CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001712
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chromodomain-helicase-DNA-binding protein Mi-2 homolog 
Protein Synonyms/Alias
 ATP-dependent helicase Mi-2; dMi-2 
Gene Name
 Mi-2 
Gene Synonyms/Alias
 CG8103 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
1570SPAPASEKGEDKDKDacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702] 
Functional 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. 
Sequence Annotation
 DOMAIN 488 566 Chromo 1.
 DOMAIN 612 673 Chromo 2.
 DOMAIN 742 924 Helicase ATP-binding.
 DOMAIN 1056 1218 Helicase C-terminal.
 ZN_FING 377 424 PHD-type 1.
 ZN_FING 437 484 PHD-type 2.
 NP_BIND 755 762 ATP (Potential).
 MOTIF 875 878 DEAH box.
 MOD_RES 79 79 Phosphoserine.
 MOD_RES 83 83 Phosphoserine.
 MOD_RES 201 201 Phosphoserine.
 MOD_RES 204 204 Phosphoserine.
 MOD_RES 210 210 Phosphoserine.
 MOD_RES 221 221 Phosphoserine.
 MOD_RES 284 284 Phosphoserine.
 MOD_RES 285 285 Phosphoserine.
 MOD_RES 292 292 Phosphoserine.
 MOD_RES 295 295 Phosphoserine.
 MOD_RES 299 299 Phosphoserine.
 MOD_RES 310 310 Phosphoserine.
 MOD_RES 313 313 Phosphoserine.
 MOD_RES 701 701 Phosphotyrosine.
 MOD_RES 702 702 Phosphothreonine.
 MOD_RES 1691 1691 Phosphoserine.
 MOD_RES 1694 1694 Phosphoserine.  
Keyword
 ATP-binding; Complete proteome; DNA-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1982 AA 
Protein Sequence
MASEEENDDN FQEEEEAQED NAPAAELSND SDAPLKPNND EDDDYDPEDS RRKKKGKKRK 60
TRKGEEKGRK KKKRKKNESE EDSDFVQHDE EVEYPSTSKR GRKRKEEKQA AKEKESASSG 120
MPSVEDVCSA FSVCNVEIEY SEEELQSLTT YKAFMHHVRP ILQKENPKIA APKLVMLVAA 180
KWREFCESNP HIQQEGGAAG SGGSAGQARS VTGDEPEEPR SSRSSRNEKP DDIYEEAVEE 240
EEEEEEEEKK PRRKRSGRGK KGRRPSGKVP TLKIKLLGKR KRDSSDEEQD ASGASERDSD 300
LEFERMLQKS DDSADEKEAP VSSKADNSAP AAQDDGSGAP VVRKKAKTKI GNKFKKKNKL 360
KKTKNFPEGE DGEHEHQDYC EVCQQGGEII LCDTCPRAYH LVCLEPELDE PPEGKWSCPH 420
CEADGGAAEE EDDDEHQEFC RVCKDGGELL CCDSCPSAYH TFCLNPPLDT IPDGDWRCPR 480
CSCPPLTGKA EKIITWRWAQ RSNDDGPSTS KGSKNSNSRV REYFIKWHNM SYWHCEWVPE 540
VQLDVHHPLM IRSFQRKYDM EEPPKFEESL DEADTRYKRI QRHKDKVGMK ANDDAEVLEE 600
RFYKNGVKPE WLIVQRVINH RTARDGSTMY LVKWRELPYD KSTWEEEGDD IQGLRQAIDY 660
YQDLRAVCTS ETTQSRSKKS KKGRKSKLKV EDDEDRPVKH YTPPPEKPTT DLKKKYEDQP 720
AFLEGTGMQL HPYQIEGINW LRYSWGQGID TILADEMGLG KTIQTVTFLY SLYKEGHCRG 780
PFLVAVPLST LVNWEREFEL WAPDFYCITY IGDKDSRAVI RENELSFEEG AIRGSKVSRL 840
RTTQYKFNVL LTSYELISMD AACLGSIDWA VLVVDEAHRL KSNQSKFFRI LNSYTIAYKL 900
LLTGTPLQNN LEELFHLLNF LSRDKFNDLQ AFQGEFADVS KEEQVKRLHE MLGPHMLRRL 960
KTDVLKNMPS KSEFIVRVEL SAMQKKFYKF ILTKNYEALN SKSGGGSCSL INIMMDLKKC 1020
CNHPYLFPSA AEEATTAAGG LYEINSLTKA AGKLVLLSKM LKQLKAQNHR VLIFSQMTKM 1080
LDILEDFLEG EQYKYERIDG GITGTLRQEA IDRFNAPGAQ QFVFLLSTRA GGLGINLATA 1140
DTVIIYDSDW NPHNDIQAFS RAHRIGQANK VMIYRFVTRN SVEERVTQVA KRKMMLTHLV 1200
VRPGMGGKGA NFTKQELDDI LRFGTEDLFK EDDKEEAIHY DDKAVAELLD RTNRGIEEKE 1260
SWANEYLSSF KVASYATKEE EEEEETEIIK QDAENSDPAY WVKLLRHHYE QHQEDVGRSL 1320
GKGKRVRKQV NYTDGGVVAA DTTRDDSNWQ DNGSEYNSEY SAGSDEDGGD DDFDDQNGAE 1380
RKAKRRLERR DDRPLPPLLA RVGGNIEVLG FNARQRKSFL NAIMRYGMPP QDAFNSQWLV 1440
RDLRGKSERN FKAYVSLFMR HLCEPGADNA ETFADGVPRE GLSRQHVLTR IGVMSLIRKK 1500
VQEFEHINGY YSMPELILKP CEPVRSALKQ DVAALEAPPT GGNVDKSATT SNSVTPATSA 1560
APSPAPASEK GEDKDKDSEK EKDKTSAEKS EVKQEQEAEE DKKPGDVKQE NPVEEAAGDT 1620
KPSDAEVKTE VAKTEPKEET KDPEVKEEPK TEEKEKEKVD DKKPIPPTTV IDDDDDDVMI 1680
VKEDGELEKP SASSPKDQKA VAAATSAATG ATGKGAEDSL EVLKRKFMFN IADGGFTELH 1740
TLWLNEEKAA VPGREYEIWH RRHDYWLLAG IVTHGYGRWQ DIQNDIRFAI INEPFKMDVG 1800
KGNFLEIKNK FLARRFKLLE QALVIEEQLR RAAYLNLAQD PSHPAMSLNA RFAEVECLAE 1860
SHQHLSKESL AGNKPANAVL HKVLNQLEEL LSDMKSDVSR LPATLARIPP VAQRLQMSER 1920
SILSRLAATA GNASNAAQLM AQFPAGFQGT TLPAFTSGPA GNFANFRPQF SVPGQLSNNS 1980
GV 1982 
Gene Ontology
 GO:0016581; C:NuRD complex; ISS:FlyBase.
 GO:0005700; C:polytene chromosome; IDA:FlyBase.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004003; F:ATP-dependent DNA helicase activity; ISS:FlyBase.
 GO:0003677; F:DNA binding; IDA:FlyBase.
 GO:0031491; F:nucleosome binding; IDA:FlyBase.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
 GO:0007517; P:muscle organ development; IMP:FlyBase.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:FlyBase.
 GO:0042766; P:nucleosome mobilization; IDA:FlyBase.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR012957; CHD_C2.
 IPR012958; CHD_N.
 IPR023780; Chromo_domain.
 IPR000953; Chromo_domain/shadow.
 IPR016197; Chromodomain-like.
 IPR002464; DNA/RNA_helicase_DEAH_CS.
 IPR009462; DUF1086.
 IPR009463; DUF1087.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR000330; SNF2_N.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF08074; CHDCT2
 PF08073; CHDNT
 PF00385; Chromo
 PF06461; DUF1086
 PF06465; DUF1087
 PF00271; Helicase_C
 PF00628; PHD
 PF00176; SNF2_N 
SMART
 SM00298; CHROMO
 SM00487; DEXDc
 SM00490; HELICc
 SM00249; PHD
 SM00184; RING 
PROSITE
 PS00598; CHROMO_1
 PS50013; CHROMO_2
 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS