CHD4_HUMAN - dbPTM
CHD4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHD4_HUMAN
UniProt AC Q14839
Protein Name Chromodomain-helicase-DNA-binding protein 4
Gene Name CHD4
Organism Homo sapiens (Human).
Sequence Length 1912
Subcellular Localization Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Associates with centrosomes in interphase.
Protein Description Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones..
Protein Sequence MASGLGSPSPCSAGSEEEDMDALLNNSLPPPHPENEEDPEEDLSETETPKLKKKKKPKKPRDPKIPKSKRQKKERMLLCRQLGDSSGEGPEFVEEEEEVALRSDSEGSDYTPGKKKKKKLGPKKEKKSKSKRKEEEEEEDDDDDSKEPKSSAQLLEDWGMEDIDHVFSEEDYRTLTNYKAFSQFVRPLIAAKNPKIAVSKMMMVLGAKWREFSTNNPFKGSSGASVAAAAAAAVAVVESMVTATEVAPPPPPVEVPIRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPKKVAPLKIKLGGFGSKRKRSSSEDDDLDVESDFDDASINSYSVSDGSTSRSSRSRKKLRTTKKKKKGEEEVTAVDGYETDHQDYCEVCQQGGEIILCDTCPRAYHMVCLDPDMEKAPEGKWSCPHCEKEGIQWEAKEDNSEGEEILEEVGGDLEEEDDHHMEFCRVCKDGGELLCCDTCPSSYHIHCLNPPLPEIPNGEWLCPRCTCPALKGKVQKILIWKWGQPPSPTPVPRPPDADPNTPSPKPLEGRPERQFFVKWQGMSYWHCSWVSELQLELHCQVMFRNYQRKNDMDEPPSGDFGGDEEKSRKRKNKDPKFAEMEERFYRYGIKPEWMMIHRILNHSVDKKGHVHYLIKWRDLPYDQASWESEDVEIQDYDLFKQSYWNHRELMRGEEGRPGKKLKKVKLRKLERPPETPTVDPTVKYERQPEYLDATGGTLHPYQMEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVGDKDSRAIIRENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRRLKADVFKNMPSKTELIVRVELSPMQKKYYKYILTRNFEALNARGGGNQVSLLNVVMDLKKCCNHPYLFPVAAMEAPKMPNGMYDGSALIRASGKLLLLQKMLKNLKEGGHRVLIFSQMTKMLDLLEDFLEHEGYKYERIDGGITGNMRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKKKMMLTHLVVRPGLGSKTGSMSKQELDDILKFGTEELFKDEATDGGGDNKEGEDSSVIHYDDKAIERLLDRNQDETEDTELQGMNEYLSSFKVAQYVVREEEMGEEEEVEREIIKQEESVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDGSQEDRDWQDDQSDNQSDYSVASEEGDEDFDERSEAPRRPSRKGLRNDKDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRYGMPPQDAFTTQWLVRDLRGKSEKEFKAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLIRKKVQEFEHVNGRWSMPELAEVEENKKMSQPGSPSPKTPTPSTPGDTQPNTPAPVPPAEDGIKIEENSLKEEESIEGEKEVKSTAPETAIECTQAPAPASEDEKVVVEPPEGEEKVEKAEVKERTEEPMETEPKGAADVEKVEEKSAIDLTPIVVEDKEEKKEEEEKKEVMLQNGETPKDLNDEKQKKNIKQRFMFNIADGGFTELHSLWQNEERAATVTKKTYEIWHRRHDYWLLAGIINHGYARWQDIQNDPRYAILNEPFKGEMNRGNFLEIKNKFLARRFKLLEQALVIEEQLRRAAYLNMSEDPSHPSMALNTRFAEVECLAESHQHLSKESMAGNKPANAVLHKVLKQLEELLSDMKADVTRLPATIARIPPVAVRLQMSERNILSRLANRAPEPTPQQVAQQQ
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
3Phosphorylation-----MASGLGSPSP
-----CCCCCCCCCC
46.5422468782
7Phosphorylation-MASGLGSPSPCSAG
-CCCCCCCCCCCCCC
27.5225921289
9PhosphorylationASGLGSPSPCSAGSE
CCCCCCCCCCCCCCC
39.9922468782
12PhosphorylationLGSPSPCSAGSEEED
CCCCCCCCCCCCHHH
38.7622468782
15PhosphorylationPSPCSAGSEEEDMDA
CCCCCCCCCHHHHHH
41.3625921289
27PhosphorylationMDALLNNSLPPPHPE
HHHHHHCCCCCCCCC
40.9726074081
44PhosphorylationEDPEEDLSETETPKL
CCCHHCCCCCCCHHH
55.5920164059
46PhosphorylationPEEDLSETETPKLKK
CHHCCCCCCCHHHCC
41.6129632367
48PhosphorylationEDLSETETPKLKKKK
HCCCCCCCHHHCCCC
32.8920363803
85PhosphorylationLCRQLGDSSGEGPEF
HHHHHCCCCCCCCCC
38.1430266825
86PhosphorylationCRQLGDSSGEGPEFV
HHHHCCCCCCCCCCC
45.6730266825
103PhosphorylationEEEVALRSDSEGSDY
HHHHHHCCCCCCCCC
46.4623927012
105PhosphorylationEVALRSDSEGSDYTP
HHHHCCCCCCCCCCC
45.1423927012
