P20193 · SUV37_DROME
- ProteinProtein suppressor of variegation 3-7
- GeneSu(var)3-7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1250 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Dose-limiting factor in position-effect variegation, the inactivation in some cells of a gene translocated next to heterochromatin. It could play a role in chromosome condensation.
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 | cytoplasm | |
Cellular Component | heterochromatin | |
Cellular Component | nucleus | |
Cellular Component | pericentric heterochromatin | |
Molecular Function | chromatin binding | |
Molecular Function | DNA binding | |
Molecular Function | metal ion binding | |
Biological Process | dosage compensation by hyperactivation of X chromosome | |
Biological Process | positive regulation of heterochromatin formation | |
Biological Process | positive regulation of pericentric heterochromatin formation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein suppressor of variegation 3-7
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP20193
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000047060 | 1-1250 | Protein suppressor of variegation 3-7 | |||
Sequence: MDRDSSMQAKNLDAQCNPDLKMASANSETLASATHELKIMDVEGGALVDPDHIEEVETSMVIVVDDDDGDVAMVVEEDKHPMRDDPCIEDIMDDEHAPLVAELQSALNNPDDKQASEDPLLEDQEREPDAMSTKTEPSSDAESSHSYHDPMGLLERIEIHDPGDSQDDDDEDDESSNGGGVDGGMRRKMPRAQRWLLWMKRWPWILHEDSDGTLAFCLYCNISINVNNRSRHIQQHNVSLSHQERECNYLAFKKSEEETRGAISDNEIKHEFGTKSYVAAMKQKRISETEAFNNFNWLRWLRWHPWLERSMPTGTIGTCRICSVRMNVEFVYLRKRHETTKGHMEALRNLDSDKRSRKRKRSKSNSVTNSGGDEAEREKESEPEVGPEDAQDTPVVMMNGDVDSGDDPGKWCALIPDTNPQQCRCTLCNCTMAITSFLRHCKTRAHCHMLSTPAEKGSSDIRGIWAVFADMHPWLIADPEDPSIGYCSVCRKRFMYGNSEIKRKNHEKSEKHTLALASAKAGIEVGSADGRGGDNMDEEEAAASDQAQSSQTDDSEDNDDDNWSEIQKLGKGFAHKSSSEPRKATVRAGVRFYPWLCYSKDRKTQICKFCRVRFHNEAAKARHELSARHVKLVKQFKMRQAKLHQGTNTQTKHNAQDDEESQEQDEEYGEEEEDAEEDSQSNFDLGTVQARKTARADNKLFVKPIPATMKGKVMVWKGRFPWLSYKKNEQRGNYAWCKLCEVSLYLPSSKWASKHQRTSRHIRLRIDRKRNGGNPLKTSNKNSGEISTVVATASALASAEARQKAAMAELQAKYDWLDPDANDENHCHCRVCDSRLPIKVFYLRQHDASRKHVENKERQRANAAAAANAPSVSPTSTVDAERQESGMDKESENDMSVRSDGSTAEPLAKRSRRSMEVRRIIRALRDSMGKRQEERSQMDMARDMICSSFDIVTRLRTLERESVAHNESMAQAPPSVTVSPIKPPEPRHVMDLFFDSISPTMKSLPPDLAAEGKSKIMQLVCSLELRAMQRNATTPTPATVSASSKWPSSTTVTPVKTPPAPISAPLASVDADLHSSVVTTPHEYNNGQNNNNDKETVPKEPVTGASSAQVTINGSAKDLPENIRRILTSNQTQVTNRLETDSVRCVPLDKLTTQSRTNVNGRLSQGGTSEAPSTPQADLSNGNTLAMIRQIRVNNNNSSKITVTNTPQMQQPQQAQASITSSTPIMRGGPSSNGCQITTFRTMVNHNRRP | ||||||
Modified residue | 165 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 175 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 176 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 871 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 873 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 975 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 107-148 | Disordered | ||||
Sequence: LNNPDDKQASEDPLLEDQEREPDAMSTKTEPSSDAESSHSYH | ||||||
Compositional bias | 115-133 | Basic and acidic residues | ||||
Sequence: ASEDPLLEDQEREPDAMST | ||||||
Region | 160-186 | Disordered | ||||
Sequence: HDPGDSQDDDDEDDESSNGGGVDGGMR | ||||||
Zinc finger | 217-236 | C2H2-type 1 | ||||
Sequence: CLYCNISINVNNRSRHIQQH | ||||||
Zinc finger | 319-343 | C2H2-type 2 | ||||
Sequence: CRICSVRMNVEFVYLRKRHETTKGH | ||||||
Region | 343-398 | Disordered | ||||
Sequence: HMEALRNLDSDKRSRKRKRSKSNSVTNSGGDEAEREKESEPEVGPEDAQDTPVVMM | ||||||
Compositional bias | 372-386 | Basic and acidic residues | ||||
Sequence: GDEAEREKESEPEVG | ||||||
Zinc finger | 425-446 | C2H2-type 3 | ||||
Sequence: CTLCNCTMAITSFLRHCKTRAH | ||||||
Zinc finger | 487-512 | C2H2-type 4 | ||||
Sequence: CSVCRKRFMYGNSEIKRKNHEKSEKH | ||||||
Region | 525-564 | Disordered | ||||
Sequence: VGSADGRGGDNMDEEEAAASDQAQSSQTDDSEDNDDDNWS | ||||||
Zinc finger | 605-629 | C2H2-type 5 | ||||
Sequence: QICKFCRVRFHNEAAKARHELSARH | ||||||
Region | 642-684 | Disordered | ||||
Sequence: KLHQGTNTQTKHNAQDDEESQEQDEEYGEEEEDAEEDSQSNFD | ||||||
Compositional bias | 660-680 | Acidic residues | ||||
Sequence: ESQEQDEEYGEEEEDAEEDSQ | ||||||
Zinc finger | 737-761 | C2H2-type 6 | ||||
Sequence: CKLCEVSLYLPSSKWASKHQRTSRH | ||||||
Zinc finger | 829-852 | C2H2-type 7 | ||||
Sequence: CRVCDSRLPIKVFYLRQHDASRKH | ||||||
Region | 851-915 | Disordered | ||||
Sequence: KHVENKERQRANAAAAANAPSVSPTSTVDAERQESGMDKESENDMSVRSDGSTAEPLAKRSRRSM | ||||||
Compositional bias | 866-881 | Polar residues | ||||
Sequence: AANAPSVSPTSTVDAE | ||||||
Compositional bias | 882-896 | Basic and acidic residues | ||||
Sequence: RQESGMDKESENDMS | ||||||
Domain | 987-1026 | BESS | ||||
Sequence: RHVMDLFFDSISPTMKSLPPDLAAEGKSKIMQLVCSLELR | ||||||
Compositional bias | 1032-1057 | Polar residues | ||||
Sequence: ATTPTPATVSASSKWPSSTTVTPVKT | ||||||
Region | 1032-1060 | Disordered | ||||
Sequence: ATTPTPATVSASSKWPSSTTVTPVKTPPA | ||||||
Region | 1079-1116 | Disordered | ||||
Sequence: TTPHEYNNGQNNNNDKETVPKEPVTGASSAQVTINGSA | ||||||
Region | 1154-1180 | Disordered | ||||
Sequence: QSRTNVNGRLSQGGTSEAPSTPQADLS | ||||||
Region | 1205-1236 | Disordered | ||||
Sequence: NTPQMQQPQQAQASITSSTPIMRGGPSSNGCQ |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,250
- Mass (Da)139,990
- Last updated2004-07-19 v4
- Checksum90D0338C894D074C
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E1JIJ9 | E1JIJ9_DROME | Su(var)3-7 | 1248 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 53-54 | in Ref. 1; CAA36434 | ||||
Sequence: IE → MQ | ||||||
Compositional bias | 115-133 | Basic and acidic residues | ||||
Sequence: ASEDPLLEDQEREPDAMST | ||||||
Sequence conflict | 265 | in Ref. 1; CAA36434 | ||||
Sequence: D → S | ||||||
Compositional bias | 372-386 | Basic and acidic residues | ||||
Sequence: GDEAEREKESEPEVG | ||||||
Sequence conflict | 385 | in Ref. 1; CAA36434 | ||||
Sequence: V → A | ||||||
Compositional bias | 660-680 | Acidic residues | ||||
Sequence: ESQEQDEEYGEEEEDAEEDSQ | ||||||
Compositional bias | 866-881 | Polar residues | ||||
Sequence: AANAPSVSPTSTVDAE | ||||||
Compositional bias | 882-896 | Basic and acidic residues | ||||
Sequence: RQESGMDKESENDMS | ||||||
Sequence conflict | 943 | in Ref. 1; CAA36434 | ||||
Sequence: D → N | ||||||
Compositional bias | 1032-1057 | Polar residues | ||||
Sequence: ATTPTPATVSASSKWPSSTTVTPVKT | ||||||
Sequence conflict | 1148 | in Ref. 1; CAA36434 | ||||
Sequence: L → V | ||||||
Sequence conflict | 1159 | in Ref. 1; CAA36434 | ||||
Sequence: V → A | ||||||
Sequence conflict | 1193 | in Ref. 1; CAA36434 | ||||
Sequence: V → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X52187 EMBL· GenBank· DDBJ | CAA36434.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AE014297 EMBL· GenBank· DDBJ | AAF54918.2 EMBL· GenBank· DDBJ | Genomic DNA |