LD08669p

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• protein dimerization activity Source: InterPro

GO - Biological processⁱ

• chorion-containing eggshell formation Source: FlyBase <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Multiple roles of the F-box protein Slimb in Drosophila egg chamber development."
    Muzzopappa M., Wappner P.
    Development 132:2561-2571(2005) [PubMed] [Europe PMC] [Abstract]
• circadian rhythm Source: FlyBaseInferred from mutant phenotypeⁱ
  • "The F-box protein slimb controls the levels of clock proteins period and timeless."
    Grima B., Lamouroux A., Chelot E., Papin C., Limbourg-Bouchon B., Rouyer F.
    Nature 420:178-182(2002) [PubMed] [Europe PMC] [Abstract]
• dorsal appendage formation Source: FlyBaseInferred from mutant phenotypeⁱ
  • "Multiple roles of the F-box protein Slimb in Drosophila egg chamber development."
    Muzzopappa M., Wappner P.
    Development 132:2561-2571(2005) [PubMed] [Europe PMC] [Abstract]
• establishment of epithelial cell polarity Source: FlyBaseInferred from mutant phenotypeⁱ
  • "Slmb antagonises the aPKC/Par-6 complex to control oocyte and epithelial polarity."
    Morais-de-Sa E., Mukherjee A., Lowe N., St Johnston D.
    Development 141:2984-2992(2014) [PubMed] [Europe PMC] [Abstract]
• germarium-derived egg chamber formation Source: FlyBaseInferred from mutant phenotypeⁱ
  • "Multiple roles of the F-box protein Slimb in Drosophila egg chamber development."
    Muzzopappa M., Wappner P.
    Development 132:2561-2571(2005) [PubMed] [Europe PMC] [Abstract]
• germarium-derived female germ-line cyst encapsulation Source: FlyBaseInferred from mutant phenotypeⁱ
  • "Multiple roles of the F-box protein Slimb in Drosophila egg chamber development."
    Muzzopappa M., Wappner P.
    Development 132:2561-2571(2005) [PubMed] [Europe PMC] [Abstract]
• germarium-derived female germ-line cyst formation Source: FlyBaseInferred from mutant phenotypeⁱ
  • "Multiple roles of the F-box protein Slimb in Drosophila egg chamber development."
    Muzzopappa M., Wappner P.
    Development 132:2561-2571(2005) [PubMed] [Europe PMC] [Abstract]
• locomotor rhythm Source: FlyBaseInferred from mutant phenotypeⁱ
  • "The F-box protein slimb controls the levels of clock proteins period and timeless."
    Grima B., Lamouroux A., Chelot E., Papin C., Limbourg-Bouchon B., Rouyer F.
    Nature 420:178-182(2002) [PubMed] [Europe PMC] [Abstract]
• negative regulation of apoptotic process Source: FlyBaseInferred from mutant phenotypeⁱ
  • "A novel dRYBP-SCF complex functions to inhibit apoptosis in Drosophila."
    Fereres S., Simon R., Busturia A.
    Apoptosis 18:1500-1512(2013) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cell population proliferation Source: FlyBaseInferred from mutant phenotypeⁱ
  • "The F-box protein Slmb restricts the activity of aPKC to polarize epithelial cells."
    Skwarek L.C., Windler S.L., de Vreede G., Rogers G.C., Bilder D.
    Development 141:2978-2983(2014) [PubMed] [Europe PMC] [Abstract]
• negative regulation of glial cell proliferation Source: FlyBase <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Gcm protein degradation suppresses proliferation of glial progenitors."
    Ho M.S., Chen H., Chen M., Jacques C., Giangrande A., Chien C.T.
    Proc Natl Acad Sci U S A 106:6778-6783(2009) [PubMed] [Europe PMC] [Abstract]
• negative regulation of nurse cell apoptotic process Source: FlyBaseInferred from mutant phenotypeⁱ
  • "Multiple roles of the F-box protein Slimb in Drosophila egg chamber development."
    Muzzopappa M., Wappner P.
    Development 132:2561-2571(2005) [PubMed] [Europe PMC] [Abstract]
• oocyte axis specification Source: FlyBaseInferred from mutant phenotypeⁱ
  • "Slmb antagonises the aPKC/Par-6 complex to control oocyte and epithelial polarity."
    Morais-de-Sa E., Mukherjee A., Lowe N., St Johnston D.
    Development 141:2984-2992(2014) [PubMed] [Europe PMC] [Abstract]
• oocyte localization involved in germarium-derived egg chamber formation Source: FlyBaseInferred from mutant phenotypeⁱ
  • "Multiple roles of the F-box protein Slimb in Drosophila egg chamber development."
    Muzzopappa M., Wappner P.
    Development 132:2561-2571(2005) [PubMed] [Europe PMC] [Abstract]
• ovarian follicle cell development Source: FlyBaseInferred from mutant phenotypeⁱ
  • "Multiple roles of the F-box protein Slimb in Drosophila egg chamber development."
    Muzzopappa M., Wappner P.
    Development 132:2561-2571(2005) [PubMed] [Europe PMC] [Abstract]
• ovarian follicle cell stalk formation Source: FlyBaseInferred from mutant phenotypeⁱ
  • "Multiple roles of the F-box protein Slimb in Drosophila egg chamber development."
    Muzzopappa M., Wappner P.
    Development 132:2561-2571(2005) [PubMed] [Europe PMC] [Abstract]
• positive regulation of border follicle cell migration Source: FlyBaseInferred from mutant phenotypeⁱ
  • "A sensitized PiggyBac-based screen for regulators of border cell migration in Drosophila."
    Mathieu J., Sung H.H., Pugieux C., Soetaert J., Rorth P.
    Genetics 176:1579-1590(2007) [PubMed] [Europe PMC] [Abstract]
• proteolysis Source: FlyBaseInferred from mutant phenotypeⁱ
  • "Drosophila Roc1a encodes a RING-H2 protein with a unique function in processing the Hh signal transducer Ci by the SCF E3 ubiquitin ligase."
    Noureddine M.A., Donaldson T.D., Thacker S.A., Duronio R.J.
    Dev. Cell 2:757-770(2002) [PubMed] [Europe PMC] [Abstract]
• regulation of centriole replication Source: FlyBase <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "The SCF Slimb ubiquitin ligase regulates Plk4/Sak levels to block centriole reduplication."
    Rogers G.C., Rusan N.M., Roberts D.M., Peifer M., Rogers S.L.
    J. Cell Biol. 184:225-239(2009) [PubMed] [Europe PMC] [Abstract]
• regulation of chromosome condensation Source: FlyBaseInferred from mutant phenotypeⁱ
  • "SCFSlimb ubiquitin ligase suppresses condensin II-mediated nuclear reorganization by degrading Cap-H2."
    Buster D.W., Daniel S.G., Nguyen H.Q., Windler S.L., Skwarek L.C., Peterson M., Roberts M., Meserve J.H., Hartl T., Klebba J.E., Bilder D., Bosco G., Rogers G.C.
    J Cell Biol 201:49-63(2013) [PubMed] [Europe PMC] [Abstract]
• regulation of establishment of cell polarity Source: FlyBaseInferred from mutant phenotypeⁱ
  • "The F-box protein Slmb restricts the activity of aPKC to polarize epithelial cells."
    Skwarek L.C., Windler S.L., de Vreede G., Rogers G.C., Bilder D.
    Development 141:2978-2983(2014) [PubMed] [Europe PMC] [Abstract]
• regulation of mitotic nuclear division Source: FlyBaseInferred from mutant phenotypeⁱ
  • "Multiple roles of the F-box protein Slimb in Drosophila egg chamber development."
    Muzzopappa M., Wappner P.
    Development 132:2561-2571(2005) [PubMed] [Europe PMC] [Abstract]
• SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: FlyBase

