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Entry version 220 (13 Feb 2019)
Sequence version 2 (01 Feb 1996)
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Protein

Collagen alpha-1(VII) chain

Gene

COL7A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Stratified squamous epithelial basement membrane protein that forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence by interacting with extracellular matrix (ECM) proteins such as type IV collagen.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei2886 – 2887Reactive bondBy similarity2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionProtease inhibitor, Serine protease inhibitor
Biological processCell adhesion

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1442490 Collagen degradation
R-HSA-1474244 Extracellular matrix organization
R-HSA-1650814 Collagen biosynthesis and modifying enzymes
R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures
R-HSA-204005 COPII-mediated vesicle transport
R-HSA-216083 Integrin cell surface interactions
R-HSA-2214320 Anchoring fibril formation
R-HSA-3000157 Laminin interactions
R-HSA-5694530 Cargo concentration in the ER
R-HSA-8948216 Collagen chain trimerization

SIGNOR Signaling Network Open Resource

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SIGNORi
Q02388

Protein family/group databases

MEROPS protease database

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MEROPSi
I02.967

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Collagen alpha-1(VII) chain
Alternative name(s):
Long-chain collagen
Short name:
LC collagen
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:COL7A1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000114270.15

Human Gene Nomenclature Database

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HGNCi
HGNC:2214 COL7A1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
120120 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q02388

