EPC1_HUMAN - dbPTM
EPC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPC1_HUMAN
UniProt AC Q9H2F5
Protein Name Enhancer of polycomb homolog 1
Gene Name EPC1
Organism Homo sapiens (Human).
Sequence Length 836
Subcellular Localization Nucleus .
Protein Description Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage..
Protein Sequence MSKLSFRARALDASKPLPVFRCEDLPDLHEYASINRAVPQMPTGMEKEEESEHHLQRAISAQQVYGEKRDNMVIPVPEAESNIAYYESIYPGEFKMPKQLIHIQPFSLDAEQPDYDLDSEDEVFVNKLKKKMDICPLQFEEMIDRLEKGSGQQPVSLQEAKLLLKEDDELIREVYEYWIKKRKNCRGPSLIPSVKQEKRDGSSTNDPYVAFRRRTEKMQTRKNRKNDEASYEKMLKLRRDLSRAVTILEMIKRREKSKRELLHLTLEIMEKRYNLGDYNGEIMSEVMAQRQPMKPTYAIPIIPITNSSQFKHQEAMDVKEFKVNKQDKADLIRPKRKYEKKPKVLPSSAAATPQQTSPAALPVFNAKDLNQYDFPSSDEEPLSQVLSGSSEAEEDNDPDGPFAFRRKAGCQYYAPHLDQTGNWPWTSPKDGGLGDVRYRYCLTTLTVPQRCIGFARRRVGRGGRVLLDRAHSDYDSVFHHLDLEMLSSPQHSPVNQFANTSETNTSDKSFSKDLSQILVNIKSCRWRHFRPRTPSLHDSDNDELSCRKLYRSINRTGTAQPGTQTCSTSTQSKSSSGSAHFAFTAEQYQQHQQQLALMQKQQLAQIQQQQANSNSSTNTSQNLASNQQKSGFRLNIQGLERTLQGFVSKTLDSASAQFAASALVTSEQLMGFKMKDDVVLGIGVNGVLPASGVYKGLHLSSTTPTALVHTSPSTAGSALLQPSNITQTSSSHSALSHQVTAANSATTQVLIGNNIRLTVPSSVATVNSIAPINARHIPRTLSAVPSSALKLAAAANCQVSKVPSSSSVDSVPRENHESEKPALNNIADNTVAMEVT
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
------CCCCHHHHH		42.1620068231
3Methylation-----MSKLSFRARA
-----CCCCHHHHHH		47.02-
5Phosphorylation---MSKLSFRARALD
---CCCCHHHHHHCC		19.2020068231
14PhosphorylationRARALDASKPLPVFR
HHHHCCCCCCCCEEE		34.1824719451
18UbiquitinationLDASKPLPVFRCEDL
CCCCCCCCEEECCCC		31.5629967540
60PhosphorylationHHLQRAISAQQVYGE
HHHHHHHHHHHHHCC		21.0224247654
68UbiquitinationAQQVYGEKRDNMVIP
HHHHHCCCCCCCEEE		61.7729967540
77UbiquitinationDNMVIPVPEAESNIA
CCCEEECCCHHHCEE		29.7129967540
98UbiquitinationPGEFKMPKQLIHIQP
CCCCCCCCEEEEEEC		54.9929967540
115PhosphorylationLDAEQPDYDLDSEDE
CCCCCCCCCCCCCCH		25.7022199227
119PhosphorylationQPDYDLDSEDEVFVN
CCCCCCCCCCHHHHH		55.0022617229
148UbiquitinationEMIDRLEKGSGQQPV
HHHHHHHCCCCCCCC		64.0729967540
175PhosphorylationDELIREVYEYWIKKR
HHHHHHHHHHHHHHC		9.8822817900
189PhosphorylationRKNCRGPSLIPSVKQ
CCCCCCCCCCCCCCC		41.58-
193PhosphorylationRGPSLIPSVKQEKRD
CCCCCCCCCCCCCCC		34.6529449344
195AcetylationPSLIPSVKQEKRDGS
CCCCCCCCCCCCCCC		58.0126051181
215PhosphorylationYVAFRRRTEKMQTRK
HHHHHHHHHHHHHHH		37.8429496963
222AcetylationTEKMQTRKNRKNDEA
HHHHHHHHHCCCCHH		65.5711790931
230PhosphorylationNRKNDEASYEKMLKL
HCCCCHHHHHHHHHH		31.6026074081
231PhosphorylationRKNDEASYEKMLKLR
CCCCHHHHHHHHHHH		26.9826074081
233UbiquitinationNDEASYEKMLKLRRD
CCHHHHHHHHHHHHH		41.10-
242PhosphorylationLKLRRDLSRAVTILE
HHHHHHHHHHHHHHH		23.6026074081
246PhosphorylationRDLSRAVTILEMIKR
HHHHHHHHHHHHHHH		20.8926074081
257PhosphorylationMIKRREKSKRELLHL
HHHHHHHHHHHHHHH		31.9926074081
284PhosphorylationDYNGEIMSEVMAQRQ
CCCCHHHHHHHHHCC		32.4724719451
294AcetylationMAQRQPMKPTYAIPI
HHHCCCCCCCEEEEE		40.6723236377
319SumoylationHQEAMDVKEFKVNKQ
CCCCCCHHHHCCCCC		53.8428112733
347PhosphorylationKKPKVLPSSAAATPQ
CCCCCCCCCCCCCCC		28.5729978859
348PhosphorylationKPKVLPSSAAATPQQ
CCCCCCCCCCCCCCC		21.7129978859
352PhosphorylationLPSSAAATPQQTSPA
CCCCCCCCCCCCCCC		19.5326055452
355PhosphorylationSAAATPQQTSPAALP
CCCCCCCCCCCCCCC		45.1932142685
356PhosphorylationAAATPQQTSPAALPV
CCCCCCCCCCCCCCC		31.2825159151
357PhosphorylationAATPQQTSPAALPVF
CCCCCCCCCCCCCCC		14.2725159151
376PhosphorylationLNQYDFPSSDEEPLS
HCCCCCCCCCCCCHH		50.8732142685
426PhosphorylationQTGNWPWTSPKDGGL
CCCCCCCCCCCCCCC		30.9525159151
427PhosphorylationTGNWPWTSPKDGGLG
CCCCCCCCCCCCCCC		26.5328348404
441AcetylationGDVRYRYCLTTLTVP
CCCEEEEEEEEEECC		1.6919608861
462AcetylationARRRVGRGGRVLLDR
HHHHCCCCCCEEECC		23.4819608861
468PhosphorylationRGGRVLLDRAHSDYD
CCCCEEECCCCCCCH		41.3733259812
488PhosphorylationLDLEMLSSPQHSPVN
CCHHHHCCCCCCCCH		25.3125921289
489PhosphorylationDLEMLSSPQHSPVNQ
CHHHHCCCCCCCCHH		32.3133259812
492PhosphorylationMLSSPQHSPVNQFAN
HHCCCCCCCCHHCCC		25.8725921289
509PhosphorylationETNTSDKSFSKDLSQ
CCCCCCCCCCHHHHH		39.4824719451
512AcetylationTSDKSFSKDLSQILV
CCCCCCCHHHHHHHH		61.7623954790
522UbiquitinationSQILVNIKSCRWRHF
HHHHHHHHHCCCCCC		38.00-
533PhosphorylationWRHFRPRTPSLHDSD
CCCCCCCCCCCCCCC		21.6627794612
535PhosphorylationHFRPRTPSLHDSDND
CCCCCCCCCCCCCCC		37.4122617229
539PhosphorylationRTPSLHDSDNDELSC
CCCCCCCCCCCHHHH		27.8023898821
545PhosphorylationDSDNDELSCRKLYRS
CCCCCHHHHHHHHHH		15.1629978859
573AcetylationCSTSTQSKSSSGSAH
CCCCCCCCCCCCCEE		44.5326051181
625PhosphorylationNTSQNLASNQQKSGF
CHHHHHHHHHHCCCE		38.03-
630PhosphorylationLASNQQKSGFRLNIQ
HHHHHHCCCEEEEHH		38.53-
673SumoylationSEQLMGFKMKDDVVL
HHHHCCCCCCCCEEE		39.0328112733
723O-linked_GlycosylationGSALLQPSNITQTSS
CCCCCCCCCCEECCC		28.0930379171
736O-linked_GlycosylationSSSHSALSHQVTAAN
CCCHHHHHHCCCCCC		16.1630379171
756MethylationVLIGNNIRLTVPSSV
EEECCCEEEECCCCE		26.82-
780PhosphorylationNARHIPRTLSAVPSS
CCCCCCCCCCCCCHH		21.5130001349
780O-linked_GlycosylationNARHIPRTLSAVPSS
CCCCCCCCCCCCCHH		21.5130379171
782PhosphorylationRHIPRTLSAVPSSAL
CCCCCCCCCCCHHHH		26.9729978859
787PhosphorylationTLSAVPSSALKLAAA
CCCCCCHHHHHHHHH		31.3924719451
801AcetylationAANCQVSKVPSSSSV
HCCCEEEECCCCCCC		60.3525953088
801UbiquitinationAANCQVSKVPSSSSV
HCCCEEEECCCCCCC		60.35-
807PhosphorylationSKVPSSSSVDSVPRE
EECCCCCCCCCCCCC		31.7128857561
820AcetylationRENHESEKPALNNIA
CCCCCCCCCCHHCCC		44.8925953088
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 EPC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPC1_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 EPC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRF_HUMANSRFphysical
19359245
E2F6_HUMANE2F6physical
15536069
EZH2_HUMANEZH2physical
15536069
EED_HUMANEEDphysical
15536069
TRI27_HUMANTRIM27physical
10976108
HOP_HUMANHOPXphysical
17192267
TRRAP_HUMANTRRAPphysical
27153538
EP400_HUMANEP400physical
27153538
BRD8_HUMANBRD8physical
27153538
MBTD1_HUMANMBTD1physical
27153538
DMAP1_HUMANDMAP1physical
27153538
KAT5_HUMANKAT5physical
27153538
ING3_HUMANING3physical
27153538
RUVB1_HUMANRUVBL1physical
27153538
RUVB2_HUMANRUVBL2physical
27153538
VPS72_HUMANVPS72physical
27153538
ACTB_HUMANACTBphysical
27153538
MRGBP_HUMANMRGBPphysical
27153538
YETS4_HUMANYEATS4physical
27153538
EAF6_HUMANMEAF6physical
27153538
MO4L1_HUMANMORF4L1physical
27153538
MO4L2_HUMANMORF4L2physical
27153538
ACL6A_HUMANACTL6Aphysical
27153538
H2AZ_HUMANH2AFZphysical
27153538
MYCL_HUMANMYCLphysical
29028833
PP2AA_HUMANPPP2CAphysical
29028833
DMAP1_HUMANDMAP1physical
29028833
KAT5_HUMANKAT5physical
29028833
TRRAP_HUMANTRRAPphysical
29028833
EP400_HUMANEP400physical
29028833
VPS72_HUMANVPS72physical
29028833
MAX_HUMANMAXphysical
29028833
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 EPC1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-512, AND MASS SPECTROMETRY.
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-357, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND MASSSPECTROMETRY.

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