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Protein

Chromodomain-helicase-DNA-binding protein Mi-2 homolog

Gene

Mi-2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri377 – 42448PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri437 – 48448PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi755 – 7628ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATPase activity Source: FlyBase
  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: FlyBase
  • chromatin binding Source: FlyBase
  • DNA binding Source: FlyBase
  • DNA helicase activity Source: FlyBase
  • helicase activity Source: FlyBase
  • nucleosome binding Source: FlyBase
  • nucleosome-dependent ATPase activity Source: FlyBase
  • zinc ion binding Source: FlyBase

GO - Biological processi

  • ATP-dependent chromatin remodeling Source: CACAO
  • chromosome decondensation Source: CACAO
  • chromosome organization Source: CACAO
  • dendrite morphogenesis Source: FlyBase
  • DNA duplex unwinding Source: GOC
  • muscle organ development Source: FlyBase
  • negative regulation of cohesin localization to chromatin Source: FlyBase
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • nucleosome mobilization Source: FlyBase
  • regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • spermatogenesis Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Chromodomain-helicase-DNA-binding protein Mi-2 homolog (EC:3.6.4.12)
Alternative name(s):
ATP-dependent helicase Mi-2
Short name:
dMi-2
Gene namesi
Name:Mi-2
ORF Names:CG8103
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0262519. Mi-2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: FlyBase
  • nucleus Source: FlyBase
  • NuRD complex Source: FlyBase
  • polytene chromosome Source: FlyBase
  • transcriptionally active chromatin Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi737 – 7371G → D in allele MI-2-5; larval lethal. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19821982Chromodomain-helicase-DNA-binding protein Mi-2 homologPRO_0000080236Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791Phosphoserine1 Publication
Modified residuei83 – 831Phosphoserine1 Publication
Modified residuei201 – 2011Phosphoserine1 Publication
Modified residuei204 – 2041Phosphoserine1 Publication
Modified residuei210 – 2101Phosphoserine1 Publication
Modified residuei221 – 2211Phosphoserine1 Publication
Modified residuei284 – 2841Phosphoserine1 Publication
Modified residuei285 – 2851Phosphoserine1 Publication
Modified residuei292 – 2921Phosphoserine1 Publication
Modified residuei295 – 2951Phosphoserine1 Publication
Modified residuei299 – 2991Phosphoserine1 Publication
Modified residuei310 – 3101Phosphoserine1 Publication
Modified residuei313 – 3131Phosphoserine1 Publication
Modified residuei701 – 7011Phosphotyrosine1 Publication
Modified residuei702 – 7021Phosphothreonine1 Publication
Modified residuei1691 – 16911Phosphoserine1 Publication
Modified residuei1694 – 16941Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO97159.
PRIDEiO97159.

PTM databases

iPTMnetiO97159.

Expressioni

Gene expression databases

BgeeiO97159.
ExpressionAtlasiO97159. differential.
GenevisibleiO97159. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CDK2AP1Q9VZ274EBI-112333,EBI-196367
MEP-1Q0E8J013EBI-112333,EBI-91014

GO - Molecular functioni

  • nucleosome binding Source: FlyBase

Protein-protein interaction databases

BioGridi65438. 20 interactions.
DIPiDIP-22862N.
IntActiO97159. 226 interactions.
MINTiMINT-864813.
STRINGi7227.FBpp0099808.

Structurei

3D structure databases

ProteinModelPortaliO97159.
SMRiO97159. Positions 373-425, 434-489.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini488 – 56679Chromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini612 – 67362Chromo 2PROSITE-ProRule annotationAdd
BLAST
Domaini742 – 924183Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1056 – 1218163Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi875 – 8784DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 164Poly-Glu
Compositional biasi70 – 767Poly-Lys
Compositional biasi239 – 24810Poly-Glu
Compositional biasi1279 – 12879Poly-Glu
Compositional biasi1672 – 16776Poly-Asp

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 2 chromo domains.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri377 – 42448PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri437 – 48448PHD-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0383. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00760000119067.
InParanoidiO97159.
OrthoDBiEOG7C8GG7.
PhylomeDBiO97159.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR012957. CHD_C2.
IPR012958. CHD_N.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
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.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF08074. CHDCT2. 1 hit.
PF08073. CHDNT. 1 hit.
PF00385. Chromo. 2 hits.
PF06461. DUF1086. 1 hit.
PF06465. DUF1087. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00628. PHD. 2 hits.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM01146. DUF1086. 1 hit.
SM01147. DUF1087. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 2 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50013. CHROMO_2. 2 hits.
PS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O97159-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASEEENDDN FQEEEEAQED NAPAAELSND SDAPLKPNND EDDDYDPEDS
60 70 80 90 100
RRKKKGKKRK TRKGEEKGRK KKKRKKNESE EDSDFVQHDE EVEYPSTSKR
110 120 130 140 150
GRKRKEEKQA AKEKESASSG MPSVEDVCSA FSVCNVEIEY SEEELQSLTT
160 170 180 190 200
YKAFMHHVRP ILQKENPKIA APKLVMLVAA KWREFCESNP HIQQEGGAAG
210 220 230 240 250
SGGSAGQARS VTGDEPEEPR SSRSSRNEKP DDIYEEAVEE EEEEEEEEKK
260 270 280 290 300
PRRKRSGRGK KGRRPSGKVP TLKIKLLGKR KRDSSDEEQD ASGASERDSD
310 320 330 340 350
LEFERMLQKS DDSADEKEAP VSSKADNSAP AAQDDGSGAP VVRKKAKTKI
360 370 380 390 400
GNKFKKKNKL KKTKNFPEGE DGEHEHQDYC EVCQQGGEII LCDTCPRAYH
410 420 430 440 450
LVCLEPELDE PPEGKWSCPH CEADGGAAEE EDDDEHQEFC RVCKDGGELL
460 470 480 490 500
CCDSCPSAYH TFCLNPPLDT IPDGDWRCPR CSCPPLTGKA EKIITWRWAQ
510 520 530 540 550
RSNDDGPSTS KGSKNSNSRV REYFIKWHNM SYWHCEWVPE VQLDVHHPLM
560 570 580 590 600
IRSFQRKYDM EEPPKFEESL DEADTRYKRI QRHKDKVGMK ANDDAEVLEE
610 620 630 640 650
RFYKNGVKPE WLIVQRVINH RTARDGSTMY LVKWRELPYD KSTWEEEGDD
660 670 680 690 700
IQGLRQAIDY YQDLRAVCTS ETTQSRSKKS KKGRKSKLKV EDDEDRPVKH
710 720 730 740 750
YTPPPEKPTT DLKKKYEDQP AFLEGTGMQL HPYQIEGINW LRYSWGQGID
760 770 780 790 800
TILADEMGLG KTIQTVTFLY SLYKEGHCRG PFLVAVPLST LVNWEREFEL
810 820 830 840 850
WAPDFYCITY IGDKDSRAVI RENELSFEEG AIRGSKVSRL RTTQYKFNVL
860 870 880 890 900
LTSYELISMD AACLGSIDWA VLVVDEAHRL KSNQSKFFRI LNSYTIAYKL
910 920 930 940 950
LLTGTPLQNN LEELFHLLNF LSRDKFNDLQ AFQGEFADVS KEEQVKRLHE
960 970 980 990 1000
MLGPHMLRRL KTDVLKNMPS KSEFIVRVEL SAMQKKFYKF ILTKNYEALN
1010 1020 1030 1040 1050
SKSGGGSCSL INIMMDLKKC CNHPYLFPSA AEEATTAAGG LYEINSLTKA
1060 1070 1080 1090 1100
AGKLVLLSKM LKQLKAQNHR VLIFSQMTKM LDILEDFLEG EQYKYERIDG
1110 1120 1130 1140 1150
GITGTLRQEA IDRFNAPGAQ QFVFLLSTRA GGLGINLATA DTVIIYDSDW
1160 1170 1180 1190 1200
NPHNDIQAFS RAHRIGQANK VMIYRFVTRN SVEERVTQVA KRKMMLTHLV
1210 1220 1230 1240 1250
VRPGMGGKGA NFTKQELDDI LRFGTEDLFK EDDKEEAIHY DDKAVAELLD
1260 1270 1280 1290 1300
RTNRGIEEKE SWANEYLSSF KVASYATKEE EEEEETEIIK QDAENSDPAY
1310 1320 1330 1340 1350
WVKLLRHHYE QHQEDVGRSL GKGKRVRKQV NYTDGGVVAA DTTRDDSNWQ
1360 1370 1380 1390 1400
DNGSEYNSEY SAGSDEDGGD DDFDDQNGAE RKAKRRLERR DDRPLPPLLA
1410 1420 1430 1440 1450
RVGGNIEVLG FNARQRKSFL NAIMRYGMPP QDAFNSQWLV RDLRGKSERN
1460 1470 1480 1490 1500
FKAYVSLFMR HLCEPGADNA ETFADGVPRE GLSRQHVLTR IGVMSLIRKK
1510 1520 1530 1540 1550
VQEFEHINGY YSMPELILKP CEPVRSALKQ DVAALEAPPT GGNVDKSATT
1560 1570 1580 1590 1600
SNSVTPATSA APSPAPASEK GEDKDKDSEK EKDKTSAEKS EVKQEQEAEE
1610 1620 1630 1640 1650
DKKPGDVKQE NPVEEAAGDT KPSDAEVKTE VAKTEPKEET KDPEVKEEPK
1660 1670 1680 1690 1700
TEEKEKEKVD DKKPIPPTTV IDDDDDDVMI VKEDGELEKP SASSPKDQKA
1710 1720 1730 1740 1750
VAAATSAATG ATGKGAEDSL EVLKRKFMFN IADGGFTELH TLWLNEEKAA
1760 1770 1780 1790 1800
VPGREYEIWH RRHDYWLLAG IVTHGYGRWQ DIQNDIRFAI INEPFKMDVG
1810 1820 1830 1840 1850
KGNFLEIKNK FLARRFKLLE QALVIEEQLR RAAYLNLAQD PSHPAMSLNA
1860 1870 1880 1890 1900
RFAEVECLAE SHQHLSKESL AGNKPANAVL HKVLNQLEEL LSDMKSDVSR
1910 1920 1930 1940 1950
LPATLARIPP VAQRLQMSER SILSRLAATA GNASNAAQLM AQFPAGFQGT
1960 1970 1980
TLPAFTSGPA GNFANFRPQF SVPGQLSNNS GV
Length:1,982
Mass (Da):224,201
Last modified:June 1, 2000 - v2
Checksum:iED8E256D1AD0AC2F
GO

Sequence cautioni

The sequence AAM29373.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011G → A in AAD17276 (PubMed:9836641).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF119716 mRNA. Translation: AAD17276.1.
AE014296 Genomic DNA. Translation: AAF49099.2.
AY113368 mRNA. Translation: AAM29373.1. Different initiation.
RefSeqiNP_001163476.1. NM_001170005.2.
NP_649154.2. NM_140897.4.
UniGeneiDm.28317.

Genome annotation databases

EnsemblMetazoaiFBtr0074919; FBpp0074688; FBgn0262519.
FBtr0302046; FBpp0291256; FBgn0262519.
GeneIDi40170.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF119716 mRNA. Translation: AAD17276.1.
AE014296 Genomic DNA. Translation: AAF49099.2.
AY113368 mRNA. Translation: AAM29373.1. Different initiation.
RefSeqiNP_001163476.1. NM_001170005.2.
NP_649154.2. NM_140897.4.
UniGeneiDm.28317.

3D structure databases

ProteinModelPortaliO97159.
SMRiO97159. Positions 373-425, 434-489.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65438. 20 interactions.
DIPiDIP-22862N.
IntActiO97159. 226 interactions.
MINTiMINT-864813.
STRINGi7227.FBpp0099808.

PTM databases

iPTMnetiO97159.

Proteomic databases

PaxDbiO97159.
PRIDEiO97159.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074919; FBpp0074688; FBgn0262519.
FBtr0302046; FBpp0291256; FBgn0262519.
GeneIDi40170.

Organism-specific databases

CTDi40170.
FlyBaseiFBgn0262519. Mi-2.

Phylogenomic databases

eggNOGiKOG0383. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00760000119067.
InParanoidiO97159.
OrthoDBiEOG7C8GG7.
PhylomeDBiO97159.

Miscellaneous databases

ChiTaRSiMi-2. fly.
GenomeRNAii40170.
NextBioi817384.
PROiO97159.

Gene expression databases

BgeeiO97159.
ExpressionAtlasiO97159. differential.
GenevisibleiO97159. DM.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProiIPR012957. CHD_C2.
IPR012958. CHD_N.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
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.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF08074. CHDCT2. 1 hit.
PF08073. CHDNT. 1 hit.
PF00385. Chromo. 2 hits.
PF06461. DUF1086. 1 hit.
PF06465. DUF1087. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00628. PHD. 2 hits.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM01146. DUF1086. 1 hit.
SM01147. DUF1087. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 2 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50013. CHROMO_2. 2 hits.
PS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "dMi-2, a hunchback-interacting protein that functions in Polycomb repression."
    Kehle J., Beuchle D., Treuheit S., Christen B., Kennison J.A., Bienz M., Muller J.
    Science 282:1897-1900(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLY-737.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1191-1982.
    Strain: Berkeley.
    Tissue: Embryo.
  5. "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) [PubMed] [Europe PMC] [Abstract]
    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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiCHDM_DROME
AccessioniPrimary (citable) accession number: O97159
Secondary accession number(s): Q8MZ43, Q9VW50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: June 1, 2000
Last modified: May 11, 2016
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.