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P18824 (ARM_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Armadillo segment polarity protein
Gene names
Name:arm
ORF Names:CG11579
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length843 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform neuralmay associate with CadN and participate in the transmission of developmental information. Can associate with alpha-catenin. Isoform cytoplasmicaccumulates 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. Ref.2

Subunit structure

Interacts with Mer and Moe at the adherens junction. Interacts with Inx2. Ref.8 Ref.9

Subcellular location

Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junctionadherens junction By similarity. Note: Inner surface of cell membrane and adherens junction. Ref.8

Tissue specificity

Isoform cytoplasmicaccumulates at low levels in axons, at high levels in specific cells along the CNS midline and in leg and eye imaginal disks. Isoform neuralaccumulates in the axon tracts of the CNS. Both isoforms accumulate in the peripheral nervous system. Ref.2

Developmental stage

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

Post-translational modification

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. Ref.7

Sequence similarities

Belongs to the beta-catenin family.

Contains 13 ARM repeats.

Ontologies

Keywords
   Biological processCell adhesion
Wnt signaling pathway
   Cellular componentCell junction
Cell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
   Molecular functionDevelopmental protein
Segmentation polarity protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from mutant phenotype PubMed 15043810PubMed 8149915. Source: FlyBase

branch fusion, open tracheal system

Inferred from mutant phenotype PubMed 11003842PubMed 14597571. Source: FlyBase

branching morphogenesis of an epithelial tube

Inferred from mutant phenotype PubMed 11003842. Source: FlyBase

cell adhesion

Inferred from mutant phenotype PubMed 14527345PubMed 20194639. Source: FlyBase

cell fate determination

Inferred from mutant phenotype PubMed 20516152. Source: FlyBase

cell morphogenesis

Inferred from mutant phenotype PubMed 15479740. Source: FlyBase

chitin-based larval cuticle pattern formation

Inferred from mutant phenotype PubMed 19737741. Source: FlyBase

compound eye morphogenesis

Inferred from mutant phenotype PubMed 14602079. Source: FlyBase

compound eye retinal cell programmed cell death

Inferred from mutant phenotype PubMed 9657150. Source: FlyBase

cuticle pattern formation

Inferred from mutant phenotype PubMed 16005293. Source: FlyBase

cytoskeletal anchoring at plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

delamination

Inferred from mutant phenotype PubMed 16962574. Source: FlyBase

dorsal closure

Inferred from mutant phenotype PubMed 12551951. Source: FlyBase

epithelial cell type specification, open tracheal system

Inferred from mutant phenotype PubMed 11003842. Source: FlyBase

establishment or maintenance of cell polarity

Non-traceable author statement PubMed 12766944. Source: FlyBase

heart development

Inferred from mutant phenotype PubMed 22398840. Source: FlyBase

heart formation

Inferred from mutant phenotype PubMed 8660881. Source: FlyBase

imaginal disc-derived wing expansion

Inferred from mutant phenotype PubMed 16962574. Source: FlyBase

long-term memory

Inferred from mutant phenotype PubMed 24035392. Source: FlyBase

negative regulation of heart induction by canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 8660881. Source: FlyBase

negative regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

nervous system development

Inferred from mutant phenotype PubMed 17376868. Source: FlyBase

neuroblast development

Inferred from mutant phenotype PubMed 15479740. Source: FlyBase

neuroblast fate commitment

Inferred from mutant phenotype Ref.2. Source: UniProtKB

oocyte development

Inferred from Biological aspect of Ancestor. Source: RefGenome

oocyte localization involved in germarium-derived egg chamber formation

Traceable author statement PubMed 11131529. Source: FlyBase

oogenesis

Inferred from mutant phenotype PubMed 12783796. Source: FlyBase

ovarian follicle cell development

Traceable author statement PubMed 10822261. Source: FlyBase

photoreceptor cell differentiation

Inferred from mutant phenotype PubMed 15897260. Source: FlyBase

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12556495PubMed 15043810. Source: FlyBase

