Q02388 · CO7A1_HUMAN
- ProteinCollagen alpha-1(VII) chain
- GeneCOL7A1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2944 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 2886-2887 | Reactive bond | ||||
Sequence: TA |
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 | basement membrane | |
Cellular Component | collagen type VII trimer | |
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | COPII-coated ER to Golgi transport vesicle | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | endoplasmic reticulum-Golgi intermediate compartment membrane | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Molecular Function | extracellular matrix structural constituent conferring tensile strength | |
Molecular Function | serine-type endopeptidase inhibitor activity | |
Biological Process | cell adhesion | |
Biological Process | endodermal cell differentiation | |
Biological Process | epidermis development | |
Biological Process | extracellular matrix organization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCollagen alpha-1(VII) chain
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ02388
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Epidermolysis bullosa dystrophica, autosomal dominant (DDEB)
- Note
- DescriptionA group of autosomal dominant blistering skin diseases characterized by tissue separation which occurs below the dermal-epidermal basement membrane at the level of the anchoring fibrils. Various clinical types with different severity are recognized, ranging from severe mutilating forms to mild forms with limited and localized scarring, and less frequent extracutaneous manifestations.
- See alsoMIM:131750
Natural variants in DDEB
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_011162 | 1522 | G>E | in DDEB; dbSNP:rs387906605 | |
VAR_001812 | 1557 | G>R | in DDEB | |
VAR_011167 | 1776 | G>R | in DDEB | |
VAR_001815 | 2003 | G>R | in DDEB; dbSNP:rs121912832 | |
VAR_011170 | 2006 | G>A | in DDEB | |
VAR_011171 | 2006 | G>D | in DDEB; interferes with collagen VII folding and secretion; dbSNP:rs121912842 | |
VAR_011174 | 2015 | G>E | in DDEB; interferes with collagen VII folding and secretion; dbSNP:rs121912843 | |
VAR_011175 | 2028 | G>A | in DDEB | |
VAR_011176 | 2028 | G>R | in DDEB and EBP; dbSNP:rs762162799 | |
VAR_001818 | 2034 | G>R | in DDEB and EBDSC; interferes with collagen VII folding and secretion; dbSNP:rs121912844 | |
VAR_011178 | 2034 | G>W | in DDEB | |
VAR_011179 | 2037 | G>E | in DDEB; dbSNP:rs121912846 | |
VAR_011180 | 2040 | G>D | in DDEB | |
VAR_001819 | 2040 | G>S | in DDEB; dbSNP:rs121912829 | |
VAR_011181 | 2040 | G>V | in DDEB | |
VAR_001820 | 2043 | G>R | in DDEB; dbSNP:rs121912836 | |
VAR_011182 | 2043 | G>W | in DDEB; localized type; dbSNP:rs121912836 | |
VAR_011183 | 2046 | G>V | in DDEB | |
VAR_001822 | 2055 | G>E | in DDEB; dbSNP:rs1553854678 | |
VAR_011184 | 2064 | G>R | in DDEB; dbSNP:rs866061439 | |
VAR_064997 | 2070 | G>R | in DDEB | |
VAR_001826 | 2076 | G>D | in DDEB; also in recessive forms; dbSNP:rs121912850 | |
VAR_001827 | 2079 | G>E | in DDEB | |
VAR_011185 | 2079 | G>R | in DDEB | |
VAR_011188 | 2207 | G>R | in DDEB | |
VAR_011197 | 2713 | G>D | in DDEB; dbSNP:rs369591910 | |
VAR_011201 | 2791 | R>W | in DDEB; dbSNP:rs142566193 |
Epidermolysis bullosa dystrophica, autosomal recessive (RDEB)
- Note
- DescriptionA group of autosomal recessive blistering skin diseases characterized by tissue separation which occurs below the dermal-epidermal basement membrane at the level of the anchoring fibrils. Various clinical types with different severity are recognized, ranging from severe mutilating forms, such as epidermolysis bullosa dystrophica Hallopeau-Siemens type, to mild forms with limited localized scarring and less frequent extracutaneous manifestations. Mild forms include epidermolysis bullosa mitis and epidermolysis bullosa localisata.
- See alsoMIM:226600
Natural variants in RDEB
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_001809 | 142 | K>R | in RDEB; uncertain significance; may affect exon 3 splicing; dbSNP:rs121912856 | |
VAR_011160 | 1347 | G>R | in RDEB; localized type; mild; dbSNP:rs121912833 | |
VAR_011163 | 1604 | G>R | in RDEB; dbSNP:rs1560234201 | |
VAR_011164 | 1652 | G>R | in RDEB; mitis type; dbSNP:rs1439299333 | |
VAR_011165 | 1703 | G>E | in RDEB; dbSNP:rs770304825 | |
VAR_011166 | 1772 | R>W | in RDEB; dbSNP:rs1032335328 | |
VAR_001813 | 1782 | G>R | in RDEB; mitis type; dbSNP:rs374718902 | |
VAR_011169 | 1812 | G>R | in RDEB | |
VAR_064994 | 1845 | G>R | in RDEB | |
VAR_064995 | 1981 | K>R | in RDEB; mild form | |
VAR_001814 | 1982 | G>W | in RDEB | |
VAR_011172 | 2008 | R>C | in RDEB; dbSNP:rs1055680335 | |
VAR_001816 | 2008 | R>G | in RDEB; dbSNP:rs1055680335 | |
VAR_011173 | 2009 | G>R | in RDEB | |
VAR_001817 | 2025 | G>A | in RDEB; mitis type; dbSNP:rs766931219 | |
VAR_011177 | 2031 | G>S | in RDEB; severe phenotype; dbSNP:rs121912838 | |
VAR_001821 | 2049 | G>E | in RDEB | |
VAR_001823 | 2063 | R>W | in RDEB; dbSNP:rs121912849 | |
VAR_064996 | 2069 | R>C | in RDEB; dbSNP:rs121912855 | |
VAR_001825 | 2073 | G>D | in RDEB; mitis type | |
VAR_011186 | 2132 | G>D | in RDEB; dbSNP:rs755669902 | |
VAR_011187 | 2192 | G>S | in RDEB | |
VAR_064998 | 2221 | G>A | in RDEB | |
VAR_011190 | 2263 | G>V | in RDEB | |
VAR_011191 | 2287 | G>R | in RDEB; also found in isolated toenail dystrophy; dbSNP:rs121912839 | |
VAR_064999 | 2296 | G>E | in RDEB | |
VAR_011192 | 2316 | G>R | in RDEB | |
VAR_011194 | 2366 | G>S | in RDEB; mitis type; dbSNP:rs1560204600 | |
VAR_065000 | 2557 | G>R | in RDEB | |
VAR_001830 | 2569 | G>R | in RDEB; severe and mitis type | |
VAR_001831 | 2575 | G>R | in RDEB; dbSNP:rs760891216 | |
VAR_065001 | 2622 | R>W | in RDEB; dbSNP:rs139318843 | |
VAR_001833 | 2653 | G>R | in RDEB; mitis type; dbSNP:rs121912851 | |
VAR_001834 | 2671 | G>V | in RDEB | |
VAR_011196 | 2674 | G>D | in RDEB | |
VAR_001835 | 2674 | G>R | in RDEB; mitis type | |
VAR_011199 | 2740 | G>A | in RDEB | |
VAR_001836 | 2749 | G>R | in RDEB; dbSNP:rs121912853 | |
VAR_011200 | 2775 | G>S | in RDEB; mitis type; dbSNP:rs1333259313 | |
VAR_001837 | 2798 | M>K | in RDEB; dbSNP:rs121912828 |
Transient bullous dermolysis of the newborn (TBDN)
- Note
- DescriptionTBDN is a neonatal form of dystrophic epidermolysis bullosa characterized by sub-epidermal blisters, reduced or abnormal anchoring fibrils at the dermo-epidermal junction, and electron-dense inclusions in keratinocytes. TBDN heals spontaneously or strongly improves within the first months and years of life.
