MRE11_ARATH - dbPTM
MRE11_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MRE11_ARATH
UniProt AC Q9XGM2
Protein Name Double-strand break repair protein MRE11
Gene Name MRE11
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 720
Subcellular Localization Nucleus .
Protein Description Involved in DNA double-strand break repair (DSBR). Possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. Also involved in meiotic DSB processing (By similarity)..
Protein Sequence MSREDFSDTLRVLVATDCHLGYMEKDEIRRHDSFKAFEEICSIAEEKQVDFLLLGGDLFHENKPSRTTLVKAIEILRRHCLNDKPVQFQVVSDQTVNFQNAFGQVNYEDPHFNVGLPVFSIHGNHDDPAGVDNLSAIDILSACNLVNYFGKMVLGGSGVGQITLYPILMKKGSTTVALYGLGNIRDERLNRMFQTPHAVQWMRPEVQEGCDVSDWFNILVLHQNRVKSNPKNAISEHFLPRFLDFIVWGHEHECLIDPQEVSGMGFHITQPGSSVATSLIDGESKPKHVLLLEIKGNQYRPTKIPLTSVRPFEYTEIVLKDESDIDPNDQNSILEHLDKVVRNLIEKASKKAVNRSEIKLPLVRIKVDYSGFMTINPQRFGQKYVGKVANPQDILIFSKASKKGRSEANIDDSERLRPEELNQQNIEALVAESNLKMEILPVNDLDVALHNFVNKDDKLAFYSCVQYNLQETRGKLAKDSDAKKFEEDDLILKVGECLEERLKDRSTRPTGSSQFLSTGLTSENLTKGSSGIANASFSDDEDTTQMSGLAPPTRGRRGSSTANTTRGRAKAPTRGRGRGKASSAMKQTTLDSSLGFRQSQRSASAAASAAFKSASTIGEDDVDSPSSEEVEPEDFNKPDSSSEDDESTKGKGRKRPATTKRGRGRGSGTSKRGRKNESSSSLNRLLSSKDDDEDEDDEDREKKLNKSQPRVTRNYGALRR
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
163PhosphorylationGSGVGQITLYPILMK
CCCCCCEEEEEEEEC		16.6124894044
413PhosphorylationSEANIDDSERLRPEE
CCCCCCHHHHCCHHH		22.3725561503
433PhosphorylationIEALVAESNLKMEIL
HHHHHHHCCCCCEEE		37.4122074104
536PhosphorylationSSGIANASFSDDEDT
CCCCCCCCCCCCCCC		25.7030407730
538PhosphorylationGIANASFSDDEDTTQ
CCCCCCCCCCCCCCC		41.4730407730
543PhosphorylationSFSDDEDTTQMSGLA
CCCCCCCCCCCCCCC		19.5130407730
544PhosphorylationFSDDEDTTQMSGLAP
CCCCCCCCCCCCCCC		34.3030407730
561PhosphorylationRGRRGSSTANTTRGR
CCCCCCCCCCCCCCC		26.1423572148
564PhosphorylationRGSSTANTTRGRAKA
CCCCCCCCCCCCCCC		18.5323572148
565PhosphorylationGSSTANTTRGRAKAP
CCCCCCCCCCCCCCC		30.8223572148
599PhosphorylationSSLGFRQSQRSASAA
HHHCCCHHHHHHHHH		24.2519880383
604PhosphorylationRQSQRSASAAASAAF
CHHHHHHHHHHHHHH		21.4919880383
608PhosphorylationRSASAAASAAFKSAS
HHHHHHHHHHHHHHH		18.5319880383
678PhosphorylationKRGRKNESSSSLNRL
CCCCCCCCCHHHHHH		44.9325561503
679PhosphorylationRGRKNESSSSLNRLL
CCCCCCCCHHHHHHH		20.1225561503
680PhosphorylationGRKNESSSSLNRLLS
CCCCCCCHHHHHHHC		48.3925561503
681PhosphorylationRKNESSSSLNRLLSS
CCCCCCHHHHHHHCC		31.4525561503
687PhosphorylationSSLNRLLSSKDDDED
HHHHHHHCCCCCCCC		39.6819880383
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 MRE11_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MRE11_ARATH !!
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 MRE11_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAF1_ARATHHAF01physical
26358508
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MRE11_ARATH

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory