A1ZBW7 · WASC2_DROME
- ProteinWASH complex subunit 2
- GeneFAM21
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1469 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Acts at least in part as component of the WASH complex which may regulate wash nucleation-promoting factor (NPF) activity and is required for its membrane targeting during endosomal sorting.
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | early endosome | |
Cellular Component | nucleoplasm | |
Cellular Component | WASH complex | |
Molecular Function | phosphatidylinositol phosphate binding | |
Molecular Function | retromer complex binding | |
Biological Process | nuclear envelope budding | |
Biological Process | positive regulation of cell adhesion | |
Biological Process | protein localization to endosome | |
Biological Process | retrograde transport, endosome to Golgi |
Names & Taxonomy
Protein names
- Recommended nameWASH complex subunit 2
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionA1ZBW7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000372653 | 1-1469 | WASH complex subunit 2 | |||
Sequence: MDISADVDQIIAQAPDWTFAGDCALLALMKRISQNLEERGERTSRNLRDFETSVKQVDIALNNATTSLRSLQFGNQFVEYRVEEVDDADLAMPEEKKKKPELPLKSSEELAKEFLENNLRMFRKNYEPVTIEVPDSDDEDGPVHSTTVFRAKNPYDAIPLPYIIGTKEWQEHKYAGLYDSKENSEDDRSEEFSSSSSDEKEPETKKIATPANKLEEQHLSDSSSLASFAREPAIVSPVINPAVQVAEPVIRTQPRPIINSQRNPHERDMFAALRQSPPSDDPPSTSSSPTSSPAFRNPSSRLPIVSTASLSSSSSSPAQQPPRLFDEAVSTQTPKEAEIKPSQTKRMPVNLFNEDEFKSFMSEIVDKVQSKTPSSSVSPATTISTKEPPKTKKPVEEYPKPGPPKQIVEQTVPKRVNLFDDSPPLSPTPRSEPVFNNTKATGAIPKRSPVVVANNDEDNSLFGSSPAMPKENPSKKPPKPVTKSLFDDDLEDDDFLSSFTPKAKPPEQKLLSKPKPSLFDDDDLDIDDIFTKPSAQPKKLSERVAGKTSLFEDDDQDDVTDLFGSKKAKVIPKETSSGVSPNKNVETPVASKKSLFDDIEDEDLFGTPKAKNLIRSEPDNDPEAVGEDKKQSEIAEQKSKNIETGEKQHQVIAENASVPILRDSPPPMEVTEQKSDDKEWEAVKDDTSAANITKSKDLFSEDLTDDELFSSTSNNMAEPKSANETNEFNKPIEKYTSQTEENVSPVNPPTKLSIKPTDLFNEDFSDDDTFLSASMSKNEPLVGTENEDIKKPSEVQLVKEIKAEELPQQLPENKIYEITAVVEKDELVPEMLSKPQIDEPVSETPPPDDYQSNVDPIISMVADVTNKTSVDTLTPRKPADLAAAQQIMQNYSNLFSDEPPDDSEFFQTLGSSGLSSLSASKIFDNEHDFFEPALPNIPSATKPSPVTPGDQPSVSSDYGAMCLFSDVPPEDNDHAGEEVQKEAEPQKDELASTTRIHTIFYDDFSETARAGAVQPAPKRFPFDDEPPPADETDRSEVKETPELQKPTSPVKKLKMPNININVHALLPGSGSVPKLIRKQESSSSERDEPQATVQTEAEAPSSGQNTVSSADGVLQHVNKSRARGPAKRRPSTRRGRKENYAKSLLDAGQNEGPTASTRDSPEVEHSERSSIKAPSPQYVKPEKLFSTPAQQIQPQLQRPPPSNTGGSFLDSPDEDDSFFNSVPTKTVEGKQGTDPPKSYRSFLDSPDADDKLFSDLENNKAGINVVPVEKKPPKMANSFLASPDEDDFLFDSVKTNATTTAQKAFAAEIMNAFQKVTTAPPKPSNAKEAAKPKSQAAPKLFDDSDDDDDDLFARAPSIQTASKPVQAKQPPKPAATSLFSSDDEEAEVPVKSAPAKKLPVKPSKSLFSDDDDDDDLFGGSSTSKAAAAKKTKPAARTASKPPASKTTTPTATIPSNSGDNPLADLLDFK | ||||||
