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A1Z6W3

- PRIC1_DROME

UniProt

A1Z6W3 - PRIC1_DROME

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Protein

Protein prickle

Gene

pk

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

Functioni

Acts in a planar cell polarity (PCP) complex; polarization along the apical/basal axis of epithelial cells. Correct expression of the alternative isoforms is required for PCP signaling in imaginal disks. PCP signaling in the wing disk requires the receptor fz and the cytoplasmic proteins dsh and pk. These act in a feedback loop leading to activation of the jnk cascade and subsequent polarized arrangement of hairs and bristles. Dgo and pk compete with one another for dsh binding, thereby modulating fz dsh activity and ensuring tight control over fz PCP signaling. Vang, stan and pk function together to regulate the establishment of tissue polarity in the adult eye.3 Publications

GO - Molecular functioni

  1. zinc ion binding Source: InterPro

GO - Biological processi

  1. anterior/posterior axis specification Source: UniProtKB
  2. establishment of imaginal disc-derived wing hair orientation Source: FlyBase
  3. establishment of ommatidial planar polarity Source: FlyBase
  4. establishment of planar polarity Source: UniProtKB
  5. establishment of protein localization Source: FlyBase
  6. establishment of tissue polarity Source: UniProtKB
  7. establishment or maintenance of cell polarity Source: FlyBase
  8. imaginal disc-derived leg joint morphogenesis Source: FlyBase
  9. maintenance of protein location Source: FlyBase
  10. morphogenesis of a polarized epithelium Source: FlyBase
  11. negative regulation of Notch signaling pathway Source: FlyBase
  12. protein localization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_184330. Asymmetric localization of PCP proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein prickle
Alternative name(s):
Protein spiny legs
Gene namesi
Name:pkImported
ORF Names:CG11084
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003090. pk.

Subcellular locationi

Cell membrane 4 Publications; Peripheral membrane protein 4 Publications; Cytoplasmic side 4 Publications
Note: Localized to the proximal wing cell boundary where fz and dsh localization is antagonized by binding the dsh DEP domain and preventing dsh cortical localization. Localization to the anterior photoreceptor cell membrane.4 Publications

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. membrane Source: FlyBase
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Flies exhibit aberrant hair and bristle orientation on the wings and aberrant ommatidial arrangement in the compound eye.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12991299Protein pricklePRO_0000288834Add
BLAST

Proteomic databases

PaxDbiA1Z6W3.
PRIDEiA1Z6W3.

Expressioni

Tissue specificityi

Expressed in the wing, leg and eye imaginal disks. Expressed within the photoreceptors of the eye.4 Publications

Developmental stagei

Expressed both maternally and zygotically. Isoform B is expressed in embryos only. Isoform A and isoform C are expressed in embryos and pupae.1 Publication

Gene expression databases

BgeeiA1Z6W3.
ExpressionAtlasiA1Z6W3. differential.

Interactioni

Subunit structurei

Interacts with dsh; PET and LIM domains interact with dsh DEP domain, in wing cells. Interacts with Vang in photoreceptor cells.4 Publications

Protein-protein interaction databases

BioGridi69608. 8 interactions.
DIPiDIP-59584N.
IntActiA1Z6W3. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliA1Z6W3.
SMRiA1Z6W3. Positions 624-806.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini515 – 623109PETPROSITE-ProRule annotationAdd
BLAST
Domaini622 – 68665LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini687 – 74761LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini748 – 81063LIM zinc-binding 3PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi245 – 29248Pro-richSequence AnalysisAdd
BLAST
Compositional biasi412 – 49079Pro-richSequence AnalysisAdd
BLAST
Compositional biasi857 – 87721Gln-richSequence AnalysisAdd
BLAST
Compositional biasi1157 – 124993Ser-richSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the prickle / espinas / testin family.Curated
Contains 3 LIM zinc-binding domains.PROSITE-ProRule annotation
Contains 1 PET domain.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiNOG314122.
GeneTreeiENSGT00550000074438.
InParanoidiA1Z6W3.
KOiK04511.
OMAiWHATDEC.
OrthoDBiEOG7P8P7M.
PhylomeDBiA1Z6W3.