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Epidermolysis bullosa acquisita (EBA) is an autoimmune acquired blistering skin disease resulting from autoantibodies to type VII collagen.
Epidermolysis bullosa dystrophica, autosomal dominant (DDEB)14 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:131750
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0111621522G → E in DDEB. Corresponds to variant dbSNP:rs387906605EnsemblClinVar.1
Natural variantiVAR_0018121557G → R in DDEB. 1
Natural variantiVAR_0111671776G → R in DDEB. 1
Natural variantiVAR_0018152003G → R in DDEB. 1 PublicationCorresponds to variant dbSNP:rs121912832EnsemblClinVar.1
Natural variantiVAR_0111702006G → A in DDEB. 1
Natural variantiVAR_0111712006G → D in DDEB; interferes with collagen VII folding and secretion. 2 PublicationsCorresponds to variant dbSNP:rs121912842EnsemblClinVar.1
Natural variantiVAR_0111742015G → E in DDEB; interferes with collagen VII folding and secretion. 2 PublicationsCorresponds to variant dbSNP:rs121912843EnsemblClinVar.1
Natural variantiVAR_0111752028G → A in DDEB. 1 Publication1
Natural variantiVAR_0111762028G → R in DDEB and EBP. 2 PublicationsCorresponds to variant dbSNP:rs762162799EnsemblClinVar.1
Natural variantiVAR_0018182034G → R in DDEB and EBDSC; interferes with collagen VII folding and secretion. 4 PublicationsCorresponds to variant dbSNP:rs121912844EnsemblClinVar.1
Natural variantiVAR_0111782034G → W in DDEB. 2 Publications1
Natural variantiVAR_0111792037G → E in DDEB. 1 PublicationCorresponds to variant dbSNP:rs121912846EnsemblClinVar.1
Natural variantiVAR_0111802040G → D in DDEB. 1 Publication1
Natural variantiVAR_0018192040G → S in DDEB. 1 PublicationCorresponds to variant dbSNP:rs121912829EnsemblClinVar.1
Natural variantiVAR_0111812040G → V in DDEB. 1 Publication1
Natural variantiVAR_0018202043G → R in DDEB. 5 PublicationsCorresponds to variant dbSNP:rs121912836EnsemblClinVar.1
Natural variantiVAR_0111822043G → W in DDEB; localized type. 1 PublicationCorresponds to variant dbSNP:rs121912836EnsemblClinVar.1
Natural variantiVAR_0111832046G → V in DDEB. 1
Natural variantiVAR_0018222055G → E in DDEB. 1
Natural variantiVAR_0111842064G → R in DDEB. 2 PublicationsCorresponds to variant dbSNP:rs866061439EnsemblClinVar.1
Natural variantiVAR_0649972070G → R in DDEB. 1 Publication1
Natural variantiVAR_0018262076G → D in DDEB; also in recessive forms. 1 PublicationCorresponds to variant dbSNP:rs121912850EnsemblClinVar.1
Natural variantiVAR_0018272079G → E in DDEB. 1 Publication1
Natural variantiVAR_0111852079G → R in DDEB; associated with squamous cell carcinoma. 1 Publication1
Natural variantiVAR_0111882207G → R in DDEB. 1 Publication1
Natural variantiVAR_0111972713G → D in DDEB. 1 PublicationCorresponds to variant dbSNP:rs369591910Ensembl.1
Natural variantiVAR_0112012791R → W in DDEB. Corresponds to variant dbSNP:rs142566193EnsemblClinVar.1
Epidermolysis bullosa dystrophica, autosomal recessive (RDEB)14 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:226600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001809142K → R in RDEB; unknown pathological significance; may affect exon 3 splicing. 1 PublicationCorresponds to variant dbSNP:rs121912856EnsemblClinVar.1
Natural variantiVAR_0111601347G → R in RDEB; localized type; mild. 1 PublicationCorresponds to variant dbSNP:rs121912833EnsemblClinVar.1
Natural variantiVAR_0111631604G → R in RDEB. 1
Natural variantiVAR_0111641652G → R in RDEB; mitis type. 1 PublicationCorresponds to variant dbSNP:rs1439299333Ensembl.1
Natural variantiVAR_0111651703G → E in RDEB. Corresponds to variant dbSNP:rs770304825Ensembl.1
Natural variantiVAR_0111661772R → W in RDEB. Corresponds to variant dbSNP:rs1032335328Ensembl.1
Natural variantiVAR_0018131782G → R in RDEB; mitis type. 1 PublicationCorresponds to variant dbSNP:rs374718902EnsemblClinVar.1
Natural variantiVAR_0111691812G → R in RDEB. 1 Publication1
Natural variantiVAR_0649941845G → R in RDEB. 1 Publication1
Natural variantiVAR_0649951981K → R in RDEB; mild form. 1 Publication1
Natural variantiVAR_0018141982G → W in RDEB. 1 Publication1
Natural variantiVAR_0111722008R → C in RDEB. 2 PublicationsCorresponds to variant dbSNP:rs1055680335EnsemblClinVar.1
Natural variantiVAR_0018162008R → G in RDEB. 2 PublicationsCorresponds to variant dbSNP:rs1055680335EnsemblClinVar.1
Natural variantiVAR_0111732009G → R in RDEB. 2 Publications1
Natural variantiVAR_0018172025G → A in RDEB; mitis type. 1 PublicationCorresponds to variant dbSNP:rs766931219Ensembl.1
Natural variantiVAR_0111772031G → S in RDEB; severe phenotype. 1 PublicationCorresponds to variant dbSNP:rs121912838EnsemblClinVar.1
Natural variantiVAR_0018212049G → E in RDEB. 2 Publications1
Natural variantiVAR_0018232063R → W in RDEB. 3 PublicationsCorresponds to variant dbSNP:rs121912849EnsemblClinVar.1
Natural variantiVAR_0649962069R → C in RDEB. 2 PublicationsCorresponds to variant dbSNP:rs121912855EnsemblClinVar.1
Natural variantiVAR_0018252073G → D in RDEB; mitis type. 1 Publication1
Natural variantiVAR_0111862132G → D in RDEB. Corresponds to variant dbSNP:rs755669902Ensembl.1
Natural variantiVAR_0111872192G → S in RDEB. 1
Natural variantiVAR_0649982221G → A in RDEB. 1 Publication1
Natural variantiVAR_0111902263G → V in RDEB. 1
Natural variantiVAR_0111912287G → R in RDEB; moderately severe phenotype when compound heterozygous with R-2316; leads to isolated toenail dystrophy when heterozygous with a normal allele. 1 PublicationCorresponds to variant dbSNP:rs121912839EnsemblClinVar.1
Natural variantiVAR_0649992296G → E in RDEB. 1 Publication1
Natural variantiVAR_0111922316G → R in RDEB; moderately severe phenotype when compound heterozygous with R-2287. 1 Publication1
Natural variantiVAR_0111942366G → S in RDEB; mitis type. 1 Publication1
Natural variantiVAR_0650002557G → R in RDEB. 1 Publication1
Natural variantiVAR_0018302569G → R in RDEB; severe and mitis type. 1
Natural variantiVAR_0018312575G → R in RDEB. 2 PublicationsCorresponds to variant dbSNP:rs760891216EnsemblClinVar.1
Natural variantiVAR_0650012622R → W in RDEB. 1 PublicationCorresponds to variant dbSNP:rs139318843EnsemblClinVar.1
Natural variantiVAR_0018332653G → R in RDEB; mitis type. Corresponds to variant dbSNP:rs121912851EnsemblClinVar.1
Natural variantiVAR_0018342671G → V in RDEB. 1
Natural variantiVAR_0111962674G → D in RDEB. 1
Natural variantiVAR_0018352674G → R in RDEB; mitis type. 1
Natural variantiVAR_0111992740G → A in RDEB. 1
Natural variantiVAR_0018362749G → R in RDEB. Corresponds to variant dbSNP:rs121912853EnsemblClinVar.1
Natural variantiVAR_0112002775G → S in RDEB; mitis type. 1 PublicationCorresponds to variant dbSNP:rs1333259313Ensembl.1
Natural variantiVAR_0018372798M → K in RDEB. 1 PublicationCorresponds to variant dbSNP:rs121912828EnsemblClinVar.1
Transient bullous dermolysis of the newborn (TBDN)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:131705
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0111611519G → D in TBDN; compound heterozygous with E-2251; clinically silent when heterozygous with a normal allele. 2 PublicationsCorresponds to variant dbSNP:rs121912835EnsemblClinVar.1
Natural variantiVAR_0111892251G → E in TBDN; compound heterozygous with D-1519; leads to isolated toenail dystrophy when heterozygous with a normal allele. 1 PublicationCorresponds to variant dbSNP:rs121912834EnsemblClinVar.1
Epidermolysis bullosa dystrophica, pretibial type (PR-DEB)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:131850
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0018322623G → C in PR-DEB; dominant. 1 PublicationCorresponds to variant dbSNP:rs121912831EnsemblClinVar.1
Epidermolysis bullosa dystrophica, Bart type (B-DEB)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant form of dystrophic epidermolysis bullosa characterized by congenital localized absence of skin, skin fragility and deformity of nails.
See also OMIM:132000
Epidermolysis bullosa pruriginosa (EBP)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:604129
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0111681791G → E in EBP. 1 Publication1
Natural variantiVAR_0111762028G → R in DDEB and EBP. 2 PublicationsCorresponds to variant dbSNP:rs762162799EnsemblClinVar.1
Natural variantiVAR_0018282242G → R in EBP. 1 PublicationCorresponds to variant dbSNP:rs121912837EnsemblClinVar.1
Natural variantiVAR_0111952369G → S in EBP. 1 Publication1
Natural variantiVAR_0111982713G → R in EBP. 1 Publication1
Nail disorder, non-syndromic congenital, 8 (NDNC8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:607523
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0155191595G → R in NDNC8. 1 PublicationCorresponds to variant dbSNP:rs121912840EnsemblClinVar.1
Natural variantiVAR_0155201815G → R in NDNC8. 1 PublicationCorresponds to variant dbSNP:rs121912841EnsemblClinVar.1
Epidermolysis bullosa dystrophica, with subcorneal cleavage (EBDSC)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:131750
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0018182034G → R in DDEB and EBDSC; interferes with collagen VII folding and secretion. 4 PublicationsCorresponds to variant dbSNP:rs121912844EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Epidermolysis bullosa

