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Protein

Kinesin-like protein costa

Gene

cos

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

Functioni

Regulates cubitus interruptus (ci) processing by recruiting multiple kinases to promote its efficient phosphorylation. Scaffolds multiple kinases and ci into proximity to promote its hyperphosphorylation, which then targets it for SCFSlimb/proteasome-mediated processing to generate its repressor form. Hh signaling inhibits ci phosphorylation by interfering with the cos-ci-kinases complex formation.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi175 – 1828ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • microtubule binding Source: FlyBase
  • microtubule motor activity Source: FlyBase
  • motor activity Source: FlyBase
  • protein homodimerization activity Source: FlyBase
  • protein kinase binding Source: FlyBase
  • smoothened binding Source: FlyBase
  • transcription factor binding Source: FlyBase

GO - Biological processi

  • cytoplasmic sequestering of transcription factor Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • intraciliary transport Source: FlyBase
  • microtubule-based movement Source: FlyBase
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: FlyBase
  • negative regulation of smoothened signaling pathway Source: FlyBase
  • negative regulation of transcription factor import into nucleus Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • positive regulation of hh target transcription factor activity Source: FlyBase
  • positive regulation of smoothened signaling pathway Source: FlyBase
  • regulation of apoptotic process Source: FlyBase
  • regulation of protein stability Source: FlyBase
  • regulation of proteolysis Source: FlyBase
  • smoothened signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Repressor

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiO16844.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein costa
Alternative name(s):
Kinesin-like protein costal2
Gene namesi
Name:cos
Synonyms:cos2, costal-2
ORF Names:CG1708
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0000352. cos.

Subcellular locationi

  • Cytoplasmcytoskeleton 1 Publication

GO - Cellular componenti

  • cilium Source: GOC
  • cytoplasm Source: FlyBase
  • Hedgehog signaling complex Source: FlyBase
  • kinesin complex Source: FlyBase
  • microtubule Source: UniProtKB-KW
  • microtubule associated complex Source: FlyBase
  • plasma membrane Source: FlyBase
  • vesicle membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12011201Kinesin-like protein costaPRO_0000307148Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei599 – 5991Phosphoserine1 Publication
Modified residuei605 – 6051Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO16844.
PRIDEiO16844.

PTM databases

iPTMnetiO16844.

Expressioni

Developmental stagei

Present at high levels during the first 4 hours of embryogenesis and at moderate levels between 4-12 hours.1 Publication

Gene expression databases

BgeeiO16844.
GenevisibleiO16844. DM.

Interactioni

Subunit structurei

Homodimer (Potential). Binds microtubules. Interacts with ci, smo, sgg, CkIalpha and protein kinase A catalytic subunit.Curated2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ciP1953812EBI-102069,EBI-94976
fuP236474EBI-102069,EBI-165536
smoP916825EBI-102069,EBI-142245

GO - Molecular functioni

  • microtubule binding Source: FlyBase
  • protein homodimerization activity Source: FlyBase
  • protein kinase binding Source: FlyBase
  • smoothened binding Source: FlyBase
  • transcription factor binding Source: FlyBase

Protein-protein interaction databases

BioGridi61534. 13 interactions.
DIPiDIP-22550N.
IntActiO16844. 7 interactions.
STRINGi7227.FBpp0088087.

Structurei

3D structure databases

ProteinModelPortaliO16844.
SMRiO16844. Positions 142-389.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 391388Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili652 – 821170Sequence analysisAdd
BLAST
Coiled coili968 – 100134Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi622 – 6254Poly-Pro
Compositional biasi1119 – 11246Poly-Ala
Compositional biasi1130 – 115425Thr-richAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIF27 subfamily.PROSITE-ProRule annotation
Contains 1 kinesin motor domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IGAQ. Eukaryota.
ENOG4110CRV. LUCA.
GeneTreeiENSGT00810000125470.
HOGENOMiHOG000263945.
InParanoidiO16844.
KOiK06227.
OMAiNTMIVQP.
OrthoDBiEOG7TXKFX.
PhylomeDBiO16844.

