EXO1_HUMAN - dbPTM
EXO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXO1_HUMAN
UniProt AC Q9UQ84
Protein Name Exonuclease 1
Gene Name EXO1
Organism Homo sapiens (Human).
Sequence Length 846
Subcellular Localization Nucleus . Colocalizes with PCNA to discrete nuclear foci in S-phase.
Protein Description 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair (MMR) to excise mismatch-containing DNA tracts directed by strand breaks located either 5' or 3' to the mismatch. Also exhibits endonuclease activity against 5'-overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Required for somatic hypermutation (SHM) and class switch recombination (CSR) of immunoglobulin genes. Essential for male and female meiosis..
Protein Sequence MGIQGLLQFIKEASEPIHVRKYKGQVVAVDTYCWLHKGAIACAEKLAKGEPTDRYVGFCMKFVNMLLSHGIKPILVFDGCTLPSKKEVERSRRERRQANLLKGKQLLREGKVSEARECFTRSINITHAMAHKVIKAARSQGVDCLVAPYEADAQLAYLNKAGIVQAIITEDSDLLAFGCKKVILKMDQFGNGLEIDQARLGMCRQLGDVFTEEKFRYMCILSGCDYLSSLRGIGLAKACKVLRLANNPDIVKVIKKIGHYLKMNITVPEDYINGFIRANNTFLYQLVFDPIKRKLIPLNAYEDDVDPETLSYAGQYVDDSIALQIALGNKDINTFEQIDDYNPDTAMPAHSRSHSWDDKTCQKSANVSSIWHRNYSPRPESGTVSDAPQLKENPSTVGVERVISTKGLNLPRKSSIVKRPRSAELSEDDLLSQYSLSFTKKTKKNSSEGNKSLSFSEVFVPDLVNGPTNKKSVSTPPRTRNKFATFLQRKNEESGAVVVPGTRSRFFCSSDSTDCVSNKVSIQPLDETAVTDKENNLHESEYGDQEGKRLVDTDVARNSSDDIPNNHIPGDHIPDKATVFTDEESYSFESSKFTRTISPPTLGTLRSCFSWSGGLGDFSRTPSPSPSTALQQFRRKSDSPTSLPENNMSDVSQLKSEESSDDESHPLREEACSSQSQESGEFSLQSSNASKLSQCSSKDSDSEESDCNIKLLDSQSDQTSKLRLSHFSKKDTPLRNKVPGLYKSSSADSLSTTKIKPLGPARASGLSKKPASIQKRKHHNAENKPGLQIKLNELWKNFGFKKDSEKLPPCKKPLSPVRDNIQLTPEAEEDIFNKPECGRVQRAIFQ
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
68PhosphorylationKFVNMLLSHGIKPIL
HHHHHHHHCCCCEEE		18.73-
84PhosphorylationFDGCTLPSKKEVERS
ECCCCCCCHHHHHHH		60.5224719451
126PhosphorylationFTRSINITHAMAHKV
HHHHHCHHHHHHHHH		10.0929083192
185UbiquitinationGCKKVILKMDQFGNG
CCCEEEEEHHHHCCC		29.34-
214UbiquitinationGDVFTEEKFRYMCIL
HHCCCHHHHHHHHHH		28.98-
228PhosphorylationLSGCDYLSSLRGIGL
HHCCCHHHHCCCHHH		22.5430301811
229PhosphorylationSGCDYLSSLRGIGLA
HCCCHHHHCCCHHHH		21.3525954137
240UbiquitinationIGLAKACKVLRLANN
HHHHHHHHHHHHCCC		49.52-
271PhosphorylationNITVPEDYINGFIRA
CEECCHHHHCCEEEC		8.4722210691
281PhosphorylationGFIRANNTFLYQLVF
CEEECCCCEEEHHHH		18.1522210691
284PhosphorylationRANNTFLYQLVFDPI
ECCCCEEEHHHHCHH		8.8022210691
292UbiquitinationQLVFDPIKRKLIPLN
HHHHCHHHCCCCCCC		49.20-
353PhosphorylationAMPAHSRSHSWDDKT
CCCCCCCCCCCCCCC		25.5324719451
375PhosphorylationSSIWHRNYSPRPESG
HHHHCCCCCCCCCCC		21.7323663014
376PhosphorylationSIWHRNYSPRPESGT
HHHCCCCCCCCCCCC		20.2725159151
381PhosphorylationNYSPRPESGTVSDAP
CCCCCCCCCCCCCCH		42.3123663014