Organism-specific databases

DisGeNET

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DisGeNETi
1294

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
COL7A1

MalaCards human disease database

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MalaCardsi
COL7A1
MIMi131705 phenotype
131750 phenotype
131850 phenotype
132000 phenotype
226600 phenotype
604129 phenotype
607523 phenotype

Open Targets

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OpenTargetsi
ENSG00000114270

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
158673 Acral dystrophic epidermolysis bullosa
89841 Centripetalis recessive dystrophic epidermolysis bullosa
158676 Dominant dystrophic epidermolysis bullosa, nails only
89843 Dystrophic epidermolysis bullosa pruriginosa
89839 Epidermolysis bullosa simplex superficialis
231568 Generalized dominant dystrophic epidermolysis bullosa
79410 Pretibial dystrophic epidermolysis bullosa
79409 Recessive dystrophic epidermolysis bullosa inversa
89842 Recessive dystrophic epidermolysis bullosa, generalized intermediate
79408 Severe generalized recessive dystrophic epidermolysis bullosa
79411 Transient bullous dermolysis of the newborn

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26730

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
COL7A1

Domain mapping of disease mutations (DMDM)

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DMDMi
1345650

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 16Sequence analysisAdd BLAST16
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000576117 – 2944Collagen alpha-1(VII) chainAdd BLAST2928

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi337N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi786N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1109N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei20364-hydroxyproline1 Publication1
Modified residuei20394-hydroxyproline1 Publication1
Modified residuei20844-hydroxyproline1 Publication1
Modified residuei20874-hydroxyproline1 Publication1
Modified residuei20904-hydroxyproline1 Publication1
Modified residuei21674-hydroxyproline1 Publication1
Modified residuei21764-hydroxyproline1 Publication1
Modified residuei21854-hydroxyproline1 Publication1
Modified residuei21884-hydroxyproline1 Publication1
Modified residuei26255-hydroxylysine; alternate1 Publication1
Glycosylationi2625O-linked (Gal...) hydroxylysine; alternate1
Modified residuei26315-hydroxylysine; alternate1 Publication1
Glycosylationi2631O-linked (Gal...) hydroxylysine; alternate1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi2634InterchainPROSITE-ProRule annotation
Modified residuei26644-hydroxyproline1 Publication1
Modified residuei26674-hydroxyproline1 Publication1
Modified residuei26734-hydroxyproline1 Publication1
Disulfide bondi2802InterchainPROSITE-ProRule annotation
Disulfide bondi2804InterchainPROSITE-ProRule annotation
Disulfide bondi2876 ↔ 2929PROSITE-ProRule annotation
Disulfide bondi2885 ↔ 2912PROSITE-ProRule annotation
Disulfide bondi2904 ↔ 2925PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q02388

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q02388

MaxQB - The MaxQuant DataBase

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MaxQBi
Q02388

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q02388

PeptideAtlas

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PeptideAtlasi
Q02388

PRoteomics IDEntifications database

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PRIDEi
Q02388

ProteomicsDB human proteome resource

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ProteomicsDBi
58086
58087 [Q02388-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q02388

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q02388

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000114270 Expressed in 211 organ(s), highest expression level in skin of abdomen

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q02388 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q02388 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB016357
HPA042420

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotrimer. Interacts with MIA3/TANGO1; facilitating its loading into transport carriers and subsequent secretion.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
MIA3Q5JRA62EBI-724237,EBI-2291868

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107691, 17 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1737 Collagen type VII trimer

Protein interaction database and analysis system

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IntActi
Q02388, 14 interactors

Molecular INTeraction database

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MINTi
Q02388

STRING: functional protein association networks

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STRINGi
9606.ENSP00000332371

