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Q24478 (CP190_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centrosome-associated zinc finger protein CP190
Alternative name(s):
Protein enhancer of mod(mdg4)4-1
dMAP190
Gene names
Name:Cp190
Synonyms:E(mod)4-1
ORF Names:CG6384
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1096 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the gypsy chromatin insulator complex which is required for the function of the gypsy chromatin insulator and other endogenous chromatin insulators. Chromatin insulators are regulatory elements which establish independent domains of transcriptional activity within eukaryotic genomes. Insulators have two defining properties; they can block the communication between an enhancer and a promoter when placed between them and can also buffer transgenes from position effect variegation (PEV). Insulators are proposed to structure the chromatin fiber into independent domains of differing transcriptional potential by promoting the formation of distinct chromatin loops. This chromatin looping may involve the formation of insulator bodies, where homotypic interactions between individual subunits of the insulator complex could promote the clustering of widely spaced insulators at the nuclear periphery. Within the gypsy insulator complex, this protein may directly bind to insulator DNA at sites distinct from those recognized by su(Hw). Required during embryogenesis for axial expansion, an actin/myosin dependent process that distributes the dividing nuclei along the anterior-posterior axis of the syncytial embryo. Does not appear to play a crucial role in organizing centrosomal microtubules during mitosis. Ref.12 Ref.14 Ref.15

Subunit structure

Component of the gypsy chromatin insulator complex, composed of Cp190, mod(mdg4) and su(Hw). The gypsy chromatin insulator complex interacts with Topors via mod(mdg4) and su(Hw). Interacts with Cp60 and microtubules. Ref.5 Ref.6 Ref.7 Ref.8 Ref.11 Ref.12 Ref.14

Subcellular location

Nucleus. Cytoplasmcytoskeleton. Chromosome. Note: Nucleus in interphase. Colocalizes with other elements of the gypsy chromatin insulator complex at multiple sites on polytene chromosomes and at nuclear insulator bodies. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Tissue specificity

Expressed in spermatids but not in mature spermatozoa. Localizes within the spermatids to a sheath of microtubules around the nucleus and to microtubules within the tail. Ref.10

Developmental stage

Localizes to the centrosome throughout the nuclear division cycle in early syncytial embryos. Localization to the interphase nucleus is seen from nuclear cycle 9 onwards. Ref.1 Ref.5 Ref.6 Ref.8

Sequence similarities

Contains 1 BTB (POZ) domain.

Contains 2 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentChromosome
Cytoplasm
Cytoskeleton
Microtubule
Nucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionChromatin regulator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

gene looping

Inferred from mutant phenotype PubMed 21981916. Source: FlyBase

microtubule-based process

Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase

nuclear axial expansion

Inferred from mutant phenotype Ref.15. Source: FlyBase

regulation of cytoskeleton organization

Inferred from mutant phenotype Ref.15. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentrosome

Inferred from direct assay Ref.1Ref.9. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule associated complex

Inferred from direct assay PubMed 18433294. Source: FlyBase

nucleus

Inferred from direct assay Ref.1Ref.9. Source: UniProtKB

polytene chromosome

Inferred from direct assay Ref.14Ref.1. Source: UniProtKB

polytene chromosome band

Inferred from direct assay PubMed 21194420. Source: FlyBase

   Molecular_functionDNA binding

Inferred from direct assay Ref.14. Source: UniProtKB

POZ domain binding

Inferred from direct assay PubMed 21821048. Source: FlyBase

chromatin binding

Inferred from direct assay Ref.1. Source: UniProtKB

chromatin insulator sequence binding

Inferred from direct assay PubMed 17805343PubMed 20082086PubMed 21194420. Source: FlyBase

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule binding

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10961096Centrosome-associated zinc finger protein CP190
PRO_0000232629

Regions

Domain30 – 9768BTB
Zinc finger538 – 56124C2H2-type 1
Zinc finger567 – 59024C2H2-type 2
Region207 – 27165Nuclear localization
Region385 – 508124Centrosomal localization and interaction with microtubules

Amino acid modifications

Modified residue1971Phosphoserine Ref.18
Modified residue2111Phosphoserine Ref.17
Modified residue2291Phosphothreonine Ref.18
Modified residue2331Phosphoserine Ref.18
Modified residue2981Phosphoserine Ref.18
Modified residue3191Phosphoserine Ref.17
Modified residue6031Phosphothreonine Ref.18
Modified residue6101Phosphoserine Ref.18
Modified residue7081Phosphoserine Ref.18
Modified residue7231Phosphoserine Ref.18
Modified residue7271Phosphothreonine Ref.18
Modified residue7451Phosphoserine Ref.18
Modified residue7481Phosphoserine Ref.18
Modified residue7571Phosphoserine Ref.18
Modified residue7601Phosphoserine Ref.18
Modified residue8171Phosphothreonine Ref.18
Modified residue9201Phosphoserine Ref.17 Ref.18
Modified residue9251Phosphoserine Ref.17
Modified residue9271Phosphoserine Ref.18
Modified residue9361Phosphothreonine Ref.18
Modified residue9381Phosphoserine Ref.18
Modified residue10711Phosphoserine Ref.18
Modified residue10741Phosphoserine Ref.18

Experimental info

Sequence conflict10611G → D in CAA90324. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q24478 [UniParc].

Last modified April 18, 2006. Version 2.
Checksum: 5CD5C5492B948D39

FASTA1,096121,679
        10         20         30         40         50         60 
MGEVKSVKVD NWGVFFLQKL QNFFNKTDYC DLTLQFRDNS QLKVHRLVLS ACTDYFNVLE 

        70         80         90        100        110        120 
QTCEIVDDAL IMPNEFQADV VVPIVNFMYT GTLEFELKMY GKLLRTAKEM NMTVLLKLLE 

       130        140        150        160        170        180 
AHRRTMENVN RQQRPPSPKG IRRRTVGQPS SGLPQQRVLG PSPQSRNVAT PIAQRANTQR 

       190        200        210        220        230        240 
GSTGNTMSRT SGGSNRSPYG DSSNVKQEPT SPFEQLRKGY NNNKRPAQTS LLSPPSKKPS 

       250        260        270        280        290        300 
LEEVKEFAEQ QRMRKQIAAE YGDNDPEYDG GMLYDDVHAG DDDDDDMPPQ PSTSKQQSPQ 

       310        320        330        340        350        360 
GTQTQLEHGS TTIILKQDSP SQTPTIIVKD SSNAKLNHTK IIAEVLRQYP HIVKGHKNIK 

       370        380        390        400        410        420 
LKIMPNTPAA PTEKSAPATV KPPANQSSAT TSPHKKLHVS FKADKSTPLI TAQQKAASSQ 

       430        440        450        460        470        480 
QKSGTSQTTG NQGTGANPPA NTAAAQKRRI DSKTMHALIA QGAENTTGPW LCLRCGVNGR 

       490        500        510        520        530        540 
PISIPSYRGF RRHLINTHKE TIDPALCEHC GWRSVNNREL HFHMYMEHQT KSLLYTFAEC 

       550        560        570        580        590        600 
ALCNQSYRTK GELEAHINEV HTDDNKQQCI YCNKVFEQEL QLYRHMKSYH KEQALEDGII 

       610        620        630        640        650        660 
DETDEEFLGS QDEEEEAEGD EEQEPEQTGK VRILSDISLP ATSAITVQQA QQEQLQEEDV 

       670        680        690        700        710        720 
EQVQQEVKFV GADGNEVELT DEQRKEILSQ LNQQQAGATA GGVVMVLSEP EAEHVKQETD 

       730        740        750        760        770        780 
EKSLAGTEEE YDDSQIYSEL GAADSVESAK KNIADESKES IDNLEWAENL IAESEEQSNK 

       790        800        810        820        830        840 
EPKSDKPRDD ISEKLKELTG DWTEDENDDD VDDKPATAEL ASELANKDPE PTVHEEEDDI 

       850        860        870        880        890        900 
DLALQSLHKG PEEATEEKAS EESVTSADDA VDAVPNINSQ PEKMDVDSEA ADEKASKAEV 

       910        920        930        940        950        960 
QIKKEAELEN DQEEFIKEDS PIPHSDSVAE LREAVTASEG EDDVHLEADN IRKELLDELI 

       970        980        990       1000       1010       1020 
AEAEKPDQEK DIVQSEENAT TEALDRSVTD EDDLVPPTQV STEQMEIDEP AAEKAAENNE 

      1030       1040       1050       1060       1070       1080 
DTRTADEKEA VEDKPNQTQD VTTAEKPTLE SAKAGDEATS GEAASVDKVK SLISEWGDDD 