Family and domain databases

Gene3Di2.10.110.10. 3 hits.
InterProiIPR010442. PET_domain.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 2 hits.
PF06297. PET. 1 hit.
[Graphical view]
SMARTiSM00132. LIM. 3 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
PS51303. PET. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform C1 Publication (identifier: A1Z6W3-1) [UniParc]FASTAAdd to Basket

Also known as: sple1 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSSLSTGGGA GGSSGGPGGA DAAAAPAAGQ ATVTATGNME PAMVPRTANL
60 70 80 90 100
LACKQWWRVC FLYGDQQKYY RQLYSKAAAQ RLADANQEPD NARDREYDTV
110 120 130 140 150
DCDLIAGQLD AVEDADDGID LGDHSSTPKG GATTAGRPLF PHSSSPRRSK
160 170 180 190 200
KLLRSLRAHV RGEKLPKNDT TTANESSEVT QRNARVTVLD DPFLFGIDAD
210 220 230 240 250
HLGDLVVRGK RYSTLDATEN MARFYAEQEA TAQVLEIIEQ EEESPEQEAP
260 270 280 290 300
KPALPPKQKQ QRPVPPLPPP PANRVTQDQG TQPAAPQVPL QPLTAGDLQF
310 320 330 340 350
LNLSLRQRSL PRSMKPFKDA HDISFTFNEL DTSAEPEVAT GAAQQESNEP
360 370 380 390 400
ISRTPLTQIS YLQKIPTLPR HFSPSGQGLA TPPALGSGGM GLPSSSSASA
410 420 430 440 450
LYAAQAAAGI LPTSPLPLQR HQQYLPPHHQ QHPGAGMGPG PGSGAAAGPP
460 470 480 490 500
LGPQYSPGCS ANPKYSNAQL PPPPHHHHQL SPALSTPSPP SLLHHPAGGT
510 520 530 540 550
SSASAHAPFL GGPHMDMQRQ SHSDDDSGCA LEEYTWVPPG LRPDQVRLYF
560 570 580 590 600
SQIPDDKVPY VNSPGEQYRV RQLLHQLPPH DNEVRYCHSL TDEERKELRL
610 620 630 640 650
FSTQRKRDAL GRGNVRQLMS ARPCDGCDDL ISTGDIAVFA TRLGPNASWH
660 670 680 690 700
PACFACSVCR ELLVDLIYFH RDGRMYCGRH HAETLKPRCS ACDEIILADE
710 720 730 740 750
CTEAEGRAWH MNHFACHECD KQLGGQRYIM REGKPYCLHC FDAMFAEYCD
760 770 780 790 800
YCGEAIGVDQ GQMSHDGQHW HATDECFSCN TCRCSLLGRA FLPRRGAIYC
810 820 830 840 850
SIACSKGEPP TPSDSSGTGM YTTPTPPTQR VRPHPQAPLP ARIPSSHASS
860 870 880 890 900
SPPMSPQQQQ QHQATFNQAM YQMQSQQMEA AGGLVDQSKS YAASDSDAGV
910 920 930 940 950
VKDLEHGGHM GGGDLTDFSG GRASSTSQNL SPLNSPGDFQ PHFLPKPMEL
960 970 980 990 1000
QRDGVYNFNE MSSNLDAAWS AKPTNSYHLQ RQLLENPHTA SMPELAGKLV
1010 1020 1030 1040 1050
APPAHMQHLS QLHAVSSHQF QQHEYADILH PPPPPPGEIP ELPTPNLSVA
1060 1070 1080 1090 1100
STALPPELMG SPTHSAGDRS LNTPMSTQSA SHAPPHPVSI LSGASSSSPM
1110 1120 1130 1140 1150
SGEPAKKKGV RFEGIPDTLP RSRSYSGNGA GTSGGGERER DRDKDKEGGG
1160 1170 1180 1190 1200
RHGHGHSSRR RRRRKSSSSS SHHRSGSGHR SHSTTRADTY APAQPLSSSY
1210 1220 1230 1240 1250
QGPPSVLQAA NLVHESPSRQ QRERERERER EESEESDVCS TCSSSSSSSE
1260 1270 1280 1290
DYMMMYQLPQ RRHYGGVRVS YVPNDALAYD RKRKPSELGG DKDKNCIIS
Length:1,299
Mass (Da):140,722
Last modified:February 6, 2007 - v1
Checksum:i8BFAF1F75F352485
GO
Isoform A1 Publication (identifier: A1Z6W3-2) [UniParc]FASTAAdd to Basket

Also known as: pk1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     2-13: SSLSTGGGAGGS → DTPNQMPVELER
     14-349: Missing.

Show »
Length:963
Mass (Da):104,682
Checksum:iC01685B61EA4C367
GO
Isoform B1 Publication (identifier: A1Z6W3-3) [UniParc]FASTAAdd to Basket

Also known as: pkM1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     2-80: SSLSTGGGAG...RQLYSKAAAQ → NDSTDNLHAD...KAIIKSAEVR
     81-349: Missing.

Show »
Length:1,029
Mass (Da):111,765
Checksum:iD532D80FFFDAC461
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti175 – 1773ESS → VSN in CAB57345. (PubMed:10485852)Curated
Sequence conflicti188 – 1881V → A in CAB57345. (PubMed:10485852)Curated
Sequence conflicti279 – 2791Q → P in CAB57345. (PubMed:10485852)Curated
Sequence conflicti715 – 7151A → G in CAB57344. (PubMed:10485852)Curated
Sequence conflicti715 – 7151A → G in CAB57345. (PubMed:10485852)Curated
Sequence conflicti715 – 7151A → G in CAB99211. (PubMed:10485852)Curated
Sequence conflicti746 – 7461A → G in CAB57344. (PubMed:10485852)Curated
Sequence conflicti746 – 7461A → G in CAB57345. (PubMed:10485852)Curated
Sequence conflicti746 – 7461A → G in CAB99211. (PubMed:10485852)Curated
Sequence conflicti755 – 7551A → G in CAB57344. (PubMed:10485852)Curated
Sequence conflicti755 – 7551A → G in CAB57345. (PubMed:10485852)Curated
Sequence conflicti755 – 7551A → G in CAB99211. (PubMed:10485852)Curated
Sequence conflicti797 – 7971A → G in CAB57344. (PubMed:10485852)Curated
Sequence conflicti797 – 7971A → G in CAB57345. (PubMed:10485852)Curated
Sequence conflicti797 – 7971A → G in CAB99211. (PubMed:10485852)Curated
Sequence conflicti830 – 8301R → G in CAB57344. (PubMed:10485852)Curated
Sequence conflicti830 – 8301R → G in CAB57345. (PubMed:10485852)Curated
Sequence conflicti830 – 8301R → G in CAB99211. (PubMed:10485852)Curated
Sequence conflicti970 – 9701S → P in CAB57344. (PubMed:10485852)Curated
Sequence conflicti970 – 9701S → P in CAB57345. (PubMed:10485852)Curated
Sequence conflicti970 – 9701S → P in CAB99211. (PubMed:10485852)Curated
Sequence conflicti1029 – 10291L → V in CAB57344. (PubMed:10485852)Curated
Sequence conflicti1029 – 10291L → V in CAB57345. (PubMed:10485852)Curated
Sequence conflicti1029 – 10291L → V in CAB99211. (PubMed:10485852)Curated
Sequence conflicti1134 – 11341G → S in CAB57344. (PubMed:10485852)Curated
Sequence conflicti1134 – 11341G → S in CAB57345. (PubMed:10485852)Curated
Sequence conflicti1134 – 11341G → S in CAB99211. (PubMed:10485852)Curated
Sequence conflicti1231 – 12311E → K in CAB57344. (PubMed:10485852)Curated
Sequence conflicti1231 – 12311E → K in CAB57345. (PubMed:10485852)Curated
Sequence conflicti1231 – 12311E → K in CAB99211. (PubMed:10485852)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 8079SSLST…KAAAQ → NDSTDNLHADCDGRVSNNNN GNSNTNDGPNNDGDSDEEVI EGMALLEGNYQVLRQWVPPA PNYWDAPPKAIIKSAEVR in isoform B. 1 PublicationVSP_052412Add
BLAST
Alternative sequencei2 – 1312SSLST…GAGGS → DTPNQMPVELER in isoform A. 1 PublicationVSP_052413Add
BLAST
Alternative sequencei14 – 349336Missing in isoform A. 1 PublicationVSP_052414Add
BLAST
Alternative sequencei81 – 349269Missing in isoform B. 1 PublicationVSP_052415Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ243708 mRNA. Translation: CAB57344.3.
AJ243710 mRNA. Translation: CAB57345.3.
AJ243709 mRNA. Translation: CAB99211.2.
AE013599 Genomic DNA. Translation: AAF59281.2.
AE013599 Genomic DNA. Translation: AAF59284.2.
AE013599 Genomic DNA. Translation: AAM68908.1.
RefSeqiNP_724534.1. NM_165508.2. [A1Z6W3-2]
NP_724535.1. NM_165509.2. [A1Z6W3-3]
NP_724538.1. NM_165512.2. [A1Z6W3-1]
UniGeneiDm.3470.

Genome annotation databases

EnsemblMetazoaiFBtr0089044; FBpp0088115; FBgn0003090. [A1Z6W3-1]
GeneIDi45343.
KEGGidme:Dmel_CG11084.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ243708 mRNA. Translation: CAB57344.3 .
AJ243710 mRNA. Translation: CAB57345.3 .
AJ243709 mRNA. Translation: CAB99211.2 .
AE013599 Genomic DNA. Translation: AAF59281.2 .
AE013599 Genomic DNA. Translation: AAF59284.2 .
AE013599 Genomic DNA. Translation: AAM68908.1 .
RefSeqi NP_724534.1. NM_165508.2. [A1Z6W3-2 ]
NP_724535.1. NM_165509.2. [A1Z6W3-3 ]
NP_724538.1. NM_165512.2. [A1Z6W3-1 ]
UniGenei Dm.3470.

3D structure databases

ProteinModelPortali A1Z6W3.
SMRi A1Z6W3. Positions 624-806.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 69608. 8 interactions.
DIPi DIP-59584N.
IntActi A1Z6W3. 2 interactions.

Proteomic databases

PaxDbi A1Z6W3.
PRIDEi A1Z6W3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0089044 ; FBpp0088115 ; FBgn0003090 . [A1Z6W3-1 ]
GeneIDi 45343.
KEGGi dme:Dmel_CG11084.

Organism-specific databases

CTDi 18745.
FlyBasei FBgn0003090. pk.

Phylogenomic databases

eggNOGi NOG314122.
GeneTreei ENSGT00550000074438.
InParanoidi A1Z6W3.
KOi K04511.
OMAi WHATDEC.
OrthoDBi EOG7P8P7M.
PhylomeDBi A1Z6W3.

Enzyme and pathway databases

Reactomei REACT_184330. Asymmetric localization of PCP proteins.

Miscellaneous databases

GenomeRNAii 45343.
NextBioi 838057.

Gene expression databases

Bgeei A1Z6W3.
ExpressionAtlasi A1Z6W3. differential.

Family and domain databases

Gene3Di 2.10.110.10. 3 hits.
InterProi IPR010442. PET_domain.
IPR001781. Znf_LIM.
[Graphical view ]
Pfami PF00412. LIM. 2 hits.
PF06297. PET. 1 hit.
[Graphical view ]
SMARTi SM00132. LIM. 3 hits.
[Graphical view ]
PROSITEi PS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
PS51303. PET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The balance between isoforms of the prickle LIM domain protein is critical for planar polarity in Drosophila imaginal discs."
    Gubb D., Green C., Huen D., Coulson D., Johnson G., Tree D.R.P., Collier S., Roote J.
    Genes Dev. 13:2315-2327(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: DP CN BW.
    Tissue: Embryo1 Publication.
  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: Berkeley1 Publication.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. "Prickle mediates feedback amplification to generate asymmetric planar cell polarity signaling."
    Tree D.R.P., Shulman J.M., Rousset R., Scott M.P., Gubb D., Axelrod J.D.
    Cell 109:371-381(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DSH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  5. "Prickle and Strabismus form a functional complex to generate a correct axis during planar cell polarity signaling."
    Jenny A., Darken R.S., Wilson P.A., Mlodzik M.
    EMBO J. 22:4409-4420(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VANG, SUBCELLULAR LOCATION.
  6. "Strabismus requires Flamingo and Prickle function to regulate tissue polarity in the Drosophila eye."
    Rawls A.S., Wolff T.
    Development 130:1877-1887(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VANG, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  7. "Diego and Prickle regulate Frizzled planar cell polarity signalling by competing for Dishevelled binding."
    Jenny A., Reynolds-Kenneally J., Das G., Burnett M., Mlodzik M.
    Nat. Cell Biol. 7:691-697(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DSH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiPRIC1_DROME
AccessioniPrimary (citable) accession number: A1Z6W3
Secondary accession number(s): A1Z6V4
, A1Z6V8, Q9N9H6, Q9U5X0, Q9U5X1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: February 6, 2007
Last modified: October 29, 2014
This is version 69 of the entry and version 1 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

External Data

Dasty 3