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Protein

Ras-like GTP-binding protein Rho1

Gene

Rho1

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

Functioni

Has a role in regulating actin cytoskeletal organization: required during early development for proper execution of morphogenetic movements of individual cells and groups of cells important for the formation of the embryonic body plan (PubMed:10556060, PubMed:25739458). Plays a role in regulating dorsal closure during embryogenesis (PubMed:10556060, PubMed:10323867). During embryogenesis, acts upstream of wash to regulate the developmental migration of tail hemocytes anteriorly along the ventral midline (PubMed:25739458). May have a role in eye development (PubMed:7835340).4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 198GTPBy similarity
Nucleotide bindingi59 – 635GTPBy similarity
Nucleotide bindingi117 – 1204GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: FlyBase
  • GTP binding Source: UniProtKB-KW
  • kinase binding Source: FlyBase

GO - Biological processi

  • actin cytoskeleton organization Source: FlyBase
  • actin cytoskeleton reorganization Source: FlyBase
  • actin filament bundle assembly Source: FlyBase
  • actin filament organization Source: FlyBase
  • actin-mediated cell contraction Source: FlyBase
  • axon guidance Source: FlyBase
  • border follicle cell migration Source: FlyBase
  • branch fusion, open tracheal system Source: FlyBase
  • cell elongation involved in imaginal disc-derived wing morphogenesis Source: FlyBase
  • cellularization Source: FlyBase
  • cellular protein localization Source: FlyBase
  • cellular response to DNA damage stimulus Source: FlyBase
  • compound eye morphogenesis Source: FlyBase
  • cortical actin cytoskeleton organization Source: FlyBase
  • cytoskeleton organization Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • dendrite self-avoidance Source: FlyBase
  • determination of left/right symmetry Source: FlyBase
  • dorsal closure Source: UniProtKB
  • dorsal closure, leading edge cell differentiation Source: FlyBase
  • dorsal closure, spreading of leading edge cells Source: FlyBase
  • endocytosis Source: FlyBase
  • epidermal growth factor receptor signaling pathway Source: FlyBase
  • establishment of imaginal disc-derived wing hair orientation Source: FlyBase
  • establishment of planar polarity Source: FlyBase
  • establishment of planar polarity of embryonic epithelium Source: FlyBase
  • establishment of protein localization Source: FlyBase
  • establishment of tissue polarity Source: FlyBase
  • establishment or maintenance of actin cytoskeleton polarity Source: FlyBase
  • gastrulation Source: FlyBase
  • gastrulation involving germ band extension Source: FlyBase
  • germ-band extension Source: FlyBase
  • germ cell migration Source: FlyBase
  • glial cell migration Source: FlyBase
  • hemocyte migration Source: FlyBase
  • imaginal disc-derived leg morphogenesis Source: FlyBase
  • imaginal disc-derived wing hair organization Source: FlyBase
  • JNK cascade Source: FlyBase
  • lumen formation, open tracheal system Source: FlyBase
  • maintenance of epithelial cell apical/basal polarity Source: FlyBase
  • melanization defense response Source: FlyBase
  • mitotic actomyosin contractile ring assembly Source: FlyBase
  • mitotic cytokinesis Source: FlyBase
  • motor neuron axon guidance Source: FlyBase
  • negative regulation of canonical Wnt signaling pathway Source: FlyBase
  • neuroblast proliferation Source: FlyBase
  • neuron projection morphogenesis Source: FlyBase
  • ommatidial rotation Source: FlyBase
  • open tracheal system development Source: FlyBase
  • peripheral nervous system development Source: FlyBase
  • positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  • positive regulation of wound healing Source: FlyBase
  • posterior midgut invagination Source: FlyBase
  • protein localization involved in establishment of planar polarity Source: FlyBase
  • protein localization to adherens junction Source: FlyBase
  • pseudocleavage involved in syncytial blastoderm formation Source: FlyBase
  • regulation of axonogenesis Source: FlyBase
  • regulation of cell migration Source: FlyBase
  • regulation of cytoskeleton organization Source: FlyBase
  • regulation of embryonic cell shape Source: FlyBase
  • regulation of filopodium assembly Source: FlyBase
  • regulation of locomotor rhythm Source: FlyBase
  • regulation of Malpighian tubule size Source: FlyBase
  • regulation of myoblast fusion Source: FlyBase
  • regulation of tube length, open tracheal system Source: FlyBase
  • salivary gland morphogenesis Source: FlyBase
  • small GTPase mediated signal transduction Source: InterPro
  • spiracle morphogenesis, open tracheal system Source: FlyBase
  • ventral furrow formation Source: FlyBase
  • visual perception Source: UniProtKB-KW
  • Wnt signaling pathway Source: FlyBase
  • wound healing Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Actin-binding, GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-114604. GPVI-mediated activation cascade.
R-DME-193634. Axonal growth inhibition (RHOA activation).
R-DME-194840. Rho GTPase cycle.
R-DME-198203. PI3K/AKT activation.
R-DME-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-DME-392451. G beta:gamma signalling through PI3Kgamma.
R-DME-3928662. EPHB-mediated forward signaling.
R-DME-3928663. EPHA-mediated growth cone collapse.
R-DME-4086400. PCP/CE pathway.
R-DME-416482. G alpha (12/13) signalling events.
R-DME-416572. Sema4D induced cell migration and growth-cone collapse.
R-DME-4420097. VEGFA-VEGFR2 Pathway.
R-DME-5625740. RHO GTPases activate PKNs.
R-DME-5625900. RHO GTPases activate CIT.
R-DME-5627117. RHO GTPases Activate ROCKs.
R-DME-5663220. RHO GTPases Activate Formins.
R-DME-5666185. RHO GTPases Activate Rhotekin and Rhophilins.
R-DME-6785631. ERBB2 Regulates Cell Motility.
R-DME-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-like GTP-binding protein Rho1
Gene namesi
Name:Rho1Imported
ORF Names:CG8416Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0014020. Rho1.

