Q8TD16 · BICD2_HUMAN
- ProteinProtein bicaudal D homolog 2
- GeneBICD2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids824 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates and stabilizes the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) (PubMed:25814576).
Facilitates the binding of RAB6A to the Golgi by stabilizing its GTP-bound form. Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport via its interaction with RAB6A and recruitment of the dynein-dynactin motor complex (PubMed:25962623).
Contributes to nuclear and centrosomal positioning prior to mitotic entry through regulation of both dynein and kinesin-1. During G2 phase of the cell cycle, associates with RANBP2 at the nuclear pores and recruits dynein and dynactin to the nuclear envelope to ensure proper positioning of the nucleus relative to centrosomes prior to the onset of mitosis (By similarity).
Facilitates the binding of RAB6A to the Golgi by stabilizing its GTP-bound form. Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport via its interaction with RAB6A and recruitment of the dynein-dynactin motor complex (PubMed:25962623).
Contributes to nuclear and centrosomal positioning prior to mitotic entry through regulation of both dynein and kinesin-1. During G2 phase of the cell cycle, associates with RANBP2 at the nuclear pores and recruits dynein and dynactin to the nuclear envelope to ensure proper positioning of the nucleus relative to centrosomes prior to the onset of mitosis (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 | |||
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Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein bicaudal D homolog 2
- Short namesBic-D 2
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8TD16
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In interphase cells mainly localizes to the Golgi complex and colocalizes with dynactin at microtubule plus ends (By similarity).
Localizes to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae in a RANBP2-dependent manner during G2 phase of the cell cycle (PubMed:20386726).
Localizes to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae in a RANBP2-dependent manner during G2 phase of the cell cycle (PubMed:20386726).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Spinal muscular atrophy, lower extremity-predominant 2A, childhood onset, autosomal dominant (SMALED2A)
- Note
- DescriptionAn autosomal dominant form of spinal muscular atrophy characterized by early-childhood onset of muscle weakness and atrophy predominantly affecting the proximal and distal muscles of the lower extremity, although some patients may show upper extremity involvement. The disorder results in delayed walking, waddling gait, difficulty walking, and loss of distal reflexes. Some patients may have foot deformities or hyperlordosis, and some show mild upper motor signs, such as spasticity. Sensation, bulbar function, and cognitive function are preserved. The disorder shows very slow progression throughout life.
- See alsoMIM:615290
Natural variants in SMALED2A
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_070112 | 107 | S>L | in SMALED2A; causes Golgi fragmentation; affects interaction with RAB6A and DNAI1 and the subcellular location of the protein; dbSNP:rs398123028 | |
VAR_070113 | 188 | N>T | in SMALED2A; causes Golgi fragmentation; dbSNP:rs398123029 | |
VAR_070114 | 189 | I>F | in SMALED2A; dbSNP:rs1587671674 | |
VAR_070115 | 501 | R>P | in SMALED2A; the mutation causes increased interaction with dynein; the mutant protein accumulates abnormally in the perinuclear region where it forms ring-like structures that colocalize with RAB6A; dbSNP:rs398123032 | |
VAR_070116 | 508 | K>T | in SMALED2A; dbSNP:rs398123031 | |
VAR_070117 | 703 | T>M | in SMALED2A; causes Golgi fragmentation; dbSNP:rs371707778 | |
VAR_070118 | 774 | E>G | in SMALED2A; affects interaction with RAB6A and DNAI1 and the subcellular location of the protein; dbSNP:rs398123030 |
Spinal muscular atrophy, lower extremity-predominant, 2B, prenatal onset, autosomal dominant (SMALED2B)
- Note
- DescriptionAn autosomal dominant neuromuscular disorder characterized by decreased fetal movements, fractures in utero, severe congenital joint contractures, arthrogryposis multiplex congenita, severe hypotonia, muscle atrophy, and respiratory insufficiency and failure due to muscle weakness. Some patients may have dysmorphic facial features and/or abnormalities on brain imaging. Death in early childhood may occur.
