Q9UHB6 · LIMA1_HUMAN
- ProteinLIM domain and actin-binding protein 1
- GeneLIMA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids759 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity).
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 | actin cytoskeleton | |
Cellular Component | brush border membrane | |
Cellular Component | cleavage furrow | |
Cellular Component | cytosol | |
Cellular Component | focal adhesion | |
Cellular Component | plasma membrane | |
Cellular Component | ruffle | |
Cellular Component | stress fiber | |
Molecular Function | actin filament binding | |
Molecular Function | actin monomer binding | |
Molecular Function | cadherin binding | |
Molecular Function | metal ion binding | |
Biological Process | actin filament bundle assembly | |
Biological Process | cell migration | |
Biological Process | cholesterol homeostasis | |
Biological Process | cholesterol metabolic process | |
Biological Process | intestinal cholesterol absorption | |
Biological Process | negative regulation of actin filament depolymerization | |
Biological Process | ruffle organization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLIM domain and actin-binding protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UHB6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Colocalizes with PXN at focal adhesions in mesangial cells (PubMed:24694988).
Colocalizes with actin stress fibers in quiescent cells. PDGF stimulation induced disassembly of stress fibers and formation of peripheral and dorsal ruffles, where LIMA1 is relocalized (By similarity).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_080864 | 25 | correlated with lower plasma levels of low-density lipoprotein cholesterol; reduces protein stability; dbSNP:rs140372565 | |||
Sequence: L → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 885 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 modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Modified residue | 1 | UniProt | In isoform Q9UHB6-2; N-acetylmethionine | ||||
Sequence: M | |||||||
Modified residue | 1 | UniProt | In isoform Q9UHB6-5; N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000075730 | 1-759 | UniProt | LIM domain and actin-binding protein 1 | |||
Sequence: MESSPFNRRQWTSLSLRVTAKELSLVNKNKSSAIVEIFSKYQKAAEETNMEKKRSNTENLSQHFRKGTLTVLKKKWENPGLGAESHTDSLRNSSTEIRHRADHPPAEVTSHAASGAKADQEEQIHPRSRLRSPPEALVQGRYPHIKDGEDLKDHSTESKKMENCLGESRHEVEKSEISENTDASGKIEKYNVPLNRLKMMFEKGEPTQTKILRAQSRSASGRKISENSYSLDDLEIGPGQLSSSTFDSEKNESRRNLELPRLSETSIKDRMAKYQAAVSKQSSSTNYTNELKASGGEIKIHKMEQKENVPPGPEVCITHQEGEKISANENSLAVRSTPAEDDSRDSQVKSEVQQPVHPKPLSPDSRASSLSESSPPKAMKKFQAPARETCVECQKTVYPMERLLANQQVFHISCFRCSYCNNKLSLGTYASLHGRIYCKPHFNQLFKSKGNYDEGFGHRPHKDLWASKNENEEILERPAQLANARETPHSPGVEDAPIAKVGVLAASMEAKASSQQEKEDKPAETKKLRIAWPPPTELGSSGSALEEGIKMSKPKWPPEDEISKPEVPEDVDLDLKKLRRSSSLKERSRPFTVAASFQSTSVKSPKTVSPPIRKGWSMSEQSEESVGGRVAERKQVENAKASKKNGNVGKTTWQNKESKGETGKRSKEGHSLEMENENLVENGADSDEDDNSFLKQQSPQEPKSLNWSSFVDNTFAEEFTTQNQKSQDVELWEGEVVKELSVEEQIKRNRYYDEDEDEE | |||||||
Modified residue | 4 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 4 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 12 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 13 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 15 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 15 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 55 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 55 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 61 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 89 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 114 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 128 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 132 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 168 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 178 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 183 | UniProt | In isoform Q9UHB6-5; Phosphoserine | ||||
Sequence: A | |||||||
Modified residue (large scale data) | 184 | 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) | 228 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 229 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 230 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 230 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 242 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 263 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 263 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 266 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 287 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 326 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 331 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 337 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 343 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 343 | UniProt | In isoform Q9UHB6-4; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 343 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 346 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 350 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 362 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 362 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 365 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 365 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 368 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 369 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 369 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 371 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 373 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 374 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 374 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 439 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 452 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 487 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 490 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 490 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 507 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 541 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 583 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 600 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 601 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 601 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 604 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 604 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 607 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 609 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 609 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 617 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 617 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 619 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 671 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 686 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 686 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 692 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 692 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 698 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 698 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 704 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 708 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 709 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 714 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 726 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 726 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 741 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 741 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with MYO5B; bridges NPC1L1 with MYO5B (PubMed:29880681).
Interacts with PXN; this complex stabilizes actin dynamics (PubMed:24694988).
Interacts with F-actin and G-actin (PubMed:12566430).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9UHB6 | CDH1 P12830 | 2 | EBI-351479, EBI-727477 | |
BINARY | Q9UHB6 | CTNNA1 P35221 | 2 | EBI-351479, EBI-701918 | |
BINARY | Q9UHB6 | DAPK1 P53355 | 2 | EBI-351479, EBI-358616 | |
XENO | Q9UHB6 | SVIL O46385 | 3 | EBI-351479, EBI-6995105 | |
BINARY | Q9UHB6 | YWHAZ P63104 | 2 | EBI-351479, EBI-347088 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 78-131 | Disordered | ||||
Sequence: NPGLGAESHTDSLRNSSTEIRHRADHPPAEVTSHAASGAKADQEEQIHPRSRLR | ||||||
Compositional bias | 91-106 | Basic and acidic residues | ||||
Sequence: RNSSTEIRHRADHPPA | ||||||
Region | 146-182 | Disordered | ||||
Sequence: KDGEDLKDHSTESKKMENCLGESRHEVEKSEISENTD | ||||||
Motif | 164-166 | Required for interaction with NPC1L1 | ||||
Sequence: CLG | ||||||
Compositional bias | 211-227 | Polar residues | ||||
Sequence: ILRAQSRSASGRKISEN | ||||||
Region | 211-264 | Disordered | ||||
Sequence: ILRAQSRSASGRKISENSYSLDDLEIGPGQLSSSTFDSEKNESRRNLELPRLSE | ||||||
Compositional bias | 248-264 | Basic and acidic residues | ||||
Sequence: SEKNESRRNLELPRLSE | ||||||
Compositional bias | 323-337 | Polar residues | ||||
Sequence: EKISANENSLAVRST | ||||||
Region | 323-381 | Disordered | ||||
Sequence: EKISANENSLAVRSTPAEDDSRDSQVKSEVQQPVHPKPLSPDSRASSLSESSPPKAMKK | ||||||
Domain | 388-448 | LIM zinc-binding | ||||
Sequence: ETCVECQKTVYPMERLLANQQVFHISCFRCSYCNNKLSLGTYASLHGRIYCKPHFNQLFKS | ||||||
Region | 493-513 | Required for interaction with MYO5B | ||||
Sequence: VEDAPIAKVGVLAASMEAKAS | ||||||
Region | 509-709 | Disordered | ||||
Sequence: EAKASSQQEKEDKPAETKKLRIAWPPPTELGSSGSALEEGIKMSKPKWPPEDEISKPEVPEDVDLDLKKLRRSSSLKERSRPFTVAASFQSTSVKSPKTVSPPIRKGWSMSEQSEESVGGRVAERKQVENAKASKKNGNVGKTTWQNKESKGETGKRSKEGHSLEMENENLVENGADSDEDDNSFLKQQSPQEPKSLNWSS | ||||||
Compositional bias | 513-527 | Basic and acidic residues | ||||
Sequence: SSQQEKEDKPAETKK | ||||||
Compositional bias | 552-586 | Basic and acidic residues | ||||
Sequence: SKPKWPPEDEISKPEVPEDVDLDLKKLRRSSSLKE | ||||||
Compositional bias | 587-607 | Polar residues | ||||
Sequence: RSRPFTVAASFQSTSVKSPKT | ||||||
Compositional bias | 626-640 | Basic and acidic residues | ||||
Sequence: VGGRVAERKQVENAK | ||||||
Compositional bias | 641-656 | Polar residues | ||||
Sequence: ASKKNGNVGKTTWQNK | ||||||
Compositional bias | 657-675 | Basic and acidic residues | ||||
Sequence: ESKGETGKRSKEGHSLEME | ||||||
Compositional bias | 695-709 | Polar residues | ||||
Sequence: KQQSPQEPKSLNWSS |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative promoter usage & Alternative splicing.
Q9UHB6-1
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.
- NameBeta
- NoteProduced by alternative promoter usage.
- Length759
- Mass (Da)85,226
- Last updated2000-05-01 v1
- Checksum996378AFD3B003D5
Q9UHB6-2
- NameAlpha
- NoteProduced by alternative promoter usage.
