EME1_HUMAN - dbPTM
EME1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EME1_HUMAN
UniProt AC Q96AY2
Protein Name Crossover junction endonuclease EME1
Gene Name EME1
Organism Homo sapiens (Human).
Sequence Length 570
Subcellular Localization Nucleus, nucleolus . Recruited to regions of DNA damage in S-phase cells.
Protein Description Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks..
Protein Sequence MALKKSSPSLDSGDSDSEELPTFAFLKKEPSSTKRRQPEREEKIVVVDISDCEASCPPAPELFSPPVPEIAETVTQTQPVRLLSSESEDEEEFIPLAQRLTCKFLTHKQLSPEDSSSPVKSVLDHQNNEGASCDWKKPFPKIPEVPLHDTPERSAADNKDLILDPCCQLPAYLSTCPGQSSSLAVTKTNSDILPPQKKTKPSQKVQGRGSHGCRQQRQARQKESTLRRQERKNAALVTRMKAQRPEECLKHIIVVLDPVLLQMEGGGQLLGALQTMECRCVIEAQAVPCSVTWRRRAGPSEDREDWVEEPTVLVLLRAEAFVSMIDNGKQGSLDSTMKGKETLQGFVTDITAKTAGKALSLVIVDQEKCFSAQNPPRRGKQGANKQTKKQQQRQPEASIGSMVSRVDAEEALVDLQLHTEAQAQIVQSWKELADFTCAFTKAVAEAPFKKLRDETTFSFCLESDWAGGVKVDLAGRGLALVWRRQIQQLNRVSLEMASAVVNAYPSPQLLVQAYQQCFSDKERQNLLADIQVRRGEGVTSTSRRIGPELSRRIYLQMTTLQPHLSLDSAD
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
6 (in isoform 2)Phosphorylation-45.9927251275
6Phosphorylation--MALKKSSPSLDSG
--CCCCCCCCCCCCC		45.9921955146
7Phosphorylation-MALKKSSPSLDSGD
-CCCCCCCCCCCCCC		27.6426503892
7 (in isoform 2)Phosphorylation-27.64-
9 (in isoform 2)Phosphorylation-46.91-
9PhosphorylationALKKSSPSLDSGDSD
CCCCCCCCCCCCCCC		46.9126503892
12PhosphorylationKSSPSLDSGDSDSEE
CCCCCCCCCCCCCCC		50.2026503892
12 (in isoform 2)Phosphorylation-50.20-
15 (in isoform 2)Phosphorylation-46.7027251275
15PhosphorylationPSLDSGDSDSEELPT
CCCCCCCCCCCCCCC		46.7026503892
17PhosphorylationLDSGDSDSEELPTFA
CCCCCCCCCCCCCEE		36.6026503892
17 (in isoform 2)Phosphorylation-36.60-
22PhosphorylationSDSEELPTFAFLKKE
CCCCCCCCEEHCCCC		39.9728450419
33PhosphorylationLKKEPSSTKRRQPER
CCCCCCCCCCCCCCC		32.67-
64PhosphorylationPPAPELFSPPVPEIA
CCCHHHCCCCCHHHH		40.70-
84PhosphorylationTQPVRLLSSESEDEE
CCCEEECCCCCCCHH		36.3326503892
84 (in isoform 2)Phosphorylation-36.3321406692
85PhosphorylationQPVRLLSSESEDEEE
CCEEECCCCCCCHHH		45.1525159151
85 (in isoform 2)Phosphorylation-45.1524719451
87PhosphorylationVRLLSSESEDEEEFI
EEECCCCCCCHHHHH		52.9025159151
87 (in isoform 2)Phosphorylation-52.9024719451
103SumoylationLAQRLTCKFLTHKQL
HHHHHHHHHCCCCCC		37.8728112733
103AcetylationLAQRLTCKFLTHKQL
HHHHHHHHHCCCCCC		37.8725953088
103SumoylationLAQRLTCKFLTHKQL
HHHHHHHHHCCCCCC		37.87-
108AcetylationTCKFLTHKQLSPEDS
HHHHCCCCCCCCCCC		47.9325953088
111 (in isoform 2)Phosphorylation-24.6124719451
111PhosphorylationFLTHKQLSPEDSSSP
HCCCCCCCCCCCCCC		24.6130266825
115PhosphorylationKQLSPEDSSSPVKSV
CCCCCCCCCCCHHHH		30.9330266825
116PhosphorylationQLSPEDSSSPVKSVL
CCCCCCCCCCHHHHH		51.4930266825
117PhosphorylationLSPEDSSSPVKSVLD
CCCCCCCCCHHHHHC		37.3523401153
117 (in isoform 2)Phosphorylation-37.3527251275
121PhosphorylationDSSSPVKSVLDHQNN
CCCCCHHHHHCCCCC		28.3128111955
132PhosphorylationHQNNEGASCDWKKPF
CCCCCCCCCCCCCCC		24.3825159151
136SumoylationEGASCDWKKPFPKIP
CCCCCCCCCCCCCCC		37.0028112733
136SumoylationEGASCDWKKPFPKIP
CCCCCCCCCCCCCCC		37.00-
141SumoylationDWKKPFPKIPEVPLH
CCCCCCCCCCCCCCC		71.8728112733
150PhosphorylationPEVPLHDTPERSAAD
CCCCCCCCCCCCCCC		19.1230266825
150 (in isoform 2)Phosphorylation-19.12-
154PhosphorylationLHDTPERSAADNKDL
CCCCCCCCCCCCCCC		26.5828555341
232SumoylationTLRRQERKNAALVTR
HHHHHHHHHHHHHHH		50.62-
232UbiquitinationTLRRQERKNAALVTR
HHHHHHHHHHHHHHH		50.6229967540
232SumoylationTLRRQERKNAALVTR
HHHHHHHHHHHHHHH		50.62-
238PhosphorylationRKNAALVTRMKAQRP
HHHHHHHHHHHHCCH		26.37-
241 (in isoform 2)Ubiquitination-37.77-
241UbiquitinationAALVTRMKAQRPEEC
HHHHHHHHHCCHHHH		37.77-
329UbiquitinationVSMIDNGKQGSLDST
HHHHHCCCCCCCCHH		58.71-
329 (in isoform 2)Ubiquitination-58.71-
332 (in isoform 2)Phosphorylation-26.89-
332PhosphorylationIDNGKQGSLDSTMKG
HHCCCCCCCCHHHCC		26.8918452278
336 (in isoform 2)Phosphorylation-23.67-
336PhosphorylationKQGSLDSTMKGKETL
CCCCCCHHHCCHHHH		23.6718452278
338UbiquitinationGSLDSTMKGKETLQG
CCCCHHHCCHHHHHH		67.91-
338 (in isoform 2)Ubiquitination-67.91-
338SumoylationGSLDSTMKGKETLQG
CCCCHHHCCHHHHHH		67.91-
338MethylationGSLDSTMKGKETLQG
CCCCHHHCCHHHHHH		67.91-
338"N6,N6-dimethyllysine"GSLDSTMKGKETLQG
CCCCHHHCCHHHHHH		67.91-
340"N6,N6-dimethyllysine"LDSTMKGKETLQGFV
CCHHHCCHHHHHHHH		41.84-
340UbiquitinationLDSTMKGKETLQGFV
CCHHHCCHHHHHHHH		41.8429967540
340 (in isoform 2)Ubiquitination-41.84-
340MethylationLDSTMKGKETLQGFV
CCHHHCCHHHHHHHH		41.84-
353UbiquitinationFVTDITAKTAGKALS
HHHHHHHCCCCCEEE		30.2029967540
353 (in isoform 2)Ubiquitination-30.20-
357UbiquitinationITAKTAGKALSLVIV
HHHCCCCCEEEEEEE		43.63-
357 (in isoform 2)Ubiquitination-43.63-
441UbiquitinationDFTCAFTKAVAEAPF
HHHHHHHHHHHHCCH		34.12-
449UbiquitinationAVAEAPFKKLRDETT
HHHHCCHHHCCCCCE		50.2529967540
454 (in isoform 2)Ubiquitination-43.23-
462UbiquitinationTTFSFCLESDWAGGV
CEEEEEECCCCCCCE		48.0829967540
463 (in isoform 2)Ubiquitination-26.04-
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 EME1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EME1_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 EME1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MUS81_HUMANMUS81physical
19596236
SLX4_HUMANSLX4physical
19596236
A4_HUMANAPPphysical
21832049
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 EME1_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-85 AND SER-111, AND MASSSPECTROMETRY.
"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-111 AND SER-117, ANDMASS 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-12; SER-15; SER-84;SER-85; SER-87 AND THR-150, 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-84; SER-85 AND SER-87,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-15, 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 THR-150, AND MASSSPECTROMETRY.

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