EME1_SCHPO - dbPTM
EME1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EME1_SCHPO
UniProt AC Q9C103
Protein Name Crossover junction endonuclease eme1
Gene Name eme1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 735
Subcellular Localization Nucleus .
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, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI)..
Protein Sequence MTLQSTDSAIVIDSEADVDISSSQASPSKDNIALSEHNVITVLDTPQRSTQCDSLLKSFSTPLVSGSEDVLPSPRDALNITNKKSVTDNLLLSLTSSNQSTNTNLNPSSRVEIINLNSSPPNSLSSQPKHQEFHLFHTPTIPRTTQLSSKTSSPIVIPDDNEQVASPLSKKAASLTSSPLKDFQSSPPLSTVLQKSHSLHDILLDTNDDDHFPFTQSPLTKTKSFNDALTSSSSILKPCMPSIASPTSNRLSHAPSTPNLFPNQDSSNTIDLINNRSKTSVENQERTFNLTSDVHLDSPTSPSKHSSIEPNTSQEDSFQELPSLNKLSIQSRAFKKMRLPKISRTTDTPPASTSNSNKKNLDKLKKMRKLCSRSLEPYELDSNTQRKRKRYEDSLKKSKTLDKVDSLNRKMAKELDRKNSKELQKINKVKRTKEECLSEIILLSPDDWASSWYSTVRSQLDSYNCQFVVNSNQPKDSIMWKRKVNNVFNSSTNRFELSIEHEQIEPFALLRLKCRDFIKYIEEDQADTFFHEMSEKFKGCKLILLLEGIPNYFKSLKAELNRQYAAAVNSGTRPLLFGSLSKYQNFTKEKLESEIVRFSFEHSILINTSNDEKETAQWIVSFTGDIALSRYKHFSKFSARASTTEIGHVKSADRIENSLNFMLRQILRVTPNIANAICDQFDSIPSLIHHLKTHGEESLTNVVIQSSISERNLGPVLSRRIYNTFLCKEASSDAP
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
118PhosphorylationVEIINLNSSPPNSLS
EEEEECCCCCCCCCC		47.6025720772
119PhosphorylationEIINLNSSPPNSLSS
EEEECCCCCCCCCCC		43.2125720772
174PhosphorylationPLSKKAASLTSSPLK
HHHHHHHHCCCCCCH		36.7221712547
176PhosphorylationSKKAASLTSSPLKDF
HHHHHHCCCCCCHHC		25.3524763107
177PhosphorylationKKAASLTSSPLKDFQ
HHHHHCCCCCCHHCC		34.9424763107
178PhosphorylationKAASLTSSPLKDFQS
HHHHCCCCCCHHCCC		29.0821712547
185PhosphorylationSPLKDFQSSPPLSTV
CCCHHCCCCCCHHHH		44.8224763107
186PhosphorylationPLKDFQSSPPLSTVL
CCHHCCCCCCHHHHH		21.5424763107
196PhosphorylationLSTVLQKSHSLHDIL
HHHHHHHCCCHHHHC		12.8321712547
198PhosphorylationTVLQKSHSLHDILLD
HHHHHCCCHHHHCCC		34.1921712547
206PhosphorylationLHDILLDTNDDDHFP
HHHHCCCCCCCCCCC		40.2821712547
215PhosphorylationDDDHFPFTQSPLTKT
CCCCCCCCCCCCCCC		28.5121712547
374PhosphorylationMRKLCSRSLEPYELD
HHHHHHHCCCCCCCC		22.3128889911
400PhosphorylationDSLKKSKTLDKVDSL
HHHHHCHHHHHHHHH		47.4828889911
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_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EME1_SCHPO !!
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_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SWI5_SCHPOswi5genetic
17353272
BZZ1_SCHPObzz1genetic
18818364
RNH2B_SCHPOSPBC1347.08cgenetic
18818364
PPB_SCHPOpho8genetic
18818364
KLP6_SCHPOklp6genetic
18818364
PAB2_SCHPOpab2genetic
18818364
BAG1A_SCHPObag101genetic
18818364
RSC4_SCHPOrsc4genetic
18818364
ELP5_SCHPOelp5genetic
18818364
SWD2_SCHPOswd2genetic
18818364
MED14_SCHPOpmc1genetic
18818364
ASK1_SCHPOask1genetic
18818364
EXO1_SCHPOexo1genetic
18818364
YGSA_SCHPOdbl8genetic
18818364
VPS71_SCHPOvps71genetic
18818364
YB89_SCHPOSPBC29A3.09cgenetic
18818364
YB33_SCHPOebs1genetic
18818364
CLR4_SCHPOclr4genetic
18818364
POB3_SCHPOpob3genetic
18818364
RAD14_SCHPOrhp14genetic
18818364
CLR3_SCHPOclr3genetic
18818364
TAS3_SCHPOtas3genetic
18818364
CTF18_SCHPOctf18genetic
18818364
HPC2_SCHPOhip4genetic
18818364
UTP16_SCHPOutp16genetic
18818364
EI2BA_SCHPOSPCC11E10.07cgenetic
18818364
RIK1_SCHPOrik1genetic
18818364
RPA12_SCHPOrpa12genetic
18818364
HST2_SCHPOhst2genetic
18818364
HRR1_SCHPOhrr1genetic
18818364
DCR1_SCHPOdcr1genetic
18818364
CCR4_SCHPOccr4genetic
18818364
RAD7_SCHPOrhp7genetic
18818364
MU154_SCHPOmug154genetic
18818364
NOT2_SCHPOnot2genetic
18818364
SPP1_SCHPOspf1genetic
18818364
RAF1_SCHPOraf1genetic
18818364
AGO1_SCHPOago1genetic
18818364
VPH2_SCHPOvph2genetic
18818364
RAF2_SCHPOraf2genetic
18818364
VRP1_SCHPOvrp1genetic
18818364
AIR1_SCHPOair1genetic
18818364
EAF1_SCHPOeaf1genetic
18818364
MED19_SCHPOrox3genetic
18818364
CEK1_SCHPOcek1genetic
18818364
TRM82_SCHPOSPCC18.13genetic
18818364
AAKB_SCHPOamk2genetic
18818364
CID12_SCHPOcid12genetic
18818364
HCS1_SCHPOSPCC737.07cgenetic
18818364
ELP2_SCHPOelp2genetic
18818364
MUS81_SCHPOmus81physical
12084712
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EME1_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-400, AND MASSSPECTROMETRY.

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