- See alsoMIM:618291
Natural variants in SMALED2B
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_081854 | 194 | Q>R | in SMALED2B; dbSNP:rs1564061982 | |
VAR_081855 | 542 | C>W | in SMALED2B | |
VAR_081856 | 546 | missing | in SMALED2B; dbSNP:rs1064795760 | |
VAR_081857 | 694 | R>C | in SMALED2B; dbSNP:rs797045412 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_070111 | 90 | in dbSNP:rs61754130 | |||
Sequence: K → R | ||||||
Natural variant | VAR_070112 | 107 | in SMALED2A; causes Golgi fragmentation; affects interaction with RAB6A and DNAI1 and the subcellular location of the protein; dbSNP:rs398123028 | |||
Sequence: S → L | ||||||
Natural variant | VAR_070113 | 188 | in SMALED2A; causes Golgi fragmentation; dbSNP:rs398123029 | |||
Sequence: N → T | ||||||
Natural variant | VAR_070114 | 189 | in SMALED2A; dbSNP:rs1587671674 | |||
Sequence: I → F | ||||||
Natural variant | VAR_081854 | 194 | in SMALED2B; dbSNP:rs1564061982 | |||
Sequence: Q → R | ||||||
Natural variant | VAR_070115 | 501 | in SMALED2A; the mutation causes increased interaction with dynein; the mutant protein accumulates abnormally in the perinuclear region where it forms ring-like structures that colocalize with RAB6A; dbSNP:rs398123032 | |||
Sequence: R → P | ||||||
Natural variant | VAR_070116 | 508 | in SMALED2A; dbSNP:rs398123031 | |||
Sequence: K → T | ||||||
Natural variant | VAR_081855 | 542 | in SMALED2B | |||
Sequence: C → W | ||||||
Natural variant | VAR_081856 | 546 | in SMALED2B; dbSNP:rs1064795760 | |||
Sequence: Missing | ||||||
Natural variant | VAR_081857 | 694 | in SMALED2B; dbSNP:rs797045412 | |||
Sequence: R → C | ||||||
Natural variant | VAR_070117 | 703 | in SMALED2A; causes Golgi fragmentation; dbSNP:rs371707778 | |||
Sequence: T → M | ||||||
Natural variant | VAR_070118 | 774 | in SMALED2A; affects interaction with RAB6A and DNAI1 and the subcellular location of the protein; dbSNP:rs398123030 | |||
Sequence: E → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 979 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 initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Chain | PRO_0000205359 | 2-824 | UniProt | Protein bicaudal D homolog 2 | |||
Sequence: SAPSEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKELSHYMSINDSFYTSHLHVSLDGLKFSDDAAEPNNDAEALVNGFEHGGLAKLPLDNKTSTPKKEGLAPPSPSLVSDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRLQASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYREGQGGAGRTSPGGRTSPEARGRRSPILLPKGLLAPEAGRADGGTGDSSPSPGSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLELDHEQTRRGRAKAAPKTKPATPSL | |||||||
Modified residue (large scale data) | 98 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 182 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 190 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 190 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 224 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 224 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 286 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 317 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 318 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 318 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 319 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 319 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 329 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 331 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 334 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 343 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 343 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 379 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 395 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 395 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 418 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 486 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 567 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 568 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 568 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 573 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 574 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 574 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 582 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 582 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 602 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 605 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 606 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 608 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 615 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 821 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 823 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 823 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by NEK9 in vitro.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Part of a tripartite complex with dynein and dynactin, acts an adapter linking the dynein motor complex and dynactin (PubMed:25814576).
Interacts with CPNE4 (via VWFA domain) (By similarity).
Interacts with RAB6A (PubMed:23664119).
Interacts with NEK9 (PubMed:11864968).
Interacts with DNAI1 (PubMed:23664119, PubMed:23664120).
Interacts with DYNC1H1 (PubMed:25512093).
Interacts with RANBP2 (PubMed:20386726).