Modified residue | 136 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 227 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 422 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 426 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 580 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 587 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 693 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1241 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1245 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1254 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1344 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1380 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1381 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1408 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Component of the WASH complex.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 178-212 | Basic and acidic residues | ||||
Sequence: YDSKENSEDDRSEEFSSSSSDEKEPETKKIATPAN | ||||||
Region | 178-349 | Disordered | ||||
Sequence: YDSKENSEDDRSEEFSSSSSDEKEPETKKIATPANKLEEQHLSDSSSLASFAREPAIVSPVINPAVQVAEPVIRTQPRPIINSQRNPHERDMFAALRQSPPSDDPPSTSSSPTSSPAFRNPSSRLPIVSTASLSSSSSSPAQQPPRLFDEAVSTQTPKEAEIKPSQTKRMPV | ||||||
Compositional bias | 215-229 | Polar residues | ||||
Sequence: EEQHLSDSSSLASFA | ||||||
Compositional bias | 278-327 | Polar residues | ||||
Sequence: PSDDPPSTSSSPTSSPAFRNPSSRLPIVSTASLSSSSSSPAQQPPRLFDE | ||||||
Motif | 351-372 | LFa 1 | ||||
Sequence: LFNEDEFKSFMSEIVDKVQSKT | ||||||
Compositional bias | 367-388 | Polar residues | ||||
Sequence: KVQSKTPSSSVSPATTISTKEP | ||||||
Region | 367-546 | Disordered | ||||
Sequence: KVQSKTPSSSVSPATTISTKEPPKTKKPVEEYPKPGPPKQIVEQTVPKRVNLFDDSPPLSPTPRSEPVFNNTKATGAIPKRSPVVVANNDEDNSLFGSSPAMPKENPSKKPPKPVTKSLFDDDLEDDDFLSSFTPKAKPPEQKLLSKPKPSLFDDDDLDIDDIFTKPSAQPKKLSERVAG | ||||||
Compositional bias | 453-467 | Polar residues | ||||
Sequence: ANNDEDNSLFGSSPA | ||||||
Motif | 550-563 | LFa 5 | ||||
Sequence: LFEDDDQDDVTDLF | ||||||
Region | 571-591 | Disordered | ||||
Sequence: IPKETSSGVSPNKNVETPVAS | ||||||
Compositional bias | 575-589 | Polar residues | ||||
Sequence: TSSGVSPNKNVETPV | ||||||
Motif | 595-605 | LFa 6 | ||||
Sequence: LFDDIEDEDLF | ||||||
Compositional bias | 607-647 | Basic and acidic residues | ||||
Sequence: TPKAKNLIRSEPDNDPEAVGEDKKQSEIAEQKSKNIETGEK | ||||||
Region | 607-760 | Disordered | ||||
Sequence: TPKAKNLIRSEPDNDPEAVGEDKKQSEIAEQKSKNIETGEKQHQVIAENASVPILRDSPPPMEVTEQKSDDKEWEAVKDDTSAANITKSKDLFSEDLTDDELFSSTSNNMAEPKSANETNEFNKPIEKYTSQTEENVSPVNPPTKLSIKPTDLF | ||||||
Compositional bias | 669-685 | Basic and acidic residues | ||||
Sequence: EVTEQKSDDKEWEAVKD | ||||||
Motif | 698-709 | LFa 8 | ||||
Sequence: LFSEDLTDDELF | ||||||
Compositional bias | 705-751 | Polar residues | ||||
Sequence: DDELFSSTSNNMAEPKSANETNEFNKPIEKYTSQTEENVSPVNPPTK | ||||||
Region | 933-1254 | Disordered | ||||
Sequence: ALPNIPSATKPSPVTPGDQPSVSSDYGAMCLFSDVPPEDNDHAGEEVQKEAEPQKDELASTTRIHTIFYDDFSETARAGAVQPAPKRFPFDDEPPPADETDRSEVKETPELQKPTSPVKKLKMPNININVHALLPGSGSVPKLIRKQESSSSERDEPQATVQTEAEAPSSGQNTVSSADGVLQHVNKSRARGPAKRRPSTRRGRKENYAKSLLDAGQNEGPTASTRDSPEVEHSERSSIKAPSPQYVKPEKLFSTPAQQIQPQLQRPPPSNTGGSFLDSPDEDDSFFNSVPTKTVEGKQGTDPPKSYRSFLDSPDADDKLFS | ||||||
Compositional bias | 970-991 | Basic and acidic residues | ||||
Sequence: EDNDHAGEEVQKEAEPQKDELA | ||||||
Compositional bias | 1023-1041 | Basic and acidic residues | ||||
Sequence: DDEPPPADETDRSEVKETP | ||||||
Compositional bias | 1086-1115 | Polar residues | ||||
Sequence: RDEPQATVQTEAEAPSSGQNTVSSADGVLQ | ||||||
Compositional bias | 1121-1135 | Basic residues | ||||
Sequence: RARGPAKRRPSTRRG | ||||||
Compositional bias | 1184-1210 | Polar residues | ||||
Sequence: LFSTPAQQIQPQLQRPPPSNTGGSFLD | ||||||
Region | 1316-1469 | Disordered | ||||
Sequence: VTTAPPKPSNAKEAAKPKSQAAPKLFDDSDDDDDDLFARAPSIQTASKPVQAKQPPKPAATSLFSSDDEEAEVPVKSAPAKKLPVKPSKSLFSDDDDDDDLFGGSSTSKAAAAKKTKPAARTASKPPASKTTTPTATIPSNSGDNPLADLLDFK | ||||||
Compositional bias | 1440-1459 | Polar residues | ||||
Sequence: KPPASKTTTPTATIPSNSGD |
Sequence similarities
Belongs to the FAM21 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,469
- Mass (Da)160,899
- Last updated2007-02-06 v1
- Checksum945E8CD6C834677D
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 66 | in Ref. 3; ABF85753 | ||||
Sequence: T → N | ||||||
Compositional bias | 178-212 | Basic and acidic residues | ||||
Sequence: YDSKENSEDDRSEEFSSSSSDEKEPETKKIATPAN | ||||||
Compositional bias | 215-229 | Polar residues | ||||
Sequence: EEQHLSDSSSLASFA | ||||||
Sequence conflict | 240 | in Ref. 3; ABF85753 | ||||
Sequence: N → K | ||||||
Sequence conflict | 249 | in Ref. 3; ABF85753 | ||||
Sequence: V → A | ||||||
Sequence conflict | 259 | in Ref. 3; ABF85753 | ||||
Sequence: N → S | ||||||
Compositional bias | 278-327 | Polar residues | ||||
Sequence: PSDDPPSTSSSPTSSPAFRNPSSRLPIVSTASLSSSSSSPAQQPPRLFDE | ||||||
Compositional bias | 367-388 | Polar residues | ||||
Sequence: KVQSKTPSSSVSPATTISTKEP | ||||||
Sequence conflict | 397-399 | in Ref. 3; ABF85753 | ||||
Sequence: EYP → PYS | ||||||
Sequence conflict | 405 | in Ref. 3; ABF85753 | ||||
Sequence: K → T | ||||||
Sequence conflict | 411 | in Ref. 3; ABF85753 | ||||
Sequence: T → I | ||||||
Sequence conflict | 447 | in Ref. 3; ABF85753 | ||||
Sequence: R → Q | ||||||
Compositional bias | 453-467 | Polar residues | ||||
Sequence: ANNDEDNSLFGSSPA | ||||||
Sequence conflict | 455 | in Ref. 3; ABF85753 | ||||
Sequence: N → D | ||||||
Sequence conflict | 502 | in Ref. 3; ABF85753 | ||||
Sequence: K → R | ||||||
Sequence conflict | 506 | in Ref. 3; ABF85753 | ||||
Sequence: P → T | ||||||
Compositional bias | 575-589 | Polar residues | ||||
Sequence: TSSGVSPNKNVETPV | ||||||
Compositional bias | 607-647 | Basic and acidic residues | ||||
Sequence: TPKAKNLIRSEPDNDPEAVGEDKKQSEIAEQKSKNIETGEK | ||||||
Sequence conflict | 619 | in Ref. 3; ABF85753 | ||||
Sequence: D → Y | ||||||
Sequence conflict | 623-624 | in Ref. 3; ABF85753 | ||||
Sequence: EA → DT | ||||||
Compositional bias | 669-685 | Basic and acidic residues | ||||
Sequence: EVTEQKSDDKEWEAVKD | ||||||
Compositional bias | 705-751 | Polar residues | ||||
Sequence: DDELFSSTSNNMAEPKSANETNEFNKPIEKYTSQTEENVSPVNPPTK | ||||||
Sequence conflict | 925 | in Ref. 3; ABF85753 | ||||
Sequence: N → S | ||||||
Compositional bias | 970-991 | Basic and acidic residues | ||||
Sequence: EDNDHAGEEVQKEAEPQKDELA | ||||||
Sequence conflict | 981-982 | in Ref. 3; ABF85753 | ||||
Sequence: KE → NQ | ||||||
Sequence conflict | 1021 | in Ref. 3; ABF85753 | ||||
Sequence: P → T | ||||||
Compositional bias | 1023-1041 | Basic and acidic residues | ||||
Sequence: DDEPPPADETDRSEVKETP | ||||||
Sequence conflict | 1035 | in Ref. 3; ABF85753 | ||||
Sequence: S → N | ||||||
Sequence conflict | 1065 | in Ref. 3; ABF85753 | ||||
Sequence: L → H | ||||||
Sequence conflict | 1071 | in Ref. 3; ABF85753 | ||||
Sequence: S → G | ||||||
Sequence conflict | 1086 | in Ref. 3; ABF85753 | ||||
Sequence: R → K | ||||||
Compositional bias | 1086-1115 | Polar residues | ||||
Sequence: RDEPQATVQTEAEAPSSGQNTVSSADGVLQ | ||||||
Sequence conflict | 1095 | in Ref. 3; ABF85753 | ||||
Sequence: T → P | ||||||
Compositional bias | 1121-1135 | Basic residues | ||||
Sequence: RARGPAKRRPSTRRG | ||||||
Sequence conflict | 1150 | in Ref. 3; ABF85753 | ||||
Sequence: N → D | ||||||
Sequence conflict | 1155 | in Ref. 3; ABF85753 | ||||
Sequence: A → S | ||||||
Compositional bias | 1184-1210 | Polar residues | ||||
Sequence: LFSTPAQQIQPQLQRPPPSNTGGSFLD | ||||||
Sequence conflict | 1208 | in Ref. 3; ABF85753 | ||||
Sequence: F → L | ||||||
Sequence conflict | 1222-1224 | in Ref. 3; ABF85753 | ||||
Sequence: VPT → IPK | ||||||
Sequence conflict | 1233 | in Ref. 3; ABF85753 | ||||
Sequence: T → S | ||||||
Sequence conflict | 1259 | in Ref. 3; ABF85753 | ||||
Sequence: N → S | ||||||
Sequence conflict | 1262-1266 | in Ref. 3; ABF85753 | ||||
Sequence: GINVV → CFNEP | ||||||
Sequence conflict | 1271 | in Ref. 3; ABF85753 | ||||
Sequence: K → NLQ | ||||||
Sequence conflict | 1281 | in Ref. 3; ABF85753 | ||||
Sequence: A → D | ||||||
Sequence conflict | 1296 | in Ref. 3; ABF85753 | ||||
Sequence: N → K | ||||||
Sequence conflict | 1310 | in Ref. 3; ABF85753 | ||||
Sequence: M → V | ||||||
Sequence conflict | 1319 | in Ref. 3; ABF85753 | ||||
Sequence: A → S | ||||||
Sequence conflict | 1392 | in Ref. 3; ABF85753 | ||||
Sequence: S → T | ||||||
Sequence conflict | 1402 | in Ref. 3; ABF85753 | ||||
Sequence: P → T | ||||||
Compositional bias | 1440-1459 | Polar residues | ||||
Sequence: KPPASKTTTPTATIPSNSGD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE013599 EMBL· GenBank· DDBJ | AAF57444.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT025853 EMBL· GenBank· DDBJ | ABF85753.1 EMBL· GenBank· DDBJ | mRNA | ||
AY052012 EMBL· GenBank· DDBJ | AAK93436.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |