Q9UBX5 · FBLN5_HUMAN
- ProteinFibulin-5
- GeneFBLN5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids448 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Essential for elastic fiber formation, is involved in the assembly of continuous elastin (ELN) polymer and promotes the interaction of microfibrils and ELN (PubMed:18185537).
Stabilizes and organizes elastic fibers in the skin, lung and vasculature (By similarity).
Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Vascular ligand for integrin receptors which may play a role in vascular development and remodeling (PubMed:10428823).
May act as an adapter that mediates the interaction between FBN1 and ELN (PubMed:17255108).
Stabilizes and organizes elastic fibers in the skin, lung and vasculature (By similarity).
Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Vascular ligand for integrin receptors which may play a role in vascular development and remodeling (PubMed:10428823).
May act as an adapter that mediates the interaction between FBN1 and ELN (PubMed:17255108).
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 | collagen-containing extracellular matrix | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular matrix | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Molecular Function | calcium ion binding | |
Molecular Function | integrin binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | cell-matrix adhesion | |
Biological Process | elastic fiber assembly | |
Biological Process | protein localization to cell surface | |
Biological Process | regulation of removal of superoxide radicals | |
Biological Process | secretion |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFibulin-5
- Short namesFIBL-5
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UBX5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: co-localizes with ELN in elastic fibers.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Charcot-Marie-Tooth disease, demyelinating, 1H (CMT1H)
- Note
- DescriptionAn autosomal dominant demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. CMT1H is characterized by peripheral sensorimotor neuropathy with onset usually in adulthood. Affected individuals present with foot deformities, upper or lower limb sensory disturbances, and motor deficits, mainly impaired gait. Rare patients may have hyperelastic skin or develop age-related macular degeneration.
- See alsoMIM:619764
Natural variants in CMT1H
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_076289 | 48 | T>I | in CMT1H; dbSNP:rs141200859 | |
VAR_076290 | 90 | G>S | in CMT1H; dbSNP:rs144288844 | |
VAR_072393 | 267 | G>S | in ARMD3, ARCL1A and CMT1H; produces protein misolding; decreases secretion; no effect on homodimerization; dbSNP:rs149396611 | |
VAR_076291 | 373 | R>C | in CMT1H; dbSNP:rs864309526 |
Cutis laxa, autosomal dominant, 2 (ADCL2)
- Note
- DescriptionA connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. Additional variable clinical features are gastrointestinal diverticula, hernia, and genital prolapse. Rare manifestations are pulmonary artery stenosis, aortic aneurysm, bronchiectasis, and emphysema.
- See alsoMIM:614434
Cutis laxa, autosomal recessive, 1A (ARCL1A)
- Note
- DescriptionA connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. The clinical spectrum of autosomal recessive cutis laxa is highly heterogeneous with respect to organ involvement and severity. Type I autosomal recessive cutis laxa is a specific, life-threatening disorder with organ involvement, lung atelectasis and emphysema, diverticula of the gastrointestinal and genitourinary systems, and vascular anomalies. Associated cranial anomalies, late closure of the fontanel, joint laxity, hip dislocation, and inguinal hernia have been observed but are uncommon.
- See alsoMIM:219100
Natural variants in ARCL1A
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_072392 | 217 | C>R | in ARCL1A; formation of extracellular globular aggregates; decreases cell growth; reduces interaction with ELN; abolishes secretion; increases homodimerization; dbSNP:rs80338766 | |
VAR_017153 | 227 | S>P | in ARCL1A; decreases expression; produces protein misfolding; abolishes secretion; reduces interaction with ELN; increases homodimerization; impairs elastic fiber development; dbSNP:rs28939370 | |
VAR_072393 | 267 | G>S | in ARMD3, ARCL1A and CMT1H; produces protein misolding; decreases secretion; no effect on homodimerization; dbSNP:rs149396611 |
Macular degeneration, age-related, 3 (ARMD3)
- Note
- DescriptionA form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.
