B4KFE1 · AFFL_DROMO
- ProteinAF4/FMR2 family member lilli
- Genelilli
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1782 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Has a role in transcriptional regulation. Acts in parallel with the Ras/MAPK and the PI3K/PKB pathways in the control of cell identity and cellular growth. Essential for regulation of the cytoskeleton and cell growth but not for cell proliferation or growth rate. Required specifically for the microtubule-based basal transport of lipid droplets. Plays a partially redundant function downstream of Raf in cell fate specification in the developing eye. Pair-rule protein that regulates embryonic cellularization, gastrulation and segmentation (By similarity).
Features
Showing features for dna binding.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 920-932 | A.T hook | ||||
Sequence: KKGRGRPRKQAQQ |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | transcription coregulator activity | |
Biological Process | periodic partitioning by pair rule gene | |
Biological Process | regulation of cytoskeleton organization | |
Biological Process | regulation of DNA-templated transcription | |
Biological Process | regulation of lipid transport |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameAF4/FMR2 family member lilli
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila
Accessions
- Primary accessionB4KFE1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000394676 | 1-1782 | AF4/FMR2 family member lilli | |||
Sequence: MAQQQQQQHQQQQHHQQQQQLLLQQQQQLLQYNNNLYNLNYNMEDNERRKRREREKYERQQGIQSDDRETSLFGEPRRLNPSEGDAEITAALGEFIDARDHMNSSTVGIYRHASTNASSSRLPALSFGGSSLANSYSTSSASVNPAASLASSSASVPGQLPTSQQQQQQQQQQQHYQQQQRAPTYLKQADNKPPYNGRGGYPGQPMKNDIPSSSGMAPPRGPPRSSSSASQSNSNSNSINSSSATNNATSGATSASMSSPLGPPLSTQMPNGREKSFLGPPAPALPNGGRFVPPAASSKRPSNSVGLQPPPPEKDISKIITEMTNNYRVTPLTSIAATPHAPMSENYNLNGPNKFKYAFDSIGPLNSPPAAGASSLMTPLLAPIAPITSPIAPLLTTPPQASQLPLPLAPLAGATTVPPALGGMAAVAPIQQLMPTPPKASPTPPAIKPMKTEKNHSLEKQDSCLENDLELSESDDERKKEGRSAGNSSNSSESDSSESGSEASSKGDTQQQQQQQQQQQQQQLLLQQQQQQQLLLQQQQQRLAASANGSKKKYSQTIIASGANTISGLLTSSGLGGAGAGSVAGGAGGAGGAINATNNTCGGGGGSSGSCMGTMSSSSSSNKTPSPTDSNRWNLSRFFPKPANQTAAESVSPGVANAIGNVSMKVPGILPGGAQIIPESIDVTTAIVKNEKLHDEPRHVGDDEDDEADEQHRQQQQQQQQQQQQQQQQQRYGLSVTVKKEQLEQQQQQQLLLQQQQQLTTEQLALAGALPKNQIKRESRLSDSGSASSGSGSGSSSSDSAGGSSEVLQMPGPGETLQIPGVPAAITTVLRVPQAMQHKVQPNSVTLTPIGPLPASPKPRQKKPRKKKMSAATAPLDSSDEDEPTASSNKKHALELAATAAAAAAAVAVPVAAAAAPAIKKGRGRPRKQAQQQQQQQQQQLQQSGNLSSASASSSQAKGPTLTAAKKPLAKASVSNSNSTAPATVAAGTRKREHSSNSSSNSNTPTKKPTATFATMAAKLDRADALSSDDDSSSSSSCSSTKSSSSSGSDSETPAAAAAGAAASTATTVVTTSAQNPAKKRIVKINKVGVAGNSSSSSKAKRRYSVGSSSNSSSSSETEEQQQHKQQQLLLLQQQQQKQQLQHQQQLQQQQQQQQSLLGQFAAESLPQSAQRLSSSDCSSSSNSDSSSNSSGSSSSSDEDGEHRSGKRKSDKKKICTLTRIFNPKEGGAKKQGQVVIIDQSEEQQQQQQQQQQQAKELKPRATPTQLLGATLASPARTTTPHLTSLMCKIDLSKLARQHHHQPERLKAQQNGHLSSRSAEGARTPKDLQQICTPNGYVGGAAGGGAAASKLLGGVKHEHGVKPEPELEPGYEGKYKLNSVKQEFMLKQELPARRRKRSSSSSSSPYKEKKRKKEKAEQLSKELLPVPVLLPANNHERLSRDKLELLMQQQESAANGSPNKLQQQQQQSRLSQSQQQQQQQQQQQSLSQSTTAAATVAAAPIQLPTTCSEAVQTTPPPAAPQPEPRLIYRSHFDKEEENENDDLRKNDFLLQEAIRRKRAADSERDSFSQMTLYLEAIVYFLLTADAMERCNMEATWTMYKDTLSLIKYISSKNRPYQLSTNGNHESHNIVAILSLRCQSLISLKLYKLRRVNCRAIIASCTEFFRSGRGDILNGNTPSSISPSNSVGSQGSGSNTPPGKIVPQDIHNMLCKQNEYLTYVNSAHELWDQADRLVRNGNHIDFIRKLDHENGPLTLHSTMHEVFRYVQAGLKTLRDAVSYPQSQ | ||||||
Modified residue | 443 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 472 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 474 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 878 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 879 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 949 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 951 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1457 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 42-84 | Disordered | ||||
Sequence: NMEDNERRKRREREKYERQQGIQSDDRETSLFGEPRRLNPSEG | ||||||
Compositional bias | 43-74 | Basic and acidic residues | ||||
Sequence: MEDNERRKRREREKYERQQGIQSDDRETSLFG | ||||||
Compositional bias | 150-186 | Polar residues | ||||
Sequence: ASSSASVPGQLPTSQQQQQQQQQQQHYQQQQRAPTYL | ||||||
Region | 150-313 | Disordered | ||||
Sequence: ASSSASVPGQLPTSQQQQQQQQQQQHYQQQQRAPTYLKQADNKPPYNGRGGYPGQPMKNDIPSSSGMAPPRGPPRSSSSASQSNSNSNSINSSSATNNATSGATSASMSSPLGPPLSTQMPNGREKSFLGPPAPALPNGGRFVPPAASSKRPSNSVGLQPPPPE | ||||||
Compositional bias | 219-273 | Polar residues | ||||
Sequence: PRGPPRSSSSASQSNSNSNSINSSSATNNATSGATSASMSSPLGPPLSTQMPNGR | ||||||
Region | 434-515 | Disordered | ||||
Sequence: MPTPPKASPTPPAIKPMKTEKNHSLEKQDSCLENDLELSESDDERKKEGRSAGNSSNSSESDSSESGSEASSKGDTQQQQQQ | ||||||
Compositional bias | 452-484 | Basic and acidic residues | ||||
Sequence: TEKNHSLEKQDSCLENDLELSESDDERKKEGRS | ||||||
Compositional bias | 485-515 | Polar residues | ||||
Sequence: AGNSSNSSESDSSESGSEASSKGDTQQQQQQ | ||||||
Region | 605-637 | Disordered | ||||
Sequence: GGSSGSCMGTMSSSSSSNKTPSPTDSNRWNLSR | ||||||
Region | 691-732 | Disordered | ||||
Sequence: EKLHDEPRHVGDDEDDEADEQHRQQQQQQQQQQQQQQQQQRY | ||||||
Compositional bias | 714-732 | Polar residues | ||||
Sequence: QQQQQQQQQQQQQQQQQRY | ||||||
Region | 768-820 | Disordered | ||||
Sequence: GALPKNQIKRESRLSDSGSASSGSGSGSSSSDSAGGSSEVLQMPGPGETLQIP | ||||||
Compositional bias | 780-805 | Polar residues | ||||
Sequence: RLSDSGSASSGSGSGSSSSDSAGGSS | ||||||
Region | 839-891 | Disordered | ||||
Sequence: KVQPNSVTLTPIGPLPASPKPRQKKPRKKKMSAATAPLDSSDEDEPTASSNKK | ||||||
Region | 911-1064 | Disordered | ||||
Sequence: VAAAAAPAIKKGRGRPRKQAQQQQQQQQQQLQQSGNLSSASASSSQAKGPTLTAAKKPLAKASVSNSNSTAPATVAAGTRKREHSSNSSSNSNTPTKKPTATFATMAAKLDRADALSSDDDSSSSSSCSSTKSSSSSGSDSETPAAAAAGAAAS | ||||||
Compositional bias | 928-961 | Polar residues | ||||
Sequence: KQAQQQQQQQQQQLQQSGNLSSASASSSQAKGPT | ||||||