383PhosphorylationSPRPESGTVSDAPQL
CCCCCCCCCCCCHHH		26.5623663014
391UbiquitinationVSDAPQLKENPSTVG
CCCCHHHCCCCCCCC		50.6421906983
391 (in isoform 1)Ubiquitination-50.6421890473
391 (in isoform 4)Ubiquitination-50.6421890473
404PhosphorylationVGVERVISTKGLNLP
CCCEEEECCCCCCCC		22.62-
405PhosphorylationGVERVISTKGLNLPR
CCEEEECCCCCCCCC		20.29-
406UbiquitinationVERVISTKGLNLPRK
CEEEECCCCCCCCCC		55.39-
414PhosphorylationGLNLPRKSSIVKRPR
CCCCCCCCCCCCCCC		26.9523882029
415PhosphorylationLNLPRKSSIVKRPRS
CCCCCCCCCCCCCCC		34.1423882029
422PhosphorylationSIVKRPRSAELSEDD
CCCCCCCCCCCCHHH		28.8622617229
426PhosphorylationRPRSAELSEDDLLSQ
CCCCCCCCHHHHHHH		30.4122210691
437PhosphorylationLLSQYSLSFTKKTKK
HHHHHHHCEECCCCC		25.5724719451
446PhosphorylationTKKTKKNSSEGNKSL
ECCCCCCCCCCCCCC		38.3529978859
447PhosphorylationKKTKKNSSEGNKSLS
CCCCCCCCCCCCCCC		59.9429978859
452PhosphorylationNSSEGNKSLSFSEVF
CCCCCCCCCCCEEEC		32.9928348404
454PhosphorylationSEGNKSLSFSEVFVP
CCCCCCCCCEEECCH		33.5429978859
456PhosphorylationGNKSLSFSEVFVPDL
CCCCCCCEEECCHHH		29.4928348404
472PhosphorylationNGPTNKKSVSTPPRT
CCCCCCCCCCCCCCH		23.9426437602
474PhosphorylationPTNKKSVSTPPRTRN
CCCCCCCCCCCCHHH		42.1423312004
475PhosphorylationTNKKSVSTPPRTRNK
CCCCCCCCCCCHHHH		34.8522210691
479PhosphorylationSVSTPPRTRNKFATF
CCCCCCCHHHHHHHH		44.3524719451
482AcetylationTPPRTRNKFATFLQR
CCCCHHHHHHHHHHH		32.8418048416
482SumoylationTPPRTRNKFATFLQR
CCCCHHHHHHHHHHH		32.84-
482SumoylationTPPRTRNKFATFLQR
CCCCHHHHHHHHHHH		32.8418048416
494PhosphorylationLQRKNEESGAVVVPG
HHHCCCCCCCEEECC		26.3519413330
502PhosphorylationGAVVVPGTRSRFFCS
CCEEECCCCCCEEEC		21.28-
509PhosphorylationTRSRFFCSSDSTDCV
CCCCEEECCCCCCCC		31.8329116813
510PhosphorylationRSRFFCSSDSTDCVS
CCCEEECCCCCCCCC		36.4421815630
512PhosphorylationRFFCSSDSTDCVSNK
CEEECCCCCCCCCCC		28.2628450419
513PhosphorylationFFCSSDSTDCVSNKV
EEECCCCCCCCCCCE		38.1128450419
517PhosphorylationSDSTDCVSNKVSIQP
CCCCCCCCCCEEEEE		36.9529978859
533UbiquitinationDETAVTDKENNLHES
CCCCCCCCCCCCCHH		53.64-
548UbiquitinationEYGDQEGKRLVDTDV
HHCCCCCCEEECHHH		41.6321906983
548 (in isoform 1)Ubiquitination-41.6321890473
548 (in isoform 4)Ubiquitination-41.6321890473
559PhosphorylationDTDVARNSSDDIPNN
CHHHHCCCCCCCCCC		29.5925850435
560PhosphorylationTDVARNSSDDIPNNH
HHHHCCCCCCCCCCC		42.7425850435
581PhosphorylationPDKATVFTDEESYSF
CCCCEEECCCCCCEE		37.8622817900
585PhosphorylationTVFTDEESYSFESSK
EEECCCCCCEEECCC		24.8328985074
596PhosphorylationESSKFTRTISPPTLG
ECCCCEEECCCCCHH		23.8126074081
598PhosphorylationSKFTRTISPPTLGTL
CCCEEECCCCCHHHH		24.9822617229
601PhosphorylationTRTISPPTLGTLRSC
EEECCCCCHHHHHHH		41.0026074081
604PhosphorylationISPPTLGTLRSCFSW
CCCCCHHHHHHHHCC		23.3126074081