Family and domain databases

Gene3Di3.40.850.10. 2 hits.
InterProiIPR027640. Kinesin-like_fam.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 6 hits.
PfamiPF00225. Kinesin. 2 hits.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O16844-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIPIQVAVR IFPHRELKDL LRSFGPTEPK KDAQAVDEGA DSKDSEAQVP
60 70 80 90 100
AAEKDNPSIS ETDPNGNAEQ DSAADSKTIP DANGNDSGQK DYPDSAYCVQ
110 120 130 140 150
AIPISASALG LPSALPGGDP MDSIAAGLIQ VGPHTVPVTH ALPSSSSQEQ
160 170 180 190 200
VYHQTVFPLI TLFLEGFDAS VVTYGQRGQG KSYTLYGNVQ DPTLTDSTEG
210 220 230 240 250
VVQLCVRDIF SHISLHPERT YAINVGFVEI CGGDVCDLLG MGNIHCTNVD
260 270 280 290 300
AVFHWLQVGL SARQSLPAHT LFTLTLEQQW VSKEGLLQHR LSTASFSDLC
310 320 330 340 350
GTERCGDQPP GRPLDAGLCM LEQVISTLTD PGLMYGVNGN IPYGQTTLTT
360 370 380 390 400
LLKDSFGGRA QTLVILCVSP LEEHLPETLG NLQFAFKVQC VRNFVIMNTY
410 420 430 440 450
SDDNTMIVQP AEPVPESNSS AGPLSQAGPG DNFGLQFAAS QWSKLVTNAE
460 470 480 490 500
GLFSKLIDSK LITEVEKEQI EEWLFLKQEC EECLSSTEAM RQQKQLVPIL
510 520 530 540 550
EAEEPEDVNS EAANSESPNS DNENDTDNES HRPDLDDKIE SLMEEFRDKT
560 570 580 590 600
DALILEKHAE YLSKHPKAVM QSQDREIEAQ PPEENGDDRK VSIGSRRRSV
610 620 630 640 650
QPGASLSTAE LAMLNRVASQ QPPPPIDPES VVDPLESSSG EGIRQAALAA
660 670 680 690 700
AAATAPIEQL QKKLRKLVAE IEGKQRQLRE IEETIQVKQN IIAELVKNSD
710 720 730 740 750
TRSHAKQRFH KKRAKLEAEC DKAKKQLGKA LVQGRDQSEI ERWTTIIGHL
760 770 780 790 800
ERRLEDLSSM KHIAGESGQK VKKLQQSVGE SRKQADDLQK KLRKECKLRC
810 820 830 840 850
QMEAELAKLR ESRETGKELV KAQGSPEQQG RQLKAVQARI THLNHILREK
860 870 880 890 900
SDNLEEQPGP EQQETLRHEI RNLRGTRDLL LEERCHLDRK LKRDKVLTQK
910 920 930 940 950
EERKLLECDE AIEAIDAAIE FKNEMITGHR SIDTSDRIQR EKGEQMLMAR
960 970 980 990 1000
LNRLSTEEMR TLLYKYFTKV IDLRDSSRKL ELQLVQLERE RDAWEWKERV
1010 1020 1030 1040 1050
LSNAVRQARL EGERNAVLLQ RQHEMKLTLM LRHMAEETSA SSASYGERAL
1060 1070 1080 1090 1100
APACVAPPVQ ASSDFDYDHF YKGGGNPSKA LIKAPKPMPT GSALDKYKDK
1110 1120 1130 1140 1150
EQRSGRNIFA KFHVLTRYAS AAAAGSSGST AEESTALIES TTTATATTTS
1160 1170 1180 1190 1200
TTTTGAVGKV KDKALVSFRP EQLKRLMPAP TATKVTRQKN KIIIQDASRR

N
Length:1,201
Mass (Da):133,148
Last modified:October 23, 2007 - v2
Checksum:i6DC898F8B4C8F20F
GO

Sequence cautioni

The sequence AAN71259.1 differs from that shown. Reason: Frameshift at position 415. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71V → L in AAB66813 (PubMed:9244298).Curated
Sequence conflicti471 – 4711E → D in AAB66813 (PubMed:9244298).Curated
Sequence conflicti568 – 5681A → E in AAT94488 (Ref. 5) Curated
Sequence conflicti736 – 7361D → G in AAB66813 (PubMed:9244298).Curated
Sequence conflicti807 – 8071A → V in AAB66813 (PubMed:9244298).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019250 mRNA. Translation: AAB66813.1.
AE013599 Genomic DNA. Translation: AAF59270.1.
BT001504 mRNA. Translation: AAN71259.1. Frameshift.
BT015259 mRNA. Translation: AAT94488.1.
BT044167 mRNA. Translation: ACH92232.1.
PIRiT08603.
RefSeqiNP_001260765.1. NM_001273836.1.
NP_477092.1. NM_057744.3.
UniGeneiDm.5775.

Genome annotation databases

EnsemblMetazoaiFBtr0089015; FBpp0088087; FBgn0000352.
FBtr0336916; FBpp0307854; FBgn0000352.
GeneIDi35653.
KEGGidme:Dmel_CG1708.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019250 mRNA. Translation: AAB66813.1.
AE013599 Genomic DNA. Translation: AAF59270.1.
BT001504 mRNA. Translation: AAN71259.1. Frameshift.
BT015259 mRNA. Translation: AAT94488.1.
BT044167 mRNA. Translation: ACH92232.1.
PIRiT08603.
RefSeqiNP_001260765.1. NM_001273836.1.
NP_477092.1. NM_057744.3.
UniGeneiDm.5775.

3D structure databases

ProteinModelPortaliO16844.
SMRiO16844. Positions 142-389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61534. 13 interactions.
DIPiDIP-22550N.
IntActiO16844. 7 interactions.
STRINGi7227.FBpp0088087.

PTM databases

iPTMnetiO16844.

Proteomic databases

PaxDbiO16844.
PRIDEiO16844.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089015; FBpp0088087; FBgn0000352.
FBtr0336916; FBpp0307854; FBgn0000352.
GeneIDi35653.
KEGGidme:Dmel_CG1708.

Organism-specific databases

CTDi35653.
FlyBaseiFBgn0000352. cos.

Phylogenomic databases

eggNOGiENOG410IGAQ. Eukaryota.
ENOG4110CRV. LUCA.
GeneTreeiENSGT00810000125470.
HOGENOMiHOG000263945.
InParanoidiO16844.
KOiK06227.
OMAiNTMIVQP.
OrthoDBiEOG7TXKFX.
PhylomeDBiO16844.

Enzyme and pathway databases

SignaLinkiO16844.

Miscellaneous databases

GenomeRNAii35653.
PROiO16844.

Gene expression databases

BgeeiO16844.
GenevisibleiO16844. DM.

Family and domain databases

Gene3Di3.40.850.10. 2 hits.
InterProiIPR027640. Kinesin-like_fam.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 6 hits.
PfamiPF00225. Kinesin. 2 hits.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DEVELOPMENTAL STAGE, INTERACTION WITH CI.
  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. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "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: FUNCTION, INTERACTION WITH SMO; SGG; CKI ALPHA AND PROTEIN KINASE A CATALYTIC SUBUNIT.
  7. "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-599 AND SER-605, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiCOS_DROME
AccessioniPrimary (citable) accession number: O16844
Secondary accession number(s): A1Z6X4
, B5RIP3, Q6AWI9, Q8IH04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 23, 2007
Last modified: June 8, 2016
This is version 126 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.