CHDM_DROME - dbPTM
CHDM_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHDM_DROME
UniProt AC O97159
Protein Name Chromodomain-helicase-DNA-binding protein Mi-2 homolog
Gene Name Mi-2
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1982
Subcellular Localization Nucleus.
Protein Description Vital role in development. Protein binds to a portion of Hunchback (HB) protein that is critical for repression of bithorax complex (BXC) genes. May also function in polycomb group (PcG) repression of Hox genes..
Protein Sequence MASEEENDDNFQEEEEAQEDNAPAAELSNDSDAPLKPNNDEDDDYDPEDSRRKKKGKKRKTRKGEEKGRKKKKRKKNESEEDSDFVQHDEEVEYPSTSKRGRKRKEEKQAAKEKESASSGMPSVEDVCSAFSVCNVEIEYSEEELQSLTTYKAFMHHVRPILQKENPKIAAPKLVMLVAAKWREFCESNPHIQQEGGAAGSGGSAGQARSVTGDEPEEPRSSRSSRNEKPDDIYEEAVEEEEEEEEEEKKPRRKRSGRGKKGRRPSGKVPTLKIKLLGKRKRDSSDEEQDASGASERDSDLEFERMLQKSDDSADEKEAPVSSKADNSAPAAQDDGSGAPVVRKKAKTKIGNKFKKKNKLKKTKNFPEGEDGEHEHQDYCEVCQQGGEIILCDTCPRAYHLVCLEPELDEPPEGKWSCPHCEADGGAAEEEDDDEHQEFCRVCKDGGELLCCDSCPSAYHTFCLNPPLDTIPDGDWRCPRCSCPPLTGKAEKIITWRWAQRSNDDGPSTSKGSKNSNSRVREYFIKWHNMSYWHCEWVPEVQLDVHHPLMIRSFQRKYDMEEPPKFEESLDEADTRYKRIQRHKDKVGMKANDDAEVLEERFYKNGVKPEWLIVQRVINHRTARDGSTMYLVKWRELPYDKSTWEEEGDDIQGLRQAIDYYQDLRAVCTSETTQSRSKKSKKGRKSKLKVEDDEDRPVKHYTPPPEKPTTDLKKKYEDQPAFLEGTGMQLHPYQIEGINWLRYSWGQGIDTILADEMGLGKTIQTVTFLYSLYKEGHCRGPFLVAVPLSTLVNWEREFELWAPDFYCITYIGDKDSRAVIRENELSFEEGAIRGSKVSRLRTTQYKFNVLLTSYELISMDAACLGSIDWAVLVVDEAHRLKSNQSKFFRILNSYTIAYKLLLTGTPLQNNLEELFHLLNFLSRDKFNDLQAFQGEFADVSKEEQVKRLHEMLGPHMLRRLKTDVLKNMPSKSEFIVRVELSAMQKKFYKFILTKNYEALNSKSGGGSCSLINIMMDLKKCCNHPYLFPSAAEEATTAAGGLYEINSLTKAAGKLVLLSKMLKQLKAQNHRVLIFSQMTKMLDILEDFLEGEQYKYERIDGGITGTLRQEAIDRFNAPGAQQFVFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQANKVMIYRFVTRNSVEERVTQVAKRKMMLTHLVVRPGMGGKGANFTKQELDDILRFGTEDLFKEDDKEEAIHYDDKAVAELLDRTNRGIEEKESWANEYLSSFKVASYATKEEEEEEETEIIKQDAENSDPAYWVKLLRHHYEQHQEDVGRSLGKGKRVRKQVNYTDGGVVAADTTRDDSNWQDNGSEYNSEYSAGSDEDGGDDDFDDQNGAERKAKRRLERRDDRPLPPLLARVGGNIEVLGFNARQRKSFLNAIMRYGMPPQDAFNSQWLVRDLRGKSERNFKAYVSLFMRHLCEPGADNAETFADGVPREGLSRQHVLTRIGVMSLIRKKVQEFEHINGYYSMPELILKPCEPVRSALKQDVAALEAPPTGGNVDKSATTSNSVTPATSAAPSPAPASEKGEDKDKDSEKEKDKTSAEKSEVKQEQEAEEDKKPGDVKQENPVEEAAGDTKPSDAEVKTEVAKTEPKEETKDPEVKEEPKTEEKEKEKVDDKKPIPPTTVIDDDDDDVMIVKEDGELEKPSASSPKDQKAVAAATSAATGATGKGAEDSLEVLKRKFMFNIADGGFTELHTLWLNEEKAAVPGREYEIWHRRHDYWLLAGIVTHGYGRWQDIQNDIRFAIINEPFKMDVGKGNFLEIKNKFLARRFKLLEQALVIEEQLRRAAYLNLAQDPSHPAMSLNARFAEVECLAESHQHLSKESLAGNKPANAVLHKVLNQLEELLSDMKSDVSRLPATLARIPPVAQRLQMSERSILSRLAATAGNASNAAQLMAQFPAGFQGTTLPAFTSGPAGNFANFRPQFSVPGQLSNNSGV
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
79PhosphorylationKKRKKNESEEDSDFV
HHCCCCCCHHCCCCC		56.5321082442
83PhosphorylationKNESEEDSDFVQHDE
CCCCHHCCCCCCCCH		35.9121082442
94PhosphorylationQHDEEVEYPSTSKRG
CCCHHCCCCCCCCHH		13.9925749252
201PhosphorylationQEGGAAGSGGSAGQA
CCCCCCCCCCCCCCC		34.9418327897
204PhosphorylationGAAGSGGSAGQARSV
CCCCCCCCCCCCCCC		32.5218327897
210PhosphorylationGSAGQARSVTGDEPE
CCCCCCCCCCCCCCC		27.3519429919
221PhosphorylationDEPEEPRSSRSSRNE
CCCCCCCCCCCCCCC		40.6018327897
284PhosphorylationLGKRKRDSSDEEQDA
CCCCCCCCCCHHCCC		43.6622668510
285PhosphorylationGKRKRDSSDEEQDAS
CCCCCCCCCHHCCCC		54.0219060867
292PhosphorylationSDEEQDASGASERDS
CCHHCCCCCCCHHHH		43.0918327897
295PhosphorylationEQDASGASERDSDLE
HCCCCCCCHHHHHHH		36.3718327897
299PhosphorylationSGASERDSDLEFERM
CCCCHHHHHHHHHHH		50.7619429919
310PhosphorylationFERMLQKSDDSADEK
HHHHHHHCCCCCCHH		33.4219429919
313PhosphorylationMLQKSDDSADEKEAP
HHHHCCCCCCHHCCC		42.4819429919
569PhosphorylationEPPKFEESLDEADTR
CCCCHHHHHHHHHHH		33.6418327897
701PhosphorylationEDRPVKHYTPPPEKP
CCCCCCCCCCCCCCC		18.4119429919
702PhosphorylationDRPVKHYTPPPEKPT
CCCCCCCCCCCCCCC		29.1019429919
709PhosphorylationTPPPEKPTTDLKKKY
CCCCCCCCCCHHHHH		43.9719429919
710PhosphorylationPPPEKPTTDLKKKYE
CCCCCCCCCHHHHHC		48.1119429919
1555PhosphorylationATTSNSVTPATSAAP
CCCCCCCCCCCCCCC		13.6627794539
1563PhosphorylationPATSAAPSPAPASEK
CCCCCCCCCCCCCCC		29.0322817900
1568PhosphorylationAPSPAPASEKGEDKD
CCCCCCCCCCCCCCC		38.4927794539
1570AcetylationSPAPASEKGEDKDKD
CCCCCCCCCCCCCCC		66.1721791702
1691PhosphorylationDGELEKPSASSPKDQ
CCCCCCCCCCCHHHH		52.4219429919
1693PhosphorylationELEKPSASSPKDQKA
CCCCCCCCCHHHHHH		52.0619429919
1694PhosphorylationLEKPSASSPKDQKAV
CCCCCCCCHHHHHHH		35.3719429919
1971PhosphorylationANFRPQFSVPGQLSN
CCCCCCCCCCCCCCC		23.3522817900
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 CHDM_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHDM_DROME !!
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 CHDM_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAF1_DROMECaf1physical
15516265
NAT10_DROMEl(1)G0020physical
22036573
RRP12_DROMECG2691physical
22036573
TTKB_DROMEttkphysical
20733004
TTKA_DROMEttkphysical
20733004
CHDM_DROMEMi-2physical
20733004
DDX17_DROMERm62physical
20733004
CAF1_DROMECaf1physical
20733004
HDAC1_DROMERpd3physical
20733004
RCC1_DROMERcc1genetic
25501812
TOP2_DROMETop2physical
25776889
MLE_DROMEmlephysical
25776889
CTBP_DROMECtBPphysical
20733004
TTKB_DROMEttkphysical
25242320
TTKA_DROMEttkphysical
25242320
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHDM_DROME

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-83; SER-201;SER-204; SER-210; SER-221; SER-284; SER-285; SER-292; SER-295;SER-299; SER-310; SER-313; TYR-701; THR-702; SER-1691 AND SER-1694,AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory