGLKESAEEMVKN
ECCCCHHHHHHHHHH
39.1223186163
626UbiquitinationVKNKLEGKDKLTPWE
HHHHHCCCCCCCHHH
42.1722817900
628UbiquitinationNKLEGKDKLTPWEQF
HHHCCCCCCCHHHHH
58.7221906983
630PhosphorylationLEGKDKLTPWEQFLE
HCCCCCCCHHHHHHH
31.9025159151
657PhosphorylationKALAEEASEEELPSD
HHHHHHHCCCCCCCC
49.1529255136
663PhosphorylationASEEELPSDVDLNDP
HCCCCCCCCCCCCCH
63.9929255136
671PhosphorylationDVDLNDPYFAEEVKQ
CCCCCCHHHHHHHHH
20.4829255136
687UbiquitinationGINKKSVKSAKDGTS
CCCHHHHCCCCCCCC
52.3522817900
688PhosphorylationINKKSVKSAKDGTSP
CCHHHHCCCCCCCCH
38.0924732914
690AcetylationKKSVKSAKDGTSPEE
HHHHCCCCCCCCHHH
64.8826051181
690UbiquitinationKKSVKSAKDGTSPEE
HHHHCCCCCCCCHHH
64.8822817900
693PhosphorylationVKSAKDGTSPEEEIE
HCCCCCCCCHHHHHH
51.7725159151
694PhosphorylationKSAKDGTSPEEEIEI
CCCCCCCCHHHHHHH
35.5225159151
719PhosphorylationMMDEDEDSKKHFNYN
HCCCCCHHHHHCCHH
41.3727251275
720AcetylationMDEDEDSKKHFNYNK
CCCCCHHHHHCCHHH
63.6930588581
721AcetylationDEDEDSKKHFNYNKI
CCCCHHHHHCCHHHH
58.3330588587
721UbiquitinationDEDEDSKKHFNYNKI
CCCCHHHHHCCHHHH
58.3329967540
727UbiquitinationKKHFNYNKIVEHQNL
HHHCCHHHHHHCCCC
37.4629967540
735PhosphorylationIVEHQNLSKKKKKQL
HHHCCCCCHHHHHHH
50.4025159151
7362-HydroxyisobutyrylationVEHQNLSKKKKKQLM
HHCCCCCHHHHHHHH
72.31-
766PhosphorylationDARFQAMYTSHLFNL
HHHHHHHHHHHHHCC
14.2224043423
767PhosphorylationARFQAMYTSHLFNLD
HHHHHHHHHHHHCCC
9.1524043423
768PhosphorylationRFQAMYTSHLFNLDP
HHHHHHHHHHHCCCC
10.7424043423
776PhosphorylationHLFNLDPSDPNFKKT
HHHCCCCCCCCHHHH
66.4224719451
781AcetylationDPSDPNFKKTKAMEK
CCCCCCHHHHHHHHH
67.2024431643
783PhosphorylationSDPNFKKTKAMEKIL
CCCCHHHHHHHHHHH
25.3220068231
7932-HydroxyisobutyrylationMEKILEEKARQRERK
HHHHHHHHHHHHHHH
39.22-
793UbiquitinationMEKILEEKARQRERK
HHHHHHHHHHHHHHH
39.22-
800UbiquitinationKARQRERKEQELTQA
HHHHHHHHHHHHHHH
60.02-
805PhosphorylationERKEQELTQAIKKKE
HHHHHHHHHHHHHHH
18.4020068231
809UbiquitinationQELTQAIKKKESEIE
HHHHHHHHHHHHHHH
61.8922817900
810UbiquitinationELTQAIKKKESEIEK
HHHHHHHHHHHHHHH
56.5122817900
811UbiquitinationLTQAIKKKESEIEKE
HHHHHHHHHHHHHHH
62.5622817900
817UbiquitinationKKESEIEKESQRKSI
HHHHHHHHHHHHCCH
69.22-
819PhosphorylationESEIEKESQRKSIDP
HHHHHHHHHHCCHHH
46.4821712546
822UbiquitinationIEKESQRKSIDPALS
HHHHHHHCCHHHHHH
44.0929967540
823PhosphorylationEKESQRKSIDPALSM
HHHHHHCCHHHHHHH
34.1229255136
829PhosphorylationKSIDPALSMLIKSIK
CCHHHHHHHHHHHHH
17.4129396449
830SulfoxidationSIDPALSMLIKSIKT
CHHHHHHHHHHHHHH
4.7021406390
838SumoylationLIKSIKTKTEQFQAR
HHHHHHHHHHHHHHH
45.09-
838SumoylationLIKSIKTKTEQFQAR
HHHHHHHHHHHHHHH
45.09-
838UbiquitinationLIKSIKTKTEQFQAR
HHHHHHHHHHHHHHH
45.0929967540

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 ESF1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ESF1_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 ESF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AATF_HUMANAATFphysical
26344197
DDX52_HUMANDDX52physical
26344197
PUM3_HUMANKIAA0020physical
26344197
MPP10_HUMANMPHOSPH10physical
26344197
SEPT7_HUMANSEPT7physical
26344197
SAS10_HUMANUTP3physical
26344197

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 ESF1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-75; SER-77; SER-79;SER-82; SER-153; SER-657; SER-663 AND SER-694, AND MASS SPECTROMETRY.
"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-153; SER-657 ANDSER-663, AND MASS SPECTROMETRY.
"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; SER-77; SER-79;SER-82; SER-90; SER-153; SER-179; SER-180; SER-198; THR-311; SER-312;SER-313; SER-657; SER-663; THR-693; SER-694 AND SER-823, 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-153, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; SER-298 ANDTHR-693, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-735, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657; SER-663 ANDSER-694, AND MASS SPECTROMETRY.
"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-75; SER-77; SER-79;SER-82; SER-153; SER-296; SER-298; THR-311; SER-312; SER-313; SER-657AND SER-663, AND MASS SPECTROMETRY.
"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-75, AND MASSSPECTROMETRY.

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