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q02388

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q02388

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini38 – 211VWFA 1PROSITE-ProRule annotationAdd BLAST174
Domaini234 – 329Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST96
Domaini330 – 416Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST87
Domaini417 – 507Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST91
Domaini510 – 597Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST88
Domaini600 – 687Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST88
Domaini688 – 775Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST88
Domaini778 – 866Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST89
Domaini869 – 957Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST89
Domaini958 – 1051Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST94
Domaini1054 – 1229VWFA 2PROSITE-ProRule annotationAdd BLAST176
Domaini2872 – 2944BPTI/Kunitz inhibitorPROSITE-ProRule annotationAdd BLAST73

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni17 – 1253Nonhelical region (NC1)Add BLAST1237
Regioni1254 – 2784Triple-helical regionAdd BLAST1531
Regioni1254 – 1477Interrupted collagenous regionAdd BLAST224
Regioni2785 – 2944Nonhelical region (NC2)Add BLAST160

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1170 – 1172Cell attachment siteSequence analysis3
Motifi1334 – 1336Cell attachment siteSequence analysis3
Motifi2008 – 2010Cell attachment siteSequence analysis3
Motifi2553 – 2555Cell attachment siteSequence analysis3

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3544 Eukaryota
ENOG410XNMM LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154865

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000111866

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG051053

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q02388

KEGG Orthology (KO)

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KOi
K16628

Identification of Orthologs from Complete Genome Data

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OMAi
YRVSWHS

Database of Orthologous Groups

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OrthoDBi
67372at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q02388

TreeFam database of animal gene trees

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TreeFami
TF351645

Family and domain databases

Conserved Domains Database

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CDDi
cd00063 FN3, 9 hits
cd00109 KU, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 9 hits
3.40.50.410, 2 hits
4.10.410.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR008160 Collagen
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR013783 Ig-like_fold
IPR002223 Kunitz_BPTI
IPR036880 Kunitz_BPTI_sf
IPR020901 Prtase_inh_Kunz-CS
IPR002035 VWF_A
IPR036465 vWFA_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01391 Collagen, 15 hits
PF00041 fn3, 8 hits
PF00014 Kunitz_BPTI, 1 hit
PF00092 VWA, 2 hits

