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Protein

Armadillo segment polarity protein

Gene

arm

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

Functioni

Isoform neural may associate with CadN and participate in the transmission of developmental information. Can associate with alpha-catenin. Isoform cytoplasmic accumulates through wg signaling; arm function in wg signal transduction is required early in development for determination of neuroblast fate. Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis.1 Publication

GO - Molecular functioni

  • alpha-catenin binding Source: GO_Central
  • cadherin binding Source: UniProtKB
  • cytoskeletal protein binding Source: FlyBase
  • kinase binding Source: FlyBase
  • nuclear hormone receptor binding Source: GO_Central
  • protein complex binding Source: FlyBase
  • protein phosphatase binding Source: GO_Central
  • signal transducer activity Source: InterPro
  • transcription coactivator activity Source: FlyBase
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • branch fusion, open tracheal system Source: FlyBase
  • branching morphogenesis of an epithelial tube Source: FlyBase
  • cell adhesion Source: FlyBase
  • cell fate determination Source: FlyBase
  • cell morphogenesis Source: FlyBase
  • chitin-based larval cuticle pattern formation Source: FlyBase
  • compound eye morphogenesis Source: FlyBase
  • compound eye retinal cell programmed cell death Source: FlyBase
  • cuticle pattern formation Source: FlyBase
  • cytoskeletal anchoring at plasma membrane Source: FlyBase
  • delamination Source: FlyBase
  • dorsal closure Source: FlyBase
  • epithelial cell type specification, open tracheal system Source: FlyBase
  • epithelium development Source: FlyBase
  • establishment or maintenance of cell polarity Source: FlyBase
  • germarium-derived egg chamber formation Source: FlyBase
  • heart development Source: FlyBase
  • heart formation Source: FlyBase
  • imaginal disc-derived wing expansion Source: FlyBase
  • long-term memory Source: FlyBase
  • negative regulation of heart induction by canonical Wnt signaling pathway Source: FlyBase
  • nervous system development Source: FlyBase
  • neuroblast development Source: FlyBase
  • neuroblast fate commitment Source: UniProtKB
  • oocyte localization involved in germarium-derived egg chamber formation Source: FlyBase
  • oogenesis Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • photoreceptor cell differentiation Source: FlyBase
  • positive regulation of transcription, DNA-templated Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • protein localization to adherens junction Source: FlyBase
  • protein localization to plasma membrane Source: FlyBase
  • regulation of cell shape Source: FlyBase
  • segment polarity determination Source: UniProtKB-KW
  • single organismal cell-cell adhesion Source: FlyBase
  • somatic stem cell maintenance Source: FlyBase
  • ventral furrow formation Source: FlyBase
  • wing disc morphogenesis Source: FlyBase
  • Wnt signaling pathway Source: UniProtKB
  • zonula adherens assembly Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Segmentation polarity protein

Keywords - Biological processi

Cell adhesion, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_275906. formation of the beta-catenin:TCF transactivating complex.
REACT_277739. deactivation of the beta-catenin transactivating complex.
REACT_293913. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_298215. Ca2+ pathway.
REACT_322963. TCF dependent signaling in response to WNT.
REACT_328335. Apoptotic cleavage of cell adhesion proteins.
REACT_341998. CDO in myogenesis.
REACT_343579. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_351382. Beta-catenin phosphorylation cascade.
REACT_354443. Degradation of beta-catenin by the destruction complex.
SignaLinkiP18824.

Names & Taxonomyi

Protein namesi
Recommended name:
Armadillo segment polarity protein
Gene namesi
Name:arm
ORF Names:CG11579
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0000117. arm.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
  • Cell junctionadherens junction By similarity

  • Note: Inner surface of cell membrane and adherens junction.

GO - Cellular componenti

  • adherens junction Source: UniProtKB
  • apical plasma membrane Source: FlyBase
  • apicolateral plasma membrane Source: FlyBase
  • axon Source: FlyBase
  • catenin complex Source: FlyBase
  • cytoplasm Source: FlyBase
  • endocytic vesicle Source: FlyBase
  • nucleus Source: FlyBase
  • plasma membrane Source: UniProtKB
  • spot adherens junction Source: FlyBase
  • zonula adherens Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 843843Armadillo segment polarity proteinPRO_0000064292Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei650 – 6501Phosphothreonine1 Publication
Modified residuei688 – 6881Phosphoserine1 Publication
Modified residuei694 – 6941Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on Ser, Thr and Tyr residues. Level of phosphorylation varies both during embryonic development and from embryonic tissue to tissue. Sgg is required for phosphorylation and wg signal negatively regulates arm phosphorylation. Hypophosphorylated form of arm increases in steady-state levels.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP18824.
PRIDEiP18824.