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• protein dimerization activity Source: InterPro

Protein-protein interaction databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MMKMETDKIM DETNSNAQAF TTTMLYDPVR KKDSSPTYQT ERELCFQYFT 
        60         70         80         90        100
QWSESGQVDF VEHLLSRMCH YQHGQINAYL KPMLQRDFIT LLPIKGLDHI 
       110        120        130        140        150
AENILSYLDA ESLKSSELVC KEWLRVISEG MLWKKLIERK VRTDSLWRGL 
       160        170        180        190        200
AERRNWMQYL FKPRPGQTQR PHSFHRELFP KIMNDIDSIE NNWRTGRHML 
       210        220        230        240        250
RRINCRSENS KGVYCLQYDD GKIVSGLRDN TIKIWDRTDL QCVKTLMGHT 
       260        270        280        290        300
GSVLCLQYDD KVIISGSSDS TVRVWDVNTG EMVNTLIHHC EAVLHLRFNN 
       310        320        330        340        350
GMMVTCSKDR SIAVWDMTSP SEITLRRVLV GHRAAVNVVD FDEKYIVSAS 
       360        370        380        390        400
GDRTIKVWST SSCEFVRTLN GHKRGIACLQ YRDRLVVSGS SDNSIRLWDI 
       410        420        430        440        450
ECGACLRVLE GHEELVRCIR FDTKRIVSGA YDGKIKVWDL VAALDPRAAS 
       460        470        480        490        500
NTLCLNTLVE HTGRVFRLQF DEFQIVSSSH DDTILIWDFL NFTPNENKTG 
       510
RTPSPALMEH                                             

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