Q9NQW6 · ANLN_HUMAN
- ProteinAnillin
- GeneANLN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1124 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. Plays a role in bleb assembly during metaphase and anaphase of mitosis (PubMed:23870127).
May play a significant role in podocyte cell migration (PubMed:24676636).
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 | actin cytoskeleton | |
Cellular Component | actomyosin contractile ring | |
Cellular Component | bleb | |
Cellular Component | cell cortex | |
Cellular Component | cytosol | |
Cellular Component | midbody | |
Cellular Component | nucleoplasm | |
Molecular Function | actin binding | |
Molecular Function | cadherin binding | |
Biological Process | actomyosin contractile ring assembly | |
Biological Process | hematopoietic progenitor cell differentiation | |
Biological Process | mitotic cytokinesis | |
Biological Process | podocyte cell migration | |
Biological Process | positive regulation of bleb assembly | |
Biological Process | regulation of exit from mitosis | |
Biological Process | septin ring assembly | |
Biological Process | septin ring organization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAnillin
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NQW6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Focal segmental glomerulosclerosis 8 (FSGS8)
- Note
- DescriptionA renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation.
- See alsoMIM:616032
Natural variants in FSGS8
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_072418 | 431 | R>C | in FSGS8; results in decreased interaction with CD2AP; dbSNP:rs587777741 | |
VAR_072419 | 618 | G>C | in FSGS8; dbSNP:rs1184529372 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 32 | Abrogates interaction with CD2AP. | ||||
Sequence: R → A | ||||||
Mutagenesis | 41 | Abrogates ubiquitin-mediated proteolysis; when associated with A-44. | ||||
Sequence: R → A | ||||||
Mutagenesis | 44 | Abrogates ubiquitin-mediated proteolysis; when associated with A-41. | ||||
Sequence: L → A | ||||||
Natural variant | VAR_025661 | 65 | in dbSNP:rs3735400 | |||
Sequence: S → W | ||||||
Natural variant | VAR_025662 | 185 | in dbSNP:rs197367 | |||
Sequence: R → K | ||||||
Natural variant | VAR_072418 | 431 | in FSGS8; results in decreased interaction with CD2AP; dbSNP:rs587777741 | |||
Sequence: R → C | ||||||
Natural variant | VAR_072419 | 618 | in FSGS8; dbSNP:rs1184529372 | |||
Sequence: G → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,168 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000227965 | 1-1124 | UniProt | Anillin | |||
Sequence: MDPFTEKLLERTRARRENLQRKMAERPTAAPRSMTHAKRARQPLSEASNQQPLSGGEEKSCTKPSPSKKRCSDNTEVEVSNLENKQPVESTSAKSCSPSPVSPQVQPQAADTISDSVAVPASLLGMRRGLNSRLEATAASSVKTRMQKLAEQRRRWDNDDMTDDIPESSLFSPMPSEEKAASPPRPLLSNASATPVGRRGRLANLAATICSWEDDVNHSFAKQNSVQEQPGTACLSKFSSASGASARINSSSVKQEATFCSQRDGDASLNKALSSSADDASLVNASISSSVKATSPVKSTTSITDAKSCEGQNPELLPKTPISPLKTGVSKPIVKSTLSQTVPSKGELSREICLQSQSKDKSTTPGGTGIKPFLERFGERCQEHSKESPARSTPHRTPIITPNTKAIQERLFKQDTSSSTTHLAQQLKQERQKELACLRGRFDKGNIWSAEKGGNSKSKQLETKQETHCQSTPLKKHQGVSKTQSLPVTEKVTENQIPAKNSSTEPKGFTECEMTKSSPLKITLFLEEDKSLKVTSDPKVEQKIEVIREIEMSVDDDDINSSKVINDLFSDVLEEGELDMEKSQEEMDQALAESSEEQEDALNISSMSLLAPLAQTVGVVSPESLVSTPRLELKDTSRSDESPKPGKFQRTRVPRAESGDSLGSEDRDLLYSIDAYRSQRFKETERPSIKQVIVRKEDVTSKLDEKNNAFPCQVNIKQKMQELNNEINMQQTVIYQASQALNCCVDEEHGKGSLEEAEAERLLLIATGKRTLLIDELNKLKNEGPQRKNKASPQSEFMPSKGSVTLSEIRLPLKADFVCSTVQKPDAANYYYLIILKAGAENMVATPLASTSNSLNGDALTFTTTFTLQDVSNDFEINIEVYSLVQKKDPSGLDKKKKTSKSKAITPKRLLTSITTKSNIHSSVMASPGGLSAVRTSNFALVGSYTLSLSSVGNTKFVLDKVPFLSSLEGHIYLKIKCQVNSSVEERGFLTIFEDVSGFGAWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREFCARRNTFELITVRPQREDDRETLVSQCRDTLCVTKNWLSADTKEERDLWMQKLNQVLVDIRLWQPDACYKPIGKP | |||||||
Modified residue (large scale data) | 45 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 48 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 54 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 54 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 62 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 65 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 72 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 72 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 75 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 95 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 97 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 102 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 140 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 141 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 172 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 172 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 182 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 182 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 194 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 194 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 211 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 219 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 225 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 225 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 245 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 252 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 252 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 254 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) | ||||
Sequence: K | |||||||
Modified residue | 261 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 274 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 275 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 276 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 281 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 294 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 295 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 308 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 320 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 320 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 323 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 323 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 327 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 336 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 339 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 339 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 341 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 344 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 349 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 356 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 358 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 362 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 363 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 364 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 364 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 371 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 385 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 388 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 392 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 393 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 397 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 397 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 401 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 401 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 416 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 417 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 417 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 418 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 419 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 419 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 449 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 449 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 471 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 472 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 485 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 485 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 502 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 515 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 517 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 518 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 518 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 536 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 553 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 553 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 561 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 561 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 562 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 637 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 642 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 642 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 658 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 658 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 661 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 661 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 664 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 664 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 671 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 671 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 678 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 678 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 688 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 792 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 792 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 795 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 927 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 927 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expression is significantly increased in renal biopsy specimens from idiopathic FSGS (PubMed:24676636).
Overexpressed in many tumor types including breast, colorectal, endometrial, hepatic, kidney, lung, ovarian and pancreatic tumors
Developmental stage
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with CD2AP (PubMed:15800069).
May interact with RHOA (PubMed:16357138).
Interacts with FZR1/CDH1 during mitotic exit (PubMed:16040610).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9NQW6-2 | MARCHF10 Q8NA82 | 3 | EBI-10312488, EBI-2341554 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-23 | Basic and acidic residues | ||||
Sequence: MDPFTEKLLERTRARRENLQRKM | ||||||
Region | 1-45 | Required for ubiquitination | ||||
Sequence: MDPFTEKLLERTRARRENLQRKMAERPTAAPRSMTHAKRARQPLS | ||||||
Region | 1-113 | Disordered | ||||
Sequence: MDPFTEKLLERTRARRENLQRKMAERPTAAPRSMTHAKRARQPLSEASNQQPLSGGEEKSCTKPSPSKKRCSDNTEVEVSNLENKQPVESTSAKSCSPSPVSPQVQPQAADTI | ||||||
Region | 1-155 | Interaction with CD2AP | ||||
Sequence: MDPFTEKLLERTRARRENLQRKMAERPTAAPRSMTHAKRARQPLSEASNQQPLSGGEEKSCTKPSPSKKRCSDNTEVEVSNLENKQPVESTSAKSCSPSPVSPQVQPQAADTISDSVAVPASLLGMRRGLNSRLEATAASSVKTRMQKLAEQRRR | ||||||
Region | 1-230 | Nuclear localization | ||||
Sequence: MDPFTEKLLERTRARRENLQRKMAERPTAAPRSMTHAKRARQPLSEASNQQPLSGGEEKSCTKPSPSKKRCSDNTEVEVSNLENKQPVESTSAKSCSPSPVSPQVQPQAADTISDSVAVPASLLGMRRGLNSRLEATAASSVKTRMQKLAEQRRRWDNDDMTDDIPESSLFSPMPSEEKAASPPRPLLSNASATPVGRRGRLANLAATICSWEDDVNHSFAKQNSVQEQP | ||||||
Compositional bias | 42-61 | Polar residues | ||||
Sequence: QPLSEASNQQPLSGGEEKSC | ||||||
Compositional bias | 62-76 | Basic and acidic residues | ||||
Sequence: TKPSPSKKRCSDNTE | ||||||
Compositional bias | 77-113 | Polar residues | ||||
Sequence: VEVSNLENKQPVESTSAKSCSPSPVSPQVQPQAADTI | ||||||
Region | 136-196 | Disordered | ||||
Sequence: ATAASSVKTRMQKLAEQRRRWDNDDMTDDIPESSLFSPMPSEEKAASPPRPLLSNASATPV | ||||||
Compositional bias | 147-162 | Basic and acidic residues | ||||
Sequence: QKLAEQRRRWDNDDMT | ||||||
Region | 231-676 | Interaction with F-actin | ||||
Sequence: GTACLSKFSSASGASARINSSSVKQEATFCSQRDGDASLNKALSSSADDASLVNASISSSVKATSPVKSTTSITDAKSCEGQNPELLPKTPISPLKTGVSKPIVKSTLSQTVPSKGELSREICLQSQSKDKSTTPGGTGIKPFLERFGERCQEHSKESPARSTPHRTPIITPNTKAIQERLFKQDTSSSTTHLAQQLKQERQKELACLRGRFDKGNIWSAEKGGNSKSKQLETKQETHCQSTPLKKHQGVSKTQSLPVTEKVTENQIPAKNSSTEPKGFTECEMTKSSPLKITLFLEEDKSLKVTSDPKVEQKIEVIREIEMSVDDDDINSSKVINDLFSDVLEEGELDMEKSQEEMDQALAESSEEQEDALNISSMSLLAPLAQTVGVVSPESLVSTPRLELKDTSRSDESPKPGKFQRTRVPRAESGDSLGSEDRDLLYSIDAY | ||||||
Compositional bias | 294-309 | Polar residues | ||||
Sequence: TSPVKSTTSITDAKSC | ||||||
Region | 294-328 | Disordered | ||||
Sequence: TSPVKSTTSITDAKSCEGQNPELLPKTPISPLKTG | ||||||
Region | 380-399 | Disordered | ||||
Sequence: RCQEHSKESPARSTPHRTPI | ||||||
Coiled coil | 569-604 | |||||
Sequence: FSDVLEEGELDMEKSQEEMDQALAESSEEQEDALNI | ||||||
Region | 579-600 | Disordered | ||||
Sequence: DMEKSQEEMDQALAESSEEQED | ||||||
Region | 625-664 | Disordered | ||||
Sequence: LVSTPRLELKDTSRSDESPKPGKFQRTRVPRAESGDSLGS | ||||||