- See alsoMIM:131705
Natural variants in TBDN
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_011161 | 1519 | G>D | in TBDN; dbSNP:rs121912835 | |
VAR_011189 | 2251 | G>E | in TBDN; also found in isolated toenail dystrophy; dbSNP:rs121912834 |
Epidermolysis bullosa dystrophica, pretibial type (PR-DEB)
- Note
- DescriptionA form of dystrophic epidermolysis bullosa characterized by pretibial blisters that develop into prurigo-like hyperkeratotic lesions. It predominantly affects the pretibial areas, sparing the knees and other parts of the skin. Other clinical features include nail dystrophy, albopapuloid skin lesions, and hypertrophic scars without pretibial predominance. The phenotype shows considerable interindividual variability. Inheritance is autosomal dominant.
- See alsoMIM:131850
Natural variants in PR-DEB
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_001832 | 2623 | G>C | in PR-DEB; dominant; dbSNP:rs121912831 |
Epidermolysis bullosa dystrophica, Bart type (B-DEB)
- Note
- DescriptionAn autosomal dominant form of dystrophic epidermolysis bullosa characterized by congenital localized absence of skin, skin fragility and deformity of nails.
- See alsoMIM:132000
Epidermolysis bullosa pruriginosa (EBP)
- Note
- DescriptionA distinct clinical subtype of epidermolysis bullosa dystrophica. It is characterized by skin fragility, blistering, scar formation, intense pruritus and excoriated prurigo nodules. Onset is in early childhood, but in some cases is delayed until the second or third decade of life. Inheritance can be autosomal dominant or recessive.
- See alsoMIM:604129
Natural variants in EBP
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_011168 | 1791 | G>E | in EBP; dbSNP:rs1575450640 | |
VAR_011176 | 2028 | G>R | in DDEB and EBP; dbSNP:rs762162799 | |
VAR_001828 | 2242 | G>R | in EBP; dbSNP:rs121912837 | |
VAR_011195 | 2369 | G>S | in EBP | |
VAR_011198 | 2713 | G>R | in EBP |
Nail disorder, non-syndromic congenital, 8 (NDNC8)
- Note
- DescriptionA nail disorder characterized by isolated toenail dystrophy. The nail changes are most severe in the great toes and consist of the nail plate being buried in the nail bed with a deformed and narrow free edge.
- See alsoMIM:607523
Natural variants in NDNC8
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_015519 | 1595 | G>R | in NDNC8; dbSNP:rs121912840 | |
VAR_015520 | 1815 | G>R | in NDNC8; dbSNP:rs121912841 |
Epidermolysis bullosa dystrophica, with subcorneal cleavage (EBDSC)
- Note
- DescriptionA bullous skin disorder with variable sized clefts just beneath the level of the stratum corneum. Clinical features include blisters, milia, atrophic scarring, nail dystrophy, and oral and conjunctival involvement, as seen in dystrophic epidermolysis bullosa.
- See alsoMIM:131750
Natural variants in EBDSC
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_001818 | 2034 | G>R | in DDEB and EBDSC; interferes with collagen VII folding and secretion; dbSNP:rs121912844 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_035740 | 119 | in a breast cancer sample; somatic mutation | |||
Sequence: T → P | ||||||
Natural variant | VAR_001809 | 142 | in RDEB; uncertain significance; may affect exon 3 splicing; dbSNP:rs121912856 | |||
Sequence: K → R | ||||||
Natural variant | VAR_001810 | 595 | in dbSNP:rs2228561 | |||
Sequence: P → L | ||||||
Natural variant | VAR_048766 | 1120 | in dbSNP:rs2228563 | |||
Sequence: R → K | ||||||
Natural variant | VAR_001811 | 1277 | in dbSNP:rs35761247 | |||
Sequence: P → L | ||||||
Natural variant | VAR_011160 | 1347 | in RDEB; localized type; mild; dbSNP:rs121912833 | |||
Sequence: G → R | ||||||
Natural variant | VAR_035741 | 1364 | in a breast cancer sample; somatic mutation | |||
Sequence: P → T | ||||||
Natural variant | VAR_035742 | 1366 | in a breast cancer sample; somatic mutation; dbSNP:rs147089666 | |||
Sequence: R → W | ||||||
Natural variant | VAR_011161 | 1519 | in TBDN; dbSNP:rs121912835 | |||
Sequence: G → D | ||||||
Natural variant | VAR_011162 | 1522 | in DDEB; dbSNP:rs387906605 | |||
Sequence: G → E | ||||||
Natural variant | VAR_001812 | 1557 | in DDEB | |||