- Differences from canonical
- 1-160: Missing
Q9UHB6-3
Q9UHB6-4
- Name4
- NoteProduced by alternative splicing.
- Differences from canonical
- 344-344: R → PG
Q9UHB6-5
- Name5
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_003116 | 1-160 | in isoform Alpha and isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_003117 | 1-302 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 91-106 | Basic and acidic residues | ||||
Sequence: RNSSTEIRHRADHPPA | ||||||
Compositional bias | 211-227 | Polar residues | ||||
Sequence: ILRAQSRSASGRKISEN | ||||||
Compositional bias | 248-264 | Basic and acidic residues | ||||
Sequence: SEKNESRRNLELPRLSE | ||||||
Compositional bias | 323-337 | Polar residues | ||||
Sequence: EKISANENSLAVRST | ||||||
Alternative sequence | VSP_040136 | 344 | in isoform 4 and isoform 5 | |||
Sequence: R → PG | ||||||
Sequence conflict | 381 | in Ref. 4; BAA90914 and 7; AAH01247 | ||||
Sequence: Missing | ||||||
Sequence conflict | 415 | in Ref. 8; AAG17267 | ||||
Sequence: F → L | ||||||
Sequence conflict | 463 | in Ref. 4; BAA90914 | ||||
Sequence: D → G | ||||||
Sequence conflict | 491 | in Ref. 2; AAF67491 | ||||
Sequence: P → Q | ||||||
Compositional bias | 513-527 | Basic and acidic residues | ||||
Sequence: SSQQEKEDKPAETKK | ||||||
Sequence conflict | 520-521 | in Ref. 2; AAF67491 | ||||
Sequence: DK → NR | ||||||
Compositional bias | 552-586 | Basic and acidic residues | ||||
Sequence: SKPKWPPEDEISKPEVPEDVDLDLKKLRRSSSLKE | ||||||
Compositional bias | 587-607 | Polar residues | ||||
Sequence: RSRPFTVAASFQSTSVKSPKT | ||||||
Compositional bias | 626-640 | Basic and acidic residues | ||||
Sequence: VGGRVAERKQVENAK | ||||||
Compositional bias | 641-656 | Polar residues | ||||
Sequence: ASKKNGNVGKTTWQNK | ||||||
Compositional bias | 657-675 | Basic and acidic residues | ||||
Sequence: ESKGETGKRSKEGHSLEME | ||||||
Compositional bias | 695-709 | Polar residues | ||||
Sequence: KQQSPQEPKSLNWSS |
Polymorphism
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF198454 EMBL· GenBank· DDBJ | AAF23755.1 EMBL· GenBank· DDBJ | mRNA | ||
AF198455 EMBL· GenBank· DDBJ | AAF23756.1 EMBL· GenBank· DDBJ | mRNA | ||
AF157325 EMBL· GenBank· DDBJ | AAF67491.1 EMBL· GenBank· DDBJ | mRNA | ||
AL136911 EMBL· GenBank· DDBJ | CAB66845.1 EMBL· GenBank· DDBJ | mRNA | ||
AK000372 EMBL· GenBank· DDBJ | BAA91120.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK000335 EMBL· GenBank· DDBJ | BAA91092.1 EMBL· GenBank· DDBJ | mRNA | ||
AK023649 EMBL· GenBank· DDBJ | BAB14625.1 EMBL· GenBank· DDBJ | mRNA | ||
AK000057 EMBL· GenBank· DDBJ | BAA90914.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314447 EMBL· GenBank· DDBJ | BAG37056.1 EMBL· GenBank· DDBJ | mRNA | ||
AB209512 EMBL· GenBank· DDBJ | BAD92749.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
CH471111 EMBL· GenBank· DDBJ | EAW58135.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001247 EMBL· GenBank· DDBJ | AAH01247.2 EMBL· GenBank· DDBJ | mRNA | ||
BC010664 EMBL· GenBank· DDBJ | AAH10664.1 EMBL· GenBank· DDBJ | mRNA | ||
BC110815 EMBL· GenBank· DDBJ | AAI10816.1 EMBL· GenBank· DDBJ | mRNA | ||
BC136763 EMBL· GenBank· DDBJ | AAI36764.1 EMBL· GenBank· DDBJ | mRNA | ||
AF218025 EMBL· GenBank· DDBJ | AAG17267.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |