Q8TED9 · AF1L1_HUMAN
- ProteinActin filament-associated protein 1-like 1
- GeneAFAP1L1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids768 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May be involved in podosome and invadosome formation.
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 | anchoring junction | |
Cellular Component | cell projection | |
Cellular Component | cytosol | |
Cellular Component | podosome | |
Cellular Component | stress fiber | |
Molecular Function | SH3 domain binding |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameActin filament-associated protein 1-like 1
- Short namesAFAP1-like protein 1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8TED9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 866 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000295239 | 1-768 | UniProt | Actin filament-associated protein 1-like 1 | |||
Sequence: MDRGQVLEQLLPELTGLLSLLDHEYLSDTTLEKKMAVASILQSLQPLPAKEVSYLYVNTADLHSGPSFVESLFEEFDCDLSDLRDMPEDDGEPSKGASPELAKSPRLRNAADLPPPLPNKPPPEDYYEEALPLGPGKSPEYISSHNGCSPSHSIVDGYYEDADSSYPATRVNGELKSSYNDSDAMSSSYESYDEEEEEGKSPQPRHQWPSEEASMHLVRECRICAFLLRKKRFGQWAKQLTVIREDQLLCYKSSKDRQPHLRLALDTCSIIYVPKDSRHKRHELRFTQGATEVLVLALQSREQAEEWLKVIREVSKPVGGAEGVEVPRSPVLLCKLDLDKRLSQEKQTSDSDSVGVGDNCSTLGRRETCDHGKGKKSSLAELKGSMSRAAGRKITRIIGFSKKKTLADDLQTSSTEEEVPCCGYLNVLVNQGWKERWCRLKCNTLYFHKDHMDLRTHVNAIALQGCEVAPGFGPRHPFAFRILRNRQEVAILEASCSEDMGRWLGLLLVEMGSRVTPEALHYDYVDVETLTSIVSAGRNSFLYARSCQNQWPEPRVYDDVPYEKMQDEEPERPTGAQVKRHASSCSEKSHRVDPQVKVKRHASSANQYKYGKNRAEEDARRYLVEKEKLEKEKETIRTELIALRQEKRELKEAIRSSPGAKLKALEEAVATLEAQCRAKEERRIDLELKLVAVKERLQQSLAGGPALGLSVSSKPKSGETANKPQNSVPEQPLPVNCVSELRKRSPSIVASNQGRVLQKAKEWEMKKT | |||||||
Modified residue | 94 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 98 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 98 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 104 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 104 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 153 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 329 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 329 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 343 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 349 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 362 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 385 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 557 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 745 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 747 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 747 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in breast, colon and brain. In all 3 tissues, expressed in the microvasculature (at protein level). In addition, in the breast, found in the contractile myoepithelial cell layer which surrounds the breast ducts (at protein level). In the colon, expressed in the mucous membrane and colonic crypts and in the smooth muscle cell layer which provide movement of the colon (at protein level). In the cerebellum, localized around the Purkinje neurons and the granule cells of the granular layer, but not inside cell bodies (at protein level). Outside of the cerebellar cortex, expressed in glial cells (at protein level). Highly expressed away from the cell bodies within the dentate nucleus (at protein level).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with CTTN.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8TED9 | GADD45G O95257 | 8 | EBI-1053644, EBI-448202 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 82-145 | Disordered | ||||
Sequence: DLRDMPEDDGEPSKGASPELAKSPRLRNAADLPPPLPNKPPPEDYYEEALPLGPGKSPEYISSH | ||||||
Compositional bias | 111-125 | Pro residues | ||||
Sequence: ADLPPPLPNKPPPED | ||||||
Compositional bias | 173-187 | Polar residues | ||||
Sequence: GELKSSYNDSDAMSS | ||||||
Region | 173-211 | Disordered | ||||
Sequence: GELKSSYNDSDAMSSSYESYDEEEEEGKSPQPRHQWPSE | ||||||
Domain | 220-316 | PH 1 | ||||
Sequence: ECRICAFLLRKKRFGQWAKQLTVIREDQLLCYKSSKDRQPHLRLALDTCSIIYVPKDSRHKRHELRFTQGATEVLVLALQSREQAEEWLKVIREVSK | ||||||
Domain | 418-512 | PH 2 | ||||
Sequence: EVPCCGYLNVLVNQGWKERWCRLKCNTLYFHKDHMDLRTHVNAIALQGCEVAPGFGPRHPFAFRILRNRQEVAILEASCSEDMGRWLGLLLVEMG | ||||||
Region | 566-604 | Disordered | ||||
Sequence: QDEEPERPTGAQVKRHASSCSEKSHRVDPQVKVKRHASS | ||||||
Compositional bias | 583-598 | Basic and acidic residues | ||||
Sequence: SSCSEKSHRVDPQVKV | ||||||
Coiled coil | 611-700 | |||||
Sequence: GKNRAEEDARRYLVEKEKLEKEKETIRTELIALRQEKRELKEAIRSSPGAKLKALEEAVATLEAQCRAKEERRIDLELKLVAVKERLQQS | ||||||
Region | 705-768 | Disordered | ||||
Sequence: PALGLSVSSKPKSGETANKPQNSVPEQPLPVNCVSELRKRSPSIVASNQGRVLQKAKEWEMKKT | ||||||
Compositional bias | 713-733 | Polar residues | ||||
Sequence: SKPKSGETANKPQNSVPEQPL |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q8TED9-1
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
- Length768
- Mass (Da)86,432
- Last updated2007-07-24 v2
- Checksum5DC1B952E797110F
Q8TED9-2
- Name2
- Differences from canonical
- 719-761: Missing
Q8TED9-3
- Name3
Q8TED9-4
- Name4
- Differences from canonical
- 1-385: Missing
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_026856 | 1-385 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 84 | in Ref. 2; BAC04664 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 106 | in Ref. 2; BAC04664 | ||||
Sequence: R → C | ||||||
Compositional bias | 111-125 | Pro residues | ||||
Sequence: ADLPPPLPNKPPPED | ||||||
Compositional bias | 173-187 | Polar residues | ||||
Sequence: GELKSSYNDSDAMSS | ||||||
Sequence conflict | 325 | in Ref. 2; BAC04664 | ||||
Sequence: E → G | ||||||
Alternative sequence | VSP_026857 | 341-377 | in isoform 3 | |||
Sequence: RLSQEKQTSDSDSVGVGDNCSTLGRRETCDHGKGKKS → VYLSPLSLPQARQWPLNTGSTPGELTGWGESQATAKL | ||||||
Alternative sequence | VSP_026858 | 378-768 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 583-598 | Basic and acidic residues | ||||
Sequence: SSCSEKSHRVDPQVKV | ||||||
Compositional bias | 713-733 | Polar residues | ||||
Sequence: SKPKSGETANKPQNSVPEQPL | ||||||
Alternative sequence | VSP_026859 | 719-761 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK074185 EMBL· GenBank· DDBJ | BAB85011.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK094067 EMBL· GenBank· DDBJ | BAC04277.1 EMBL· GenBank· DDBJ | mRNA | ||
AK095980 EMBL· GenBank· DDBJ | BAC04664.1 EMBL· GenBank· DDBJ | mRNA | ||
BC040723 EMBL· GenBank· DDBJ | AAH40723.1 EMBL· GenBank· DDBJ | mRNA | ||
BC125093 EMBL· GenBank· DDBJ | AAI25094.1 EMBL· GenBank· DDBJ | mRNA | ||
BC125094 EMBL· GenBank· DDBJ | AAI25095.1 EMBL· GenBank· DDBJ | mRNA |