Sequence: G → R | ||||||
Natural variant | VAR_015519 | 1595 | in NDNC8; dbSNP:rs121912840 | |||
Sequence: G → R | ||||||
Natural variant | VAR_011163 | 1604 | in RDEB; dbSNP:rs1560234201 | |||
Sequence: G → R | ||||||
Natural variant | VAR_011164 | 1652 | in RDEB; mitis type; dbSNP:rs1439299333 | |||
Sequence: G → R | ||||||
Natural variant | VAR_011165 | 1703 | in RDEB; dbSNP:rs770304825 | |||
Sequence: G → E | ||||||
Natural variant | VAR_011166 | 1772 | in RDEB; dbSNP:rs1032335328 | |||
Sequence: R → W | ||||||
Natural variant | VAR_011167 | 1776 | in DDEB | |||
Sequence: G → R | ||||||
Natural variant | VAR_001813 | 1782 | in RDEB; mitis type; dbSNP:rs374718902 | |||
Sequence: G → R | ||||||
Natural variant | VAR_011168 | 1791 | in EBP; dbSNP:rs1575450640 | |||
Sequence: G → E | ||||||
Natural variant | VAR_011169 | 1812 | in RDEB | |||
Sequence: G → R | ||||||
Natural variant | VAR_015520 | 1815 | in NDNC8; dbSNP:rs121912841 | |||
Sequence: G → R | ||||||
Natural variant | VAR_064994 | 1845 | in RDEB | |||
Sequence: G → R | ||||||
Natural variant | VAR_064995 | 1981 | in RDEB; mild form | |||
Sequence: K → R | ||||||
Natural variant | VAR_001814 | 1982 | in RDEB | |||
Sequence: G → W | ||||||
Natural variant | VAR_001815 | 2003 | in DDEB; dbSNP:rs121912832 | |||
Sequence: G → R | ||||||
Natural variant | VAR_011170 | 2006 | in DDEB | |||
Sequence: G → A | ||||||
Natural variant | VAR_011171 | 2006 | in DDEB; interferes with collagen VII folding and secretion; dbSNP:rs121912842 | |||
Sequence: G → D | ||||||
Natural variant | VAR_011172 | 2008 | in RDEB; dbSNP:rs1055680335 | |||
Sequence: R → C | ||||||
Natural variant | VAR_001816 | 2008 | in RDEB; dbSNP:rs1055680335 | |||
Sequence: R → G | ||||||
Natural variant | VAR_011173 | 2009 | in RDEB | |||
Sequence: G → R | ||||||
Natural variant | VAR_011174 | 2015 | in DDEB; interferes with collagen VII folding and secretion; dbSNP:rs121912843 | |||
Sequence: G → E | ||||||
Natural variant | VAR_001817 | 2025 | in RDEB; mitis type; dbSNP:rs766931219 | |||
Sequence: G → A | ||||||
Natural variant | VAR_011175 | 2028 | in DDEB | |||
Sequence: G → A | ||||||
Natural variant | VAR_011176 | 2028 | in DDEB and EBP; dbSNP:rs762162799 | |||
Sequence: G → R | ||||||
Natural variant | VAR_011177 | 2031 | in RDEB; severe phenotype; dbSNP:rs121912838 | |||
Sequence: G → S | ||||||
Natural variant | VAR_001818 | 2034 | in DDEB and EBDSC; interferes with collagen VII folding and secretion; dbSNP:rs121912844 | |||
Sequence: G → R | ||||||
Natural variant | VAR_011178 | 2034 | in DDEB | |||
Sequence: G → W | ||||||
Natural variant | VAR_011179 | 2037 | in DDEB; dbSNP:rs121912846 | |||
Sequence: G → E | ||||||
Natural variant | VAR_011180 | 2040 | in DDEB | |||
Sequence: G → D | ||||||
Natural variant | VAR_001819 | 2040 | in DDEB; dbSNP:rs121912829 | |||
Sequence: G → S | ||||||
Natural variant | VAR_011181 | 2040 | in DDEB | |||
Sequence: G → V | ||||||
Natural variant | VAR_001820 | 2043 | in DDEB; dbSNP:rs121912836 | |||
Sequence: G → R | ||||||
Natural variant | VAR_011182 | 2043 | in DDEB; localized type; dbSNP:rs121912836 | |||
Sequence: G → W | ||||||
Natural variant | VAR_011183 | 2046 | in DDEB | |||
Sequence: G → V | ||||||
Natural variant | VAR_001821 | 2049 | in RDEB | |||
Sequence: G → E | ||||||
Natural variant | VAR_001822 | 2055 | in DDEB; dbSNP:rs1553854678 | |||
Sequence: G → E | ||||||
Natural variant | VAR_001823 | 2063 | in RDEB; dbSNP:rs121912849 | |||
Sequence: R → W | ||||||
Natural variant | VAR_011184 | 2064 | in DDEB; dbSNP:rs866061439 | |||
Sequence: G → R | ||||||
Natural variant | VAR_064996 | 2069 | in RDEB; dbSNP:rs121912855 | |||
Sequence: R → C | ||||||
Natural variant | VAR_064997 | 2070 | in DDEB | |||
Sequence: G → R | ||||||
Natural variant | VAR_001825 | 2073 | in RDEB; mitis type | |||
Sequence: G → D | ||||||
Natural variant | VAR_001826 | 2076 | in DDEB; also in recessive forms; dbSNP:rs121912850 | |||
Sequence: G → D | ||||||
Natural variant | VAR_001827 | 2079 | in DDEB | |||
Sequence: G → E | ||||||
Natural variant | VAR_011185 | 2079 | in DDEB | |||
Sequence: G → R | ||||||
Natural variant | VAR_011186 | 2132 | in RDEB; dbSNP:rs755669902 | |||
Sequence: G → D | ||||||
Natural variant | VAR_011187 | 2192 | in RDEB | |||
Sequence: G → S | ||||||
Natural variant | VAR_011188 | 2207 | in DDEB | |||
Sequence: G → R | ||||||
Natural variant | VAR_064998 | 2221 | in RDEB | |||
Sequence: G → A | ||||||
Natural variant | VAR_001828 | 2242 | in EBP; dbSNP:rs121912837 | |||
Sequence: G → R | ||||||
Natural variant | VAR_011189 | 2251 | in TBDN; also found in isolated toenail dystrophy; dbSNP:rs121912834 | |||
Sequence: G → E | ||||||
Natural variant | VAR_011190 | 2263 | in RDEB | |||
Sequence: G → V | ||||||
Natural variant | VAR_011191 | 2287 | in RDEB; also found in isolated toenail dystrophy; dbSNP:rs121912839 | |||
Sequence: G → R | ||||||
Natural variant | VAR_064999 | 2296 | in RDEB | |||
Sequence: G → E | ||||||
Natural variant | VAR_011192 | 2316 | in RDEB | |||
Sequence: G → R | ||||||
Natural variant | VAR_011193 | 2348 | in DDEB/RDEB; mild form | |||
Sequence: G → R | ||||||
Natural variant | VAR_001829 | 2351 | in a patient with dystrophic epidermolysis bullosa; mitis type; dbSNP:rs1800013 | |||
Sequence: G → R | ||||||
Natural variant | VAR_011194 | 2366 | in RDEB; mitis type; dbSNP:rs1560204600 | |||
Sequence: G → S | ||||||
Natural variant | VAR_011195 | 2369 | in EBP | |||
Sequence: G → S | ||||||
Natural variant | VAR_033786 | 2429 | in dbSNP:rs2229822 | |||
Sequence: P → L | ||||||
Natural variant | VAR_065000 | 2557 | in RDEB | |||
Sequence: G → R | ||||||
Natural variant | VAR_001830 | 2569 | in RDEB; severe and mitis type | |||
Sequence: G → R | ||||||
Natural variant | VAR_001831 | 2575 | in RDEB; dbSNP:rs760891216 | |||
Sequence: G → R | ||||||
Natural variant | VAR_065001 | 2622 | in RDEB; dbSNP:rs139318843 | |||
Sequence: R → W | ||||||
Natural variant | VAR_001832 | 2623 | in PR-DEB; dominant; dbSNP:rs121912831 | |||
Sequence: G → C | ||||||
Natural variant | VAR_001833 | 2653 | in RDEB; mitis type; dbSNP:rs121912851 | |||
Sequence: G → R | ||||||
Natural variant | VAR_001834 | 2671 | in RDEB | |||
Sequence: G → V | ||||||
Natural variant | VAR_011196 | 2674 | in RDEB | |||
Sequence: G → D | ||||||
Natural variant | VAR_001835 | 2674 | in RDEB; mitis type | |||
Sequence: G → R | ||||||
Natural variant | VAR_011197 | 2713 | in DDEB; dbSNP:rs369591910 | |||
Sequence: G → D | ||||||
Natural variant | VAR_011198 | 2713 | in EBP | |||
Sequence: G → R | ||||||
Natural variant | VAR_011199 | 2740 | in RDEB | |||
Sequence: G → A | ||||||
Natural variant | VAR_001836 | 2749 | in RDEB; dbSNP:rs121912853 | |||
Sequence: G → R | ||||||
Natural variant | VAR_011200 | 2775 | in RDEB; mitis type; dbSNP:rs1333259313 | |||
Sequence: G → S | ||||||
Natural variant | VAR_011201 | 2791 | in DDEB; dbSNP:rs142566193 | |||
Sequence: R → W | ||||||
Natural variant | VAR_001837 | 2798 | in RDEB; dbSNP:rs121912828 | |||
Sequence: M → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3,739 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, glycosylation, modified residue (large scale data), modified residue, disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-16 | UniProt | |||||
Sequence: MTLRLLVAALCAGILA | |||||||
Chain | PRO_0000005761 | 17-2944 | UniProt | Collagen alpha-1(VII) chain | |||
Sequence: EAPRVRAQHRERVTCTRLYAADIVFLLDGSSSIGRSNFREVRSFLEGLVLPFSGAASAQGVRFATVQYSDDPRTEFGLDALGSGGDVIRAIRELSYKGGNTRTGAAILHVADHVFLPQLARPGVPKVCILITDGKSQDLVDTAAQRLKGQGVKLFAVGIKNADPEELKRVASQPTSDFFFFVNDFSILRTLLPLVSRRVCTTAGGVPVTRPPDDSTSAPRDLVLSEPSSQSLRVQWTAASGPVTGYKVQYTPLTGLGQPLPSERQEVNVPAGETSVRLRGLRPLTEYQVTVIALYANSIGEAVSGTARTTALEGPELTIQNTTAHSLLVAWRSVPGATGYRVTWRVLSGGPTQQQELGPGQGSVLLRDLEPGTDYEVTVSTLFGRSVGPATSLMARTDASVEQTLRPVILGPTSILLSWNLVPEARGYRLEWRRETGLEPPQKVVLPSDVTRYQLDGLQPGTEYRLTLYTLLEGHEVATPATVVPTGPELPVSPVTDLQATELPGQRVRVSWSPVPGATQYRIIVRSTQGVERTLVLPGSQTAFDLDDVQAGLSYTVRVSARVGPREGSASVLTVRREPETPLAVPGLRVVVSDATRVRVAWGPVPGASGFRISWSTGSGPESSQTLPPDSTATDITGLQPGTTYQVAVSVLRGREEGPAAVIVARTDPLGPVRTVHVTQASSSSVTITWTRVPGATGYRVSWHSAHGPEKSQLVSGEATVAELDGLEPDTEYTVHVRAHVAGVDGPPASVVVRTAPEPVGRVSRLQILNASSDVLRITWVGVTGATAYRLAWGRSEGGPMRHQILPGNTDSAEIRGLEGGVSYSVRVTALVGDREGTPVSIVVTTPPEAPPALGTLHVVQRGEHSLRLRWEPVPRAQGFLLHWQPEGGQEQSRVLGPELSSYHLDGLEPATQYRVRLSVLGPAGEGPSAEVTARTESPRVPSIELRVVDTSIDSVTLAWTPVSRASSYILSWRPLRGPGQEVPGSPQTLPGISSSQRVTGLEPGVSYIFSLTPVLDGVRGPEASVTQTPVCPRGLADVVFLPHATQDNAHRAEATRRVLERLVLALGPLGPQAVQVGLLSYSHRPSPLFPLNGSHDLGIILQRIRDMPYMDPSGNNLGTAVVTAHRYMLAPDAPGRRQHVPGVMVLLVDEPLRGDIFSPIREAQASGLNVVMLGMAGADPEQLRRLAPGMDSVQTFFAVDDGPSLDQAVSGLATALCQASFTTQPRPEPCPVYCPKGQKGEPGEMGLRGQVGPPGDPGLPGRTGAPGPQGPPGSATAKGERGFPGADGRPGSPGRAGNPGTPGAPGLKGSPGLPGPRGDPGERGPRGPKGEPGAPGQVIGGEGPGLPGRKGDPGPSGPPGPRGPLGDPGPRGPPGLPGTAMKGDKGDRGERGPPGPGEGGIAPGEPGLPGLPGSPGPQGPVGPPGKKGEKGDSEDGAPGLPGQPGSPGEQGPRGPPGAIGPKGDRGFPGPLGEAGEKGERGPPGPAGSRGLPGVAGRPGAKGPEGPPGPTGRQGEKGEPGRPGDPAVVGPAVAGPKGEKGDVGPAGPRGATGVQGERGPPGLVLPGDPGPKGDPGDRGPIGLTGRAGPPGDSGPPGEKGDPGRPGPPGPVGPRGRDGEVGEKGDEGPPGDPGLPGKAGERGLRGAPGVRGPVGEKGDQGDPGEDGRNGSPGSSGPKGDRGEPGPPGPPGRLVDTGPGAREKGEPGDRGQEGPRGPKGDPGLPGAPGERGIEGFRGPPGPQGDPGVRGPAGEKGDRGPPGLDGRSGLDGKPGAAGPSGPNGAAGKAGDPGRDGLPGLRGEQGLPGPSGPPGLPGKPGEDGKPGLNGKNGEPGDPGEDGRKGEKGDSGASGREGRDGPKGERGAPGILGPQGPPGLPGPVGPPGQGFPGVPGGTGPKGDRGETGSKGEQGLPGERGLRGEPGSVPNVDRLLETAGIKASALREIVETWDESSGSFLPVPERRRGPKGDSGEQGPPGKEGPIGFPGERGLKGDRGDPGPQGPPGLALGERGPPGPSGLAGEPGKPGIPGLPGRAGGVGEAGRPGERGERGEKGERGEQGRDGPPGLPGTPGPPGPPGPKVSVDEPGPGLSGEQGPPGLKGAKGEPGSNGDQGPKGDRGVPGIKGDRGEPGPRGQDGNPGLPGERGMAGPEGKPGLQGPRGPPGPVGGHGDPGPPGAPGLAGPAGPQGPSGLKGEPGETGPPGRGLTGPTGAVGLPGPPGPSGLVGPQGSPGLPGQVGETGKPGAPGRDGASGKDGDRGSPGVPGSPGLPGPVGPKGEPGPTGAPGQAVVGLPGAKGEKGAPGGLAGDLVGEPGAKGDRGLPGPRGEKGEAGRAGEPGDPGEDGQKGAPGPKGFKGDPGVGVPGSPGPPGPPGVKGDLGLPGLPGAPGVVGFPGQTGPRGEMGQPGPSGERGLAGPPGREGIPGPLGPPGPPGSVGPPGASGLKGDKGDPGVGLPGPRGERGEPGIRGEDGRPGQEGPRGLTGPPGSRGERGEKGDVGSAGLKGDKGDSAVILGPPGPRGAKGDMGERGPRGLDGDKGPRGDNGDPGDKGSKGEPGDKGSAGLPGLRGLLGPQGQPGAAGIPGDPGSPGKDGVPGIRGEKGDVGFMGPRGLKGERGVKGACGLDGEKGDKGEAGPPGRPGLAGHKGEMGEPGVPGQSGAPGKEGLIGPKGDRGFDGQPGPKGDQGEKGERGTPGIGGFPGPSGNDGSAGPPGPPGSVGPRGPEGLQGQKGERGPPGERVVGAPGVPGAPGERGEQGRPGPAGPRGEKGEAALTEDDIRGFVRQEMSQHCACQGQFIASGSRPLPSYAADTAGSQLHAVPVLRVSHAEEEERVPPEDDEYSEYSEYSVEEYQDPEAPWDSDDPCSLPLDEGSCTAYTLRWYHRAVTGSTEACHPFVYGGCGGNANRFGTREACERRCPPRVVQSQGTGTAQD | |||||||
Glycosylation | 337 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 786 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 828 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 1109 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 2036 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2039 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2084 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2087 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2090 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2167 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2176 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2185 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2188 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue (large scale data) | 2600 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 2625 | UniProt | 5-hydroxylysine; alternate | ||||
Sequence: K | |||||||
Glycosylation | 2625 | UniProt | O-linked (Gal...) hydroxylysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 2631 | UniProt | 5-hydroxylysine; alternate | ||||
Sequence: K | |||||||
Glycosylation | 2631 | UniProt | O-linked (Gal...) hydroxylysine; alternate | ||||
Sequence: K | |||||||
Disulfide bond | 2634 | UniProt | Interchain | ||||
Sequence: C | |||||||
Modified residue | 2664 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2667 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Modified residue | 2673 | UniProt | 4-hydroxyproline | ||||
Sequence: P | |||||||
Disulfide bond | 2802 | UniProt | Interchain | ||||
Sequence: C | |||||||
Disulfide bond | 2804 | UniProt | Interchain | ||||
Sequence: C | |||||||
Disulfide bond | 2876↔2929 | UniProt | |||||
Sequence: CSLPLDEGSCTAYTLRWYHRAVTGSTEACHPFVYGGCGGNANRFGTREACERRC | |||||||
Disulfide bond | 2885↔2912 | UniProt | |||||
Sequence: CTAYTLRWYHRAVTGSTEACHPFVYGGC | |||||||
Disulfide bond | 2904↔2925 | UniProt | |||||
Sequence: CHPFVYGGCGGNANRFGTREAC |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q02388 | MIA3 Q5JRA6 | 2 | EBI-724237, EBI-2291868 |