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00759 BASICPTASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00060 FN3, 9 hits
SM00327 VWA, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49265 SSF49265, 5 hits
SSF53300 SSF53300, 2 hits
SSF57362 SSF57362, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00280 BPTI_KUNITZ_1, 1 hit
PS50279 BPTI_KUNITZ_2, 1 hit
PS50853 FN3, 9 hits
PS50234 VWFA, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q02388-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MTLRLLVAAL CAGILAEAPR VRAQHRERVT CTRLYAADIV FLLDGSSSIG
60 70 80 90 100
RSNFREVRSF LEGLVLPFSG AASAQGVRFA TVQYSDDPRT EFGLDALGSG
110 120 130 140 150
GDVIRAIREL SYKGGNTRTG AAILHVADHV FLPQLARPGV PKVCILITDG
160 170 180 190 200
KSQDLVDTAA QRLKGQGVKL FAVGIKNADP EELKRVASQP TSDFFFFVND
210 220 230 240 250
FSILRTLLPL VSRRVCTTAG GVPVTRPPDD STSAPRDLVL SEPSSQSLRV
260 270 280 290 300
QWTAASGPVT GYKVQYTPLT GLGQPLPSER QEVNVPAGET SVRLRGLRPL
310 320 330 340 350
TEYQVTVIAL YANSIGEAVS GTARTTALEG PELTIQNTTA HSLLVAWRSV
360 370 380 390 400
PGATGYRVTW RVLSGGPTQQ QELGPGQGSV LLRDLEPGTD YEVTVSTLFG
410 420 430 440 450
RSVGPATSLM ARTDASVEQT LRPVILGPTS ILLSWNLVPE ARGYRLEWRR
460 470 480 490 500
ETGLEPPQKV VLPSDVTRYQ LDGLQPGTEY RLTLYTLLEG HEVATPATVV
510 520 530 540 550
PTGPELPVSP VTDLQATELP GQRVRVSWSP VPGATQYRII VRSTQGVERT
560 570 580 590 600
LVLPGSQTAF DLDDVQAGLS YTVRVSARVG PREGSASVLT VRREPETPLA
610 620 630 640 650
VPGLRVVVSD ATRVRVAWGP VPGASGFRIS WSTGSGPESS QTLPPDSTAT
660 670 680 690 700
DITGLQPGTT YQVAVSVLRG REEGPAAVIV ARTDPLGPVR TVHVTQASSS
710 720 730 740 750
SVTITWTRVP GATGYRVSWH SAHGPEKSQL VSGEATVAEL DGLEPDTEYT
760 770 780 790 800
VHVRAHVAGV DGPPASVVVR TAPEPVGRVS RLQILNASSD VLRITWVGVT
810 820 830 840 850
GATAYRLAWG RSEGGPMRHQ ILPGNTDSAE IRGLEGGVSY SVRVTALVGD
860 870 880 890 900
REGTPVSIVV TTPPEAPPAL GTLHVVQRGE HSLRLRWEPV PRAQGFLLHW
910 920 930 940 950
QPEGGQEQSR VLGPELSSYH LDGLEPATQY RVRLSVLGPA GEGPSAEVTA
960 970 980 990 1000
RTESPRVPSI ELRVVDTSID SVTLAWTPVS RASSYILSWR PLRGPGQEVP
1010 1020 1030 1040 1050
GSPQTLPGIS SSQRVTGLEP GVSYIFSLTP VLDGVRGPEA SVTQTPVCPR
1060 1070 1080 1090 1100
GLADVVFLPH ATQDNAHRAE ATRRVLERLV LALGPLGPQA VQVGLLSYSH
1110 1120 1130 1140 1150
RPSPLFPLNG SHDLGIILQR IRDMPYMDPS GNNLGTAVVT AHRYMLAPDA
1160 1170 1180 1190 1200
PGRRQHVPGV MVLLVDEPLR GDIFSPIREA QASGLNVVML GMAGADPEQL
1210 1220 1230 1240 1250
RRLAPGMDSV QTFFAVDDGP SLDQAVSGLA TALCQASFTT QPRPEPCPVY
1260 1270 1280 1290 1300
CPKGQKGEPG EMGLRGQVGP PGDPGLPGRT GAPGPQGPPG SATAKGERGF
1310 1320 1330 1340 1350
PGADGRPGSP GRAGNPGTPG APGLKGSPGL PGPRGDPGER GPRGPKGEPG
1360 1370 1380 1390 1400
APGQVIGGEG PGLPGRKGDP GPSGPPGPRG PLGDPGPRGP PGLPGTAMKG
1410 1420 1430 1440 1450
DKGDRGERGP PGPGEGGIAP GEPGLPGLPG SPGPQGPVGP PGKKGEKGDS
1460 1470 1480 1490 1500
EDGAPGLPGQ PGSPGEQGPR GPPGAIGPKG DRGFPGPLGE AGEKGERGPP
1510 1520 1530 1540 1550
GPAGSRGLPG VAGRPGAKGP EGPPGPTGRQ GEKGEPGRPG DPAVVGPAVA
1560 1570 1580 1590 1600
GPKGEKGDVG PAGPRGATGV QGERGPPGLV LPGDPGPKGD PGDRGPIGLT
1610 1620 1630 1640 1650
GRAGPPGDSG PPGEKGDPGR PGPPGPVGPR GRDGEVGEKG DEGPPGDPGL
1660 1670 1680 1690 1700
PGKAGERGLR GAPGVRGPVG EKGDQGDPGE DGRNGSPGSS GPKGDRGEPG
1710 1720 1730 1740 1750
PPGPPGRLVD TGPGAREKGE PGDRGQEGPR GPKGDPGLPG APGERGIEGF
1760 1770 1780 1790 1800
RGPPGPQGDP GVRGPAGEKG DRGPPGLDGR SGLDGKPGAA GPSGPNGAAG
1810 1820 1830 1840 1850
KAGDPGRDGL PGLRGEQGLP GPSGPPGLPG KPGEDGKPGL NGKNGEPGDP
1860 1870 1880 1890 1900
GEDGRKGEKG DSGASGREGR DGPKGERGAP GILGPQGPPG LPGPVGPPGQ
1910 1920 1930 1940 1950
GFPGVPGGTG PKGDRGETGS KGEQGLPGER GLRGEPGSVP NVDRLLETAG
1960 1970 1980 1990 2000
IKASALREIV ETWDESSGSF LPVPERRRGP KGDSGEQGPP GKEGPIGFPG
2010 2020 2030 2040 2050
ERGLKGDRGD PGPQGPPGLA LGERGPPGPS GLAGEPGKPG IPGLPGRAGG
2060 2070 2080 2090 2100
VGEAGRPGER GERGEKGERG EQGRDGPPGL PGTPGPPGPP GPKVSVDEPG
2110 2120 2130 2140 2150
PGLSGEQGPP GLKGAKGEPG SNGDQGPKGD RGVPGIKGDR GEPGPRGQDG
2160 2170 2180 2190 2200
NPGLPGERGM AGPEGKPGLQ GPRGPPGPVG GHGDPGPPGA PGLAGPAGPQ
2210 2220 2230 2240 2250
GPSGLKGEPG ETGPPGRGLT GPTGAVGLPG PPGPSGLVGP QGSPGLPGQV
2260 2270 2280 2290 2300
GETGKPGAPG RDGASGKDGD RGSPGVPGSP GLPGPVGPKG EPGPTGAPGQ
2310 2320 2330 2340 2350
AVVGLPGAKG EKGAPGGLAG DLVGEPGAKG DRGLPGPRGE KGEAGRAGEP
2360 2370 2380 2390 2400
GDPGEDGQKG APGPKGFKGD PGVGVPGSPG PPGPPGVKGD LGLPGLPGAP
2410 2420 2430 2440 2450
GVVGFPGQTG PRGEMGQPGP SGERGLAGPP GREGIPGPLG PPGPPGSVGP
2460 2470 2480 2490 2500
PGASGLKGDK GDPGVGLPGP RGERGEPGIR GEDGRPGQEG PRGLTGPPGS
2510 2520 2530 2540 2550
RGERGEKGDV GSAGLKGDKG DSAVILGPPG PRGAKGDMGE RGPRGLDGDK
2560 2570 2580 2590 2600
GPRGDNGDPG DKGSKGEPGD KGSAGLPGLR GLLGPQGQPG AAGIPGDPGS
2610 2620 2630 2640 2650
PGKDGVPGIR GEKGDVGFMG PRGLKGERGV KGACGLDGEK GDKGEAGPPG
2660 2670 2680 2690 2700
RPGLAGHKGE MGEPGVPGQS GAPGKEGLIG PKGDRGFDGQ PGPKGDQGEK
2710 2720 2730 2740 2750
GERGTPGIGG FPGPSGNDGS AGPPGPPGSV GPRGPEGLQG QKGERGPPGE
2760 2770 2780 2790 2800
RVVGAPGVPG APGERGEQGR PGPAGPRGEK GEAALTEDDI RGFVRQEMSQ
2810 2820 2830 2840 2850
HCACQGQFIA SGSRPLPSYA ADTAGSQLHA VPVLRVSHAE EEERVPPEDD
2860 2870 2880 2890 2900
EYSEYSEYSV EEYQDPEAPW DSDDPCSLPL DEGSCTAYTL RWYHRAVTGS
2910 2920 2930 2940
TEACHPFVYG GCGGNANRFG TREACERRCP PRVVQSQGTG TAQD
Length:2,944
Mass (Da):295,220
Last modified:February 1, 1996 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i96D8BF6D0FD387DB
GO
Isoform 2 (identifier: Q02388-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1869-1900: Missing.