Subcellular locationi

GO - Cellular componenti

  • apical cortex Source: FlyBase
  • cell-cell contact zone Source: FlyBase
  • cell cortex Source: FlyBase
  • cell hair Source: FlyBase
  • cytoplasm Source: FlyBase
  • cytoskeleton Source: UniProtKB-SubCell
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Disruption phenotypei

Embryonic lethal. Embryos exhibit severe defects in head involution and imperfect dorsal closure. During head involution, the head structures fail to internalize resulting in holes in the dorsal anterior region of the cuticle. The disruption in the dorsal surface stretches the ventral surface, causing the cuticle to bow.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 293KDQ → AAA: Reduces binding to wash. Reduces the number of hemocytes migrating anteriorly from the tail during embryogenesis. 1 Publication
Mutagenesisi39 – 391F → V: No effect on binding to wash and no effect on tail hemocyte developmental migration from the tail. 1 Publication
Mutagenesisi51 – 544KQVE → AAAA: No effect on binding to wash. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Ras-like GTP-binding protein Rho1PRO_0000198885Add
BLAST
Propeptidei190 – 1923Removed in mature formBy similarityPRO_0000281238

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei189 – 1891Cysteine methyl esterBy similarity
Lipidationi189 – 1891S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiP48148.
PRIDEiP48148.

Expressioni

Tissue specificityi

Expressed in hemocytes (at protein level).1 Publication

Gene expression databases

BgeeiP48148.
ExpressionAtlasiP48148. differential.
GenevisibleiP48148. DM.

Interactioni

Subunit structurei

Interacts with capu (PubMed:10556060). Interacts (via REM repeats) with Pkn (via N-terminus) (PubMed:10323867, PubMed:17507675). Interacts (via N-terminus) with wash (via N-terminus) (PubMed:25739458).3 Publications

GO - Molecular functioni

  • kinase binding Source: FlyBase

Protein-protein interaction databases

BioGridi62500. 27 interactions.
DIPiDIP-22676N.
IntActiP48148. 1 interaction.
MINTiMINT-312636.
STRINGi7227.FBpp0086354.