Binds preferentially to tyrosinated microtubules than to detyrosinated microtubules. Interacts with DYNLL1, DYNC1I2; DCTN1, DCTN2 and KIF5A (By similarity).
Interacts with KIF1C (PubMed:24482476).
Interacts with CPNE4 (via VWFA domain) (By similarity).
Interacts with RAB6A (PubMed:23664119).
Interacts with NEK9 (PubMed:11864968).
Interacts with DNAI1 (PubMed:23664119, PubMed:23664120).
Interacts with DYNC1H1 (PubMed:25512093).
Interacts with RANBP2 (PubMed:20386726).
Binds preferentially to tyrosinated microtubules than to detyrosinated microtubules. Interacts with DYNLL1, DYNC1I2; DCTN1, DCTN2 and KIF5A (By similarity).
Interacts with KIF1C (PubMed:24482476).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 20-269 | |||||
Sequence: EWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKELSHYMSIND | ||||||
Region | 25-398 | Interacts with DYNLL1, DYNC1H1, DYNC1I2, DCTN1 and DCTN2 | ||||
Sequence: EVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKELSHYMSINDSFYTSHLHVSLDGLKFSDDAAEPNNDAEALVNGFEHGGLAKLPLDNKTSTPKKEGLAPPSPSLVSDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALR | ||||||
Region | 311-330 | Disordered | ||||
Sequence: LPLDNKTSTPKKEGLAPPSP | ||||||
Region | 334-599 | Interaction with KIF5A | ||||
Sequence: SDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRLQASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYREGQGGAGRTSPGGRTSPEARGRRSPILLPKGLLAPEAGRAD | ||||||
Coiled coil | 338-537 | |||||
Sequence: SELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRLQASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANL | ||||||
Region | 398-425 | Disordered | ||||
Sequence: RRLQASKERQTALDNEKDRDSHEDGDYY | ||||||
Compositional bias | 404-425 | Basic and acidic residues | ||||
Sequence: KERQTALDNEKDRDSHEDGDYY | ||||||
Region | 559-622 | Disordered | ||||
Sequence: EGQGGAGRTSPGGRTSPEARGRRSPILLPKGLLAPEAGRADGGTGDSSPSPGSSLPSPLSDPRR | ||||||
Region | 590-824 | Interaction with RANBP2 | ||||
Sequence: LLAPEAGRADGGTGDSSPSPGSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLELDHEQTRRGRAKAAPKTKPATPSL | ||||||
Coiled coil | 666-808 | |||||
Sequence: DKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLELDHEQTRR | ||||||
Region | 666-814 | Interacts with RAB6A | ||||
Sequence: DKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLELDHEQTRRGRAKAA | ||||||
Region | 804-824 | Disordered | ||||
Sequence: EQTRRGRAKAAPKTKPATPSL |
Domain
The fourth coiled coil region is involved in Golgi targeting and in the interaction with DCTN2.
Sequence similarities
Belongs to the BicD family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8TD16-1
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
- Length824
- Mass (Da)93,533
- Last updated2002-06-01 v1
- Checksum9C49138FF416378D
Q8TD16-2
- Name2
- NoteDue to intron retention.
- Differences from canonical
- 824-824: L → VSHTCACASDRAEGTGLANQVFCSEKHSIYCD
Sequence caution
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 404-425 | Basic and acidic residues | ||||
Sequence: KERQTALDNEKDRDSHEDGDYY | ||||||
Alternative sequence | VSP_007969 | 824 | in isoform 2 | |||
Sequence: L → VSHTCACASDRAEGTGLANQVFCSEKHSIYCD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY052562 EMBL· GenBank· DDBJ | AAL12246.1 EMBL· GenBank· DDBJ | mRNA | ||
AB014599 EMBL· GenBank· DDBJ | BAA31674.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL137074 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL136981 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC004296 EMBL· GenBank· DDBJ | AAH04296.1 EMBL· GenBank· DDBJ | mRNA | ||
BC073970 EMBL· GenBank· DDBJ | AAH73970.1 EMBL· GenBank· DDBJ | mRNA |