Protein-protein interaction databases
Miscellaneous
Family & Domains
Features
Showing features for region, domain, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 17-1253 | Nonhelical region (NC1) | ||||
Sequence: EAPRVRAQHRERVTCTRLYAADIVFLLDGSSSIGRSNFREVRSFLEGLVLPFSGAASAQGVRFATVQYSDDPRTEFGLDALGSGGDVIRAIRELSYKGGNTRTGAAILHVADHVFLPQLARPGVPKVCILITDGKSQDLVDTAAQRLKGQGVKLFAVGIKNADPEELKRVASQPTSDFFFFVNDFSILRTLLPLVSRRVCTTAGGVPVTRPPDDSTSAPRDLVLSEPSSQSLRVQWTAASGPVTGYKVQYTPLTGLGQPLPSERQEVNVPAGETSVRLRGLRPLTEYQVTVIALYANSIGEAVSGTARTTALEGPELTIQNTTAHSLLVAWRSVPGATGYRVTWRVLSGGPTQQQELGPGQGSVLLRDLEPGTDYEVTVSTLFGRSVGPATSLMARTDASVEQTLRPVILGPTSILLSWNLVPEARGYRLEWRRETGLEPPQKVVLPSDVTRYQLDGLQPGTEYRLTLYTLLEGHEVATPATVVPTGPELPVSPVTDLQATELPGQRVRVSWSPVPGATQYRIIVRSTQGVERTLVLPGSQTAFDLDDVQAGLSYTVRVSARVGPREGSASVLTVRREPETPLAVPGLRVVVSDATRVRVAWGPVPGASGFRISWSTGSGPESSQTLPPDSTATDITGLQPGTTYQVAVSVLRGREEGPAAVIVARTDPLGPVRTVHVTQASSSSVTITWTRVPGATGYRVSWHSAHGPEKSQLVSGEATVAELDGLEPDTEYTVHVRAHVAGVDGPPASVVVRTAPEPVGRVSRLQILNASSDVLRITWVGVTGATAYRLAWGRSEGGPMRHQILPGNTDSAEIRGLEGGVSYSVRVTALVGDREGTPVSIVVTTPPEAPPALGTLHVVQRGEHSLRLRWEPVPRAQGFLLHWQPEGGQEQSRVLGPELSSYHLDGLEPATQYRVRLSVLGPAGEGPSAEVTARTESPRVPSIELRVVDTSIDSVTLAWTPVSRASSYILSWRPLRGPGQEVPGSPQTLPGISSSQRVTGLEPGVSYIFSLTPVLDGVRGPEASVTQTPVCPRGLADVVFLPHATQDNAHRAEATRRVLERLVLALGPLGPQAVQVGLLSYSHRPSPLFPLNGSHDLGIILQRIRDMPYMDPSGNNLGTAVVTAHRYMLAPDAPGRRQHVPGVMVLLVDEPLRGDIFSPIREAQASGLNVVMLGMAGADPEQLRRLAPGMDSVQTFFAVDDGPSLDQAVSGLATALCQASFTTQPRPEPCPVYCPK | ||||||
Domain | 38-211 | VWFA 1 | ||||
Sequence: DIVFLLDGSSSIGRSNFREVRSFLEGLVLPFSGAASAQGVRFATVQYSDDPRTEFGLDALGSGGDVIRAIRELSYKGGNTRTGAAILHVADHVFLPQLARPGVPKVCILITDGKSQDLVDTAAQRLKGQGVKLFAVGIKNADPEELKRVASQPTSDFFFFVNDFSILRTLLPLV | ||||||
Domain | 234-329 | Fibronectin type-III 1 | ||||
Sequence: APRDLVLSEPSSQSLRVQWTAASGPVTGYKVQYTPLTGLGQPLPSERQEVNVPAGETSVRLRGLRPLTEYQVTVIALYANSIGEAVSGTARTTALE | ||||||
Domain | 330-416 | Fibronectin type-III 2 | ||||
Sequence: GPELTIQNTTAHSLLVAWRSVPGATGYRVTWRVLSGGPTQQQELGPGQGSVLLRDLEPGTDYEVTVSTLFGRSVGPATSLMARTDAS | ||||||
Domain | 417-507 | Fibronectin type-III 3 | ||||
Sequence: VEQTLRPVILGPTSILLSWNLVPEARGYRLEWRRETGLEPPQKVVLPSDVTRYQLDGLQPGTEYRLTLYTLLEGHEVATPATVVPTGPELP | ||||||
Domain | 510-597 | Fibronectin type-III 4 | ||||
Sequence: PVTDLQATELPGQRVRVSWSPVPGATQYRIIVRSTQGVERTLVLPGSQTAFDLDDVQAGLSYTVRVSARVGPREGSASVLTVRREPET | ||||||
Domain | 600-687 | Fibronectin type-III 5 | ||||
Sequence: AVPGLRVVVSDATRVRVAWGPVPGASGFRISWSTGSGPESSQTLPPDSTATDITGLQPGTTYQVAVSVLRGREEGPAAVIVARTDPLG | ||||||
Region | 632-651 | Disordered | ||||
Sequence: STGSGPESSQTLPPDSTATD | ||||||
Domain | 688-775 | Fibronectin type-III 6 | ||||
Sequence: PVRTVHVTQASSSSVTITWTRVPGATGYRVSWHSAHGPEKSQLVSGEATVAELDGLEPDTEYTVHVRAHVAGVDGPPASVVVRTAPEP | ||||||
Domain | 778-866 | Fibronectin type-III 7 | ||||
Sequence: RVSRLQILNASSDVLRITWVGVTGATAYRLAWGRSEGGPMRHQILPGNTDSAEIRGLEGGVSYSVRVTALVGDREGTPVSIVVTTPPEA | ||||||
Domain | 869-957 | Fibronectin type-III 8 | ||||
Sequence: ALGTLHVVQRGEHSLRLRWEPVPRAQGFLLHWQPEGGQEQSRVLGPELSSYHLDGLEPATQYRVRLSVLGPAGEGPSAEVTARTESPRV | ||||||
Domain | 958-1051 | Fibronectin type-III 9 | ||||
Sequence: PSIELRVVDTSIDSVTLAWTPVSRASSYILSWRPLRGPGQEVPGSPQTLPGISSSQRVTGLEPGVSYIFSLTPVLDGVRGPEASVTQTPVCPRG | ||||||
Domain | 1054-1229 | VWFA 2 | ||||
Sequence: DVVFLPHATQDNAHRAEATRRVLERLVLALGPLGPQAVQVGLLSYSHRPSPLFPLNGSHDLGIILQRIRDMPYMDPSGNNLGTAVVTAHRYMLAPDAPGRRQHVPGVMVLLVDEPLRGDIFSPIREAQASGLNVVMLGMAGADPEQLRRLAPGMDSVQTFFAVDDGPSLDQAVSGL | ||||||
Motif | 1170-1172 | Cell attachment site | ||||
Sequence: RGD | ||||||
Region | 1239-1941 | Disordered | ||||
Sequence: TTQPRPEPCPVYCPKGQKGEPGEMGLRGQVGPPGDPGLPGRTGAPGPQGPPGSATAKGERGFPGADGRPGSPGRAGNPGTPGAPGLKGSPGLPGPRGDPGERGPRGPKGEPGAPGQVIGGEGPGLPGRKGDPGPSGPPGPRGPLGDPGPRGPPGLPGTAMKGDKGDRGERGPPGPGEGGIAPGEPGLPGLPGSPGPQGPVGPPGKKGEKGDSEDGAPGLPGQPGSPGEQGPRGPPGAIGPKGDRGFPGPLGEAGEKGERGPPGPAGSRGLPGVAGRPGAKGPEGPPGPTGRQGEKGEPGRPGDPAVVGPAVAGPKGEKGDVGPAGPRGATGVQGERGPPGLVLPGDPGPKGDPGDRGPIGLTGRAGPPGDSGPPGEKGDPGRPGPPGPVGPRGRDGEVGEKGDEGPPGDPGLPGKAGERGLRGAPGVRGPVGEKGDQGDPGEDGRNGSPGSSGPKGDRGEPGPPGPPGRLVDTGPGAREKGEPGDRGQEGPRGPKGDPGLPGAPGERGIEGFRGPPGPQGDPGVRGPAGEKGDRGPPGLDGRSGLDGKPGAAGPSGPNGAAGKAGDPGRDGLPGLRGEQGLPGPSGPPGLPGKPGEDGKPGLNGKNGEPGDPGEDGRKGEKGDSGASGREGRDGPKGERGAPGILGPQGPPGLPGPVGPPGQGFPGVPGGTGPKGDRGETGSKGEQGLPGERGLRGEPGSVPN | ||||||