Structurei

3D structure databases

ProteinModelPortaliP48148.
SMRiP48148. Positions 4-180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi34 – 429Effector regionSequence analysis

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000119020.
InParanoidiP48148.
KOiK04513.
OMAiAYKSLEC.
OrthoDBiEOG73FQPD.
PhylomeDBiP48148.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P48148-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG
60 70 80 90 100
KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWT
110 120 130 140 150
PEVKHFCPNV PIILVGNKKD LRNDPNTIRD LAKMKQEPVK PQEGRAMAEK
160 170 180 190
INAFAYLECS AKSKEGVRDV FETATRAALQ VKKRKKTRCL LL
Length:192
Mass (Da):21,723
Last modified:February 1, 1996 - v1
Checksum:iB89C7D884E1743CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38311 mRNA. Translation: AAA67042.1.
AF177871 Genomic DNA. Translation: AAF01183.1.
AF177872 mRNA. Translation: AAF01184.1.
AF177873 mRNA. Translation: AAF01185.1.
AF177874 mRNA. Translation: AAF01186.1.
AE013599 Genomic DNA. Translation: AAM70944.1.
AE013599 Genomic DNA. Translation: AAM70945.1.
AE013599 Genomic DNA. Translation: AAM70946.1.
AE013599 Genomic DNA. Translation: AAS64843.1.
AE013599 Genomic DNA. Translation: AAS64844.1.
AY119536 mRNA. Translation: AAM50190.1.
BT010085 mRNA. Translation: AAQ22554.1.
PIRiS54294.
RefSeqiNP_477098.1. NM_057750.4.
NP_599135.1. NM_134308.3.
NP_599136.1. NM_134309.2.
NP_725524.1. NM_166139.3.
NP_995849.1. NM_206127.2.
NP_995850.1. NM_206128.2.
UniGeneiDm.644.

Genome annotation databases

EnsemblMetazoaiFBtr0087211; FBpp0086353; FBgn0014020.
FBtr0087212; FBpp0086354; FBgn0014020.
FBtr0087213; FBpp0086355; FBgn0014020.
FBtr0087214; FBpp0086356; FBgn0014020.
FBtr0087216; FBpp0089129; FBgn0014020.
FBtr0087217; FBpp0089130; FBgn0014020.
GeneIDi36775.
KEGGidme:Dmel_CG8416.
UCSCiCG8416-RC. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L38311 mRNA. Translation: AAA67042.1.
AF177871 Genomic DNA. Translation: AAF01183.1.
AF177872 mRNA. Translation: AAF01184.1.
AF177873 mRNA. Translation: AAF01185.1.
AF177874 mRNA. Translation: AAF01186.1.
AE013599 Genomic DNA. Translation: AAM70944.1.
AE013599 Genomic DNA. Translation: AAM70945.1.
AE013599 Genomic DNA. Translation: AAM70946.1.
AE013599 Genomic DNA. Translation: AAS64843.1.
AE013599 Genomic DNA. Translation: AAS64844.1.
AY119536 mRNA. Translation: AAM50190.1.
BT010085 mRNA. Translation: AAQ22554.1.
PIRiS54294.
RefSeqiNP_477098.1. NM_057750.4.
NP_599135.1. NM_134308.3.
NP_599136.1. NM_134309.2.
NP_725524.1. NM_166139.3.
NP_995849.1. NM_206127.2.
NP_995850.1. NM_206128.2.
UniGeneiDm.644.

3D structure databases

ProteinModelPortaliP48148.
SMRiP48148. Positions 4-180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62500. 27 interactions.
DIPiDIP-22676N.
IntActiP48148. 1 interaction.
MINTiMINT-312636.
STRINGi7227.FBpp0086354.

