EPC2_HUMAN - dbPTM
EPC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPC2_HUMAN
UniProt AC Q52LR7
Protein Name Enhancer of polycomb homolog 2
Gene Name EPC2
Organism Homo sapiens (Human).
Sequence Length 807
Subcellular Localization Nucleus.
Protein Description May play a role in transcription or DNA repair..
Protein Sequence MSKLSFRARALDAAKPLPIYRGKDMPDLNDCVSINRAVPQMPTGMEKEEESEHHLQRAISAQQVFREKKESMVIPVPEAESNVNYYNRLYKGEFKQPKQFIHIQPFNLDNEQPDYDMDSEDETLLNRLNRKMEIKPLQFEIMIDRLEKASSNQLVTLQEAKLLLNEDDYLIKAVYDYWVRKRKNCRGPSLIPQIKQEKRDGSTNNDPYVAFRRRTEKMQTRKNRKNDEASYEKMLKLRREFSRAITILEMIKRREKTKRELLHLTLEVVEKRYHLGDYGGEILNEVKISRSEKELYATPATLHNGNHHKVQECKTKHPHHLSLKEEASDVVRQKKKYPKKPKAEALITSQQPTPETLPVINKSDIKQYDFHSSDEDEFPQVLSPVSEPEEENDPDGPCAFRRRAGCQYYAPRLDQANHSCENSELADLDKLRYRHCLTTLTVPRRCIGFARRRIGRGGRVIMDRISTEHDPVLKQIDPEMLNSFSSSSQTIDFSSNFSRTNASSKHCENRLSLSEILSNIRSCRLQCFQPRLLNLQDSDSEECTSRKPGQTVNNKRVSAASVALLNTSKNGISVTGGITEEQFQTHQQQLVQMQRQQLAQLQQKQQSQHSSQQTHPKAQGSSTSDCMSKTLDSASAHFAASAVVSAPVPSRSEVAKEQNTGHNNINGVVQPSGTSKTLYSTNMALSSSPGISAVQLVRTVGHTTTNHLIPALCTSSPQTLPMNNSCLTNAVHLNNVSVVSPVNVHINTRTSAPSPTALKLATVAASMDRVPKVTPSSAISSIARENHEPERLGLNGIAETTVAMEVT
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
2Phosphorylation------MSKLSFRAR
------CCCHHHHHH		42.1620068231
3Methylation-----MSKLSFRARA
-----CCCHHHHHHH		47.02-
5Phosphorylation---MSKLSFRARALD
---CCCHHHHHHHHH		19.2020068231
15AcetylationARALDAAKPLPIYRG
HHHHHHCCCCCCCCC		49.1326051181
23AcetylationPLPIYRGKDMPDLND
CCCCCCCCCCCCHHH		41.6823749302
42UbiquitinationNRAVPQMPTGMEKEE
CCCCCCCCCCCCCHH		22.1321890473
46UbiquitinationPQMPTGMEKEEESEH
CCCCCCCCCHHHCHH		59.6722817900
60PhosphorylationHHLQRAISAQQVFRE
HHHHHHHHHHHHHHH		21.0228857561
115PhosphorylationLDNEQPDYDMDSEDE
CCCCCCCCCCCCCHH		21.6122210691
119PhosphorylationQPDYDMDSEDETLLN
CCCCCCCCCHHHHHH		40.0726657352
123PhosphorylationDMDSEDETLLNRLNR
CCCCCHHHHHHHHHH		49.2021406692
131UbiquitinationLLNRLNRKMEIKPLQ
HHHHHHHHCCCCCCE		39.5521890473
135UbiquitinationLNRKMEIKPLQFEIM
HHHHCCCCCCEEEHH		26.7722817900
135SumoylationLNRKMEIKPLQFEIM
HHHHCCCCCCEEEHH		26.7728112733
169PhosphorylationLLLNEDDYLIKAVYD
HHCCCCHHHHHHHHH		23.7325159151
195AcetylationPSLIPQIKQEKRDGS
CCCCHHHHHHCCCCC		47.3526051181
195SumoylationPSLIPQIKQEKRDGS
CCCCHHHHHHCCCCC		47.3528112733
215PhosphorylationYVAFRRRTEKMQTRK
HHHHHHHHHHHHHHH		37.8429496963
222AcetylationTEKMQTRKNRKNDEA
HHHHHHHHHCCCCHH		65.5711790817
233UbiquitinationNDEASYEKMLKLRRE
CCHHHHHHHHHHHHH		41.10-
273PhosphorylationLEVVEKRYHLGDYGG
HHHHHHHCCCCCCCH		16.6825884760
291PhosphorylationNEVKISRSEKELYAT
HEEECCCCCCCCEEC		46.35-
298PhosphorylationSEKELYATPATLHNG
CCCCCEECCCEECCC		10.4128555341
322PhosphorylationTKHPHHLSLKEEASD
CCCCCCCCHHHHHHH		32.7924719451
324SumoylationHPHHLSLKEEASDVV
CCCCCCHHHHHHHHH		50.57-
324SumoylationHPHHLSLKEEASDVV
CCCCCCHHHHHHHHH		50.5728112733
348PhosphorylationPKAEALITSQQPTPE