607PhosphorylationPTLGTLRSCFSWSGG
CCHHHHHHHHCCCCC		23.7229978859
610PhosphorylationGTLRSCFSWSGGLGD
HHHHHHHCCCCCCCC		25.3523401153
612PhosphorylationLRSCFSWSGGLGDFS
HHHHHCCCCCCCCCC		23.0629978859
619PhosphorylationSGGLGDFSRTPSPSP
CCCCCCCCCCCCCCH		39.7326552605
621PhosphorylationGLGDFSRTPSPSPST
CCCCCCCCCCCCHHH		27.2421082442
623PhosphorylationGDFSRTPSPSPSTAL
CCCCCCCCCCHHHHH		37.0819413330
625PhosphorylationFSRTPSPSPSTALQQ
CCCCCCCCHHHHHHH		35.5028450419
627PhosphorylationRTPSPSPSTALQQFR
CCCCCCHHHHHHHHH		30.5627251275
628PhosphorylationTPSPSPSTALQQFRR
CCCCCHHHHHHHHHH		34.4727251275
637PhosphorylationLQQFRRKSDSPTSLP
HHHHHHHCCCCCCCC		41.3223401153
639PhosphorylationQFRRKSDSPTSLPEN
HHHHHCCCCCCCCCC		36.8528355574
641PhosphorylationRRKSDSPTSLPENNM
HHHCCCCCCCCCCCC		47.0125159151
642PhosphorylationRKSDSPTSLPENNMS
HHCCCCCCCCCCCCH		45.3625159151
649PhosphorylationSLPENNMSDVSQLKS
CCCCCCCHHHHHHHC		36.6624144214
652PhosphorylationENNMSDVSQLKSEES
CCCCHHHHHHHCCCC		34.4824144214
656PhosphorylationSDVSQLKSEESSDDE
HHHHHHHCCCCCCCC		56.0129255136
659PhosphorylationSQLKSEESSDDESHP
HHHHCCCCCCCCCCH		34.7129255136
660PhosphorylationQLKSEESSDDESHPL
HHHCCCCCCCCCCHH		52.9729255136
664PhosphorylationEESSDDESHPLREEA
CCCCCCCCCHHHHHH		37.0829255136
674PhosphorylationLREEACSSQSQESGE
HHHHHHHHCCHHCCC		33.4622817900
693PhosphorylationSSNASKLSQCSSKDS
CCCHHHHHHCCCCCC		32.6428450419
696PhosphorylationASKLSQCSSKDSDSE
HHHHHHCCCCCCCCC		32.5530576142
697PhosphorylationSKLSQCSSKDSDSEE
HHHHHCCCCCCCCCC		48.3728450419
700PhosphorylationSQCSSKDSDSEESDC
HHCCCCCCCCCCCCC		46.9325159151
702PhosphorylationCSSKDSDSEESDCNI
CCCCCCCCCCCCCCE		47.4122617229
705PhosphorylationKDSDSEESDCNIKLL
CCCCCCCCCCCEEEE		43.3328450419
714PhosphorylationCNIKLLDSQSDQTSK
CCEEEECCCCCCCCC		31.3917525332
716PhosphorylationIKLLDSQSDQTSKLR
EEEECCCCCCCCCCH		35.3227251275
725O-linked_GlycosylationQTSKLRLSHFSKKDT
CCCCCHHHHHCCCCC		18.9530620550
732PhosphorylationSHFSKKDTPLRNKVP
HHHCCCCCCCHHCCC		32.8622798277
732O-linked_GlycosylationSHFSKKDTPLRNKVP
HHHCCCCCCCHHCCC		32.8630620550
743MethylationNKVPGLYKSSSADSL
HCCCCCCCCCCCCCC		49.24-
744PhosphorylationKVPGLYKSSSADSLS
CCCCCCCCCCCCCCC		18.9023312004
745PhosphorylationVPGLYKSSSADSLST
CCCCCCCCCCCCCCC		25.9527732954
746PhosphorylationPGLYKSSSADSLSTT
CCCCCCCCCCCCCCC		43.0925159151
749PhosphorylationYKSSSADSLSTTKIK
CCCCCCCCCCCCCCE		24.7624905233
751PhosphorylationSSSADSLSTTKIKPL
CCCCCCCCCCCCEEC		37.6723312004
752PhosphorylationSSADSLSTTKIKPLG
CCCCCCCCCCCEECC		37.0824905233
753PhosphorylationSADSLSTTKIKPLGP
CCCCCCCCCCEECCH		27.6523312004
784SumoylationKHHNAENKPGLQIKL
CCCCCCCCCCCEEHH		31.78-
784SumoylationKHHNAENKPGLQIKL
CCCCCCCCCCCEEHH		31.78-