      1090 
EDEDENGVSA AAKEEL 

« Hide

References

« Hide 'large scale' references
[1]"The 190 kDa centrosome-associated protein of Drosophila melanogaster contains four zinc finger motifs and binds to specific sites on polytene chromosomes."
Whitfield W.G.F., Chaplin M.A., Oegema K., Parry H., Glover D.M.
J. Cell Sci. 108:3377-3387(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
Strain: Oregon-R.
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Purification of a multiprotein complex containing centrosomal proteins from the Drosophila embryo by chromatography with low-affinity polyclonal antibodies."
Kellogg D.R., Alberts B.M.
Mol. Biol. Cell 3:1-11(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CP60, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[6]"Drosophila gamma-tubulin is part of a complex containing two previously identified centrosomal MAPs."
Raff J.W., Kellogg D.R., Alberts B.M.
J. Cell Biol. 121:823-835(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CP60 AND MICROTUBULES, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[7]"The cell cycle-dependent localization of the CP190 centrosomal protein is determined by the coordinate action of two separable domains."
Oegema K., Whitfield W.G.F., Alberts B.M.
J. Cell Biol. 131:1261-1273(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
[8]"CP60: a microtubule-associated protein that is localized to the centrosome in a cell cycle-specific manner."
Kellogg D.R., Oegema K., Raff J., Schneider K., Alberts B.M.
Mol. Biol. Cell 6:1673-1684(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CP60, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[9]"Two proteins that cycle asynchronously between centrosomes and nuclear structures: Drosophila CP60 and CP190."
Oegema K., Marshall W.F., Sedat J.W., Alberts B.M.
J. Cell Sci. 110:1573-1583(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Assembly of the zygotic centrosome in the fertilized Drosophila egg."
Riparbelli M.G., Whitfield W.G.F., Dallai R., Callaini G.
Mech. Dev. 65:135-144(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"Recruitment of the gamma-tubulin ring complex to Drosophila salt-stripped centrosome scaffolds."
Moritz M., Zheng Y., Alberts B.M., Oegema K.
J. Cell Biol. 142:775-786(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CP60.
[12]"The Drosophila centrosome-associated protein CP190 is essential for viability but not for cell division."
Butcher R.D.J., Chodagam S., Basto R., Wakefield J.G., Henderson D.S., Raff J.W., Whitfield W.G.F.
J. Cell Sci. 117:1191-1199(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
[13]"Elongation of centriolar microtubule triplets contributes to the formation of the mitotic spindle in gamma-tubulin-depleted cells."
Raynaud-Messina B., Mazzolini L., Moisand A., Cirinesi A.-M., Wright M.
J. Cell Sci. 117:5497-5507(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"The centrosomal protein CP190 is a component of the gypsy chromatin insulator."
Pai C.-Y., Lei E.P., Ghosh D., Corces V.G.
Mol. Cell 16:737-748(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH MOD(MDG4) AND SU(HW), SUBCELLULAR LOCATION.
[15]"The centrosomal protein CP190 regulates myosin function during early Drosophila development."
Chodagam S., Royou A., Whitfield W.G.F., Karess R., Raff J.W.
Curr. Biol. 15:1308-1313(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]"The ubiquitin ligase dTopors directs the nuclear organization of a chromatin insulator."
Capelson M., Corces V.G.
Mol. Cell 20:105-116(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[17]"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-319; SER-920 AND SER-925, IDENTIFICATION BY MASS SPECTROMETRY.
[18]"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-197; THR-229; SER-233; SER-298; THR-603; SER-610; SER-708; SER-723; THR-727; SER-745; SER-748; SER-757; SER-760; THR-817; SER-920; SER-927; THR-936; SER-938; SER-1071 AND SER-1074, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z50021 mRNA. Translation: CAA90324.1.
AE014297 Genomic DNA. Translation: AAF55159.1.
AE014297 Genomic DNA. Translation: AAN13643.1.
BT010090 mRNA. Translation: AAQ22559.1.
PIRT13802.
RefSeqNP_524359.2. NM_079635.3.
NP_731998.1. NM_169632.2.
UniGeneDm.2423.

3D structure databases

ProteinModelPortalQ24478.
SMRQ24478. Positions 8-115, 468-595.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66912. 11 interactions.
IntActQ24478. 6 interactions.
MINTMINT-1899376.
STRING7227.FBpp0082580.

Proteomic databases

PaxDbQ24478.
PRIDEQ24478.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0083126; FBpp0082580; FBgn0000283.
FBtr0083127; FBpp0082581; FBgn0000283.
GeneID41848.
KEGGdme:Dmel_CG6384.

Organism-specific databases

CTD41848.
FlyBaseFBgn0000283. Cp190.

Phylogenomic databases

eggNOGNOG279218.
InParanoidQ24478.
OMAINTHKET.
OrthoDBEOG7992PZ.
PhylomeDBQ24478.

Enzyme and pathway databases

SignaLinkQ24478.

Gene expression databases

BgeeQ24478.

Family and domain databases

Gene3D3.30.710.10. 1 hit.
InterProIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamPF00651. BTB. 1 hit.
PF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTSM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 4 hits.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
PROSITEPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi41848.
NextBio825881.

Entry information

Entry nameCP190_DROME
AccessionPrimary (citable) accession number: Q24478
Secondary accession number(s): A4V2Y3, Q9VFA1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: April 18, 2006
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase