CHD5_HUMAN - dbPTM
CHD5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHD5_HUMAN
UniProt AC Q8TDI0
Protein Name Chromodomain-helicase-DNA-binding protein 5
Gene Name CHD5 {ECO:0000312|EMBL:AAL98962.1}
Organism Homo sapiens (Human).
Sequence Length 1954
Subcellular Localization Nucleus . Associates with heterochromatin..
Protein Description Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3. Plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. Tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. Downstream activated genes may include CDKN2A that positively regulates the p53/TP53 pathway, which in turn, prevents cell proliferation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa..
Protein Sequence MRGPVGTEEELPRLFAEEMENEDEMSEEEDGGLEAFDDFFPVEPVSLPKKKKPKKLKENKCKGKRKKKEGSNDELSENEEDLEEKSESEGSDYSPNKKKKKKLKDKKEKKAKRKKKDEDEDDNDDGCLKEPKSSGQLMAEWGLDDVDYLFSEEDYHTLTNYKAFSQFLRPLIAKKNPKIPMSKMMTVLGAKWREFSANNPFKGSSAAAAAAAVAAAVETVTISPPLAVSPPQVPQPVPIRKAKTKEGKGPGVRKKIKGSKDGKKKGKGKKTAGLKFRFGGISNKRKKGSSSEEDEREESDFDSASIHSASVRSECSAALGKKSKRRRKKKRIDDGDGYETDHQDYCEVCQQGGEIILCDTCPRAYHLVCLDPELEKAPEGKWSCPHCEKEGIQWEPKDDDDEEEEGGCEEEEDDHMEFCRVCKDGGELLCCDACPSSYHLHCLNPPLPEIPNGEWLCPRCTCPPLKGKVQRILHWRWTEPPAPFMVGLPGPDVEPSLPPPKPLEGIPEREFFVKWAGLSYWHCSWVKELQLELYHTVMYRNYQRKNDMDEPPPFDYGSGDEDGKSEKRKNKDPLYAKMEERFYRYGIKPEWMMIHRILNHSFDKKGDVHYLIKWKDLPYDQCTWEIDDIDIPYYDNLKQAYWGHRELMLGEDTRLPKRLLKKGKKLRDDKQEKPPDTPIVDPTVKFDKQPWYIDSTGGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTGDKESRSVIRENEFSFEDNAIRSGKKVFRMKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRRLKADVFKNMPAKTELIVRVELSQMQKKYYKFILTRNFEALNSKGGGNQVSLLNIMMDLKKCCNHPYLFPVAAVEAPVLPNGSYDGSSLVKSSGKLMLLQKMLKKLRDEGHRVLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKRKMMLTHLVVRPGLGSKSGSMTKQELDDILKFGTEELFKDDVEGMMSQGQRPVTPIPDVQSSKGGNLAASAKKKHGSTPPGDNKDVEDSSVIHYDDAAISKLLDRNQDATDDTELQNMNEYLSSFKVAQYVVREEDGVEEVEREIIKQEENVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDASQEDQEWQDELSDNQSEYSIGSEDEDEDFEERPEGQSGRRQSRRQLKSDRDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRWGMPPQDAFNSHWLVRDLRGKSEKEFRAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLVRKKVQEFEHVNGKYSTPDLIPEGPEGKKSGEVISSDPNTPVPASPAHLLPAPLGLPDKMEAQLGYMDEKDPGAQKPRQPLEVQALPAALDRVESEDKHESPASKERAREERPEETEKAPPSPEQLPREEVLPEKEKILDKLELSLIHSRGDSSELRPDDTKAEEKEPIETQQNGDKEEDDEGKKEDKKGKFKFMFNIADGGFTELHTLWQNEERAAVSSGKIYDIWHRRHDYWLLAGIVTHGYARWQDIQNDPRYMILNEPFKSEVHKGNYLEMKNKFLARRFKLLEQALVIEEQLRRAAYLNMTQDPNHPAMALNARLAEVECLAESHQHLSKESLAGNKPANAVLHKVLNQLEELLSDMKADVTRLPSMLSRIPPVAARLQMSERSILSRLTNRAGDPTIQQGAFGSSQMYSNNFGPNFRGPGPGGIVNYNQMPLGPYVTDI
