ETAA1_HUMAN - dbPTM
ETAA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ETAA1_HUMAN
UniProt AC Q9NY74
Protein Name Ewing's tumor-associated antigen 1 {ECO:0000312|HGNC:HGNC:24648}
Gene Name ETAA1 {ECO:0000312|HGNC:HGNC:24648}
Organism Homo sapiens (Human).
Sequence Length 926
Subcellular Localization Nucleus . Localizes at sites of DNA damage following replication stress (PubMed:27601467, PubMed:27723720, PubMed:27723717). Recruited to stalled replication forks via interaction with RPA1 and RPA2 subunits of the RPA complex (PubMed:27601467, PubMe
Protein Description Replication stress response protein that accumulates at DNA damage sites and promotes replication fork progression and integrity. [PubMed: 27601467]
Protein Sequence MSRRRKHDDSPSPKKTPHKTVAAEECGSVVEPGRRRLRSARGSWPCGAREGPPGPVRQREQPPTAALCSKSNPEERYETPKRALKMDSLSSSFSSPNDPDGQNDIFWDQNSPLTKQLGKGRKKQIYTTDSDEISHIVNRIAPQDEKPTTNSMLDMWIGETAIPCTPSVAKGKSRAKISCTKLKTQSQEEELMKLAKQFDKNMEELDVIQEQNKRNYDFTQMISETEILSNYKDNIQMWSLHNIVPEIDNATKKPIKGNTKISVANNQNSSQKPFDQIAEAAFNAIFDGSTQKCSGQLSQELPEAFWSTSNTTFVKTNALKEEKIITNETLVIEKLSNKTPRSLSSQVDTPIMTKSCVTSCTKEPETSNKYIDAFTTSDFEDDWENLLGSEPFAMQNIDMPELFPSKTAHVTDQKEICTFNSKTVKNTSRANTSPDARLGDSKVLQDLSSKTYDRELIDAEYRFSPNSNKSNKLSTGNKMKFENSSNKIVIQDEIQNCIVTSNLTKIKEDILTNSTEASERKSALNTRYSNEQKNKCILNQSIKAPVNTDLFGSANLGSKTSVSNPNQTSASKVGSFFDDWNDPSFANEIIKACHQLDNTWEADDVDDDLLYQACDDIERLTQQQDIRKDSKTSESICEINNNSEHGAKLTQQQDIRKDSKTSESICEINNNSEHGAKNMFAISKQGSNLVQSKHLNPGSISVQTSLTNSSQIDKPMKMEKGEMYGNSPRFLGATNLTMYSKISNCQINNLHVSYTNTDVPIQVNSSKLVLPGSSSLNVTSDHMNTEITTYKKKLSTNQPCHKTVTDEAQSNLNTTVGFSKFTFTRMKNSQILSQFNQNCITGSMSDTKITQGVEKKKGVNPLLEEAVGQQSLVKLSESLKQSSKEEEEKNRKCSPEEIQRKRQEALVRRMAKARASSVNAAPTSFL
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
10PhosphorylationRRRKHDDSPSPKKTP
CCCCCCCCCCCCCCC
33.0828985074
12PhosphorylationRKHDDSPSPKKTPHK
CCCCCCCCCCCCCCC
53.9928985074
39PhosphorylationPGRRRLRSARGSWPC
CCCHHHHHCCCCCCC
27.2328555341
43PhosphorylationRLRSARGSWPCGARE
HHHHCCCCCCCCCCC
23.4527251275
85SumoylationETPKRALKMDSLSSS
CCHHHHHHHHHHCCC
39.4128112733
95PhosphorylationSLSSSFSSPNDPDGQ
HHCCCCCCCCCCCCC
26.22-
119MethylationPLTKQLGKGRKKQIY
HHHHHCCCCCCCEEE
65.22-
122UbiquitinationKQLGKGRKKQIYTTD
HHCCCCCCCEEEECC
58.67-
123UbiquitinationQLGKGRKKQIYTTDS
HCCCCCCCEEEECCH
40.3329967540
130PhosphorylationKQIYTTDSDEISHIV
CEEEECCHHHHHHHH
34.7425159151
146AcetylationRIAPQDEKPTTNSML
HHCCCCCCCCCCCHH
56.8219818169
165PhosphorylationGETAIPCTPSVAKGK
CCCCCCCCHHHHCCC
17.1624719451
167PhosphorylationTAIPCTPSVAKGKSR
CCCCCCHHHHCCCCC
19.2928060719
178PhosphorylationGKSRAKISCTKLKTQ
CCCCCEEEECCCCCC
18.28-
183SumoylationKISCTKLKTQSQEEE
EEEECCCCCCCHHHH
46.18-
183SumoylationKISCTKLKTQSQEEE
EEEECCCCCCCHHHH
46.18-
183UbiquitinationKISCTKLKTQSQEEE
EEEECCCCCCCHHHH
46.18-
184PhosphorylationISCTKLKTQSQEEEL
EEECCCCCCCHHHHH
43.8420363803
186PhosphorylationCTKLKTQSQEEELMK
ECCCCCCCHHHHHHH
44.8025159151
193UbiquitinationSQEEELMKLAKQFDK
CHHHHHHHHHHHHHH
58.9029967540
196SumoylationEELMKLAKQFDKNME
HHHHHHHHHHHHCHH
63.03-
196SumoylationEELMKLAKQFDKNME
HHHHHHHHHHHHCHH
63.03-
200UbiquitinationKLAKQFDKNMEELDV
HHHHHHHHCHHHHHH
60.5329967540
213UbiquitinationDVIQEQNKRNYDFTQ
HHHHHHHHCCCCHHH
41.5429967540
256AcetylationNATKKPIKGNTKISV
CCCCCCCCCCCEEEE
55.4291065
260SumoylationKPIKGNTKISVANNQ
CCCCCCCEEEECCCC
36.66-
260SumoylationKPIKGNTKISVANNQ
CCCCCCCEEEECCCC
36.66-
298PhosphorylationQKCSGQLSQELPEAF
CCCCCCHHHHCCHHH
17.4528348404
342O-linked_GlycosylationLSNKTPRSLSSQVDT
HCCCCCCCHHHCCCC
33.5330379171
342PhosphorylationLSNKTPRSLSSQVDT
HCCCCCCCHHHCCCC
33.5320363803
344PhosphorylationNKTPRSLSSQVDTPI
CCCCCCHHHCCCCCC
21.7020363803
345PhosphorylationKTPRSLSSQVDTPIM
CCCCCHHHCCCCCCC
39.2425159151
349PhosphorylationSLSSQVDTPIMTKSC
CHHHCCCCCCCCCHH
18.8329396449
354UbiquitinationVDTPIMTKSCVTSCT
CCCCCCCCHHHHCCC
25.2029967540
359PhosphorylationMTKSCVTSCTKEPET
CCCHHHHCCCCCCCC
10.2121712546
362UbiquitinationSCVTSCTKEPETSNK
HHHHCCCCCCCCCCC
75.50-
414SumoylationTAHVTDQKEICTFNS
CCCCCCCCCEEECCC
52.43-
414SumoylationTAHVTDQKEICTFNS
CCCCCCCCCEEECCC
52.4328112733
414UbiquitinationTAHVTDQKEICTFNS
CCCCCCCCCEEECCC
52.4329967540
418PhosphorylationTDQKEICTFNSKTVK
CCCCCEEECCCCCCC
31.3527174698
421PhosphorylationKEICTFNSKTVKNTS
CCEEECCCCCCCCCC
26.0527174698
422AcetylationEICTFNSKTVKNTSR
CEEECCCCCCCCCCC
59.4426051181
423PhosphorylationICTFNSKTVKNTSRA
EEECCCCCCCCCCCC
36.2127174698
427PhosphorylationNSKTVKNTSRANTSP
CCCCCCCCCCCCCCC
17.5526074081
428PhosphorylationSKTVKNTSRANTSPD
CCCCCCCCCCCCCCC
38.5027174698
432PhosphorylationKNTSRANTSPDARLG
CCCCCCCCCCCCCCC
40.4226074081
433PhosphorylationNTSRANTSPDARLGD
CCCCCCCCCCCCCCC
22.1628985074
442SumoylationDARLGDSKVLQDLSS
CCCCCCHHHHHHHHC
52.26-
442SumoylationDARLGDSKVLQDLSS
CCCCCCHHHHHHHHC
52.2628112733
442UbiquitinationDARLGDSKVLQDLSS
CCCCCCHHHHHHHHC
52.2629967540
450UbiquitinationVLQDLSSKTYDRELI
HHHHHHCCCCCHHHH
47.9629967540
461PhosphorylationRELIDAEYRFSPNSN
HHHHCCEECCCCCCC
20.7628985074
464PhosphorylationIDAEYRFSPNSNKSN
HCCEECCCCCCCCCC
17.7425159151
469UbiquitinationRFSPNSNKSNKLSTG
CCCCCCCCCCCCCCC
56.0529967540
470PhosphorylationFSPNSNKSNKLSTGN
CCCCCCCCCCCCCCC
43.3723532336
480SumoylationLSTGNKMKFENSSNK
CCCCCCEEEECCCCC
51.6528112733
507SumoylationTSNLTKIKEDILTNS
CCCCHHHHHHHHHCC
51.38-
507SumoylationTSNLTKIKEDILTNS
CCCCHHHHHHHHHCC
51.3828112733
507UbiquitinationTSNLTKIKEDILTNS
CCCCHHHHHHHHHCC
51.3829967540
514PhosphorylationKEDILTNSTEASERK
HHHHHHCCCHHHHHH
23.5325627689
528PhosphorylationKSALNTRYSNEQKNK
HHHHHHCCCHHHHCC
17.51-
529PhosphorylationSALNTRYSNEQKNKC
HHHHHCCCHHHHCCE
30.5125159151
533SumoylationTRYSNEQKNKCILNQ
HCCCHHHHCCEEECC
52.8028112733
535SumoylationYSNEQKNKCILNQSI
CCHHHHCCEEECCCC
29.68-
535SumoylationYSNEQKNKCILNQSI
CCHHHHCCEEECCCC
29.6828112733
535UbiquitinationYSNEQKNKCILNQSI
CCHHHHCCEEECCCC
29.6829967540
541PhosphorylationNKCILNQSIKAPVNT
CCEEECCCCCCCCCC
25.6125159151
543SumoylationCILNQSIKAPVNTDL
EEECCCCCCCCCCCC
52.46-
543SumoylationCILNQSIKAPVNTDL
EEECCCCCCCCCCCC
52.46-
543UbiquitinationCILNQSIKAPVNTDL
EEECCCCCCCCCCCC
52.46-
553PhosphorylationVNTDLFGSANLGSKT
CCCCCCCCCCCCCCC
13.4725159151
559UbiquitinationGSANLGSKTSVSNPN
CCCCCCCCCCCCCCC
42.9229967540
572UbiquitinationPNQTSASKVGSFFDD
CCCCCHHHHHHHCCC
50.7821963094
575PhosphorylationTSASKVGSFFDDWND
CCHHHHHHHCCCCCC
26.2327732954
584PhosphorylationFDDWNDPSFANEIIK
CCCCCCHHHHHHHHH
39.5927732954
599PhosphorylationACHQLDNTWEADDVD
HHHHCCCCCCCCCCC
25.0921712546
611PhosphorylationDVDDDLLYQACDDIE
CCCHHHHHHHHHHHH
11.0227642862
631SumoylationQDIRKDSKTSESICE
HHHHHCCCCCHHHEE
67.23-
631SumoylationQDIRKDSKTSESICE
HHHHHCCCCCHHHEE
67.23-
648AcetylationNNSEHGAKLTQQQDI
CCCHHHCCCHHHHHH
57.5726051181
648UbiquitinationNNSEHGAKLTQQQDI
CCCHHHCCCHHHHHH
57.5729967540
660SumoylationQDIRKDSKTSESICE
HHHHHCCCCCHHEEH
67.23-
660SumoylationQDIRKDSKTSESICE
HHHHHCCCCCHHEEH
67.23-
684SumoylationKNMFAISKQGSNLVQ
CCEEEEECCCCCCEE
53.19-
684SumoylationKNMFAISKQGSNLVQ
CCEEEEECCCCCCEE
53.19-
684UbiquitinationKNMFAISKQGSNLVQ
CCEEEEECCCCCCEE
53.1929967540
717SumoylationSQIDKPMKMEKGEMY
HHCCCCEEECCCCCC
53.05-
717SumoylationSQIDKPMKMEKGEMY
HHCCCCEEECCCCCC
53.05-
720UbiquitinationDKPMKMEKGEMYGNS
CCCEEECCCCCCCCC
57.59-
727PhosphorylationKGEMYGNSPRFLGAT
CCCCCCCCCCCCCCC
17.06-
740PhosphorylationATNLTMYSKISNCQI
CCCCEEEEECCCCEE
16.8224719451
795PhosphorylationTTYKKKLSTNQPCHK
EEEHHHCCCCCCCCC
33.9025159151
796PhosphorylationTYKKKLSTNQPCHKT
EEHHHCCCCCCCCCC
48.5925159151
802UbiquitinationSTNQPCHKTVTDEAQ
CCCCCCCCCCCHHHH
51.9429967540
833PhosphorylationMKNSQILSQFNQNCI
ECHHHHHHHHHCCCC
34.0628112733
856UbiquitinationITQGVEKKKGVNPLL
CCCCCHHHCCCCHHH
41.0529967540
857UbiquitinationTQGVEKKKGVNPLLE
CCCCHHHCCCCHHHH
78.2329967540
874UbiquitinationVGQQSLVKLSESLKQ
HCCHHHHHHHHHHHH
52.1429967540
880UbiquitinationVKLSESLKQSSKEEE
HHHHHHHHHHCHHHH
58.3729967540
891MethylationKEEEEKNRKCSPEEI
HHHHHHHHCCCHHHH
53.04-
894PhosphorylationEEKNRKCSPEEIQRK
HHHHHCCCHHHHHHH
38.0823663014
916PhosphorylationRMAKARASSVNAAPT
HHHHHHHHHCCCCCC
29.3022617229
917PhosphorylationMAKARASSVNAAPTS
HHHHHHHHCCCCCCC
20.5728555341

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
95SPhosphorylationKinaseATRQ13535
PSP
95SPhosphorylationKinaseCDK2P24941
PSP
111SPhosphorylationKinaseATRQ13535
PSP
111SPhosphorylationKinaseCDK2P24941
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ETAA1_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 ETAA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TZAP_HUMANZBTB48physical
26496610
SP16H_HUMANSUPT16Hphysical
26496610
SYTC2_HUMANTARSL2physical
26496610

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 ETAA1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-833, AND MASSSPECTROMETRY.

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