KDM4C_HUMAN - dbPTM
KDM4C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KDM4C_HUMAN
UniProt AC Q9H3R0
Protein Name Lysine-specific demethylase 4C
Gene Name KDM4C
Organism Homo sapiens (Human).
Sequence Length 1056
Subcellular Localization Nucleus .
Protein Description Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate..
Protein Sequence MEVAEVESPLNPSCKIMTFRPSMEEFREFNKYLAYMESKGAHRAGLAKVIPPKEWKPRQCYDDIDNLLIPAPIQQMVTGQSGLFTQYNIQKKAMTVKEFRQLANSGKYCTPRYLDYEDLERKYWKNLTFVAPIYGADINGSIYDEGVDEWNIARLNTVLDVVEEECGISIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAQGFFPSSSQGCDAFLRHKMTLISPSVLKKYGIPFDKITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATVRWIDYGKVAKLCTCRKDMVKISMDIFVRKFQPDRYQLWKQGKDIYTIDHTKPTPASTPEVKAWLQRRRKVRKASRSFQCARSTSKRPKADEEEEVSDEVDGAEVPNPDSVTDDLKVSEKSEAAVKLRNTEASSEEESSASRMQVEQNLSDHIKLSGNSCLSTSVTEDIKTEDDKAYAYRSVPSISSEADDSIPLSSGYEKPEKSDPSELSWPKSPESCSSVAESNGVLTEGEESDVESHGNGLEPGEIPAVPSGERNSFKVPSIAEGENKTSKSWRHPLSRPPARSPMTLVKQQAPSDEELPEVLSIEEEVEETESWAKPLIHLWQTKSPNFAAEQEYNATVARMKPHCAICTLLMPYHKPDSSNEENDARWETKLDEVVTSEGKTKPLIPEMCFIYSEENIEYSPPNAFLEEDGTSLLISCAKCCVRVHASCYGIPSHEICDGWLCARCKRNAWTAECCLCNLRGGALKQTKNNKWAHVMCAVAVPEVRFTNVPERTQIDVGRIPLQRLKLKCIFCRHRVKRVSGACIQCSYGRCPASFHVTCAHAAGVLMEPDDWPYVVNITCFRHKVNPNVKSKACEKVISVGQTVITKHRNTRYYSCRVMAVTSQTFYEVMFDDGSFSRDTFPEDIVSRDCLKLGPPAEGEVVQVKWPDGKLYGAKYFGSNIAHMYQVEFEDGSQIAMKREDIYTLDEELPKRVKARFSTASDMRFEDTFYGADIIQGERKRQRVLSSRFKNEYVADPVYRTFLKSSFQKKCQKRQ
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
8PhosphorylationMEVAEVESPLNPSCK
CCCEECCCCCCCCCE		39.6025159151
31UbiquitinationEEFREFNKYLAYMES
HHHHHHHHHHHHHHC		47.14-
39UbiquitinationYLAYMESKGAHRAGL
HHHHHHCCCCHHCCC		46.97-
61PhosphorylationEWKPRQCYDDIDNLL
CCCCCCCCCCCCCCE		14.3324043423
78PhosphorylationAPIQQMVTGQSGLFT
CCHHHHHHCCCCCCH		24.9424043423
81PhosphorylationQQMVTGQSGLFTQYN
HHHHHCCCCCCHHHC		38.5224043423
85PhosphorylationTGQSGLFTQYNIQKK
HCCCCCCHHHCHHHH		34.8824043423
87PhosphorylationQSGLFTQYNIQKKAM
CCCCCHHHCHHHHCC		15.9224043423
97UbiquitinationQKKAMTVKEFRQLAN
HHHCCCHHHHHHHHH		41.80-
107UbiquitinationRQLANSGKYCTPRYL
HHHHHCCCCCCCCCC		36.65-
185PhosphorylationLYFGMWKTTFAWHTE
EEEEEEEEEEEEECC		16.1926552605
186PhosphorylationYFGMWKTTFAWHTED
EEEEEEEEEEEECCC		13.9726552605
191PhosphorylationKTTFAWHTEDMDLYS
EEEEEEECCCCCEEE		23.9926552605
197PhosphorylationHTEDMDLYSINYLHF
ECCCCCEEEEEEEEC		11.8424719451
198PhosphorylationTEDMDLYSINYLHFG
CCCCCEEEEEEEECC		16.2024719451
201PhosphorylationMDLYSINYLHFGEPK
CCEEEEEEEECCCCC		10.4124719451
243UbiquitinationCDAFLRHKMTLISPS
HHHHHHHCCEEECHH		27.44-
245PhosphorylationAFLRHKMTLISPSVL
HHHHHCCEEECHHHH		26.24-
248PhosphorylationRHKMTLISPSVLKKY
HHCCEEECHHHHHHH		17.78-
250PhosphorylationKMTLISPSVLKKYGI
CCEEECHHHHHHHCC		33.04-
254UbiquitinationISPSVLKKYGIPFDK
ECHHHHHHHCCCHHH		44.54-
303UbiquitinationVRWIDYGKVAKLCTC
EEEEEHHHHHHHCCC		32.56-
306UbiquitinationIDYGKVAKLCTCRKD
EEHHHHHHHCCCCHH		47.27-
335UbiquitinationPDRYQLWKQGKDIYT
CCHHHHHHCCCCEEE		58.74-
338UbiquitinationYQLWKQGKDIYTIDH
HHHHHCCCCEEEECC		38.16-
349PhosphorylationTIDHTKPTPASTPEV
EECCCCCCCCCCHHH		32.8028555341
352PhosphorylationHTKPTPASTPEVKAW
CCCCCCCCCHHHHHH		45.7828555341
353PhosphorylationTKPTPASTPEVKAWL
CCCCCCCCHHHHHHH		26.1025159151
357UbiquitinationPASTPEVKAWLQRRR
CCCCHHHHHHHHHHH		31.98-
370PhosphorylationRRKVRKASRSFQCAR
HHHHHHHHHHHHHHH		31.3428102081
372PhosphorylationKVRKASRSFQCARST
HHHHHHHHHHHHHCC		19.7128102081
392PhosphorylationADEEEEVSDEVDGAE
CCCCCCCCCCCCCCC		31.1924260401
425PhosphorylationAAVKLRNTEASSEEE
HHHHHHCCCCCCHHH		26.8828102081
428PhosphorylationKLRNTEASSEEESSA
HHHCCCCCCHHHHHH		31.8628450419
429PhosphorylationLRNTEASSEEESSAS
HHCCCCCCHHHHHHH		56.9528450419
433PhosphorylationEASSEEESSASRMQV
CCCCHHHHHHHHHHH		34.1928102081
434PhosphorylationASSEEESSASRMQVE
CCCHHHHHHHHHHHH		33.2828102081
436PhosphorylationSEEESSASRMQVEQN
CHHHHHHHHHHHHHH		30.1828102081
445PhosphorylationMQVEQNLSDHIKLSG
HHHHHHHHHCEEECC		34.3928555341
457PhosphorylationLSGNSCLSTSVTEDI
ECCCCCCCCCCCCCC		23.9828102081
458PhosphorylationSGNSCLSTSVTEDIK
CCCCCCCCCCCCCCC		17.8028102081
459PhosphorylationGNSCLSTSVTEDIKT
CCCCCCCCCCCCCCC		24.5425627689
461PhosphorylationSCLSTSVTEDIKTED
CCCCCCCCCCCCCCC		27.9228102081
476PhosphorylationDKAYAYRSVPSISSE
CHHHEEECCCCCCCC		26.2123186163
479PhosphorylationYAYRSVPSISSEADD
HEEECCCCCCCCCCC		32.7128450419
481PhosphorylationYRSVPSISSEADDSI
EECCCCCCCCCCCCC		26.8528450419
482PhosphorylationRSVPSISSEADDSIP
ECCCCCCCCCCCCCC		34.8228450419
487PhosphorylationISSEADDSIPLSSGY
CCCCCCCCCCCCCCC		27.0128450419
500PhosphorylationGYEKPEKSDPSELSW
CCCCCCCCCHHHCCC		53.7623403867