- See alsoMIM:608895
Natural variants in ARMD3
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_019814 | 60 | V>L | in ARMD3; no effect on secretion; no effect on homodimerization; dbSNP:rs121434299 | |
VAR_019815 | 71 | R>Q | in ARMD3; no effect on secretion; no effect on homodimerization; dbSNP:rs121434300 | |
VAR_019816 | 87 | P>S | in ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca2+; dbSNP:rs121434301 | |
VAR_072389 | 124 | Q>P | in ARMD3; almost abolishes secretion; no effect on homodimerization | |
VAR_019817 | 169 | I>T | in ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca2+; no effect on protein folding; dbSNP:rs28939072 | |
VAR_072393 | 267 | G>S | in ARMD3, ARCL1A and CMT1H; produces protein misolding; decreases secretion; no effect on homodimerization; dbSNP:rs149396611 | |
VAR_019818 | 351 | R>W | in ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca2+; dbSNP:rs28939073 | |
VAR_019819 | 363 | A>T | in ARMD3; no effect on secretion; dbSNP:rs121434302 | |
VAR_019820 | 412 | G>E | in ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca2+; dbSNP:rs121434303 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_076289 | 48 | in CMT1H; dbSNP:rs141200859 | |||
Sequence: T → I | ||||||
Natural variant | VAR_019814 | 60 | in ARMD3; no effect on secretion; no effect on homodimerization; dbSNP:rs121434299 | |||
Sequence: V → L | ||||||
Natural variant | VAR_019815 | 71 | in ARMD3; no effect on secretion; no effect on homodimerization; dbSNP:rs121434300 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_019816 | 87 | in ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca2+; dbSNP:rs121434301 | |||
Sequence: P → S | ||||||
Natural variant | VAR_076290 | 90 | in CMT1H; dbSNP:rs144288844 | |||
Sequence: G → S | ||||||
Natural variant | VAR_072389 | 124 | in ARMD3; almost abolishes secretion; no effect on homodimerization | |||
Sequence: Q → P | ||||||
Natural variant | VAR_072390 | 126 | no effect on secretion; slightly increases homodimerization in absence of Ca2+; dbSNP:rs61734479 | |||
Sequence: V → M | ||||||
Natural variant | VAR_019817 | 169 | in ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca2+; no effect on protein folding; dbSNP:rs28939072 | |||
Sequence: I → T | ||||||
Natural variant | VAR_072391 | 202 | slightly increases homodimerization in absence of Ca2+; no effect on protein folding; no effect on secretion; dbSNP:rs80338765 | |||
Sequence: G → R | ||||||
Natural variant | VAR_072392 | 217 | in ARCL1A; formation of extracellular globular aggregates; decreases cell growth; reduces interaction with ELN; abolishes secretion; increases homodimerization; dbSNP:rs80338766 | |||
Sequence: C → R | ||||||
Natural variant | VAR_017153 | 227 | in ARCL1A; decreases expression; produces protein misfolding; abolishes secretion; reduces interaction with ELN; increases homodimerization; impairs elastic fiber development; dbSNP:rs28939370 | |||
Sequence: S → P | ||||||
Natural variant | VAR_072393 | 267 | in ARMD3, ARCL1A and CMT1H; produces protein misolding; decreases secretion; no effect on homodimerization; dbSNP:rs149396611 | |||
Sequence: G → S | ||||||
Natural variant | VAR_072394 | 301 | found in a patient with autosomal recessive cutis laxa also carrying a mutation in ELN; uncertain significance; dbSNP:rs377360782 | |||
Sequence: L → M | ||||||
Natural variant | VAR_019818 | 351 | in ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca2+; dbSNP:rs28939073 | |||
Sequence: R → W | ||||||
Natural variant | VAR_019819 | 363 | in ARMD3; no effect on secretion; dbSNP:rs121434302 | |||
Sequence: A → T | ||||||
Natural variant | VAR_026986 | 364 | in dbSNP:rs1802492 | |||
Sequence: D → Y | ||||||