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 19176582. Source: FlyBase

protein localization to adherens junction

Inferred from mutant phenotype PubMed 16224820. Source: FlyBase

protein localization to plasma membrane

Inferred from mutant phenotype PubMed 16224820. Source: FlyBase

regulation of cell shape

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

segment polarity determination

Inferred from electronic annotation. Source: UniProtKB-KW

single organismal cell-cell adhesion

Inferred from mutant phenotype PubMed 15479740PubMed 18460582. Source: FlyBase

somatic stem cell maintenance

Inferred from mutant phenotype PubMed 12783796. Source: FlyBase

ventral furrow formation

Inferred from mutant phenotype PubMed 15479740. Source: FlyBase

wing disc morphogenesis

Inferred from mutant phenotype PubMed 16962574. Source: FlyBase

zonula adherens assembly

Inferred from mutant phenotype PubMed 15479740. Source: FlyBase

   Cellular_componentZ disc

Inferred from Biological aspect of Ancestor. Source: RefGenome

adherens junction

Inferred from direct assay Ref.8. Source: UniProtKB

apical plasma membrane

Inferred from direct assay PubMed 9657150. Source: FlyBase

apicolateral plasma membrane

Traceable author statement PubMed 11700298. Source: FlyBase

axon

Inferred from direct assay PubMed 11756472. Source: FlyBase

basolateral plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

catenin complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasm

Inferred from direct assay PubMed 15043810PubMed 8149915. Source: FlyBase

cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

desmosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

endocytic vesicle

Inferred from direct assay PubMed 19668359. Source: FlyBase

fascia adherens

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from direct assay PubMed 12556495PubMed 15043810. Source: FlyBase

spot adherens junction

Non-traceable author statement PubMed 12231350. Source: FlyBase

transcription factor complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

zonula adherens

Inferred from direct assay PubMed 8227220. Source: FlyBase

   Molecular_functionalpha-catenin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

cadherin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoskeletal protein binding

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

kinase binding

Inferred from physical interaction PubMed 19088090. Source: FlyBase

protein binding

Inferred from physical interaction Ref.8PubMed 9707400PubMed 9751710Ref.2. Source: UniProtKB

protein complex binding

Inferred from physical interaction PubMed 16224820. Source: FlyBase

protein kinase binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

structural molecule activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription coactivator activity

Inferred from direct assay PubMed 15043810. Source: FlyBase

transcription factor binding

Inferred from direct assay PubMed 9751710. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Cytoplasmic (identifier: P18824-1)

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.
Isoform Neural (identifier: P18824-2)

Also known as: C;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 843843Armadillo segment polarity protein
PRO_0000064292

Regions

Repeat159 – 20042ARM 1
Repeat201 – 24242ARM 2
Repeat243 – 28442ARM 3
Repeat285 – 32642ARM 4
Repeat327 – 36842ARM 5
Repeat369 – 41042ARM 6
Repeat411 – 44939ARM 7
Repeat450 – 49647ARM 8
Repeat497 – 53842ARM 9
Repeat539 – 58446ARM 10
Repeat585 – 60824ARM 11
Repeat609 – 64739ARM 12
Repeat648 – 68942ARM 13; truncated
Compositional bias1 – 158158Asp/Glu-rich (acidic)
Compositional bias690 – 843154Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue6501Phosphothreonine Ref.10
Modified residue6881Phosphoserine Ref.10
Modified residue6941Phosphoserine Ref.10

Natural variations

Alternative sequence718 – 843126LGPEE…YDTDC → ILYQ in isoform Neural.
VSP_006738

Sequences

Sequence LengthMass (Da)Tools
Isoform Cytoplasmic (A) (B) [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 40DAD6FB83163049

FASTA84391,153
        10         20         30         40         50         60 
MSYMPAQNRT MSHNNQYNPP DLPPMVSAKE QTLMWQQNSY LGDSGIHSGA VTQVPSLSGK 

        70         80         90        100        110        120 
EDEEMEGDPL MFDLDTGFPQ NFTQDQVDDM NQQLSQTRSQ RVRAAMFPET LEEGIEIPST 

       130        140        150        160        170        180 
QFDPQQPTAV QRLSEPSQML KHAVVNLINY QDDAELATRA IPELIKLLND EDQVVVSQAA 

       190        200        210        220        230        240 
MMVHQLSKKE ASRHAIMNSP QMVAALVRAI SNSNDLESTK AAVGTLHNLS HHRQGLLAIF 

       250        260        270        280        290        300 
KSGGIPALVK LLSSPVESVL FYAITTLHNL LLHQDGSKMA VRLAGGLQKM VTLLQRNNVK 

       310        320        330        340        350        360 
FLAIVTDCLQ ILAYGNQESK LIILASGGPN ELVRIMRSYD YEKLLWTTSR VLKVLSVCSS 

       370        380        390        400        410        420 
NKPAIVDAGG MQALAMHLGN MSPRLVQNCL WTLRNLSDAA TKVEGLEALL QSLVQVLGST 

       430        440        450        460        470        480 
DVNVVTCAAG ILSNLTCNNQ RNKATVCQVG GVDALVRTII NAGDREEITE PAVCALRHLT 

       490        500        510        520        530        540 
SRHVDSELAQ NAVRLNYGLS VIVKLLHPPS RWPLIKAVIG LIRNLALCPA NHAPLREHGA 

       550        560        570        580        590        600 
IHHLVRLLMR AFQDTERQRS SIATTGSQQP SAYADGVRME EIVEGTVGAL HILARESHNR 

       610        620        630        640        650        660 
ALIRQQSVIP IFVRLLFNEI ENIQRVAAGV LCELAADKEG AEIIEQEGAT GPLTDLLHSR 

       670        680        690        700        710        720 
NEGVATYAAA VLFRMSEDKP QDYKKRLSIE LTNSLLREDN NIWANADLGM GPDLQDMLGP 

       730        740        750        760        770        780 
EEAYEGLYGQ GPPSVHSSHG GRAFHQQGYD TLPIDSMQGL EISSPVGGGG AGGAPGNGGA 

       790        800        810        820        830        840 
VGGASGGGGN IGAIPPSGAP TSPYSMDMDV GEIDAGALNF DLDAMPTPPN DNNNLAAWYD 


TDC 

« Hide

Isoform Neural (C) [UniParc].

Checksum: 0E19594766E0847F
Show »

FASTA72179,314

References

« Hide 'large scale' references
[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. 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.
[4]"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, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]"From sequence to chromosome: the tip of the X chromosome of D. melanogaster."
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. expand/collapse author list , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M.
Science 287:2220-2222(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Oregon-R.
[6]"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] (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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT12689.
RefSeqNP_001259149.1. NM_001272220.1. [P18824-1]
NP_476665.2. NM_057317.4. [P18824-1]
NP_476666.1. NM_057318.3. [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]
UniGeneDm.4782.

3D structure databases

ProteinModelPortalP18824.
SMRP18824. Positions 78-678.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid57697. 71 interactions.
DIPDIP-19968N.
IntActP18824. 14 interactions.
MINTMINT-344131.

Proteomic databases

PaxDbP18824.
PRIDEP18824.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0089988; FBpp0089031; FBgn0000117. [P18824-1]
FBtr0089989; FBpp0089032; FBgn0000117. [P18824-1]
FBtr0089991; FBpp0089034; FBgn0000117. [P18824-1]
FBtr0089992; FBpp0089035; FBgn0000117. [P18824-1]
FBtr0332583; FBpp0304835; FBgn0000117. [P18824-1]
GeneID31151.
KEGGdme:Dmel_CG11579.

Organism-specific databases

CTD31151.
FlyBaseFBgn0000117. arm.

Phylogenomic databases

eggNOGNOG297695.
GeneTreeENSGT00730000110821.
InParanoidP18824.
KOK02105.
OMARESHNRA.
OrthoDBEOG7X9G6B.
PhylomeDBP18824.

Enzyme and pathway databases

SignaLinkP18824.

Gene expression databases

BgeeP18824.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamPF00514. Arm. 4 hits.
[Graphical view]
PRINTSPR01869. BCATNINFAMLY.
SMARTSM00185. ARM. 12 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50176. ARM_REPEAT. 9 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSarm. drosophila.
GenomeRNAi31151.
NextBio772169.
PROP18824.

Entry information

Entry nameARM_DROME
AccessionPrimary (citable) accession number: P18824
Secondary accession number(s): A4V3V0 expand/collapse secondary AC list , O02371, Q0KHX2, Q8IRW7, Q9W546
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: July 9, 2014
This is version 165 of the entry and version 1 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