796UbiquitinationIKLNELWKNFGFKKD
EHHHHHHHHCCCCCC		55.832189047
796 (in isoform 1)Ubiquitination-55.8321890473
796 (in isoform 4)Ubiquitination-55.8321890473
804PhosphorylationNFGFKKDSEKLPPCK
HCCCCCCHHCCCCCC		45.57-
815PhosphorylationPPCKKPLSPVRDNIQ
CCCCCCCCCCCCCCC		29.8530266825
824PhosphorylationVRDNIQLTPEAEEDI
CCCCCCCCCCHHHHH		11.6023927012
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
714SPhosphorylationKinaseATRQ13535
Uniprot
746SPhosphorylationKinaseAMPKA1Q13131
PSP
746SPhosphorylationKinaseAMPKA1Q5EG47
PSP
746SPhosphorylationKinaseCHK1O14757
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
454SPhosphorylation

18048416
621TPhosphorylation

18048416
714SPhosphorylation

18048416
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 EXO1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MSH2_HUMANMSH2physical
11427529
MSH3_HUMANMSH3physical
11427529
MLH1_HUMANMLH1physical
11427529
PMS2_HUMANPMS2physical
11427529
1433Z_HUMANYWHAZphysical
21533173
1433B_HUMANYWHABphysical
21533173
1433E_HUMANYWHAEphysical
21533173
MLH1_HUMANMLH1physical
21533173
ATM_HUMANATMphysical
20019063
MLH1_HUMANMLH1physical
14676842
PCNA_HUMANPCNAphysical
15225546
SENP6_HUMANSENP6physical
26083678
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 EXO1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-482, AND MASS SPECTROMETRY.
"ATR-dependent pathways control hEXO1 stability in response to stalledforks.";
El-Shemerly M., Hess D., Pyakurel A.K., Moselhy S., Ferrari S.;
Nucleic Acids Res. 36:511-519(2008).
Cited for: PHOSPHORYLATION AT SER-376; SER-422; SER-454; THR-581; SER-598;THR-621; SER-623; SER-639; SER-660; SER-674; SER-714 AND SER-746,ACETYLATION AT LYS-482, MASS SPECTROMETRY, AND MUTAGENESIS OF SER-454;THR-621 AND SER-714.
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-598; SER-623; SER-639;SER-700 AND SER-702, 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-422, AND MASSSPECTROMETRY.
"ATR-dependent pathways control hEXO1 stability in response to stalledforks.";
El-Shemerly M., Hess D., Pyakurel A.K., Moselhy S., Ferrari S.;
Nucleic Acids Res. 36:511-519(2008).
Cited for: PHOSPHORYLATION AT SER-376; SER-422; SER-454; THR-581; SER-598;THR-621; SER-623; SER-639; SER-660; SER-674; SER-714 AND SER-746,ACETYLATION AT LYS-482, MASS SPECTROMETRY, AND MUTAGENESIS OF SER-454;THR-621 AND SER-714.
"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-598, AND MASSSPECTROMETRY.
"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-714, AND MASSSPECTROMETRY.
"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-598, AND MASSSPECTROMETRY.

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