Q8K4G5 · ABLM1_MOUSE
- ProteinActin-binding LIM protein 1
- GeneAblim1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids861 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May act as scaffold protein (By similarity).
May play a role in the development of the retina. Has been suggested to play a role in axon guidance
May play a role in the development of the retina. Has been suggested to play a role in axon guidance
Miscellaneous
Isoform 1 is not necessary for normal axon guidance.
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 | cytoplasm | |
Cellular Component | lamellipodium | |
Cellular Component | postsynaptic density | |
Cellular Component | stress fiber | |
Molecular Function | actin binding | |
Molecular Function | actin filament binding | |
Molecular Function | metal ion binding | |
Biological Process | axon guidance | |
Biological Process | cilium assembly | |
Biological Process | cytoskeleton organization | |
Biological Process | lamellipodium assembly | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | transcription by RNA polymerase II |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameActin-binding LIM protein 1
- Short namesabLIM-1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8K4G5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In a striped pattern along the myofibril axis in cardiac myocytes. Associated with the cytoskeleton.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000075698 | 1-861 | Actin-binding LIM protein 1 | |||
Sequence: MPSLLGLKCLGKLCSSEIGKVPSPERASLRNSHRRLLIEDLSVPETPDPAHRRRGTVIHLVYLYSAGCGPPELRFSSYDPSVAHPQDPHHSSEKPVIHCHKCGEPCKGEVLRVQTKHFHIKCFTCKVCGCDLAQGGFFIKNGDYLCTLDYQRMYGTRCHGCGEFVEGEVVTALGKTYHPNCFACTICKRPFPPGDRVTFNGRDCLCQLCAQPMSSSPKEASCSSNCAGCGRDIKNGQALLALDKQWHLGCFKCKSCGKVLTGEYISKDGSPYCEKDYQGLFGVKCEACHQFITGKVLEAGDKHYHPSCARCSRCNQMFTEGEEMYLQGSTVWHPDCKQSTKTEEKLRPPNIPRSSSDFFYPKSLIRRTGRSPALQLLSPPCLTNSNKNPRQPTRTSSESIYSRPGSSIPGSPGHTIYAKVDNEILDYKDLAAIPKVKAIYDIERPDLITYEPFYTSGYEDKQERQSLGESPRTLSPTPSAEGYQDVRDRMIHRSTSQGSINSPVYSRHSYTPTTSRSPQHFHRPELLSPGVHRWSPLRTSSFSSTHSDSRPNPPFRHHFLPHVKGNEPSSGRNSPLPYRPDSRPLTPTYAQAPKHFHVPDQGINIYRKPPIYKQHAALAAQSKASEDIIKFSKFPAAQAPDPNEIPKIETDHWPGPPSLAAVGTDPRRRSSGREEDEEELLRRRQLQEEQLMKLNSGLGQLILKEEMEKESRERASLASRYDSPLHSASHAPSSKTSSLPGYGKNGLHRPVSTDFAQYNSYGDISGGVRDYQTLPDGHMPAVRMDRGVSMPNMLEPKIFPYEMLMVTNRGRNKILRDVDRTRLERHLAPEVFWEIFGMSIQEFDKLPLWRRNDMKKKAKLF | ||||||
Modified residue | 216 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 411 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 417 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 440 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 466 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 470 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 475 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 477 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 479 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 483 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 496 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 499 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 502 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 582 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 671 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 704 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 723 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 738 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 760 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 789 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform 1 is detected in adult retina, where it is highly expressed in the ganglion layer. Detected in rod inner segment. Isoform 2 is highly expressed in adult retina, brain, kidney and heart. Isoform 3 is highly expressed in adult retina, brain, kidney, liver, skeletal muscle, spleen and heart. Detected in embryonic retina, brain, spinal cord, peripheral sensory ganglia and thymus.
Developmental stage
Isoform 1 is detected at low levels starting from 12 dpc and remains constant until birth. After this levels increase strongly and expression remains high in adults. Isoform 2 and isoform 3 are expressed at a constant high level throughout development.
Gene expression databases
Interaction
Subunit
Binds F-actin. Interacts with ABRA (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8K4G5 | Dlg4 Q62108 | 5 | EBI-2307994, EBI-300895 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 97-156 | LIM zinc-binding 1 | ||||
Sequence: IHCHKCGEPCKGEVLRVQTKHFHIKCFTCKVCGCDLAQGGFFIKNGDYLCTLDYQRMYGT | ||||||
Domain | 156-216 | LIM zinc-binding 2 | ||||
Sequence: TRCHGCGEFVEGEVVTALGKTYHPNCFACTICKRPFPPGDRVTFNGRDCLCQLCAQPMSSS | ||||||
Domain | 224-283 | LIM zinc-binding 3 | ||||
Sequence: SNCAGCGRDIKNGQALLALDKQWHLGCFKCKSCGKVLTGEYISKDGSPYCEKDYQGLFGV | ||||||
Domain | 283-343 | LIM zinc-binding 4 | ||||
Sequence: VKCEACHQFITGKVLEAGDKHYHPSCARCSRCNQMFTEGEEMYLQGSTVWHPDCKQSTKTE | ||||||
Region | 374-414 | Disordered | ||||
Sequence: LQLLSPPCLTNSNKNPRQPTRTSSESIYSRPGSSIPGSPGH | ||||||
Compositional bias | 377-409 | Polar residues | ||||
Sequence: LSPPCLTNSNKNPRQPTRTSSESIYSRPGSSIP | ||||||
Region | 459-590 | Disordered | ||||
Sequence: EDKQERQSLGESPRTLSPTPSAEGYQDVRDRMIHRSTSQGSINSPVYSRHSYTPTTSRSPQHFHRPELLSPGVHRWSPLRTSSFSSTHSDSRPNPPFRHHFLPHVKGNEPSSGRNSPLPYRPDSRPLTPTYA | ||||||
Compositional bias | 493-521 | Polar residues | ||||
Sequence: RSTSQGSINSPVYSRHSYTPTTSRSPQHF | ||||||
Compositional bias | 534-550 | Polar residues | ||||
Sequence: WSPLRTSSFSSTHSDSR | ||||||
Region | 634-682 | Disordered | ||||
Sequence: FPAAQAPDPNEIPKIETDHWPGPPSLAAVGTDPRRRSSGREEDEEELLR | ||||||
Compositional bias | 667-682 | Basic and acidic residues | ||||
Sequence: RRRSSGREEDEEELLR | ||||||
Coiled coil | 673-723 | |||||
Sequence: REEDEEELLRRRQLQEEQLMKLNSGLGQLILKEEMEKESRERASLASRYDS | ||||||
Region | 713-748 | Disordered | ||||
Sequence: ERASLASRYDSPLHSASHAPSSKTSSLPGYGKNGLH | ||||||
Compositional bias | 722-741 | Polar residues | ||||
Sequence: DSPLHSASHAPSSKTSSLPG | ||||||
Domain | 793-861 | HP | ||||
Sequence: MLEPKIFPYEMLMVTNRGRNKILRDVDRTRLERHLAPEVFWEIFGMSIQEFDKLPLWRRNDMKKKAKLF |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
Q8K4G5-1
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
- SynonymsAbLIM-L
- Length861
- Mass (Da)96,805
- Last updated2002-10-01 v1
- Checksum5E045F7CEF1D91EF
Q8K4G5-2
- Name2
- SynonymsAbLIM-M
Q8K4G5-3
- Name3
- SynonymsAbLIM-S
- Differences from canonical
- 1-316: Missing
Q8K4G5-4
- Name4
Q8K4G5-5
- Name5
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9Q9Q7 | E9Q9Q7_MOUSE | Ablim1 | 400 | ||
E9Q9D1 | E9Q9D1_MOUSE | Ablim1 | 426 | ||
E9Q9D2 | E9Q9D2_MOUSE | Ablim1 | 454 | ||
E9Q9C0 | E9Q9C0_MOUSE | Ablim1 | 714 | ||
E9Q9C1 | E9Q9C1_MOUSE | Ablim1 | 744 | ||
E9Q9C2 | E9Q9C2_MOUSE | Ablim1 | 777 | ||
E9Q9C4 | E9Q9C4_MOUSE | Ablim1 | 682 | ||
E9Q9C7 | E9Q9C7_MOUSE | Ablim1 | 668 | ||
E9Q030 | E9Q030_MOUSE | Ablim1 | 545 | ||
F6YHE5 | F6YHE5_MOUSE | Ablim1 | 292 | ||
E9QK41 | E9QK41_MOUSE | Ablim1 | 861 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_012105 | 1-77 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_012104 | 1-81 | in isoform 2 and isoform 4 | |||
Sequence: MPSLLGLKCLGKLCSSEIGKVPSPERASLRNSHRRLLIEDLSVPETPDPAHRRRGTVIHLVYLYSAGCGPPELRFSSYDPS → MVKEK | ||||||
Alternative sequence | VSP_012103 | 1-316 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_012106 | 78-81 | in isoform 5 | |||
Sequence: YDPS → MSTR | ||||||
Alternative sequence | VSP_012107 | 301-345 | in isoform 5 | |||
Sequence: DKHYHPSCARCSRCNQMFTEGEEMYLQGSTVWHPDCKQSTKTEEK → VTEASRTWSHIDLRWQGRSEELRAWRHSIQSLRHQSAREWFALSA | ||||||
Alternative sequence | VSP_012109 | 346-861 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_012108 | 348-391 | in isoform 2 and isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 377-409 | Polar residues | ||||
Sequence: LSPPCLTNSNKNPRQPTRTSSESIYSRPGSSIP | ||||||
Compositional bias | 493-521 | Polar residues | ||||
Sequence: RSTSQGSINSPVYSRHSYTPTTSRSPQHF | ||||||
Alternative sequence | VSP_012110 | 525-564 | in isoform 2 and isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 534-550 | Polar residues | ||||
Sequence: WSPLRTSSFSSTHSDSR | ||||||
Alternative sequence | VSP_012111 | 616-662 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 667-682 | Basic and acidic residues | ||||
Sequence: RRRSSGREEDEEELLR | ||||||
Compositional bias | 722-741 | Polar residues | ||||
Sequence: DSPLHSASHAPSSKTSSLPG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF404774 EMBL· GenBank· DDBJ | AAM73705.1 EMBL· GenBank· DDBJ | mRNA | ||
AF404775 EMBL· GenBank· DDBJ | AAM73706.1 EMBL· GenBank· DDBJ | mRNA | ||
AF404776 EMBL· GenBank· DDBJ | AAM73707.1 EMBL· GenBank· DDBJ | mRNA | ||
AK122196 EMBL· GenBank· DDBJ | BAC65478.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK029371 EMBL· GenBank· DDBJ | BAC26424.1 EMBL· GenBank· DDBJ | mRNA |