Expressioni

Tissue specificityi

Isoform cytoplasmic accumulates at low levels in axons, at high levels in specific cells along the CNS midline and in leg and eye imaginal disks. Isoform neural accumulates in the axon tracts of the CNS. Both isoforms accumulate in the peripheral nervous system.1 Publication

Developmental stagei

Present at all stages, but reaches the highest levels during early to mid-embryogenesis. Isoform cytoplasmic is the predominant one from the cellular blastoderm stage until germ-band retraction. Isoform neural is first seen after germ band retraction.

Gene expression databases

BgeeiP18824.
GenevisibleiP18824. DM.

Interactioni

Subunit structurei

Interacts with Mer and Moe at the adherens junction. Interacts with Inx2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCL9O005123EBI-216128,EBI-533127From a different organism.
ebd1Q9W0N93EBI-216128,EBI-141287
IswiQ243682EBI-216128,EBI-367628
lgsQ961D95EBI-216128,EBI-85519
nejO013683EBI-216128,EBI-868028
panP919432EBI-216128,EBI-147301

Protein-protein interaction databases

BioGridi57697. 71 interactions.
DIPiDIP-19968N.
IntActiP18824. 168 interactions.
MINTiMINT-344131.
STRINGi7227.FBpp0089035.

Structurei

3D structure databases

ProteinModelPortaliP18824.
SMRiP18824. Positions 78-678.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati159 – 20042ARM 1Add
BLAST
Repeati201 – 24242ARM 2Add
BLAST
Repeati243 – 28442ARM 3Add
BLAST
Repeati285 – 32642ARM 4Add
BLAST
Repeati327 – 36842ARM 5Add
BLAST
Repeati369 – 41042ARM 6Add
BLAST
Repeati411 – 44939ARM 7Add
BLAST
Repeati450 – 49647ARM 8Add
BLAST
Repeati497 – 53842ARM 9Add
BLAST
Repeati539 – 58446ARM 10Add
BLAST
Repeati585 – 60824ARM 11Add
BLAST
Repeati609 – 64739ARM 12Add
BLAST
Repeati648 – 68942ARM 13; truncatedAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 158158Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi690 – 843154Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the beta-catenin family.Curated
Contains 13 ARM repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG297695.
GeneTreeiENSGT00730000110821.
InParanoidiP18824.
KOiK02105.
OMAiMRAFQDT.
OrthoDBiEOG7X9G6B.
PhylomeDBiP18824.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamiPF00514. Arm. 4 hits.
[Graphical view]
PRINTSiPR01869. BCATNINFAMLY.
SMARTiSM00185. ARM. 12 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 9 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Cytoplasmic (identifier: P18824-1) [UniParc]FASTAAdd to basket