CCCCCEECCCCCCCC		22.7229255136
349PhosphorylationKAEALITSQQPTPET
CCCCEECCCCCCCCC		21.5929255136
353PhosphorylationLITSQQPTPETLPVI
EECCCCCCCCCCCCC		29.4429255136
356PhosphorylationSQQPTPETLPVINKS
CCCCCCCCCCCCCHH		37.2529255136
362SumoylationETLPVINKSDIKQYD
CCCCCCCHHHCCCCC		38.0828112733
408PhosphorylationRRRAGCQYYAPRLDQ
HHCCCCCEECCCHHH		12.9822461510
409PhosphorylationRRAGCQYYAPRLDQA
HCCCCCEECCCHHHC		5.5722461510
430AcetylationSELADLDKLRYRHCL
CCCCCHHHHHHCHHH		42.0126051181
441PhosphorylationRHCLTTLTVPRRCIG
CHHHCCCCCCHHHHH		26.7724719451
490PhosphorylationSFSSSSQTIDFSSNF
HCCCCCCEEECCCCC		25.1830576142
498PhosphorylationIDFSSNFSRTNASSK
EECCCCCCCCCCCCH		42.3130576142
514PhosphorylationCENRLSLSEILSNIR
HCCCCCHHHHHHHHH		21.1522798277
538PhosphorylationRLLNLQDSDSEECTS
HHCCCCCCCCCCHHC		30.0329255136
540PhosphorylationLNLQDSDSEECTSRK
CCCCCCCCCCHHCCC		38.9730266825
544PhosphorylationDSDSEECTSRKPGQT
CCCCCCHHCCCCCCC		34.5423927012
545PhosphorylationSDSEECTSRKPGQTV
CCCCCHHCCCCCCCC		50.3823927012
551PhosphorylationTSRKPGQTVNNKRVS
HCCCCCCCCCCCEEC		30.9929978859
558PhosphorylationTVNNKRVSAASVALL
CCCCCEECHHHHHHH		23.3528555341
558O-linked_GlycosylationTVNNKRVSAASVALL
CCCCCEECHHHHHHH		23.3530059200
561PhosphorylationNKRVSAASVALLNTS
CCEECHHHHHHHHCC		13.9824247654
567PhosphorylationASVALLNTSKNGISV
HHHHHHHCCCCCEEE		40.84-
604UbiquitinationQLAQLQQKQQSQHSS
HHHHHHHHHHHHHCC		37.0329967540
622PhosphorylationHPKAQGSSTSDCMSK
CCCCCCCCHHHHHHH		38.46-
623PhosphorylationPKAQGSSTSDCMSKT
CCCCCCCHHHHHHHH		30.22-
629AcetylationSTSDCMSKTLDSASA
CHHHHHHHHHHHHHH		26.6526051181
656AcetylationPSRSEVAKEQNTGHN
CCHHHHHHHHCCCCC		66.0826051181
688PhosphorylationTNMALSSSPGISAVQ
CCEECCCCCCCCHHH		24.6228555341
750PhosphorylationNVHINTRTSAPSPTA
EEEECCCCCCCCCHH		27.4823403867
750O-linked_GlycosylationNVHINTRTSAPSPTA
EEEECCCCCCCCCHH		27.4830059200
751O-linked_GlycosylationVHINTRTSAPSPTAL
EEECCCCCCCCCHHH		34.5930059200
751PhosphorylationVHINTRTSAPSPTAL
EEECCCCCCCCCHHH		34.5929396449
754PhosphorylationNTRTSAPSPTALKLA
CCCCCCCCCHHHHHH		34.3025159151
756PhosphorylationRTSAPSPTALKLATV
CCCCCCCHHHHHHHH		49.3023403867
774PhosphorylationMDRVPKVTPSSAISS
CCCCCCCCCHHHHHH		24.4720068231
776PhosphorylationRVPKVTPSSAISSIA
CCCCCCCHHHHHHHH		24.0420068231
777PhosphorylationVPKVTPSSAISSIAR
CCCCCCHHHHHHHHH		30.7220068231
780PhosphorylationVTPSSAISSIARENH
CCCHHHHHHHHHHCC		18.5320068231
781PhosphorylationTPSSAISSIARENHE
CCHHHHHHHHHHCCC		17.7220068231
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 EPC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPC2_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 EPC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EZH2_HUMANEZH2physical
22659877
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 EPC2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-538, AND MASSSPECTROMETRY.

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