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
86PhosphorylationEEDLEEKSESEGSDY
HHHHHHHHHHCCCCC		50.03-
100AcetylationYSPNKKKKKKLKDKK
CCCCHHHHHHHHHHH		65.1190743
102AcetylationPNKKKKKKLKDKKEK
CCHHHHHHHHHHHHH		70.4290745
106AcetylationKKKKLKDKKEKKAKR
HHHHHHHHHHHHHHH		62.3390747
107AcetylationKKKLKDKKEKKAKRK
HHHHHHHHHHHHHHH		82.1790749
174AcetylationFLRPLIAKKNPKIPM
HHHHHHHCCCCCCCH		46.20130793
175AcetylationLRPLIAKKNPKIPMS
HHHHHHCCCCCCCHH		70.25130795
186PhosphorylationIPMSKMMTVLGAKWR
CCHHHHHHHHHHHHE		14.7424114839
284UbiquitinationRFGGISNKRKKGSSS
ECCCCCCCCCCCCCC		59.8232015554
340PhosphorylationDDGDGYETDHQDYCE
CCCCCCCCCCHHHHH		30.2322817901
345PhosphorylationYETDHQDYCEVCQQG
CCCCCHHHHHHHHCC		5.50-
556PhosphorylationDEPPPFDYGSGDEDG
CCCCCCCCCCCCCCC		17.3627732954
558PhosphorylationPPPFDYGSGDEDGKS
CCCCCCCCCCCCCCC		36.5228985074
565PhosphorylationSGDEDGKSEKRKNKD
CCCCCCCCCCCCCCC		54.61-
575PhosphorylationRKNKDPLYAKMEERF
CCCCCCCHHHHHHHH		15.0129083192
583PhosphorylationAKMEERFYRYGIKPE
HHHHHHHHHCCCCHH		14.7829083192
585PhosphorylationMEERFYRYGIKPEWM
HHHHHHHCCCCHHHH		16.3029083192
588SumoylationRFYRYGIKPEWMMIH
HHHHCCCCHHHHHHH		32.30-
588SumoylationRFYRYGIKPEWMMIH
HHHHCCCCHHHHHHH		32.30-
588UbiquitinationRFYRYGIKPEWMMIH
HHHHCCCCHHHHHHH		32.30-
610PhosphorylationDKKGDVHYLIKWKDL
CCCCCEEEEEEECCC		15.2419664994
786PhosphorylationTYTGDKESRSVIREN
EEECCHHHCCCCCCC		35.2829978859
788PhosphorylationTGDKESRSVIRENEF
ECCHHHCCCCCCCCC		31.0429978859
796PhosphorylationVIRENEFSFEDNAIR
CCCCCCCCCCHHHHH		22.8820873877
825PhosphorylationKFHVLLTSYELITID
EEEEECCCCEEEECC		19.3120068231
853UbiquitinationVDEAHRLKNNQSKFF
HHHHHHHHCCCCHHH		54.5324816145
858UbiquitinationRLKNNQSKFFRVLNS
HHHCCCCHHHHHHHH		38.46-
858AcetylationRLKNNQSKFFRVLNS
HHHCCCCHHHHHHHH		38.46-
918UbiquitinationISKEDQIKKLHDLLG
CCHHHHHHHHHHHHC		43.58-
933UbiquitinationPHMLRRLKADVFKNM
HHHHHHHHCHHHCCC		40.50-
938UbiquitinationRLKADVFKNMPAKTE
HHHCHHHCCCCCCEE		52.7829967540
943UbiquitinationVFKNMPAKTELIVRV
HHCCCCCCEEEEEEE		36.34-
958"N6,N6-dimethyllysine"ELSQMQKKYYKFILT
EHHHHHHHHHHHHHH		36.60-
958MethylationELSQMQKKYYKFILT
EHHHHHHHHHHHHHH		36.60-
961MethylationQMQKKYYKFILTRNF
HHHHHHHHHHHHCCH		23.88-
961"N6,N6-dimethyllysine"QMQKKYYKFILTRNF
HHHHHHHHHHHHCCH		23.88-
1047PhosphorylationGHRVLIFSQMTKMLD
CCCEEEEHHHHHHHH		16.4324719451
1050PhosphorylationVLIFSQMTKMLDLLE
EEEEHHHHHHHHHHH		12.9827251275
1062PhosphorylationLLEDFLEYEGYKYER
HHHHHHHHCCCCEEE		19.4622817900
1067PhosphorylationLEYEGYKYERIDGGI
HHHCCCCEEEECCCC		11.2718083107
1142UbiquitinationHRIGQNKKVMIYRFV
HHCCCCCEEEEEEEE		44.5824816145
1169PhosphorylationAKRKMMLTHLVVRPG
HHHHHHHHHHHHCCC		8.68-
1181PhosphorylationRPGLGSKSGSMTKQE
CCCCCCCCCCCCHHH		37.4823532336
1183PhosphorylationGLGSKSGSMTKQELD
CCCCCCCCCCHHHHH		30.3023532336
1185PhosphorylationGSKSGSMTKQELDDI
CCCCCCCCHHHHHHH		31.1328857561
1194UbiquitinationQELDDILKFGTEELF
HHHHHHHHHCCHHHH		41.9232015554
1217PhosphorylationSQGQRPVTPIPDVQS
HCCCCCCCCCCCCCC		20.4125849741
1237AcetylationLAASAKKKHGSTPPG
CHHHHHHHCCCCCCC		53.1112433775
1241PhosphorylationAKKKHGSTPPGDNKD
HHHHCCCCCCCCCCC		37.7928985074
1273PhosphorylationLDRNQDATDDTELQN
HHCCCCCCCCHHHHH		42.5728796482
1276PhosphorylationNQDATDDTELQNMNE
CCCCCCCHHHHHHHH		41.2128796482
1284PhosphorylationELQNMNEYLSSFKVA
HHHHHHHHHHHHHEE		13.5928796482
1286PhosphorylationQNMNEYLSSFKVAQY
HHHHHHHHHHHEEEE		32.5928796482
1287PhosphorylationNMNEYLSSFKVAQYV
HHHHHHHHHHEEEEE		26.8728796482
1289UbiquitinationNEYLSSFKVAQYVVR
HHHHHHHHEEEEEEC		38.3122817900
1310UbiquitinationEVEREIIKQEENVDP
HHHHHHHHCHHCCCH		58.27-
1310SumoylationEVEREIIKQEENVDP
HHHHHHHHCHHCCCH		58.27-
1319PhosphorylationEENVDPDYWEKLLRH
HHCCCHHHHHHHHHH		22.36-
1322UbiquitinationVDPDYWEKLLRHHYE
CCHHHHHHHHHHHHH		38.3829967540
1325MethylationDYWEKLLRHHYEQQQ
HHHHHHHHHHHHHHH		25.60-
1341UbiquitinationDLARNLGKGKRIRKQ
HHHHHHCCHHHHHHH		65.51-
1390MethylationFEERPEGQSGRRQSR
HHHCCCCCCCCHHHH		40.8426797129
1406UbiquitinationQLKSDRDKPLPPLLA
HHHCCCCCCCCHHHH		49.72-
1406SumoylationQLKSDRDKPLPPLLA
HHHCCCCCCCCHHHH		49.72-
1406SumoylationQLKSDRDKPLPPLLA
HHHCCCCCCCCHHHH		49.72-
1430UbiquitinationGFNARQRKAFLNAIM
CCCHHHHHHHHHHHH		34.8423000965
1465MethylationGKSEKEFRAYVSLFM
CCCHHHHHHHHHHHH		26.54-
1511MethylationIGVMSLVRKKVQEFE
HHHHHHHHHHHHHHH		38.07-
1539PhosphorylationEGPEGKKSGEVISSD
CCCCCCCCCCCCCCC		43.6127732954
1544PhosphorylationKKSGEVISSDPNTPV
CCCCCCCCCCCCCCC		33.5927732954
1545PhosphorylationKSGEVISSDPNTPVP
CCCCCCCCCCCCCCC		46.0627732954
1549PhosphorylationVISSDPNTPVPASPA
CCCCCCCCCCCCCHH		30.9327732954
1554PhosphorylationPNTPVPASPAHLLPA
CCCCCCCCHHHHCCC		19.2927732954
1610PhosphorylationESEDKHESPASKERA
HCCCCCCCHHHHHHH		26.0328985074
1631PhosphorylationETEKAPPSPEQLPRE
HHCCCCCCHHHCCHH		39.7625849741
1654PhosphorylationILDKLELSLIHSRGD
HHHHHHHHHHHCCCC		18.8620068231
1658PhosphorylationLELSLIHSRGDSSEL
HHHHHHHCCCCCCCC		30.8520068231
1662PhosphorylationLIHSRGDSSELRPDD
HHHCCCCCCCCCCCC		28.6520068231
1663PhosphorylationIHSRGDSSELRPDDT
HHCCCCCCCCCCCCC		45.4420068231
1670PhosphorylationSELRPDDTKAEEKEP
CCCCCCCCCCHHCCC		39.26-
1755DimethylationIVTHGYARWQDIQND
HHHCCCCCHHHHCCC		24.09-
1838PhosphorylationEVECLAESHQHLSKE
HHHHHHHHHHHCCHH		23.88-
1846PhosphorylationHQHLSKESLAGNKPA
HHHCCHHHHCCCCCH		27.53-
1851UbiquitinationKESLAGNKPANAVLH
HHHHCCCCCHHHHHH		44.5929967540
1869PhosphorylationNQLEELLSDMKADVT
HHHHHHHHHHHCCHH		48.5624719451
1872UbiquitinationEELLSDMKADVTRLP
HHHHHHHHCCHHHHH		46.5622817900
1876PhosphorylationSDMKADVTRLPSMLS
HHHHCCHHHHHHHHH		27.3424719451
1895PhosphorylationVAARLQMSERSILSR
HHHHHHCCHHHHHHH		19.5224719451
1898PhosphorylationRLQMSERSILSRLTN
HHHCCHHHHHHHHHC		24.6724719451
1901PhosphorylationMSERSILSRLTNRAG
CCHHHHHHHHHCCCC		24.4724719451
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 CHD5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1390QMethylation

26797129
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 CHD5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTA2_HUMANMTA2physical
25247294
HDAC1_HUMANHDAC1physical
25247294
RBBP7_HUMANRBBP7physical
25247294
MBD3_HUMANMBD3physical
25247294
H31T_HUMANHIST3H3physical
25247294
CHD4_HUMANCHD4physical
25247294
P66B_HUMANGATAD2Bphysical
25247294
RBBP4_HUMANRBBP4physical
25247294
MTA1_HUMANMTA1physical
25247294
P66A_HUMANGATAD2Aphysical
25247294
MBD2_HUMANMBD2physical
25247294
HDAC2_HUMANHDAC2physical
25247294
MTA3_HUMANMTA3physical
25247294
HDAC1_HUMANHDAC1physical
26344197
HDAC2_HUMANHDAC2physical
26344197
MTA1_HUMANMTA1physical
26344197
MTA2_HUMANMTA2physical
26344197
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 CHD5_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-858, AND MASS SPECTROMETRY.

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