Also known as: A, B

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
MSYMPAQNRT MSHNNQYNPP DLPPMVSAKE QTLMWQQNSY LGDSGIHSGA
60 70 80 90 100
VTQVPSLSGK EDEEMEGDPL MFDLDTGFPQ NFTQDQVDDM NQQLSQTRSQ
110 120 130 140 150
RVRAAMFPET LEEGIEIPST QFDPQQPTAV QRLSEPSQML KHAVVNLINY
160 170 180 190 200
QDDAELATRA IPELIKLLND EDQVVVSQAA MMVHQLSKKE ASRHAIMNSP
210 220 230 240 250
QMVAALVRAI SNSNDLESTK AAVGTLHNLS HHRQGLLAIF KSGGIPALVK
260 270 280 290 300
LLSSPVESVL FYAITTLHNL LLHQDGSKMA VRLAGGLQKM VTLLQRNNVK
310 320 330 340 350
FLAIVTDCLQ ILAYGNQESK LIILASGGPN ELVRIMRSYD YEKLLWTTSR
360 370 380 390 400
VLKVLSVCSS NKPAIVDAGG MQALAMHLGN MSPRLVQNCL WTLRNLSDAA
410 420 430 440 450
TKVEGLEALL QSLVQVLGST DVNVVTCAAG ILSNLTCNNQ RNKATVCQVG
460 470 480 490 500
GVDALVRTII NAGDREEITE PAVCALRHLT SRHVDSELAQ NAVRLNYGLS
510 520 530 540 550
VIVKLLHPPS RWPLIKAVIG LIRNLALCPA NHAPLREHGA IHHLVRLLMR
560 570 580 590 600
AFQDTERQRS SIATTGSQQP SAYADGVRME EIVEGTVGAL HILARESHNR
610 620 630 640 650
ALIRQQSVIP IFVRLLFNEI ENIQRVAAGV LCELAADKEG AEIIEQEGAT
660 670 680 690 700
GPLTDLLHSR NEGVATYAAA VLFRMSEDKP QDYKKRLSIE LTNSLLREDN
710 720 730 740 750
NIWANADLGM GPDLQDMLGP EEAYEGLYGQ GPPSVHSSHG GRAFHQQGYD
760 770 780 790 800
TLPIDSMQGL EISSPVGGGG AGGAPGNGGA VGGASGGGGN IGAIPPSGAP
810 820 830 840
TSPYSMDMDV GEIDAGALNF DLDAMPTPPN DNNNLAAWYD TDC
Length:843
Mass (Da):91,153
Last modified:November 1, 1990 - v1
Checksum:i40DAD6FB83163049
GO
Isoform Neural (identifier: P18824-2) [UniParc]FASTAAdd to basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     718-843: LGPEEAYEGL...NLAAWYDTDC → ILYQ

Show »
Length:721
Mass (Da):79,314
Checksum:i0E19594766E0847F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei718 – 843126LGPEE…YDTDC → ILYQ in isoform Neural. 1 PublicationVSP_006738Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54468 Genomic DNA. Translation: CAA38350.1.
AF001213 mRNA. Translation: AAB58731.1.
AE014298 Genomic DNA. Translation: AAF45686.2.
AE014298 Genomic DNA. Translation: AAF45687.2.
AE014298 Genomic DNA. Translation: AAN09064.2.
AE014298 Genomic DNA. Translation: AAS65246.1.
AL021106, AL021086 Genomic DNA. Translation: CAA15946.1.
AL021086, AL021106 Genomic DNA. Translation: CAA15935.1.
AY118525 mRNA. Translation: AAM49894.1.
PIRiT12689.
RefSeqiNP_001259149.1. NM_001272220.1. [P18824-1]
NP_476665.2. NM_057317.4. [P18824-1]
NP_476666.1. NM_057318.4. [P18824-1]
NP_599100.1. NM_134273.2. [P18824-1]
NP_726775.2. NM_166912.2. [P18824-2]
NP_996328.1. NM_206605.2. [P18824-1]
UniGeneiDm.4782.

Genome annotation databases

EnsemblMetazoaiFBtr0089988; FBpp0089031; FBgn0000117. [P18824-1]
FBtr0089989; FBpp0089032; FBgn0000117. [P18824-1]
FBtr0089991; FBpp0089034; FBgn0000117. [P18824-1]
FBtr0089992; FBpp0089035; FBgn0000117. [P18824-1]
FBtr0332583; FBpp0304835; FBgn0000117. [P18824-1]
GeneIDi31151.
KEGGidme:Dmel_CG11579.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54468 Genomic DNA. Translation: CAA38350.1.
AF001213 mRNA. Translation: AAB58731.1.
AE014298 Genomic DNA. Translation: AAF45686.2.
AE014298 Genomic DNA. Translation: AAF45687.2.
AE014298 Genomic DNA. Translation: AAN09064.2.
AE014298 Genomic DNA. Translation: AAS65246.1.
AL021106, AL021086 Genomic DNA. Translation: CAA15946.1.
AL021086, AL021106 Genomic DNA. Translation: CAA15935.1.
AY118525 mRNA. Translation: AAM49894.1.
PIRiT12689.
RefSeqiNP_001259149.1. NM_001272220.1. [P18824-1]
NP_476665.2. NM_057317.4. [P18824-1]
NP_476666.1. NM_057318.4. [P18824-1]
NP_599100.1. NM_134273.2. [P18824-1]
NP_726775.2. NM_166912.2. [P18824-2]
NP_996328.1. NM_206605.2. [P18824-1]
UniGeneiDm.4782.