503PhosphorylationKPEKSDPSELSWPKS
CCCCCCHHHCCCCCC		57.0423403867
506PhosphorylationKSDPSELSWPKSPES
CCCHHHCCCCCCHHH		36.9623403867
570PhosphorylationGENKTSKSWRHPLSR
CCCCCCCCCCCCCCC		29.16-
576PhosphorylationKSWRHPLSRPPARSP
CCCCCCCCCCCCCCC		47.38-
582PhosphorylationLSRPPARSPMTLVKQ
CCCCCCCCCCCEEEE		22.5628555341
593PhosphorylationLVKQQAPSDEELPEV
EEEECCCCCCCCCCC		61.7526074081
602PhosphorylationEELPEVLSIEEEVEE
CCCCCCCCHHHHHHH		32.8828348404
610PhosphorylationIEEEVEETESWAKPL
HHHHHHHCCCCHHHH		23.0828102081
612PhosphorylationEEVEETESWAKPLIH
HHHHHCCCCHHHHHH		39.4928102081
625PhosphorylationIHLWQTKSPNFAAEQ
HHHHHCCCCCCHHHH		28.5928555341
671UbiquitinationNDARWETKLDEVVTS
CHHHHHHHHHHHHCC		42.29-
772AcetylationLKQTKNNKWAHVMCA
CEECCCCCCEEEEEE		55.9712436875
809UbiquitinationPLQRLKLKCIFCRHR
CHHHHHHEEEEECHH		24.56-
903PhosphorylationSCRVMAVTSQTFYEV
EEEEEEEECCEEEEE		12.94-
906PhosphorylationVMAVTSQTFYEVMFD
EEEEECCEEEEEECC		28.14-
908PhosphorylationAVTSQTFYEVMFDDG
EEECCEEEEEECCCC		15.82-
916PhosphorylationEVMFDDGSFSRDTFP
EEECCCCCCCCCCCC		27.35-
918PhosphorylationMFDDGSFSRDTFPED
ECCCCCCCCCCCCHH		30.83-
933UbiquitinationIVSRDCLKLGPPAEG
HHCCHHHHCCCCCCC		58.70-
946UbiquitinationEGEVVQVKWPDGKLY
CCCEEEEECCCCCEE		35.60-
951UbiquitinationQVKWPDGKLYGAKYF
EEECCCCCEEEEEEC		46.01-
985PhosphorylationMKREDIYTLDEELPK
EEHHHEEECCHHHCH		28.24-
992UbiquitinationTLDEELPKRVKARFS
ECCHHHCHHHHHHCC		80.56-
1009PhosphorylationSDMRFEDTFYGADII
CCCCCCCCCCCCCCC		16.14-
1028PhosphorylationKRQRVLSSRFKNEYV
HHHHHHHHHCCCCCC		37.2624719451
1031SumoylationRVLSSRFKNEYVADP
HHHHHHCCCCCCCCH		48.00-
1031SumoylationRVLSSRFKNEYVADP
HHHHHHCCCCCCCCH		48.00-
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
918SPhosphorylationKinasePKRP19525
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KDM4C_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 KDM4C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM4A_HUMANKDM4Aphysical
17207460
KDM4C_HUMANKDM4Cphysical
17207460
H31_HUMANHIST1H3Aphysical
16732293
HDAC1_HUMANHDAC1physical
21637537
HDAC3_HUMANHDAC3physical
21637537
H32_HUMANHIST2H3Cphysical
21575637
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KDM4C_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND MASSSPECTROMETRY.

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