ABCE1_MOUSE - dbPTM
ABCE1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABCE1_MOUSE
UniProt AC P61222
Protein Name ATP-binding cassette sub-family E member 1
Gene Name Abce1
Organism Mus musculus (Mouse).
Sequence Length 599
Subcellular Localization Cytoplasm. Mitochondrion. Localized to clusters of virus formation at the plasma membrane..
Protein Description Antagonizes the binding of 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) by RNase L through direct interaction with RNase L and therefore inhibits its endoribonuclease activity. May play a central role in the regulation of mRNA turnover. Antagonizes the anti-viral effect of the interferon-regulated 2-5A/RNase L pathway (By similarity)..
Protein Sequence MADKLTRIAIVNHDKCKPKKCRQECKKSCPVVRMGKLCIEVTPQSKIAWISETLCIGCGICIKKCPFGALSIVNLPSNLEKETTHRYCANAFKLHRLPIPRPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPDWQEILTYFRGSELQNYFTKILEDDLKAIIKPQYVDQIPKAAKGTVGSILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCLYGVPSAYGVVTMPFSVREGINIFLDGYVPTENLRFRDASLVFKVAETANEEEVKKMCMYKYPGMKKKMGEFELAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGGEVPVLNVSYKPQKISPKSTGSVRQLLHEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFDGVPSKNTVANSPQTLLAGMNKFLSQLEITFRRDPNNYRPRINKLNSIKDVEQKKSGNYFFLDD
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
16GlutathionylationAIVNHDKCKPKKCRQ
EEECCCCCCCHHHHH		13.0524333276
27MalonylationKCRQECKKSCPVVRM
HHHHHHHHHCCEEEE		69.7926320211
38GlutathionylationVVRMGKLCIEVTPQS
EEEECCEEEEECCCC		2.5824333276
42PhosphorylationGKLCIEVTPQSKIAW
CCEEEEECCCCHHHH		11.6526745281
45PhosphorylationCIEVTPQSKIAWISE
EEEECCCCHHHHHHC		27.5128066266
64UbiquitinationGCGICIKKCPFGALS
CCCCEEECCCCCCEE		27.5122790023
65GlutathionylationCGICIKKCPFGALSI
CCCEEECCCCCCEEE		2.6124333276
88GlutathionylationKETTHRYCANAFKLH
HHCCHHHHHCCHHHC		2.0724333276
93AcetylationRYCANAFKLHRLPIP
HHHHCCHHHCCCCCC		40.7622826441
93UbiquitinationRYCANAFKLHRLPIP
HHHHCCHHHCCCCCC		40.7622790023
116UbiquitinationVGTNGIGKSTALKIL
EECCCCCHHHHHHHH		42.5922790023
121MalonylationIGKSTALKILAGKQK
CCHHHHHHHHCCCCC		32.9626320211
121UbiquitinationIGKSTALKILAGKQK
CCHHHHHHHHCCCCC		32.96-
126MalonylationALKILAGKQKPNLGK
HHHHHCCCCCCCCCC		49.9326320211
128UbiquitinationKILAGKQKPNLGKYD
HHHCCCCCCCCCCCC		39.08-
158UbiquitinationELQNYFTKILEDDLK
HHHHHHHHHHHHHHH		35.0822790023
165UbiquitinationKILEDDLKAIIKPQY
HHHHHHHHHHHCHHH		44.5322790023
169UbiquitinationDDLKAIIKPQYVDQI
HHHHHHHCHHHHHHC		21.6922790023
178MalonylationQYVDQIPKAAKGTVG
HHHHHCCHHCCCCHH		63.7126320211
178UbiquitinationQYVDQIPKAAKGTVG
HHHHHCCHHCCCCHH		63.71-
181UbiquitinationDQIPKAAKGTVGSIL
HHCCHHCCCCHHHHH		61.03-
191AcetylationVGSILDRKDETKTQA
HHHHHCCCCCHHHHE		60.6323236377
191UbiquitinationVGSILDRKDETKTQA
HHHHHCCCCCHHHHE		60.6322790023
201S-palmitoylationTKTQAIVCQQLDLTH
HHHHEEEEEHHCCHH		1.4228526873
201GlutathionylationTKTQAIVCQQLDLTH
HHHHEEEEEHHCCHH		1.4224333276
250UbiquitinationPSSYLDVKQRLKAAI
CHHHCCHHHHHHHHH		29.3922790023
261PhosphorylationKAAITIRSLINPDRY
HHHHHHHHHCCCCCE		29.7424759943
328PhosphorylationNLRFRDASLVFKVAE
CCCCCHHHHEEEEEC		29.3822817900
346GlutathionylationEEEVKKMCMYKYPGM
HHHHHHHHHHCCCCH		3.5624333276
349AcetylationVKKMCMYKYPGMKKK
HHHHHHHCCCCHHHC		20.3422826441
397UbiquitinationRMLAGRLKPDEGGEV
HHHCCCCCCCCCCCC		49.4122790023
397AcetylationRMLAGRLKPDEGGEV
HHHCCCCCCCCCCCC		49.4123201123
410PhosphorylationEVPVLNVSYKPQKIS
CCCEEEEEECCCCCC		26.7722345495
411PhosphorylationVPVLNVSYKPQKISP
CCEEEEEECCCCCCC		23.5417242355
417PhosphorylationSYKPQKISPKSTGSV
EECCCCCCCCCCCHH		33.0522345495
419UbiquitinationKPQKISPKSTGSVRQ
CCCCCCCCCCCHHHH		54.59-
419MalonylationKPQKISPKSTGSVRQ
CCCCCCCCCCCHHHH		54.5926320211
431AcetylationVRQLLHEKIRDAYTH
HHHHHHHHHHHHHCC		32.0923236377
550PhosphorylationTVANSPQTLLAGMNK
CCCCCHHHHHHHHHH		27.42-
582PhosphorylationPRINKLNSIKDVEQK
CCCCCCCCCCCHHHH		41.2625159016
584SuccinylationINKLNSIKDVEQKKS
CCCCCCCCCHHHHHC		56.3923954790
584MalonylationINKLNSIKDVEQKKS
CCCCCCCCCHHHHHC		56.3926320211
591PhosphorylationKDVEQKKSGNYFFLD
CCHHHHHCCCCEECC		39.0328066266
594PhosphorylationEQKKSGNYFFLDD--
HHHHCCCCEECCC--		10.1528066266
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 ABCE1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABCE1_MOUSE !!
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 ABCE1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ABCE1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABCE1_MOUSE

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Related Literatures of Post-Translational Modification

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