Proteomic databases

PaxDbiP48148.
PRIDEiP48148.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087211; FBpp0086353; FBgn0014020.
FBtr0087212; FBpp0086354; FBgn0014020.
FBtr0087213; FBpp0086355; FBgn0014020.
FBtr0087214; FBpp0086356; FBgn0014020.
FBtr0087216; FBpp0089129; FBgn0014020.
FBtr0087217; FBpp0089130; FBgn0014020.
GeneIDi36775.
KEGGidme:Dmel_CG8416.
UCSCiCG8416-RC. d. melanogaster.

Organism-specific databases

CTDi36775.
FlyBaseiFBgn0014020. Rho1.

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000119020.
InParanoidiP48148.
KOiK04513.
OMAiAYKSLEC.
OrthoDBiEOG73FQPD.
PhylomeDBiP48148.

Enzyme and pathway databases

ReactomeiR-DME-114604. GPVI-mediated activation cascade.
R-DME-193634. Axonal growth inhibition (RHOA activation).
R-DME-194840. Rho GTPase cycle.
R-DME-198203. PI3K/AKT activation.
R-DME-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-DME-392451. G beta:gamma signalling through PI3Kgamma.
R-DME-3928662. EPHB-mediated forward signaling.
R-DME-3928663. EPHA-mediated growth cone collapse.
R-DME-4086400. PCP/CE pathway.
R-DME-416482. G alpha (12/13) signalling events.
R-DME-416572. Sema4D induced cell migration and growth-cone collapse.
R-DME-4420097. VEGFA-VEGFR2 Pathway.
R-DME-5625740. RHO GTPases activate PKNs.
R-DME-5625900. RHO GTPases activate CIT.
R-DME-5627117. RHO GTPases Activate ROCKs.
R-DME-5663220. RHO GTPases Activate Formins.
R-DME-5666185. RHO GTPases Activate Rhotekin and Rhophilins.
R-DME-6785631. ERBB2 Regulates Cell Motility.
R-DME-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.

Miscellaneous databases

ChiTaRSiRho1. fly.
GenomeRNAii36775.
PROiP48148.

Gene expression databases

BgeeiP48148.
ExpressionAtlasiP48148. differential.
GenevisibleiP48148. DM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of rho GTPase family homologues in Drosophila melanogaster: overexpressing Rho1 in retinal cells causes a late developmental defect."
    Hariharan I.K., Hu K.-Q., Asha H., Quintanilla A., Ezzell R.M., Settleman J.
    EMBO J. 14:292-302(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "Mutations in the Rho1 small GTPase disrupt morphogenesis and segmentation during early Drosophila development."
    Magie C.R., Meyer M.R., Gorsuch M.S., Parkhurst S.M.
    Development 126:5353-5364(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, INTERACTION WITH CAPU, DISRUPTION PHENOTYPE.
  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.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  7. "The Drosophila Pkn protein kinase is a Rho/Rac effector target required for dorsal closure during embryogenesis."
    Lu Y., Settleman J.
    Genes Dev. 13:1168-1180(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PKN.
  8. "A rho-binding protein kinase C-like activity is required for the function of protein kinase N in Drosophila development."
    Betson M., Settleman J.
    Genetics 176:2201-2212(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PKN.
  9. "Wash functions downstream of Rho1 GTPase in a subset of Drosophila immune cell developmental migrations."
    Verboon J.M., Rahe T.K., Rodriguez-Mesa E., Parkhurst S.M.
    Mol. Biol. Cell 26:1665-1674(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, TISSUE SPECIFICITY, MUTAGENESIS OF 27-LYS--GLN-29; PHE-39 AND 51-LYS--GLU-54.

Entry informationi

Entry nameiRHO1_DROME
AccessioniPrimary (citable) accession number: P48148
Secondary accession number(s): A4UZI6, Q0E958, Q9V3J0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 6, 2016
This is version 155 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

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.