Compositional bias | 633-664 | Basic and acidic residues | ||||
Sequence: LKDTSRSDESPKPGKFQRTRVPRAESGDSLGS | ||||||
Region | 730-1124 | Localization to the cleavage furrow | ||||
Sequence: QQTVIYQASQALNCCVDEEHGKGSLEEAEAERLLLIATGKRTLLIDELNKLKNEGPQRKNKASPQSEFMPSKGSVTLSEIRLPLKADFVCSTVQKPDAANYYYLIILKAGAENMVATPLASTSNSLNGDALTFTTTFTLQDVSNDFEINIEVYSLVQKKDPSGLDKKKKTSKSKAITPKRLLTSITTKSNIHSSVMASPGGLSAVRTSNFALVGSYTLSLSSVGNTKFVLDKVPFLSSLEGHIYLKIKCQVNSSVEERGFLTIFEDVSGFGAWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREFCARRNTFELITVRPQREDDRETLVSQCRDTLCVTKNWLSADTKEERDLWMQKLNQVLVDIRLWQPDACYKPIGKP | ||||||
Domain | 983-1107 | PH | ||||
Sequence: SVEERGFLTIFEDVSGFGAWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREFCARRNTFELITVRPQREDDRETLVSQCRDTLCVTKNWLSADTKEERDLWMQKLNQVLV |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9NQW6-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,124
- Mass (Da)124,199
- Last updated2006-03-21 v2
- Checksum79A8CC25C950DB2D
Q9NQW6-2
- Name2
- Differences from canonical
- 508-544: Missing
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-23 | Basic and acidic residues | ||||
Sequence: MDPFTEKLLERTRARRENLQRKM | ||||||
Compositional bias | 42-61 | Polar residues | ||||
Sequence: QPLSEASNQQPLSGGEEKSC | ||||||
Sequence conflict | 53 | in Ref. 1; AAF75796 | ||||
Sequence: L → F | ||||||
Sequence conflict | 62 | in Ref. 1; AAF75796 | ||||
Sequence: T → S | ||||||
Compositional bias | 62-76 | Basic and acidic residues | ||||
Sequence: TKPSPSKKRCSDNTE | ||||||
Compositional bias | 77-113 | Polar residues | ||||
Sequence: VEVSNLENKQPVESTSAKSCSPSPVSPQVQPQAADTI | ||||||
Compositional bias | 147-162 | Basic and acidic residues | ||||
Sequence: QKLAEQRRRWDNDDMT | ||||||
Sequence conflict | 294 | in Ref. 1 and 3 | ||||
Sequence: T → TS | ||||||
Compositional bias | 294-309 | Polar residues | ||||
Sequence: TSPVKSTTSITDAKSC | ||||||
Sequence conflict | 410 | in Ref. 2; AAH70066 | ||||
Sequence: R → K | ||||||
Alternative sequence | VSP_017617 | 508-544 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 625 | in Ref. 4; BAA91711 | ||||
Sequence: L → S | ||||||
Compositional bias | 633-664 | Basic and acidic residues | ||||
Sequence: LKDTSRSDESPKPGKFQRTRVPRAESGDSLGS | ||||||
Sequence conflict | 1035 | in Ref. 3; CAI56788 | ||||
Sequence: A → V |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF273437 EMBL· GenBank· DDBJ | AAF75796.1 EMBL· GenBank· DDBJ | mRNA | ||
BC034692 EMBL· GenBank· DDBJ | AAH34692.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC070066 EMBL· GenBank· DDBJ | AAH70066.1 EMBL· GenBank· DDBJ | mRNA | ||
CR936650 EMBL· GenBank· DDBJ | CAI56788.1 EMBL· GenBank· DDBJ | mRNA | ||
AK001468 EMBL· GenBank· DDBJ | BAA91710.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK001472 EMBL· GenBank· DDBJ | BAA91711.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK023208 EMBL· GenBank· DDBJ | BAB14463.1 EMBL· GenBank· DDBJ | mRNA |