Region | 1254-1477 | Interrupted collagenous region | ||||
Sequence: GQKGEPGEMGLRGQVGPPGDPGLPGRTGAPGPQGPPGSATAKGERGFPGADGRPGSPGRAGNPGTPGAPGLKGSPGLPGPRGDPGERGPRGPKGEPGAPGQVIGGEGPGLPGRKGDPGPSGPPGPRGPLGDPGPRGPPGLPGTAMKGDKGDRGERGPPGPGEGGIAPGEPGLPGLPGSPGPQGPVGPPGKKGEKGDSEDGAPGLPGQPGSPGEQGPRGPPGAIG | ||||||
Region | 1254-2784 | Triple-helical region | ||||
Sequence: GQKGEPGEMGLRGQVGPPGDPGLPGRTGAPGPQGPPGSATAKGERGFPGADGRPGSPGRAGNPGTPGAPGLKGSPGLPGPRGDPGERGPRGPKGEPGAPGQVIGGEGPGLPGRKGDPGPSGPPGPRGPLGDPGPRGPPGLPGTAMKGDKGDRGERGPPGPGEGGIAPGEPGLPGLPGSPGPQGPVGPPGKKGEKGDSEDGAPGLPGQPGSPGEQGPRGPPGAIGPKGDRGFPGPLGEAGEKGERGPPGPAGSRGLPGVAGRPGAKGPEGPPGPTGRQGEKGEPGRPGDPAVVGPAVAGPKGEKGDVGPAGPRGATGVQGERGPPGLVLPGDPGPKGDPGDRGPIGLTGRAGPPGDSGPPGEKGDPGRPGPPGPVGPRGRDGEVGEKGDEGPPGDPGLPGKAGERGLRGAPGVRGPVGEKGDQGDPGEDGRNGSPGSSGPKGDRGEPGPPGPPGRLVDTGPGAREKGEPGDRGQEGPRGPKGDPGLPGAPGERGIEGFRGPPGPQGDPGVRGPAGEKGDRGPPGLDGRSGLDGKPGAAGPSGPNGAAGKAGDPGRDGLPGLRGEQGLPGPSGPPGLPGKPGEDGKPGLNGKNGEPGDPGEDGRKGEKGDSGASGREGRDGPKGERGAPGILGPQGPPGLPGPVGPPGQGFPGVPGGTGPKGDRGETGSKGEQGLPGERGLRGEPGSVPNVDRLLETAGIKASALREIVETWDESSGSFLPVPERRRGPKGDSGEQGPPGKEGPIGFPGERGLKGDRGDPGPQGPPGLALGERGPPGPSGLAGEPGKPGIPGLPGRAGGVGEAGRPGERGERGEKGERGEQGRDGPPGLPGTPGPPGPPGPKVSVDEPGPGLSGEQGPPGLKGAKGEPGSNGDQGPKGDRGVPGIKGDRGEPGPRGQDGNPGLPGERGMAGPEGKPGLQGPRGPPGPVGGHGDPGPPGAPGLAGPAGPQGPSGLKGEPGETGPPGRGLTGPTGAVGLPGPPGPSGLVGPQGSPGLPGQVGETGKPGAPGRDGASGKDGDRGSPGVPGSPGLPGPVGPKGEPGPTGAPGQAVVGLPGAKGEKGAPGGLAGDLVGEPGAKGDRGLPGPRGEKGEAGRAGEPGDPGEDGQKGAPGPKGFKGDPGVGVPGSPGPPGPPGVKGDLGLPGLPGAPGVVGFPGQTGPRGEMGQPGPSGERGLAGPPGREGIPGPLGPPGPPGSVGPPGASGLKGDKGDPGVGLPGPRGERGEPGIRGEDGRPGQEGPRGLTGPPGSRGERGEKGDVGSAGLKGDKGDSAVILGPPGPRGAKGDMGERGPRGLDGDKGPRGDNGDPGDKGSKGEPGDKGSAGLPGLRGLLGPQGQPGAAGIPGDPGSPGKDGVPGIRGEKGDVGFMGPRGLKGERGVKGACGLDGEKGDKGEAGPPGRPGLAGHKGEMGEPGVPGQSGAPGKEGLIGPKGDRGFDGQPGPKGDQGEKGERGTPGIGGFPGPSGNDGSAGPPGPPGSVGPRGPEGLQGQKGERGPPGERVVGAPGVPGAPGERGEQGRPGPAGPRGEKGEAA | ||||||
Motif | 1334-1336 | Cell attachment site | ||||
Sequence: RGD | ||||||
Compositional bias | 1368-1392 | Pro residues | ||||
Sequence: GDPGPSGPPGPRGPLGDPGPRGPPG | ||||||
Compositional bias | 1425-1439 | Pro residues | ||||
Sequence: LPGLPGSPGPQGPVG | ||||||
Compositional bias | 1713-1730 | Basic and acidic residues | ||||
Sequence: PGAREKGEPGDRGQEGPR | ||||||
Compositional bias | 1848-1875 | Basic and acidic residues | ||||
Sequence: GDPGEDGRKGEKGDSGASGREGRDGPKG | ||||||
Compositional bias | 1885-1901 | Pro residues | ||||
Sequence: PQGPPGLPGPVGPPGQG | ||||||
Region | 1963-2782 | Disordered | ||||
Sequence: WDESSGSFLPVPERRRGPKGDSGEQGPPGKEGPIGFPGERGLKGDRGDPGPQGPPGLALGERGPPGPSGLAGEPGKPGIPGLPGRAGGVGEAGRPGERGERGEKGERGEQGRDGPPGLPGTPGPPGPPGPKVSVDEPGPGLSGEQGPPGLKGAKGEPGSNGDQGPKGDRGVPGIKGDRGEPGPRGQDGNPGLPGERGMAGPEGKPGLQGPRGPPGPVGGHGDPGPPGAPGLAGPAGPQGPSGLKGEPGETGPPGRGLTGPTGAVGLPGPPGPSGLVGPQGSPGLPGQVGETGKPGAPGRDGASGKDGDRGSPGVPGSPGLPGPVGPKGEPGPTGAPGQAVVGLPGAKGEKGAPGGLAGDLVGEPGAKGDRGLPGPRGEKGEAGRAGEPGDPGEDGQKGAPGPKGFKGDPGVGVPGSPGPPGPPGVKGDLGLPGLPGAPGVVGFPGQTGPRGEMGQPGPSGERGLAGPPGREGIPGPLGPPGPPGSVGPPGASGLKGDKGDPGVGLPGPRGERGEPGIRGEDGRPGQEGPRGLTGPPGSRGERGEKGDVGSAGLKGDKGDSAVILGPPGPRGAKGDMGERGPRGLDGDKGPRGDNGDPGDKGSKGEPGDKGSAGLPGLRGLLGPQGQPGAAGIPGDPGSPGKDGVPGIRGEKGDVGFMGPRGLKGERGVKGACGLDGEKGDKGEAGPPGRPGLAGHKGEMGEPGVPGQSGAPGKEGLIGPKGDRGFDGQPGPKGDQGEKGERGTPGIGGFPGPSGNDGSAGPPGPPGSVGPRGPEGLQGQKGERGPPGERVVGAPGVPGAPGERGEQGRPGPAGPRGEKGE | ||||||
Motif | 2008-2010 | Cell attachment site | ||||
Sequence: RGD | ||||||
Compositional bias | 2056-2073 | Basic and acidic residues | ||||
Sequence: RPGERGERGEKGERGEQG | ||||||
Compositional bias | 2079-2096 | Pro residues | ||||
Sequence: GLPGTPGPPGPPGPKVSV | ||||||
Compositional bias | 2169-2195 | Pro residues | ||||
Sequence: LQGPRGPPGPVGGHGDPGPPGAPGLAG | ||||||
Compositional bias | 2278-2292 | Pro residues | ||||
Sequence: GSPGLPGPVGPKGEP | ||||||
Compositional bias | 2334-2353 | Basic and acidic residues | ||||
Sequence: LPGPRGEKGEAGRAGEPGDP | ||||||
Compositional bias | 2434-2449 | Pro residues | ||||
Sequence: GIPGPLGPPGPPGSVG | ||||||
Compositional bias | 2537-2568 | Basic and acidic residues | ||||
Sequence: DMGERGPRGLDGDKGPRGDNGDPGDKGSKGEP | ||||||
Motif | 2553-2555 | Cell attachment site | ||||
Sequence: RGD | ||||||
Compositional bias | 2632-2646 | Basic and acidic residues | ||||
Sequence: GACGLDGEKGDKGEA | ||||||
Region | 2785-2944 | Nonhelical region (NC2) | ||||
Sequence: LTEDDIRGFVRQEMSQHCACQGQFIASGSRPLPSYAADTAGSQLHAVPVLRVSHAEEEERVPPEDDEYSEYSEYSVEEYQDPEAPWDSDDPCSLPLDEGSCTAYTLRWYHRAVTGSTEACHPFVYGGCGGNANRFGTREACERRCPPRVVQSQGTGTAQD | ||||||
Region | 2837-2872 | Disordered | ||||
Sequence: SHAEEEERVPPEDDEYSEYSEYSVEEYQDPEAPWDS | ||||||
Compositional bias | 2844-2869 | Acidic residues | ||||
Sequence: RVPPEDDEYSEYSEYSVEEYQDPEAP | ||||||
Domain | 2872-2944 | BPTI/Kunitz inhibitor | ||||
Sequence: SDDPCSLPLDEGSCTAYTLRWYHRAVTGSTEACHPFVYGGCGGNANRFGTREACERRCPPRVVQSQGTGTAQD |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q02388-1
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
- Length2,944
- Mass (Da)295,220
- Last updated1996-02-01 v2
- Checksum96D8BF6D0FD387DB
Q02388-2
- Name2
- Differences from canonical
- 1869-1900: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9JBL3 | C9JBL3_HUMAN | COL7A1 | 173 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 195-197 | in Ref. 4; BAA02853 | ||||
Sequence: FFF → EFR | ||||||
Sequence conflict | 369-371 | in Ref. 5; AAA36357/AAB24637 | ||||
Sequence: QQQ → EFR | ||||||
Sequence conflict | 518-519 | in Ref. 5; AAA36357/AAB24637 | ||||
Sequence: EL → DV | ||||||
Sequence conflict | 529 | in Ref. 4; BAA02853 | ||||
Sequence: S → C | ||||||
Sequence conflict | 541 | in Ref. 5; AAA36357/AAB24637 | ||||
Sequence: V → W | ||||||
Sequence conflict | 851 | in Ref. 4; BAA02853 | ||||
Sequence: R → H | ||||||
Sequence conflict | 893 | in Ref. 1; AAA58965, 4; BAA02853 and 6; AAA96439 | ||||
Sequence: A → E | ||||||
Sequence conflict | 1122 | in Ref. 4; BAA02853 | ||||
Sequence: R → L | ||||||
Compositional bias | 1368-1392 | Pro residues | ||||
Sequence: GDPGPSGPPGPRGPLGDPGPRGPPG | ||||||
Compositional bias | 1425-1439 | Pro residues | ||||
Sequence: LPGLPGSPGPQGPVG | ||||||
Sequence conflict | 1463-1464 | in Ref. 3; AA sequence | ||||
Sequence: SP → LR | ||||||
Compositional bias | 1713-1730 | Basic and acidic residues | ||||
Sequence: PGAREKGEPGDRGQEGPR | ||||||
Compositional bias | 1848-1875 | Basic and acidic residues | ||||
Sequence: GDPGEDGRKGEKGDSGASGREGRDGPKG | ||||||
Alternative sequence | VSP_024026 | 1869-1900 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 1885-1901 | Pro residues | ||||
Sequence: PQGPPGLPGPVGPPGQG | ||||||
Compositional bias | 2056-2073 | Basic and acidic residues | ||||
Sequence: RPGERGERGEKGERGEQG | ||||||
Compositional bias | 2079-2096 | Pro residues | ||||
Sequence: GLPGTPGPPGPPGPKVSV | ||||||
Compositional bias | 2169-2195 | Pro residues | ||||
Sequence: LQGPRGPPGPVGGHGDPGPPGAPGLAG | ||||||
Compositional bias | 2278-2292 | Pro residues | ||||
Sequence: GSPGLPGPVGPKGEP | ||||||
Compositional bias | 2334-2353 | Basic and acidic residues | ||||
Sequence: LPGPRGEKGEAGRAGEPGDP | ||||||
Compositional bias | 2434-2449 | Pro residues | ||||
Sequence: GIPGPLGPPGPPGSVG | ||||||
Compositional bias | 2537-2568 | Basic and acidic residues | ||||
Sequence: DMGERGPRGLDGDKGPRGDNGDPGDKGSKGEP | ||||||
Compositional bias | 2632-2646 | Basic and acidic residues | ||||
Sequence: GACGLDGEKGDKGEA | ||||||
Compositional bias | 2844-2869 | Acidic residues | ||||
Sequence: RVPPEDDEYSEYSEYSVEEYQDPEAP |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L23982 EMBL· GenBank· DDBJ | AAA58965.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L02870 EMBL· GenBank· DDBJ | AAA75438.1 EMBL· GenBank· DDBJ | mRNA | ||
D13694 EMBL· GenBank· DDBJ | BAA02853.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
M96984 EMBL· GenBank· DDBJ | AAA36357.2 EMBL· GenBank· DDBJ | mRNA | ||
S51236 EMBL· GenBank· DDBJ | AAB24637.1 EMBL· GenBank· DDBJ | mRNA | ||
M65158 EMBL· GenBank· DDBJ | AAA96439.1 EMBL· GenBank· DDBJ | mRNA | ||
L06862 EMBL· GenBank· DDBJ | AAA89196.1 EMBL· GenBank· DDBJ | mRNA |