ECM29_SCHPO - dbPTM
ECM29_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECM29_SCHPO
UniProt AC Q9P7H8
Protein Name Proteasome component ecm29
Gene Name ecm29
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1679
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Stabilizes the proteasome holoenzyme, probably by tethering the 20S proteolytic core particle and the 19S regulatory particle. The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity)..
Protein Sequence MAENELRLLNNAELKLALAESEDSFQSLVSVFLCPILLKLDSPHESVRNKTISIANHIMTRLNNNAQAILPLEALVSQYVEANQPLRKRFLLAFISIGEKRIPCSENLALLQICLNHVNEYPLVLLTLTIRLLRFSKPTSAITCSNDVILSLSSFYLIQKDQRIFSDLQFSQKTVDYRLSLLRWIHLSSWPSNWKWLAYFFASADSHSEVARLADEFTRDSGLPDLENLSHVNVLLDIALDKFRIEALHANFSVSISLRNKAIQHLLKSKIAANTDKAINCIEFILEAPPSMQPRLIQFTRWVVDKADPNFLKPKAAMILEKILSILSSNIIQSDLLRGFLYTTIGLLTKVDNHLITNSLLTNLLTSLQSELPDVRVSIDEALSIIIPYYSNFRFSNELLPVLEPFIFDSPESPAAYCALRFVLVAFPFDYLPARFICLKVQNPFVFHHSFIEEAKKGLNLSQWVQYNSVYSTNEAQEEDKVRAASYPSASEVISFILSDHDLKKFWESNAAEYCLAILEFIERCIYYSADRSLELYDNDKLSSIDALLIQDSKLREMVSEKCISLSNFNVFLEYVFYGTLLMHFEPTYALSRLVSFAPPEVTFSLPELDFLTSVFNFPLALRNTATRILGIILSTKDSTRISEVLSSCFTIISTSNNKNDNFFKAETALLIIGYTISYLAAQTNSAAVDSFILNSGSIKEFFSVLLEYLGSNVLHKKTTSLAIYKELFVYFTRDWITSYGVDFDEILNVLLRFLKEVEDTNVKVECLHVISRMSLSFSDDEMAEKILKAIYVTYHMDSPDILFASAEAMSILAGGHRNVFVKSTCPIFFQKQLDNYKADHYCFTLDFILTDCVNSPKPLLRRASSLWLFYIVRYCEPQTYTMTRLNDIYHSFLSFLVTQDDFVQDTASRGLKAMYDVLEGDERKSFTDNLISTIAADRVDEKTKAPLDADTALFTTNKGTVATYKDICSLASESGNPDLIYSFLSIAGNSSLWQARKGLASGISYLGIPEDQKRKTFSFDTSKSSSLLKKLYRFKHDPNPDVAKTMGEIWDTLVPSDLNLASHRKYLVEDCLEFMGSRSWRDRESSVNTLVSLLSNVPVTEYLNQLEDIWNMSFRTLDDIKESVREASFPLCKLLARSVIQSLEKTSHNTSPSGICKGKRIVSVALPFLLKHAYDQAKEVRSLTYSTITELVRTGNSTLTSFVPAIMQVMLEYLTEYESKAATFLDFHAKNYSIKQENIDNARTSAVQSSSMMDTLEKCIGLLDESSMQTLYPILNRMIAKPGGVPTKIGSAQVVMLLVIRRGPLVKQFASKLLQSLKSSCFDRNAAVSDAFASAIGYLLRVCPLEIASQTCQEIIDKFYDGNTNEQIISSKLTVYASRYAPDVFLNLGSLFFPFIFFGKHSSSISINGVLSKAWDELSSAGSSVNLYSEEIILLIQKNLIVTKWDVKRPAAAALLEFVNTSRLTYRQNDIYVLLNETMKDKSWPGKELLLEAYVKFLIKYPEFIKSQKMEEVHQVIVREFKRRNIVYKSHAMESVGELLSDENYRELDLYELSLNECGTFLQKEWFDKDDELNLEEKIALQRNSVYAMFNSSRPGNKNCNEMLLTYLSNALDENYLHWNVKLAILKNAPHLKKIMSNEEFLLYKDILYRCYEDNPSPKAKDYAEVIFGENYLSVLRN
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

Oops, there are no PTM records of ECM29_SCHPO !!

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 ECM29_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ECM29_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 ECM29_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
POM1_SCHPOpom1genetic
18818364
SDS23_SCHPOsds23genetic
22681890
MU122_SCHPOmug122genetic
22681890
ALF1_SCHPOalf1genetic
22681890
ATG11_SCHPOatg11genetic
22681890
CAPZB_SCHPOacp2genetic
22681890
PFL9_SCHPOpfl9genetic
22681890
CAND1_SCHPOknd1genetic
22681890
IWR1_SCHPOiwr1genetic
22681890
YBD1_SCHPOSPBC16C6.01cgenetic
22681890

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ECM29_SCHPO

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Related Literatures of Post-Translational Modification

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