Compositional bias | 970-1011 | Polar residues | ||||
Sequence: AKASVSNSNSTAPATVAAGTRKREHSSNSSSNSNTPTKKPTA | ||||||
Compositional bias | 1029-1053 | Polar residues | ||||
Sequence: DDDSSSSSSCSSTKSSSSSGSDSET | ||||||
Region | 1091-1126 | Disordered | ||||
Sequence: AGNSSSSSKAKRRYSVGSSSNSSSSSETEEQQQHKQ | ||||||
Compositional bias | 1166-1196 | Polar residues | ||||
Sequence: LPQSAQRLSSSDCSSSSNSDSSSNSSGSSSS | ||||||
Region | 1166-1234 | Disordered | ||||
Sequence: LPQSAQRLSSSDCSSSSNSDSSSNSSGSSSSSDEDGEHRSGKRKSDKKKICTLTRIFNPKEGGAKKQGQ | ||||||
Region | 1296-1327 | Disordered | ||||
Sequence: ARQHHHQPERLKAQQNGHLSSRSAEGARTPKD | ||||||
Region | 1386-1420 | Disordered | ||||
Sequence: LKQELPARRRKRSSSSSSSPYKEKKRKKEKAEQLS | ||||||
Compositional bias | 1387-1420 | Basic and acidic residues | ||||
Sequence: KQELPARRRKRSSSSSSSPYKEKKRKKEKAEQLS | ||||||
Region | 1450-1484 | Disordered | ||||
Sequence: QESAANGSPNKLQQQQQQSRLSQSQQQQQQQQQQQ | ||||||
Compositional bias | 1674-1700 | Polar residues | ||||
Sequence: GNTPSSISPSNSVGSQGSGSNTPPGKI | ||||||
Region | 1674-1701 | Disordered | ||||
Sequence: GNTPSSISPSNSVGSQGSGSNTPPGKIV |
Sequence similarities
Belongs to the AF4 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,782
- Mass (Da)191,052
- Last updated2008-09-23 v1
- Checksum3A0FF5ECAC87E46C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 43-74 | Basic and acidic residues | ||||
Sequence: MEDNERRKRREREKYERQQGIQSDDRETSLFG | ||||||
Compositional bias | 150-186 | Polar residues | ||||
Sequence: ASSSASVPGQLPTSQQQQQQQQQQQHYQQQQRAPTYL | ||||||
Compositional bias | 219-273 | Polar residues | ||||
Sequence: PRGPPRSSSSASQSNSNSNSINSSSATNNATSGATSASMSSPLGPPLSTQMPNGR | ||||||
Compositional bias | 452-484 | Basic and acidic residues | ||||
Sequence: TEKNHSLEKQDSCLENDLELSESDDERKKEGRS | ||||||
Compositional bias | 485-515 | Polar residues | ||||
Sequence: AGNSSNSSESDSSESGSEASSKGDTQQQQQQ | ||||||
Compositional bias | 714-732 | Polar residues | ||||
Sequence: QQQQQQQQQQQQQQQQQRY | ||||||
Compositional bias | 780-805 | Polar residues | ||||
Sequence: RLSDSGSASSGSGSGSSSSDSAGGSS | ||||||
Compositional bias | 928-961 | Polar residues | ||||
Sequence: KQAQQQQQQQQQQLQQSGNLSSASASSSQAKGPT | ||||||
Compositional bias | 970-1011 | Polar residues | ||||
Sequence: AKASVSNSNSTAPATVAAGTRKREHSSNSSSNSNTPTKKPTA | ||||||
Compositional bias | 1029-1053 | Polar residues | ||||
Sequence: DDDSSSSSSCSSTKSSSSSGSDSET | ||||||
Compositional bias | 1166-1196 | Polar residues | ||||
Sequence: LPQSAQRLSSSDCSSSSNSDSSSNSSGSSSS | ||||||
Compositional bias | 1387-1420 | Basic and acidic residues | ||||
Sequence: KQELPARRRKRSSSSSSSPYKEKKRKKEKAEQLS | ||||||
Compositional bias | 1674-1700 | Polar residues | ||||
Sequence: GNTPSSISPSNSVGSQGSGSNTPPGKI |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CH933807 EMBL· GenBank· DDBJ | EDW12041.1 EMBL· GenBank· DDBJ | Genomic DNA |