Natural variant | VAR_076291 | 373 | in CMT1H; dbSNP:rs864309526 | |||
Sequence: R → C | ||||||
Natural variant | VAR_019820 | 412 | in ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca2+; dbSNP:rs121434303 | |||
Sequence: G → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 467 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 signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MPGIKRILTVTILALCLPSPGNA | ||||||
Chain | PRO_0000007577 | 24-448 | Fibulin-5 | |||
Sequence: QAQCTNGFDLDRQSGQCLDIDECRTIPEACRGDMMCVNQNGGYLCIPRTNPVYRGPYSNPYSTPYSGPYPAAAPPLSAPNYPTISRPLICRFGYQMDESNQCVDVDECATDSHQCNPTQICINTEGGYTCSCTDGYWLLEGQCLDIDECRYGYCQQLCANVPGSYSCTCNPGFTLNEDGRSCQDVNECATENPCVQTCVNTYGSFICRCDPGYELEEDGVHCSDMDECSFSEFLCQHECVNQPGTYFCSCPPGYILLDDNRSCQDINECEHRNHTCNLQQTCYNLQGGFKCIDPIRCEEPYLRISDNRCMCPAENPGCRDQPFTILYRDMDVVSGRSVPADIFQMQATTRYPGAYYIFQIKSGNEGREFYMRQTGPISATLVMTRPIKGPREIQLDLEMITVNTVINFRGSSVIRLRIYVSQYPF | ||||||
Disulfide bond | 46↔59 | |||||
Sequence: CRTIPEACRGDMMC | ||||||
Disulfide bond | 53↔68 | |||||
Sequence: CRGDMMCVNQNGGYLC | ||||||
Disulfide bond | 131↔144 | |||||
Sequence: CATDSHQCNPTQIC | ||||||
Disulfide bond | 138↔153 | |||||
Sequence: CNPTQICINTEGGYTC | ||||||
Disulfide bond | 155↔166 | |||||
Sequence: CTDGYWLLEGQC | ||||||
Disulfide bond | 172↔181 | |||||
Sequence: CRYGYCQQLC | ||||||
Disulfide bond | 177↔190 | |||||
Sequence: CQQLCANVPGSYSC | ||||||
Disulfide bond | 192↔205 | |||||
Sequence: CNPGFTLNEDGRSC | ||||||
Disulfide bond | 211↔221 | |||||
Sequence: CATENPCVQTC | ||||||
Disulfide bond | 217↔230 | |||||
Sequence: CVQTCVNTYGSFIC | ||||||
Disulfide bond | 232↔245 | |||||
Sequence: CDPGYELEEDGVHC | ||||||
Disulfide bond | 251↔262 | |||||
Sequence: CSFSEFLCQHEC | ||||||
Disulfide bond | 258↔271 | |||||
Sequence: CQHECVNQPGTYFC | ||||||
Disulfide bond | 273↔286 | |||||
Sequence: CPPGYILLDDNRSC | ||||||
Glycosylation | 283 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 292↔305 | |||||
Sequence: CEHRNHTCNLQQTC | ||||||
Glycosylation | 296 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 299↔314 | |||||
Sequence: CNLQQTCYNLQGGFKC | ||||||
Disulfide bond | 320↔332 | |||||
Sequence: CEEPYLRISDNRC |
Post-translational modification
N-glycosylated.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Expressed in skin fibroblasts (at protein level) (PubMed:17035250).
Expressed predominantly in heart, ovary, and colon but also in kidney, pancreas, testis, lung and placenta. Not detectable in brain, liver, thymus, prostate, or peripheral blood leukocytes (PubMed:10428823).
Expressed predominantly in heart, ovary, and colon but also in kidney, pancreas, testis, lung and placenta. Not detectable in brain, liver, thymus, prostate, or peripheral blood leukocytes (PubMed:10428823).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer (PubMed:20007835).
Monomer (PubMed:15790312, PubMed:19617354), homodimerizes in presence of Ca2+ (PubMed:19617354).
Interacts with ELN (PubMed:15790312, PubMed:17035250).
Interacts (via N-terminus) with the integrins ITGAV/ITGB3, ITGAV/ITGB5 and ITGA9/ITGB1 (By similarity).
Interacts with FBN1 (via N-terminal domain). Forms a ternary complex with ELN and FBN1 (PubMed:17255108).
Interacts with EFEMP2 with moderate affinity (PubMed:19570982).
Interacts with LOXL1 (By similarity).
Monomer (PubMed:15790312, PubMed:19617354), homodimerizes in presence of Ca2+ (PubMed:19617354).
Interacts with ELN (PubMed:15790312, PubMed:17035250).
Interacts (via N-terminus) with the integrins ITGAV/ITGB3, ITGAV/ITGB5 and ITGA9/ITGB1 (By similarity).
Interacts with FBN1 (via N-terminal domain). Forms a ternary complex with ELN and FBN1 (PubMed:17255108).
Interacts with EFEMP2 with moderate affinity (PubMed:19570982).
Interacts with LOXL1 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9UBX5 | EFEMP2 O95967 | 3 | EBI-947897, EBI-743414 | |
BINARY | Q9UBX5 | ELN P15502 | 3 | EBI-947897, EBI-1222108 | |
BINARY | Q9UBX5 | FBN1 P35555 | 3 | EBI-947897, EBI-2505934 | |
BINARY | Q9UBX5 | FGFR3 P22607 | 3 | EBI-947897, EBI-348399 | |
BINARY | Q9UBX5 | GRN P28799 | 3 | EBI-947897, EBI-747754 | |
BINARY | Q9UBX5 | LOX P28300 | 2 | EBI-947897, EBI-3893481 | |
BINARY | Q9UBX5 | LTBP2 Q14767 | 2 | EBI-947897, EBI-1546118 | |
BINARY | Q9UBX5 | MEOX2 P50222 | 3 | EBI-947897, EBI-748397 | |
BINARY | Q9UBX5 | NUFIP2 Q7Z417 | 5 | EBI-947897, EBI-1210753 | |
BINARY | Q9UBX5 | OTX1 P32242 | 3 | EBI-947897, EBI-740446 | |
BINARY | Q9UBX5 | SPRED1 Q7Z699 | 3 | EBI-947897, EBI-5235340 | |
BINARY | Q9UBX5 | TRIP13 Q15645 | 3 | EBI-947897, EBI-358993 | |
BINARY | Q9UBX5 | WFS1 O76024 | 3 | EBI-947897, EBI-720609 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 42-82 | EGF-like 1; calcium-binding | ||||
Sequence: DIDECRTIPEACRGDMMCVNQNGGYLCIPRTNPVYRGPYSN | ||||||
Motif | 54-56 | Cell attachment site | ||||
Sequence: RGD | ||||||
Domain | 127-167 | EGF-like 2; calcium-binding | ||||
Sequence: DVDECATDSHQCNPTQICINTEGGYTCSCTDGYWLLEGQCL | ||||||
Domain | 168-206 | EGF-like 3; calcium-binding | ||||
Sequence: DIDECRYGYCQQLCANVPGSYSCTCNPGFTLNEDGRSCQ | ||||||
Domain | 207-246 | EGF-like 4; calcium-binding | ||||
Sequence: DVNECATENPCVQTCVNTYGSFICRCDPGYELEEDGVHCS | ||||||
Region | 245-448 | Interaction with LOXL1 | ||||
Sequence: CSDMDECSFSEFLCQHECVNQPGTYFCSCPPGYILLDDNRSCQDINECEHRNHTCNLQQTCYNLQGGFKCIDPIRCEEPYLRISDNRCMCPAENPGCRDQPFTILYRDMDVVSGRSVPADIFQMQATTRYPGAYYIFQIKSGNEGREFYMRQTGPISATLVMTRPIKGPREIQLDLEMITVNTVINFRGSSVIRLRIYVSQYPF | ||||||
Domain | 247-287 | EGF-like 5; calcium-binding | ||||
Sequence: DMDECSFSEFLCQHECVNQPGTYFCSCPPGYILLDDNRSCQ | ||||||
Domain | 288-333 | EGF-like 6; calcium-binding | ||||
Sequence: DINECEHRNHTCNLQQTCYNLQGGFKCIDPIRCEEPYLRISDNRCM |
Sequence similarities
Belongs to the fibulin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length448
- Mass (Da)50,180
- Last updated2000-05-01 v1
- Checksum19FCA51FDA328003
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
G3V4U0 | G3V4U0_HUMAN | FBLN5 | 465 | ||
G3V3Y2 | G3V3Y2_HUMAN | FBLN5 | 91 | ||
G3V2P8 | G3V2P8_HUMAN | FBLN5 | 392 | ||
G3V329 | G3V329_HUMAN | FBLN5 | 44 | ||
A0A9L9PY85 | A0A9L9PY85_HUMAN | FBLN5 | 506 | ||
A0A9L9PXD9 | A0A9L9PXD9_HUMAN | FBLN5 | 464 | ||
A0A9L9PX66 | A0A9L9PX66_HUMAN | FBLN5 | 44 | ||
G3XA98 | G3XA98_HUMAN | FBLN5 | 489 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 69-70 | in Ref. 3; AAC62107 | ||||
Sequence: IP → HS | ||||||
Sequence conflict | 147-148 | in Ref. 3; AAC62107 | ||||
Sequence: TE → MK | ||||||
Sequence conflict | 228 | in Ref. 4; AAQ89257 | ||||
Sequence: F → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ133490 EMBL· GenBank· DDBJ | CAB38568.1 EMBL· GenBank· DDBJ | mRNA | ||
AF112152 EMBL· GenBank· DDBJ | AAD41768.1 EMBL· GenBank· DDBJ | mRNA | ||
AF093118 EMBL· GenBank· DDBJ | AAC62107.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358898 EMBL· GenBank· DDBJ | AAQ89257.1 EMBL· GenBank· DDBJ | mRNA | ||
CR457140 EMBL· GenBank· DDBJ | CAG33421.1 EMBL· GenBank· DDBJ | mRNA | ||
AK075147 EMBL· GenBank· DDBJ | BAG52073.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471061 EMBL· GenBank· DDBJ | EAW81466.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC022280 EMBL· GenBank· DDBJ | AAH22280.1 EMBL· GenBank· DDBJ | mRNA |