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Protein

Transcriptional activator cubitus interruptus

Gene

ci

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

Functioni

Has a dual function as a transcriptional activator and a repressor of the hedgehog (Hh) pathway. The full-length ci form (ciFL), acts as an activator (ciA) while ciR, its C-terminally truncated form, acts as a repressor. Involved in segment polarity. Required for the normal development of the posterior half of each embryonic segment. Engrailed protein directly represses ci expression in posterior compartment cells.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri451 – 47626C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri484 – 51128C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri517 – 54125C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri547 – 57226C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri578 – 60326C2H2-type 5PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: FlyBase
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: FlyBase
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: FlyBase
  • transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding Source: FlyBase
  • transcription factor activity, sequence-specific DNA binding Source: FlyBase
  • transcription regulatory region DNA binding Source: FlyBase

GO - Biological processi

  • blastoderm segmentation Source: FlyBase
  • cuticle pattern formation Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • epidermis development Source: FlyBase
  • eye morphogenesis Source: FlyBase
  • genital disc anterior/posterior pattern formation Source: FlyBase
  • heart formation Source: FlyBase
  • labial disc development Source: FlyBase
  • mucosal immune response Source: FlyBase
  • negative regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • neuron development Source: FlyBase
  • oogenesis Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • positive regulation of epithelial cell differentiation Source: FlyBase
  • positive regulation of G1/S transition of mitotic cell cycle Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • regulation of mitotic cell cycle Source: FlyBase
  • regulation of transcription, DNA-templated Source: UniProtKB
  • segment polarity determination Source: UniProtKB
  • smoothened signaling pathway Source: FlyBase
  • spiracle morphogenesis, open tracheal system Source: FlyBase
  • transcription from RNA polymerase II promoter Source: GOC
  • wing disc anterior/posterior pattern formation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Repressor, Segmentation polarity protein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-5610780. Degradation of GLI1 by the proteasome.
R-DME-5610785. GLI3 is processed to GLI3R by the proteasome.
R-DME-5610787. Hedgehog 'off' state.
R-DME-5632684. Hedgehog 'on' state.
SignaLinkiP19538.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional activator cubitus interruptus
Short name:
Transcriptional activator ci
Alternative name(s):
ci form of 155 kDa
Short name:
ci-155
ci full length protein
Short name:
ciFL
Cleaved into the following chain:
Transcriptional repressor cubitus interruptus
Short name:
Transcriptional repressor ci
Alternative name(s):
ci C-terminally truncated form
ci form of 75 kDa
Short name:
ci-75
Gene namesi
Name:ci
Synonyms:ci-D
ORF Names:CG2125
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 4

Organism-specific databases

FlyBaseiFBgn0004859. ci.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • Hedgehog signaling complex Source: FlyBase
  • membrane Source: FlyBase
  • nucleus Source: UniProtKB
  • protein complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13971397Transcriptional activator cubitus interruptusPRO_0000046917Add
BLAST
Chaini1 – ?Transcriptional repressor cubitus interruptusPRO_0000406217

Post-translational modificationi

Polyubiquitinated by RDX in the presence of CUL3, which results in proteasomal degradation.1 Publication
Phosphorylated on multiple sites by protein kinase A (PKA) and phosphorylation by PKA primes further phosphorylation by CK1 and GSK3. Phosphorylation is essential for its proteolytic processing. cos recruits multiple kinases to promote efficient phosphorylation of ci while Hh signaling inhibits phosphorylation by restricting the accessibility of ci to the kinases (PubMed:15691767). Phosphorylation by CkIalpha and dco enhances binding to Slmb, the F-box recognition component of the SCF(slmb) E3 ubiquitin-protein ligase required for ci processing (PubMed:16326393).2 Publications
Transcriptional repressor ciR, a C-terminally truncated form, is generated from the full-length ci (ciFL/ci-155) through proteolytic processing. Hh suppresses the formation of ci75 and promotes the conversion of ci155 into a transcriptional activator (ci155A).1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP19538.

PTM databases

iPTMnetiP19538.

Expressioni

Developmental stagei

In embryos, expressed uniformly throughout the blastoderm stage and gastrulation (from stage 5). During stage 10, ci is eliminated from the posterior compartment of each segment forming 15 segmentally repeating stripes at the end of the short phase of germ-band extension.1 Publication

Gene expression databases

BgeeiP19538.
ExpressionAtlasiP19538. differential.
GenevisibleiP19538. DM.

Interactioni

Subunit structurei

Interacts with RDX (PubMed:16740475). Interacts with cos (PubMed:9244298, PubMed:15691767). Interacts with slmb; the interaction is enhanced by phosphorylation by CkIalpha and dco (PubMed:16326393).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
cosO1684412EBI-94976,EBI-102069
fuP236478EBI-94976,EBI-165536
Su(fu)Q9VG384EBI-94976,EBI-110605

GO - Molecular functioni

  • protein homodimerization activity Source: FlyBase

Protein-protein interaction databases

BioGridi68605. 153 interactions.
DIPiDIP-121N.
IntActiP19538. 5 interactions.
MINTiMINT-1328218.
STRINGi7227.FBpp0088245.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HQMX-ray1.74C/D1356-1367[»]
ProteinModelPortaliP19538.
SMRiP19538. Positions 450-604.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19538.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 440440Interaction with RDXAdd
BLAST
Regioni1161 – 1397237Interaction with RDXAdd
BLAST

Sequence similaritiesi

Contains 5 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri451 – 47626C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri484 – 51128C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri517 – 54125C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri547 – 57226C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri578 – 60326C2H2-type 5PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000118771.
HOGENOMiHOG000038200.
InParanoidiP19538.
KOiK16799.
OMAiINDMTTS.
OrthoDBiEOG7X6KZ8.
PhylomeDBiP19538.

Family and domain databases

Gene3Di3.30.160.60. 5 hits.
InterProiIPR032849. TF_Ci.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERiPTHR19818:SF78. PTHR19818:SF78. 4 hits.
SMARTiSM00355. ZnF_C2H2. 5 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19538-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDAYALPTYF PLAYSELQFL ASRRAAAVAA AATVLPGSPC INQHHPTDVS
60 70 80 90 100
SSVTVPSIIP TGGTSDSIKT SIQPQICNEN TLLGNAGHQH NHQPQHVHNI
110 120 130 140 150
NVTGQPHDFH PAYRIPGYME QLYSLQRTNS ASSFHDPYVN CASAFHLAGL
160 170 180 190 200
GLGSADFLGS RGLSSLGELH NAAVAAAAAG SLASTDFHFS VDGNRRLGSP
210 220 230 240 250
RPPGGSIRAS ISRKRALSSS PYSDSFDINS MIRFSPNSLA TIMNGSRGSS
260 270 280 290 300
AASGSYGHIS ATALNPMSHV HSTRLQQIQA HLLRASAGLL NPMTPQQVAA
310 320 330 340 350
SGFSIGHMPT SASLRVNDVH PNLSDSHIQI TTSPTVTKDV SQVPAAAFSL
360 370 380 390 400
KNLDDAREKK GPFKDVVPEQ PSSTSGGVAQ VEADSASSQL SDRCYNNVVN
410 420 430 440 450
NITGIPGDVK VNSRLDEYIN CGSISIPSNE YDCANADTTD IKDEPGDFIE
460 470 480 490 500
TNCHWRSCRI EFITQDELVK HINNDHIQTN KKAFVCRWED CTRGEKPFKA
510 520 530 540 550
QYMLVVHMRR HTGEKPHKCT FEGCFKAYSR LENLKTHLRS HTGEKPYTCE
560 570 580 590 600
YPGCSKAFSN ASDRAKHQNR THSNEKPYIC KAPGCTKRYT DPSSLRKHVK
610 620 630 640 650
TVHGAEFYAN KKHKGLPLND ANSRLQQNNS RHNLQEHNID SSPCSEDSHL
660 670 680 690 700
GKMLGTSSPS IKSESDISSS NHHLVNGVRA SDSLLTYSPD DLAENLNLDD
710 720 730 740 750
GWNCDDDVDV ADLPIVLRAM VNIGNGNASA STIGGSVLAR QRFRGRLQTK
760 770 780 790 800
GINSSTIMLC NIPESNRTFG ISELNQRITE LKMEPGTDAE IKIPKLPNTT
810 820 830 840 850
IGGYTEDPLQ NQTSFRNTVS NKQGTVSGSI QGQFRRDSQN STASTYYGSM
860 870 880 890 900
QSRRSSQSSQ VSSIPTMRPN PSCNSTASFY DPISPGCSRR SSQMSNGANC
910 920 930 940 950
NSFTSTSGLP VLNKESNKSL NACINKPNIG VQGVGIYNSS LPPPPSSHLI
960 970 980 990 1000
ATNLKRLQRK DSEYHNFTSG RFSVPSYMHS LHIKNNKPVG ENEFDKAIAS
1010 1020 1030 1040 1050
NARRQTDPVP NINLDPLTNI SRFSTTPHSF DINVGKTNNI ASSINKDNLR
1060 1070 1080 1090 1100
KDLFTVSIKA DMAMTSDQHP NERINLDEVE ELILPDEMLQ YLNLVKDDTN
1110 1120 1130 1140 1150
HLEKEHQAVP VGSNVSETIA SNHYREQSNI YYTNKQILTP PSNVDIQPNT
1160 1170 1180 1190 1200
TKFTVQDKFA MTAVGGSFSQ RELSTLAVPN EHGHAKCESF HHQSQKYMNT
1210 1220 1230 1240 1250
DIGSKQQSAL PSAHQRQTEK SNYNQIIDSS MTSLPELNVD SIYPRNETEN
1260 1270 1280 1290 1300
IFKVHGDHDN EIQCGIISQS QMSPSTNLNN DGQFSTVNMQ PITTSKLFPP
1310 1320 1330 1340 1350
EPQKIVCDTQ ASNTSVMHLD TYQRTLEYVQ SCQNWMETNN TSTNQIQSLP
1360 1370 1380 1390
GMPVNNTLFP DVSSSTHPYH GTNMVINDMT TSLTSLLEEN RYLQMMQ
Length:1,397
Mass (Da):153,280
Last modified:November 25, 2002 - v2
Checksum:iC3232A71EF9B8004
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti403 – 4031T → K in AAC47752 (PubMed:9332387).Curated
Sequence conflicti457 – 4571S → R (PubMed:2166702).Curated
Sequence conflicti457 – 4571S → R (PubMed:1686006).Curated
Sequence conflicti804 – 8052YT → IS (PubMed:2166702).Curated
Sequence conflicti804 – 8052YT → IS (PubMed:1686006).Curated
Sequence conflicti968 – 9681T → S (PubMed:2166702).Curated
Sequence conflicti968 – 9681T → S (PubMed:1686006).Curated
Sequence conflicti1043 – 10431S → L (PubMed:2166702).Curated
Sequence conflicti1043 – 10431S → L (PubMed:1686006).Curated
Sequence conflicti1152 – 11521Missing (PubMed:2166702).Curated
Sequence conflicti1152 – 11521Missing (PubMed:1686006).Curated
Sequence conflicti1155 – 11551V → L in AAC47752 (PubMed:9332387).Curated
Sequence conflicti1378 – 139720DMTTS…LQMMQ → V (PubMed:2166702).CuratedAdd
BLAST
Sequence conflicti1378 – 139720DMTTS…LQMMQ → V (PubMed:1686006).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54360 mRNA. Translation: CAA38244.1.
U66884 Genomic DNA. Translation: AAC47752.1.
AE014135 Genomic DNA. Translation: AAF59373.2.
AH003430 Genomic DNA. Translation: AAG15271.1.
AF433680 Genomic DNA. Translation: AAM17953.1.
PIRiA38926.
RefSeqiNP_524617.3. NM_079878.5.
UniGeneiDm.3166.

Genome annotation databases

EnsemblMetazoaiFBtr0089178; FBpp0088245; FBgn0004859.
GeneIDi43767.
KEGGidme:Dmel_CG2125.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54360 mRNA. Translation: CAA38244.1.
U66884 Genomic DNA. Translation: AAC47752.1.
AE014135 Genomic DNA. Translation: AAF59373.2.
AH003430 Genomic DNA. Translation: AAG15271.1.
AF433680 Genomic DNA. Translation: AAM17953.1.
PIRiA38926.
RefSeqiNP_524617.3. NM_079878.5.
UniGeneiDm.3166.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HQMX-ray1.74C/D1356-1367[»]
ProteinModelPortaliP19538.
SMRiP19538. Positions 450-604.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68605. 153 interactions.
DIPiDIP-121N.
IntActiP19538. 5 interactions.
MINTiMINT-1328218.
STRINGi7227.FBpp0088245.

PTM databases

iPTMnetiP19538.

Proteomic databases

PaxDbiP19538.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089178; FBpp0088245; FBgn0004859.
GeneIDi43767.
KEGGidme:Dmel_CG2125.

Organism-specific databases

CTDi12679.
FlyBaseiFBgn0004859. ci.

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000118771.
HOGENOMiHOG000038200.
InParanoidiP19538.
KOiK16799.
OMAiINDMTTS.
OrthoDBiEOG7X6KZ8.
PhylomeDBiP19538.

Enzyme and pathway databases

ReactomeiR-DME-5610780. Degradation of GLI1 by the proteasome.
R-DME-5610785. GLI3 is processed to GLI3R by the proteasome.
R-DME-5610787. Hedgehog 'off' state.
R-DME-5632684. Hedgehog 'on' state.
SignaLinkiP19538.

Miscellaneous databases

EvolutionaryTraceiP19538.
GenomeRNAii43767.
PROiP19538.

Gene expression databases

BgeeiP19538.
ExpressionAtlasiP19538. differential.
GenevisibleiP19538. DM.

Family and domain databases

Gene3Di3.30.160.60. 5 hits.
InterProiIPR032849. TF_Ci.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERiPTHR19818:SF78. PTHR19818:SF78. 4 hits.
SMARTiSM00355. ZnF_C2H2. 5 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the segment polarity gene cubitus interruptus Dominant of Drosophila."
    Orenic T.V., Slusarski D.C., Kroll K.L., Holmgren R.A.
    Genes Dev. 4:1053-1067(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    Strain: Oregon-R.
    Tissue: Embryo.
  2. "Lack of polymorphism on the Drosophila fourth chromosome resulting from selection."
    Berry A.J., Ajioka J.W., Kreitman M.
    Genetics 129:1111-1117(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Oregon-R.
    Tissue: Embryo.
  3. "Use of ordered deletions in genome sequencing."
    Ahmed A., Podemski L.
    Gene 197:367-373(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Embryo.
  4. "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.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. "Analysis of cubitus interruptus regulation in Drosophila embryos and imaginal disks."
    Schwartz C., Locke J., Nishida C., Kornberg T.B.
    Development 121:1625-1635(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
  7. "Nucleotide variation along the Drosophila melanogaster fourth chromosome."
    Wang W., Thornton K., Berry A., Long M.
    Science 295:134-137(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 521-769.
    Strain: 253.27.
  8. "Costal2, a novel kinesin-related protein in the Hedgehog signaling pathway."
    Sisson J.C., Ho K.S., Suyama K., Scott M.P.
    Cell 90:235-245(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COS.
  9. "Hedgehog-regulated Costal2-kinase complexes control phosphorylation and proteolytic processing of Cubitus interruptus."
    Zhang W., Zhao Y., Tong C., Wang G., Wang B., Jia J., Jiang J.
    Dev. Cell 8:267-278(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, PROTEOLYTIC PROCESSING, INTERACTION WITH COS.
  10. "Phosphorylation by double-time/CKIepsilon and CKIalpha targets cubitus interruptus for Slimb/beta-TRCP-mediated proteolytic processing."
    Jia J., Zhang L., Zhang Q., Tong C., Wang B., Hou F., Amanai K., Jiang J.
    Dev. Cell 9:819-830(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLMB, PHOSPHORYLATION.
  11. "A hedgehog-induced BTB protein modulates hedgehog signaling by degrading Ci/Gli transcription factor."
    Zhang Q., Zhang L., Wang B., Ou C.-Y., Chien C.-T., Jiang J.
    Dev. Cell 10:719-729(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RDX, UBIQUITINATION.

Entry informationi

Entry nameiCI_DROME
AccessioniPrimary (citable) accession number: P19538
Secondary accession number(s): O18525, Q8T6T1, Q9V4A8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 25, 2002
Last modified: June 8, 2016
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.