3D structure databases

ProteinModelPortaliP18824.
SMRiP18824. Positions 78-678.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57697. 71 interactions.
DIPiDIP-19968N.
IntActiP18824. 168 interactions.
MINTiMINT-344131.
STRINGi7227.FBpp0089035.

Proteomic databases

PaxDbiP18824.
PRIDEiP18824.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089988; FBpp0089031; FBgn0000117. [P18824-1]
FBtr0089989; FBpp0089032; FBgn0000117. [P18824-1]
FBtr0089991; FBpp0089034; FBgn0000117. [P18824-1]
FBtr0089992; FBpp0089035; FBgn0000117. [P18824-1]
FBtr0332583; FBpp0304835; FBgn0000117. [P18824-1]
GeneIDi31151.
KEGGidme:Dmel_CG11579.

Organism-specific databases

CTDi31151.
FlyBaseiFBgn0000117. arm.

Phylogenomic databases

eggNOGiNOG297695.
GeneTreeiENSGT00730000110821.
InParanoidiP18824.
KOiK02105.
OMAiMRAFQDT.
OrthoDBiEOG7X9G6B.
PhylomeDBiP18824.

Enzyme and pathway databases

ReactomeiREACT_275906. formation of the beta-catenin:TCF transactivating complex.
REACT_277739. deactivation of the beta-catenin transactivating complex.
REACT_293913. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
REACT_298215. Ca2+ pathway.
REACT_322963. TCF dependent signaling in response to WNT.
REACT_328335. Apoptotic cleavage of cell adhesion proteins.
REACT_341998. CDO in myogenesis.
REACT_343579. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_351382. Beta-catenin phosphorylation cascade.
REACT_354443. Degradation of beta-catenin by the destruction complex.
SignaLinkiP18824.

Miscellaneous databases

ChiTaRSiarm. fly.
GenomeRNAii31151.
NextBioi772169.
PROiP18824.

Gene expression databases

BgeeiP18824.
GenevisibleiP18824. DM.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamiPF00514. Arm. 4 hits.
[Graphical view]
PRINTSiPR01869. BCATNINFAMLY.
SMARTiSM00185. ARM. 12 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular analysis of the armadillo locus: uniformly distributed transcripts and a protein with novel internal repeats are associated with a Drosophila segment polarity gene."
    Riggleman B., Wieschaus E., Schedl P.
    Genes Dev. 3:96-113(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Oregon-R.
    Tissue: Embryo.
  2. "Roles of Armadillo, a Drosophila catenin, during central nervous system development."
    Loureiro J., Peifer M.
    Curr. Biol. 8:622-632(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CYTOPLASMIC AND NEURAL), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Head.
  3. "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.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Oregon-R.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYTOPLASMIC).
    Strain: Berkeley.
    Tissue: Embryo.
  7. "Phosphorylation of the Drosophila adherens junction protein Armadillo: roles for wingless signal and zeste-white 3 kinase."
    Peifer M., Pai L.-M., Casey M.
    Dev. Biol. 166:543-556(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  8. "Distinct cellular and subcellular patterns of expression imply distinct functions for the Drosophila homologues of moesin and the neurofibromatosis 2 tumor suppressor, merlin."
    McCartney B.M., Fehon R.G.
    J. Cell Biol. 133:843-852(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MER AND MOE, SUBCELLULAR LOCATION.
    Strain: Oregon-R.
    Tissue: Embryo.
  9. "Gap junction channel protein innexin 2 is essential for epithelial morphogenesis in the Drosophila embryo."
    Bauer R., Lehmann C., Martini J., Eckardt F., Hoch M.
    Mol. Biol. Cell 15:2992-3004(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INX2.
  10. "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 THR-650; SER-688 AND SER-694, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiARM_DROME
AccessioniPrimary (citable) accession number: P18824
Secondary accession number(s): A4V3V0
, O02371, Q0KHX2, Q8IRW7, Q9W546
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 24, 2015
This is version 176 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

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 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.