Show »
Length:2,912
Mass (Da):292,267
Checksum:iC206B8957E4333A2
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9JBL3C9JBL3_HUMAN
Collagen alpha-1(VII) chain
COL7A1
173Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA02853 differs from that shown. Reason: Frameshift at positions 275, 282, 476, 494, 523, 541 and 543.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti195 – 197FFF → EFR in BAA02853 (PubMed:1567409).Curated3
Sequence conflicti369 – 371QQQ → EFR in AAA36357 (PubMed:1469284).Curated3
Sequence conflicti369 – 371QQQ → EFR in AAB24637 (PubMed:1469284).Curated3
Sequence conflicti518 – 519EL → DV in AAA36357 (PubMed:1469284).Curated2
Sequence conflicti518 – 519EL → DV in AAB24637 (PubMed:1469284).Curated2
Sequence conflicti529S → C in BAA02853 (PubMed:1567409).Curated1
Sequence conflicti541V → W in AAA36357 (PubMed:1469284).Curated1
Sequence conflicti541V → W in AAB24637 (PubMed:1469284).Curated1
Sequence conflicti851R → H in BAA02853 (PubMed:1567409).Curated1
Sequence conflicti893A → E in AAA58965 (PubMed:8088784).Curated1
Sequence conflicti893A → E in BAA02853 (PubMed:1567409).Curated1
Sequence conflicti893A → E in AAA96439 (PubMed:1871109).Curated1
Sequence conflicti1122R → L in BAA02853 (PubMed:1567409).Curated1
Sequence conflicti1463 – 1464SP → LR AA sequence (PubMed:1307247).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035740119T → P in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_001809142K → R in RDEB; unknown pathological significance; may affect exon 3 splicing. 1 PublicationCorresponds to variant dbSNP:rs121912856EnsemblClinVar.1
Natural variantiVAR_001810595P → L. Corresponds to variant dbSNP:rs2228561EnsemblClinVar.1
Natural variantiVAR_0487661120R → K. Corresponds to variant dbSNP:rs2228563Ensembl.1
Natural variantiVAR_0018111277P → L. Corresponds to variant dbSNP:rs35761247EnsemblClinVar.1
Natural variantiVAR_0111601347G → R in RDEB; localized type; mild. 1 PublicationCorresponds to variant dbSNP:rs121912833EnsemblClinVar.1
Natural variantiVAR_0357411364P → T in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0357421366R → W in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs147089666Ensembl.1
Natural variantiVAR_0111611519G → D in TBDN; compound heterozygous with E-2251; clinically silent when heterozygous with a normal allele. 2 PublicationsCorresponds to variant dbSNP:rs121912835EnsemblClinVar.1
Natural variantiVAR_0111621522G → E in DDEB. Corresponds to variant dbSNP:rs387906605EnsemblClinVar.1
Natural variantiVAR_0018121557G → R in DDEB. 1
Natural variantiVAR_0155191595G → R in NDNC8. 1 PublicationCorresponds to variant dbSNP:rs121912840EnsemblClinVar.1
Natural variantiVAR_0111631604G → R in RDEB. 1
Natural variantiVAR_0111641652G → R in RDEB; mitis type. 1 PublicationCorresponds to variant dbSNP:rs1439299333Ensembl.1
Natural variantiVAR_0111651703G → E in RDEB. Corresponds to variant dbSNP:rs770304825Ensembl.1
Natural variantiVAR_0111661772R → W in RDEB. Corresponds to variant dbSNP:rs1032335328Ensembl.1
Natural variantiVAR_0111671776G → R in DDEB. 1
Natural variantiVAR_0018131782G → R in RDEB; mitis type. 1 PublicationCorresponds to variant dbSNP:rs374718902EnsemblClinVar.1
Natural variantiVAR_0111681791G → E in EBP. 1 Publication1
Natural variantiVAR_0111691812G → R in RDEB. 1 Publication1
Natural variantiVAR_0155201815G → R in NDNC8. 1 PublicationCorresponds to variant dbSNP:rs121912841EnsemblClinVar.1
Natural variantiVAR_0649941845G → R in RDEB. 1 Publication1
Natural variantiVAR_0649951981K → R in RDEB; mild form. 1 Publication1
Natural variantiVAR_0018141982G → W in RDEB. 1 Publication1
Natural variantiVAR_0018152003G → R in DDEB. 1 PublicationCorresponds to variant dbSNP:rs121912832EnsemblClinVar.1
Natural variantiVAR_0111702006G → A in DDEB. 1
Natural variantiVAR_0111712006G → D in DDEB; interferes with collagen VII folding and secretion. 2 PublicationsCorresponds to variant dbSNP:rs121912842EnsemblClinVar.1
Natural variantiVAR_0111722008R → C in RDEB. 2 PublicationsCorresponds to variant dbSNP:rs1055680335EnsemblClinVar.1
Natural variantiVAR_0018162008R → G in RDEB. 2 PublicationsCorresponds to variant dbSNP:rs1055680335EnsemblClinVar.1
Natural variantiVAR_0111732009G → R in RDEB. 2 Publications1
Natural variantiVAR_0111742015G → E in DDEB; interferes with collagen VII folding and secretion. 2 PublicationsCorresponds to variant dbSNP:rs121912843EnsemblClinVar.1
Natural variantiVAR_0018172025G → A in RDEB; mitis type. 1 PublicationCorresponds to variant dbSNP:rs766931219Ensembl.1
Natural variantiVAR_0111752028G → A in DDEB. 1 Publication1
Natural variantiVAR_0111762028G → R in DDEB and EBP. 2 PublicationsCorresponds to variant dbSNP:rs762162799EnsemblClinVar.1
Natural variantiVAR_0111772031G → S in RDEB; severe phenotype. 1 PublicationCorresponds to variant dbSNP:rs121912838EnsemblClinVar.1