108PhosphorylationLRSDSEGSDYTPGKK
HCCCCCCCCCCCCCH
24.3223927012
110PhosphorylationSDSEGSDYTPGKKKK
CCCCCCCCCCCCHHC
19.2823927012
111PhosphorylationDSEGSDYTPGKKKKK
CCCCCCCCCCCHHCC
30.4723927012
115AcetylationSDYTPGKKKKKKLGP
CCCCCCCHHCCCCCC
75.61130039
116AcetylationDYTPGKKKKKKLGPK
CCCCCCHHCCCCCCC
73.62130011
118AcetylationTPGKKKKKKLGPKKE
CCCCHHCCCCCCCHH
63.21130043
119AcetylationPGKKKKKKLGPKKEK
CCCHHCCCCCCCHHC
68.50130027
123AcetylationKKKKLGPKKEKKSKS
HCCCCCCCHHCCCHH
72.30130019
133SumoylationKKSKSKRKEEEEEED
CCCHHHHHHHHHCCC
73.5428112733
145PhosphorylationEEDDDDDSKEPKSSA
CCCCCCCCCCCHHHH
46.0130108239
146SumoylationEDDDDDSKEPKSSAQ
CCCCCCCCCCHHHHH
82.2528112733
150PhosphorylationDDSKEPKSSAQLLED
CCCCCCHHHHHHHHH
41.4422617229
151PhosphorylationDSKEPKSSAQLLEDW
CCCCCHHHHHHHHHH
26.5922617229
168PhosphorylationEDIDHVFSEEDYRTL
CCCCCCCCHHHHHHH
38.7027067055
179SumoylationYRTLTNYKAFSQFVR
HHHHHCHHHHHHHHH
45.0528112733
179UbiquitinationYRTLTNYKAFSQFVR
HHHHHCHHHHHHHHH
45.05-
179 (in isoform 2)Ubiquitination-45.05-
182PhosphorylationLTNYKAFSQFVRPLI
HHCHHHHHHHHHHHH
27.8026846344
195UbiquitinationLIAAKNPKIAVSKMM
HHHCCCHHHHHHHHH
53.33-
200AcetylationNPKIAVSKMMMVLGA
CHHHHHHHHHHHHCC
24.9825953088
221PhosphorylationTNNPFKGSSGASVAA
CCCCCCCCHHHHHHH
26.6225627689
222PhosphorylationNNPFKGSSGASVAAA
CCCCCCCHHHHHHHH
47.2325627689
225PhosphorylationFKGSSGASVAAAAAA
CCCCHHHHHHHHHHH
18.8027251275
273AcetylationKGPNARRKPKGSPRV
CCCCCCCCCCCCCCC
45.59130015
275AcetylationPNARRKPKGSPRVPD
CCCCCCCCCCCCCCC
75.06130031
277PhosphorylationARRKPKGSPRVPDAK
CCCCCCCCCCCCCCC
18.6925159151
285AcetylationPRVPDAKKPKPKKVA
CCCCCCCCCCCCCCC
61.05130035
295AcetylationPKKVAPLKIKLGGFG
CCCCCCCEEECCCCC
36.4125953088
297AcetylationKVAPLKIKLGGFGSK
CCCCCEEECCCCCCC
39.2225953088
297SumoylationKVAPLKIKLGGFGSK
CCCCCEEECCCCCCC
39.2228112733
297UbiquitinationKVAPLKIKLGGFGSK
CCCCCEEECCCCCCC
39.22-
303PhosphorylationIKLGGFGSKRKRSSS
EECCCCCCCCCCCCC
27.3323401153
304AcetylationKLGGFGSKRKRSSSE
ECCCCCCCCCCCCCC
63.4223749302
304SumoylationKLGGFGSKRKRSSSE
ECCCCCCCCCCCCCC
63.4228112733
304UbiquitinationKLGGFGSKRKRSSSE
ECCCCCCCCCCCCCC
63.42-
308PhosphorylationFGSKRKRSSSEDDDL
CCCCCCCCCCCCCCC
41.0521955146
309PhosphorylationGSKRKRSSSEDDDLD
CCCCCCCCCCCCCCC
41.6026503892
310PhosphorylationSKRKRSSSEDDDLDV
CCCCCCCCCCCCCCC
46.4121955146
319PhosphorylationDDDLDVESDFDDASI
CCCCCCCCCCCCCCC
43.3526503892
325PhosphorylationESDFDDASINSYSVS
CCCCCCCCCEEEECC
29.3321955146
328PhosphorylationFDDASINSYSVSDGS
CCCCCCEEEECCCCC
19.6721955146
329PhosphorylationDDASINSYSVSDGST
CCCCCEEEECCCCCC
14.4921955146
330PhosphorylationDASINSYSVSDGSTS
CCCCEEEECCCCCCC
18.2421955146
332PhosphorylationSINSYSVSDGSTSRS
CCEEEECCCCCCCCC
30.2520068231
335PhosphorylationSYSVSDGSTSRSSRS
EEECCCCCCCCCHHH
28.3520068231
336PhosphorylationYSVSDGSTSRSSRSR
EECCCCCCCCCHHHH
33.4220068231
337PhosphorylationSVSDGSTSRSSRSRK
ECCCCCCCCCHHHHH
31.6820068231
360PhosphorylationKKGEEEVTAVDGYET
CCCCCCCEEECCCCC
25.0130576142
365PhosphorylationEVTAVDGYETDHQDY
CCEEECCCCCCCHHH
15.9325849741
367PhosphorylationTAVDGYETDHQDYCE
EEECCCCCCCHHHHH
30.2325849741
372PhosphorylationYETDHQDYCEVCQQG
CCCCCHHHHHHHHCC
5.5025849741
403 (in isoform 2)Ubiquitination-63.70-
428PhosphorylationWEAKEDNSEGEEILE
EEECCCCCCHHHHHH
60.3422167270
499AcetylationRCTCPALKGKVQKIL
CCCCHHHCCCEEEEE
59.8125953088
499UbiquitinationRCTCPALKGKVQKIL
CCCCHHHCCCEEEEE
59.81-
499 (in isoform 2)Ubiquitination-59.81-
501 (in isoform 2)Ubiquitination-39.65-
504AcetylationALKGKVQKILIWKWG
HHCCCEEEEEEEECC
42.3325953088
504UbiquitinationALKGKVQKILIWKWG
HHCCCEEEEEEEECC
42.3321890473
504 (in isoform 1)Ubiquitination-42.3321890473
504 (in isoform 2)Ubiquitination-42.3321890473
515PhosphorylationWKWGQPPSPTPVPRP
EECCCCCCCCCCCCC
48.3525159151
517PhosphorylationWGQPPSPTPVPRPPD
CCCCCCCCCCCCCCC
41.0525159151
529PhosphorylationPPDADPNTPSPKPLE
CCCCCCCCCCCCCCC
30.4529255136
531PhosphorylationDADPNTPSPKPLEGR
CCCCCCCCCCCCCCC
43.4429255136
533UbiquitinationDPNTPSPKPLEGRPE
CCCCCCCCCCCCCCC
67.58-
574PhosphorylationCQVMFRNYQRKNDMD
HHHHCHHCCCCCCCC
12.8730576142
577AcetylationMFRNYQRKNDMDEPP
HCHHCCCCCCCCCCC
41.6026051181
577 (in isoform 2)Ubiquitination-41.60-
580SulfoxidationNYQRKNDMDEPPSGD
HCCCCCCCCCCCCCC
9.8121406390
585PhosphorylationNDMDEPPSGDFGGDE
CCCCCCCCCCCCCCH
62.8121815630
594AcetylationDFGGDEEKSRKRKNK
CCCCCHHHHHHHCCC
54.2126051181
594UbiquitinationDFGGDEEKSRKRKNK
CCCCCHHHHHHHCCC
54.21-
594 (in isoform 2)Ubiquitination-54.21-
604UbiquitinationKRKNKDPKFAEMEER
HHCCCCCCHHHHHHH
68.30-
604 (in isoform 2)Ubiquitination-68.30-
613PhosphorylationAEMEERFYRYGIKPE
HHHHHHHHHCCCCHH
14.7829083192
615PhosphorylationMEERFYRYGIKPEWM
HHHHHHHCCCCHHHH
16.3029083192
618SumoylationRFYRYGIKPEWMMIH
HHHHCCCCHHHHHHH
32.30-
618AcetylationRFYRYGIKPEWMMIH
HHHHCCCCHHHHHHH
32.3026051181
618SumoylationRFYRYGIKPEWMMIH
HHHHCCCCHHHHHHH
32.30-
618UbiquitinationRFYRYGIKPEWMMIH
HHHHCCCCHHHHHHH
32.30-
631PhosphorylationIHRILNHSVDKKGHV
HHHHHCCCCCCCCCE
30.8230001349
634AcetylationILNHSVDKKGHVHYL
HHCCCCCCCCCEEEE
59.5025953088
634UbiquitinationILNHSVDKKGHVHYL
HHCCCCCCCCCEEEE
59.50-
635UbiquitinationLNHSVDKKGHVHYLI
HCCCCCCCCCEEEEE
50.19-
635 (in isoform 2)Ubiquitination-50.19-
668UbiquitinationIQDYDLFKQSYWNHR
ECCHHHHHHHHCCHH
45.70-
679MethylationWNHRELMRGEEGRPG
CCHHHHHCCCCCCCC
63.09-
696SumoylationLKKVKLRKLERPPET
CCCCEEECCCCCCCC
66.2028112733
696UbiquitinationLKKVKLRKLERPPET
CCCCEEECCCCCCCC
66.20-
703PhosphorylationKLERPPETPTVDPTV
CCCCCCCCCCCCCCC
29.9923401153
705PhosphorylationERPPETPTVDPTVKY
CCCCCCCCCCCCCCC
44.9830266825
709PhosphorylationETPTVDPTVKYERQP
CCCCCCCCCCCCCCC
25.7628450419
711SumoylationPTVDPTVKYERQPEY
CCCCCCCCCCCCCHH
43.82-
711AcetylationPTVDPTVKYERQPEY
CCCCCCCCCCCCCHH
43.8226051181
711SumoylationPTVDPTVKYERQPEY
CCCCCCCCCCCCCHH
43.82-
711UbiquitinationPTVDPTVKYERQPEY
CCCCCCCCCCCCCHH
43.82-
712PhosphorylationTVDPTVKYERQPEYL
CCCCCCCCCCCCHHC
16.4126074081
822PhosphorylationIIRENEFSFEDNAIR
EEECCCCCCCHHCCC
22.8821601212
832UbiquitinationDNAIRGGKKASRMKK
HHCCCCCHHHHHCCH
48.25-
850PhosphorylationVKFHVLLTSYELITI
HHHEEECCHHEEEEC
25.7120068231
851PhosphorylationKFHVLLTSYELITID
HHEEECCHHEEEECC
19.3120068231
884AcetylationRLKNNQSKFFRVLNG
HHHCCCCHHHHHHCC
38.4619608861
884UbiquitinationRLKNNQSKFFRVLNG
HHHCCCCHHHHHHCC
38.46-
945AcetylationAKEDQIKKLHDMLGP
HHHHHHHHHHHHHCH
53.3226051181
959UbiquitinationPHMLRRLKADVFKNM
HHHHHHHHHHHHHCC
40.50-
964AcetylationRLKADVFKNMPSKTE
HHHHHHHHCCCCCCE
52.7826822725
964UbiquitinationRLKADVFKNMPSKTE
HHHHHHHHCCCCCCE
52.78-
979PhosphorylationLIVRVELSPMQKKYY
EEEEEEECHHHHHHH
12.5730622161
984AcetylationELSPMQKKYYKYILT
EECHHHHHHHHHHHH
36.60-
984 (in isoform 2)Ubiquitination-36.60-
987AcetylationPMQKKYYKYILTRNF
HHHHHHHHHHHHCCH
23.7922644589
987UbiquitinationPMQKKYYKYILTRNF
HHHHHHHHHHHHCCH
23.7919608861
987 (in isoform 1)Ubiquitination-23.7921890473
987 (in isoform 2)Ubiquitination-23.7921890473
988PhosphorylationMQKKYYKYILTRNFE
HHHHHHHHHHHCCHH
5.76-
991PhosphorylationKYYKYILTRNFEALN
HHHHHHHHCCHHHHH
17.63-
1000MethylationNFEALNARGGGNQVS
CHHHHHCCCCCCHHH
43.12-
1007PhosphorylationRGGGNQVSLLNVVMD
CCCCCHHHHHHHHHH
19.8520860994
1013SulfoxidationVSLLNVVMDLKKCCN
HHHHHHHHHHHHHCC
4.3221406390
1016AcetylationLNVVMDLKKCCNHPY
HHHHHHHHHHCCCCC
39.2326051181
1016UbiquitinationLNVVMDLKKCCNHPY
HHHHHHHHHHCCCCC
39.2321906983
1016 (in isoform 1)Ubiquitination-39.2321890473
1016 (in isoform 2)Ubiquitination-39.2321890473
1017AcetylationNVVMDLKKCCNHPYL
HHHHHHHHHCCCCCC
51.8524431269
1017UbiquitinationNVVMDLKKCCNHPYL
HHHHHHHHHCCCCCC
51.85-
1017 (in isoform 2)Malonylation-51.8532601280
1017 (in isoform 2)Ubiquitination-51.85-
1051UbiquitinationALIRASGKLLLLQKM
HHHHHHHHHHHHHHH
33.20-
1057AcetylationGKLLLLQKMLKNLKE
HHHHHHHHHHHCHHH
46.2825953088
1057UbiquitinationGKLLLLQKMLKNLKE
HHHHHHHHHHHCHHH
46.2821890473
1057 (in isoform 1)Ubiquitination-46.2821890473
1057 (in isoform 2)Ubiquitination-46.2821890473
1073PhosphorylationGHRVLIFSQMTKMLD
CEEEEEEHHHHHHHH
16.4324719451
1076PhosphorylationVLIFSQMTKMLDLLE
EEEEHHHHHHHHHHH
12.9827251275
1091PhosphorylationDFLEHEGYKYERIDG
HHHHHCCCCEEEECC
13.8618767875
1092AcetylationFLEHEGYKYERIDGG
HHHHCCCCEEEECCC
52.0426051181
1092UbiquitinationFLEHEGYKYERIDGG
HHHHCCCCEEEECCC
52.0421890473
1092 (in isoform 1)Ubiquitination-52.0421890473
1092 (in isoform 2)Ubiquitination-52.0421890473
1104SulfoxidationDGGITGNMRQEAIDR
CCCCCCCHHHHHHHH
5.0421406390
1206AcetylationVRPGLGSKTGSMSKQ
ECCCCCCCCCCCCHH
55.9225953088
1206UbiquitinationVRPGLGSKTGSMSKQ
ECCCCCCCCCCCCHH
55.92-
1207PhosphorylationRPGLGSKTGSMSKQE
CCCCCCCCCCCCHHH
35.8630108239
1209PhosphorylationGLGSKTGSMSKQELD
CCCCCCCCCCHHHHH
25.7230108239
1211PhosphorylationGSKTGSMSKQELDDI
CCCCCCCCHHHHHHH
32.6530108239
1212AcetylationSKTGSMSKQELDDIL
CCCCCCCHHHHHHHH
38.8726051181
1212SumoylationSKTGSMSKQELDDIL
CCCCCCCHHHHHHHH
38.8728112733
1212UbiquitinationSKTGSMSKQELDDIL
CCCCCCCHHHHHHHH
38.87-
1220UbiquitinationQELDDILKFGTEELF
HHHHHHHHHCCHHHH
41.92-
1228SumoylationFGTEELFKDEATDGG
HCCHHHHCCCCCCCC
68.25-
1228AcetylationFGTEELFKDEATDGG
HCCHHHHCCCCCCCC
68.2526051181
1228SumoylationFGTEELFKDEATDGG
HCCHHHHCCCCCCCC
68.2528112733
1228UbiquitinationFGTEELFKDEATDGG
HCCHHHHCCCCCCCC
68.25-
1232PhosphorylationELFKDEATDGGGDNK
HHHCCCCCCCCCCCC
32.8821406692
1239AcetylationTDGGGDNKEGEDSSV
CCCCCCCCCCCCCCC
72.3626051181
1239SumoylationTDGGGDNKEGEDSSV
CCCCCCCCCCCCCCC
72.3628112733
1244PhosphorylationDNKEGEDSSVIHYDD
CCCCCCCCCCEEECH
23.3925159151
1245PhosphorylationNKEGEDSSVIHYDDK
CCCCCCCCCEEECHH
37.1025159151
1249PhosphorylationEDSSVIHYDDKAIER
CCCCCEEECHHHHHH
18.0829396449
1252AcetylationSVIHYDDKAIERLLD
CCEEECHHHHHHHHH
48.6526051181
1252UbiquitinationSVIHYDDKAIERLLD
CCEEECHHHHHHHHH
48.6521906983
1252 (in isoform 1)Ubiquitination-48.6521890473
1252 (in isoform 2)Ubiquitination-48.6521890473
1265PhosphorylationLDRNQDETEDTELQG
HHCCCCCCCCHHHHH
47.66-
1276PhosphorylationELQGMNEYLSSFKVA
HHHHHHHHHHHHHHH
13.5928796482
1276 (in isoform 2)Phosphorylation-13.5927642862
1278PhosphorylationQGMNEYLSSFKVAQY
HHHHHHHHHHHHHHH
32.5928796482
1279PhosphorylationGMNEYLSSFKVAQYV
HHHHHHHHHHHHHHH
26.8728796482
1281UbiquitinationNEYLSSFKVAQYVVR
HHHHHHHHHHHHHHC
38.31-
1288MethylationKVAQYVVREEEMGEE
HHHHHHHCHHHCCCH
35.25-
1304SumoylationEVEREIIKQEESVDP
HHHHHHHHCHHCCCH
58.27-
1304AcetylationEVEREIIKQEESVDP
HHHHHHHHCHHCCCH
58.2726051181
1304SumoylationEVEREIIKQEESVDP
HHHHHHHHCHHCCCH
58.2728112733
1304UbiquitinationEVEREIIKQEESVDP
HHHHHHHHCHHCCCH
58.2721906983
1304 (in isoform 1)Ubiquitination-58.2721890473
1304 (in isoform 2)Ubiquitination-58.2721890473
1308PhosphorylationEIIKQEESVDPDYWE
HHHHCHHCCCHHHHH
30.9423401153
1313PhosphorylationEESVDPDYWEKLLRH
HHCCCHHHHHHHHHH
22.3630266825
1316UbiquitinationVDPDYWEKLLRHHYE
CCHHHHHHHHHHHHH
38.38-
1316 (in isoform 2)Ubiquitination-38.38-
1319MethylationDYWEKLLRHHYEQQQ
HHHHHHHHHHHHHHH
25.60-
1335UbiquitinationDLARNLGKGKRIRKQ
HHHHHCCCCHHHHHH
65.51-
1345PhosphorylationRIRKQVNYNDGSQED
HHHHHCCCCCCCCCC
18.7723927012
1349PhosphorylationQVNYNDGSQEDRDWQ
HCCCCCCCCCCCCCC
33.0123401153
1349 (in isoform 2)Phosphorylation-33.0122817900
1360PhosphorylationRDWQDDQSDNQSDYS
CCCCCCCCCCCCCCC
45.5923663014
1364PhosphorylationDDQSDNQSDYSVASE
CCCCCCCCCCCHHCC
44.7823663014
1366PhosphorylationQSDNQSDYSVASEEG
CCCCCCCCCHHCCCC
15.4223663014
1367PhosphorylationSDNQSDYSVASEEGD
CCCCCCCCHHCCCCC
19.0523663014
1370PhosphorylationQSDYSVASEEGDEDF
CCCCCHHCCCCCCCH
33.7423663014
1378 (in isoform 2)Phosphorylation-63.8225137130
1388PhosphorylationSEAPRRPSRKGLRND
CCCCCCCCCCCCCCC
44.8320068231
1390UbiquitinationAPRRPSRKGLRNDKD
CCCCCCCCCCCCCCC
67.64-
1392 (in isoform 2)Phosphorylation-5.3325137130
1394 (in isoform 2)Phosphorylation-66.7725137130
1396AcetylationRKGLRNDKDKPLPPL
CCCCCCCCCCCCCHH
71.8025953088
1396UbiquitinationRKGLRNDKDKPLPPL
CCCCCCCCCCCCCHH
71.80-
1398SumoylationGLRNDKDKPLPPLLA
CCCCCCCCCCCHHHH
54.95-
1398AcetylationGLRNDKDKPLPPLLA
CCCCCCCCCCCHHHH
54.9525953088
1398SumoylationGLRNDKDKPLPPLLA
CCCCCCCCCCCHHHH
54.95-
1398UbiquitinationGLRNDKDKPLPPLLA
CCCCCCCCCCCHHHH
54.95-
1398 (in isoform 2)Phosphorylation-54.9525137130
1422UbiquitinationGFNARQRKAFLNAIM
CCCHHHHHHHHHHHH
34.84-
1426 (in isoform 2)Ubiquitination-22.44-
1450 (in isoform 2)Ubiquitination-45.17-
1468GlutathionylationSLFMRHLCEPGADGA
HHHHHHHCCCCCCCC
4.9122555962
1500PhosphorylationLTRIGVMSLIRKKVQ
HHHHHHHHHHHHHHH
20.4520068231
1505UbiquitinationVMSLIRKKVQEFEHV
HHHHHHHHHHHCCCC
39.02-
1517PhosphorylationEHVNGRWSMPELAEV
CCCCCCCCCHHHHHH
24.0929978859
1528AcetylationLAEVEENKKMSQPGS
HHHHHHHHCCCCCCC
53.8126051181
1528SumoylationLAEVEENKKMSQPGS
HHHHHHHHCCCCCCC
53.8128112733
1528UbiquitinationLAEVEENKKMSQPGS
HHHHHHHHCCCCCCC
53.81-
1529SumoylationAEVEENKKMSQPGSP
HHHHHHHCCCCCCCC
56.20-
1529SumoylationAEVEENKKMSQPGSP
HHHHHHHCCCCCCCC
56.2028112733
1531PhosphorylationVEENKKMSQPGSPSP
HHHHHCCCCCCCCCC
41.9429255136
1535PhosphorylationKKMSQPGSPSPKTPT
HCCCCCCCCCCCCCC
28.9629255136
1537PhosphorylationMSQPGSPSPKTPTPS
CCCCCCCCCCCCCCC
40.5029255136
1540PhosphorylationPGSPSPKTPTPSTPG
CCCCCCCCCCCCCCC
35.4629255136
1542PhosphorylationSPSPKTPTPSTPGDT
CCCCCCCCCCCCCCC
34.7929255136
1544PhosphorylationSPKTPTPSTPGDTQP
CCCCCCCCCCCCCCC
50.1130266825
1545PhosphorylationPKTPTPSTPGDTQPN
CCCCCCCCCCCCCCC
32.2829255136
1549PhosphorylationTPSTPGDTQPNTPAP
CCCCCCCCCCCCCCC
52.4125159151
1553PhosphorylationPGDTQPNTPAPVPPA
CCCCCCCCCCCCCCH
27.7529255136
1565SumoylationPPAEDGIKIEENSLK
CCHHCCCCCCCCCCC
49.98-
1565SumoylationPPAEDGIKIEENSLK
CCHHCCCCCCCCCCC
49.9828112733
1570PhosphorylationGIKIEENSLKEEESI
CCCCCCCCCCHHHHC
44.0629255136
1572SumoylationKIEENSLKEEESIEG
CCCCCCCCHHHHCCC
64.00-
1572SumoylationKIEENSLKEEESIEG
CCCCCCCCHHHHCCC
64.0028112733
1572UbiquitinationKIEENSLKEEESIEG
CCCCCCCCHHHHCCC
64.0021906983
1572 (in isoform 1)Ubiquitination-64.0021890473
1576PhosphorylationNSLKEEESIEGEKEV
CCCCHHHHCCCCCHH
29.2623401153
1581AcetylationEESIEGEKEVKSTAP
HHHCCCCCHHHCCCC
77.8726051181
1584SumoylationIEGEKEVKSTAPETA
CCCCCHHHCCCCCCC
43.0828112733
1584UbiquitinationIEGEKEVKSTAPETA
CCCCCHHHCCCCCCC
43.0821906983
1584 (in isoform 1)Ubiquitination-43.0821890473
1585PhosphorylationEGEKEVKSTAPETAI
CCCCHHHCCCCCCCE
34.6723403867
1586PhosphorylationGEKEVKSTAPETAIE
CCCHHHCCCCCCCEE
40.2823403867
1590PhosphorylationVKSTAPETAIECTQA
HHCCCCCCCEEECCC
31.6926657352
1595PhosphorylationPETAIECTQAPAPAS
CCCCEEECCCCCCCC
18.2523403867
1600 (in isoform 2)Ubiquitination-34.9521890473
1602PhosphorylationTQAPAPASEDEKVVV
CCCCCCCCCCCCEEE
44.5119664994
1606AcetylationAPASEDEKVVVEPPE
CCCCCCCCEEECCCC
53.2926051181
1606SumoylationAPASEDEKVVVEPPE
CCCCCCCCEEECCCC
53.2928112733
1612 (in isoform 2)Ubiquitination-49.0421890473
1617AcetylationEPPEGEEKVEKAEVK
CCCCCHHHHHHHHHH
51.9326051181
1617SumoylationEPPEGEEKVEKAEVK
CCCCCHHHHHHHHHH
51.9328112733
1620AcetylationEGEEKVEKAEVKERT
CCHHHHHHHHHHHHC
53.4826051181
1636SumoylationEPMETEPKGAADVEK
CCCCCCCCCCCCHHH
55.7528112733
1643AcetylationKGAADVEKVEEKSAI
CCCCCHHHHHHHCCC
55.5919608861
1643SumoylationKGAADVEKVEEKSAI
CCCCCHHHHHHHCCC
55.5928112733
1643UbiquitinationKGAADVEKVEEKSAI
CCCCCHHHHHHHCCC
55.5919608861
1647SumoylationDVEKVEEKSAIDLTP
CHHHHHHHCCCCCCC
31.51-
1647SumoylationDVEKVEEKSAIDLTP
CHHHHHHHCCCCCCC
31.5128112733
1647UbiquitinationDVEKVEEKSAIDLTP
CHHHHHHHCCCCCCC
31.5121906983
1647 (in isoform 1)Ubiquitination-31.5121890473
1648PhosphorylationVEKVEEKSAIDLTPI
HHHHHHHCCCCCCCE
33.4630266825
1653PhosphorylationEKSAIDLTPIVVEDK
HHCCCCCCCEECCCH
13.7619664994
1660SumoylationTPIVVEDKEEKKEEE
CCEECCCHHHHCHHH
55.0228112733
1660UbiquitinationTPIVVEDKEEKKEEE
CCEECCCHHHHCHHH
55.02-
1670SumoylationKKEEEEKKEVMLQNG
HCHHHHHHHHHHHCC
59.84-
1670SumoylationKKEEEEKKEVMLQNG
HCHHHHHHHHHHHCC
59.8428112733
1675 (in isoform 2)Ubiquitination-37.4721890473
1679PhosphorylationVMLQNGETPKDLNDE
HHHHCCCCCCCCCHH
36.7229255136
1681AcetylationLQNGETPKDLNDEKQ
HHCCCCCCCCCHHHH
80.4423236377
1687SumoylationPKDLNDEKQKKNIKQ
CCCCCHHHHHHCHHH
70.9928112733
1722PhosphorylationEERAATVTKKTYEIW
HHHHCCCCHHHHHHH
23.59-
1724UbiquitinationRAATVTKKTYEIWHR
HHCCCCHHHHHHHHH
47.15-
1725PhosphorylationAATVTKKTYEIWHRR
HCCCCHHHHHHHHHH
28.1328152594
1726PhosphorylationATVTKKTYEIWHRRH
CCCCHHHHHHHHHHC
17.8128152594
1752 (in isoform 2)Ubiquitination-2.17-
1766AcetylationAILNEPFKGEMNRGN
EECCCCCCCCCCCCC
65.7526051181
1766UbiquitinationAILNEPFKGEMNRGN
EECCCCCCCCCCCCC
65.75-
1778AcetylationRGNFLEIKNKFLARR
CCCHHHHHHHHHHHH
44.7226051181
1780AcetylationNFLEIKNKFLARRFK
CHHHHHHHHHHHHHH
36.4326051181
1794 (in isoform 2)Ubiquitination-6.08-
1804PhosphorylationEQLRRAAYLNMSEDP
HHHHHHHHCCCCCCC
9.5323663014
1808PhosphorylationRAAYLNMSEDPSHPS
HHHHCCCCCCCCCHH
37.4623663014
1812PhosphorylationLNMSEDPSHPSMALN
CCCCCCCCCHHHHHH
61.4223663014
1815PhosphorylationSEDPSHPSMALNTRF
CCCCCCHHHHHHHHH
15.9723663014
1820PhosphorylationHPSMALNTRFAEVEC
CHHHHHHHHHHHHHH
28.1923663014
1827GlutathionylationTRFAEVECLAESHQH
HHHHHHHHHHHHHHH
5.4322555962
1831PhosphorylationEVECLAESHQHLSKE
HHHHHHHHHHHHCHH
23.8825849741
1837UbiquitinationESHQHLSKESMAGNK
HHHHHHCHHHHCCCC
61.23-
1839PhosphorylationHQHLSKESMAGNKPA
HHHHCHHHHCCCCCH
20.0521406692
1840SulfoxidationQHLSKESMAGNKPAN
HHHCHHHHCCCCCHH
6.0821406390
1844UbiquitinationKESMAGNKPANAVLH
HHHHCCCCCHHHHHH
44.59-
1852UbiquitinationPANAVLHKVLKQLEE
CHHHHHHHHHHHHHH
45.1421890473
1852 (in isoform 1)Ubiquitination-45.1421890473
1855AcetylationAVLHKVLKQLEELLS
HHHHHHHHHHHHHHH
56.6926051181
1855UbiquitinationAVLHKVLKQLEELLS
HHHHHHHHHHHHHHH
56.6921906983
1855 (in isoform 1)Ubiquitination-56.6921890473
1862PhosphorylationKQLEELLSDMKADVT
HHHHHHHHHHHCCHH
48.5625072903
1865SumoylationEELLSDMKADVTRLP
HHHHHHHHCCHHHCC
46.5628112733
1865UbiquitinationEELLSDMKADVTRLP
HHHHHHHHCCHHHCC
46.562190698
1865 (in isoform 1)Ubiquitination-46.5621890473
1865 (in isoform 2)Ubiquitination-46.56-
1872 (in isoform 2)Ubiquitination-24.86-
1880 (in isoform 2)Ubiquitination-25.0721890473
1883 (in isoform 2)Ubiquitination-6.8121890473
1888PhosphorylationVAVRLQMSERNILSR
HHHHHHCCHHHHHHH
22.0524719451
1893 (in isoform 2)Ubiquitination-2.5221890473
1904PhosphorylationANRAPEPTPQQVAQQ
HHCCCCCCHHHHHHC
31.8728555341

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
308SPhosphorylationKinaseCK2A1P68400
PSP
310SPhosphorylationKinaseCK2A1P68400
PSP
428SPhosphorylationKinaseCK2A1P68400
PSP
1349SPhosphorylationKinaseATMQ13315
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHD4_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 CHD4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATR_HUMANATRphysical
10545197
HDAC2_HUMANHDAC2physical
10545197
HDAC1_HUMANHDAC1physical
9804427
HDAC2_HUMANHDAC2physical
9804427
NAB2_HUMANNAB2physical
16574654
SMCA4_HUMANSMARCA4physical
14530259
SMCA4_HUMANSMARCA4physical
16217013
SMRC1_HUMANSMARCC1physical
16217013
HNRPC_HUMANHNRNPCphysical
16217013
MCRS1_HUMANMCRS1physical
16186106
BC11B_HUMANBCL11Bphysical
16091750
IKZF1_HUMANIKZF1physical
11003653
HDAC2_HUMANHDAC2physical
11003653
SMCA4_HUMANSMARCA4physical
11003653
SMRC1_HUMANSMARCC1physical
11003653
SMCE1_HUMANSMARCE1physical
11003653
SIN3A_HUMANSIN3Aphysical
9790534
UBS3B_HUMANUBASH3Bphysical
9790534
SAP30_HUMANSAP30physical
9790534
HDAC1_HUMANHDAC1physical
9790534
HDAC2_HUMANHDAC2physical
9790534
RBBP4_HUMANRBBP4physical
9790534
RBBP7_HUMANRBBP7physical
9790534
MTA2_HUMANMTA2physical
9790534
PCNT_HUMANPCNTphysical
17626165
H31_HUMANHIST1H3Aphysical
21278251
ATM_HUMANATMphysical
21219611
HDAC1_HUMANHDAC1physical
20693977
HDAC1_HUMANHDAC1physical
9885572
HDAC2_HUMANHDAC2physical
9885572
RBBP4_HUMANRBBP4physical
9885572
CHD3_HUMANCHD3physical
9885572
MTA1_HUMANMTA1physical
9885572
BRD4_HUMANBRD4physical
21555454
UBF1_HUMANUBTFphysical
21555454
CHD5_HUMANCHD5physical
21555454
IMA6_HUMANKPNA5physical
21555454
IMA7_HUMANKPNA6physical
21555454
NOLC1_HUMANNOLC1physical
21555454
P66A_HUMANGATAD2Aphysical
21555454
P66B_HUMANGATAD2Bphysical
21555454
DPEP3_HUMANDPEP3physical
21555454
AF9_HUMANMLLT3physical
21555454
DPEP2_HUMANDPEP2physical
21555454
MTA3_HUMANMTA3physical
22075476
HDAC1_HUMANHDAC1physical
22075476
RNF8_HUMANRNF8physical
22531782
CHD4_HUMANCHD4physical
22575888
MCPH1_HUMANMCPH1physical
22219182
NR2C2_HUMANNR2C2physical
21670149
NR2C1_HUMANNR2C1physical
21670149
DNMT1_HUMANDNMT1physical
21670149
KDM1A_HUMANKDM1Aphysical
21670149
HDAC1_HUMANHDAC1physical
21670149
HDAC2_HUMANHDAC2physical
21670149
MTA2_HUMANMTA2physical
21670149
MTA1_HUMANMTA1physical
21670149
CHD4_HUMANCHD4physical
21670149
RBBP4_HUMANRBBP4physical
21670149
MBD3_HUMANMBD3physical
21670149
DPOD3_HUMANPOLD3physical
21670149
HDAC1_HUMANHDAC1physical
22939629
HDAC2_HUMANHDAC2physical
22939629
MTA2_HUMANMTA2physical
22939629
RBBP4_HUMANRBBP4physical
22939629
RBBP7_HUMANRBBP7physical
22939629
MBD3_HUMANMBD3physical
22939629
SMRC1_HUMANSMARCC1physical
22939629
TBL1R_HUMANTBL1XR1physical
22939629
P66A_HUMANGATAD2Aphysical
22939629
H31T_HUMANHIST3H3physical
22749909
NACC2_HUMANNACC2physical
22926524
DNMT1_HUMANDNMT1physical
23708667
H31_HUMANHIST1H3Aphysical
24576085
ZFHX4_HUMANZFHX4physical
24440720
MTA1_HUMANMTA1physical
24440720
MTA2_HUMANMTA2physical
25247294
HDAC1_HUMANHDAC1physical
25247294
RBBP7_HUMANRBBP7physical
25247294
MBD3_HUMANMBD3physical
25247294
H31T_HUMANHIST3H3physical
25247294
HDAC1_HUMANHDAC1physical
26344197
HDAC2_HUMANHDAC2physical
26344197
MTA1_HUMANMTA1physical
26344197
MTA2_HUMANMTA2physical
26344197
MTA3_HUMANMTA3physical
26344197
RBBP4_HUMANRBBP4physical
26344197
TCP4_HUMANSUB1physical
26344197
PARP1_HUMANPARP1physical
26565020
EP300_HUMANEP300physical
26546801
RNF8_HUMANRNF8physical
26546801
PARP1_HUMANPARP1physical
26546801
ZN827_HUMANZNF827physical
25150861

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 CHD4_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-987 AND LYS-1643, AND MASSSPECTROMETRY.
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-1531; SER-1535 ANDSER-1602, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428; SER-515; THR-517;THR-529; SER-531; SER-1535; THR-1542; SER-1570 AND SER-1576, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1370, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1349, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428; SER-515; SER-531;SER-1531 AND SER-1535, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-1535; SER-1537AND SER-1602, AND MASS SPECTROMETRY.
"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 THR-1553, AND MASSSPECTROMETRY.

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