Natural variantiVAR_0018182034G → R in DDEB and EBDSC; interferes with collagen VII folding and secretion. 4 PublicationsCorresponds to variant dbSNP:rs121912844EnsemblClinVar.1
Natural variantiVAR_0111782034G → W in DDEB. 2 Publications1
Natural variantiVAR_0111792037G → E in DDEB. 1 PublicationCorresponds to variant dbSNP:rs121912846EnsemblClinVar.1
Natural variantiVAR_0111802040G → D in DDEB. 1 Publication1
Natural variantiVAR_0018192040G → S in DDEB. 1 PublicationCorresponds to variant dbSNP:rs121912829EnsemblClinVar.1
Natural variantiVAR_0111812040G → V in DDEB. 1 Publication1
Natural variantiVAR_0018202043G → R in DDEB. 5 PublicationsCorresponds to variant dbSNP:rs121912836EnsemblClinVar.1
Natural variantiVAR_0111822043G → W in DDEB; localized type. 1 PublicationCorresponds to variant dbSNP:rs121912836EnsemblClinVar.1
Natural variantiVAR_0111832046G → V in DDEB. 1
Natural variantiVAR_0018212049G → E in RDEB. 2 Publications1
Natural variantiVAR_0018222055G → E in DDEB. 1
Natural variantiVAR_0018232063R → W in RDEB. 3 PublicationsCorresponds to variant dbSNP:rs121912849EnsemblClinVar.1
Natural variantiVAR_0111842064G → R in DDEB. 2 PublicationsCorresponds to variant dbSNP:rs866061439EnsemblClinVar.1
Natural variantiVAR_0649962069R → C in RDEB. 2 PublicationsCorresponds to variant dbSNP:rs121912855EnsemblClinVar.1
Natural variantiVAR_0649972070G → R in DDEB. 1 Publication1
Natural variantiVAR_0018252073G → D in RDEB; mitis type. 1 Publication1
Natural variantiVAR_0018262076G → D in DDEB; also in recessive forms. 1 PublicationCorresponds to variant dbSNP:rs121912850EnsemblClinVar.1
Natural variantiVAR_0018272079G → E in DDEB. 1 Publication1
Natural variantiVAR_0111852079G → R in DDEB; associated with squamous cell carcinoma. 1 Publication1
Natural variantiVAR_0111862132G → D in RDEB. Corresponds to variant dbSNP:rs755669902Ensembl.1
Natural variantiVAR_0111872192G → S in RDEB. 1
Natural variantiVAR_0111882207G → R in DDEB. 1 Publication1
Natural variantiVAR_0649982221G → A in RDEB. 1 Publication1
Natural variantiVAR_0018282242G → R in EBP. 1 PublicationCorresponds to variant dbSNP:rs121912837EnsemblClinVar.1
Natural variantiVAR_0111892251G → E in TBDN; compound heterozygous with D-1519; leads to isolated toenail dystrophy when heterozygous with a normal allele. 1 PublicationCorresponds to variant dbSNP:rs121912834EnsemblClinVar.1
Natural variantiVAR_0111902263G → V in RDEB. 1
Natural variantiVAR_0111912287G → R in RDEB; moderately severe phenotype when compound heterozygous with R-2316; leads to isolated toenail dystrophy when heterozygous with a normal allele. 1 PublicationCorresponds to variant dbSNP:rs121912839EnsemblClinVar.1
Natural variantiVAR_0649992296G → E in RDEB. 1 Publication1
Natural variantiVAR_0111922316G → R in RDEB; moderately severe phenotype when compound heterozygous with R-2287. 1 Publication1
Natural variantiVAR_0111932348G → R in DDEB/RDEB; mild form. 1 Publication1
Natural variantiVAR_0018292351G → R in a patient with dystrophic epidermolysis bullosa; mitis type. Corresponds to variant dbSNP:rs1800013Ensembl.1
Natural variantiVAR_0111942366G → S in RDEB; mitis type. 1 Publication1
Natural variantiVAR_0111952369G → S in EBP. 1 Publication1
Natural variantiVAR_0337862429P → L. Corresponds to variant dbSNP:rs2229822EnsemblClinVar.1
Natural variantiVAR_0650002557G → R in RDEB. 1 Publication1
Natural variantiVAR_0018302569G → R in RDEB; severe and mitis type. 1
Natural variantiVAR_0018312575G → R in RDEB. 2 PublicationsCorresponds to variant dbSNP:rs760891216EnsemblClinVar.1
Natural variantiVAR_0650012622R → W in RDEB. 1 PublicationCorresponds to variant dbSNP:rs139318843EnsemblClinVar.1
Natural variantiVAR_0018322623G → C in PR-DEB; dominant. 1 PublicationCorresponds to variant dbSNP:rs121912831EnsemblClinVar.1
Natural variantiVAR_0018332653G → R in RDEB; mitis type. Corresponds to variant dbSNP:rs121912851EnsemblClinVar.1
Natural variantiVAR_0018342671G → V in RDEB. 1
Natural variantiVAR_0111962674G → D in RDEB. 1
Natural variantiVAR_0018352674G → R in RDEB; mitis type. 1
Natural variantiVAR_0111972713G → D in DDEB. 1 PublicationCorresponds to variant dbSNP:rs369591910Ensembl.1
Natural variantiVAR_0111982713G → R in EBP. 1 Publication1
Natural variantiVAR_0111992740G → A in RDEB. 1
Natural variantiVAR_0018362749G → R in RDEB. Corresponds to variant dbSNP:rs121912853EnsemblClinVar.1
Natural variantiVAR_0112002775G → S in RDEB; mitis type. 1 PublicationCorresponds to variant dbSNP:rs1333259313Ensembl.1
Natural variantiVAR_0112012791R → W in DDEB. Corresponds to variant dbSNP:rs142566193EnsemblClinVar.1
Natural variantiVAR_0018372798M → K in RDEB. 1 PublicationCorresponds to variant dbSNP:rs121912828EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0240261869 – 1900Missing in isoform 2. CuratedAdd BLAST32

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L23982 Genomic DNA Translation: AAA58965.1
L02870 mRNA Translation: AAA75438.1
D13694 mRNA Translation: BAA02853.1 Frameshift.
M96984 mRNA Translation: AAA36357.2
S51236 mRNA Translation: AAB24637.1
M65158 mRNA Translation: AAA96439.1
L06862 mRNA Translation: AAA89196.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS2773.1 [Q02388-1]

Protein sequence database of the Protein Information Resource

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PIRi
A54849

NCBI Reference Sequences

More...
RefSeqi
NP_000085.1, NM_000094.3 [Q02388-1]
XP_011531639.1, XM_011533337.1 [Q02388-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.476218

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000328333; ENSP00000332371; ENSG00000114270 [Q02388-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1294

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1294

UCSC genome browser

More...
UCSCi
uc003ctz.3 human [Q02388-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23982 Genomic DNA Translation: AAA58965.1
L02870 mRNA Translation: AAA75438.1
D13694 mRNA Translation: BAA02853.1 Frameshift.
M96984 mRNA Translation: AAA36357.2
S51236 mRNA Translation: AAB24637.1
M65158 mRNA Translation: AAA96439.1
L06862 mRNA Translation: AAA89196.1
CCDSiCCDS2773.1 [Q02388-1]
PIRiA54849
RefSeqiNP_000085.1, NM_000094.3 [Q02388-1]
XP_011531639.1, XM_011533337.1 [Q02388-1]
UniGeneiHs.476218

3D structure databases

ProteinModelPortaliQ02388
SMRiQ02388
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107691, 17 interactors
ComplexPortaliCPX-1737 Collagen type VII trimer
IntActiQ02388, 14 interactors
MINTiQ02388
STRINGi9606.ENSP00000332371

Protein family/group databases

MEROPSiI02.967

PTM databases

iPTMnetiQ02388
PhosphoSitePlusiQ02388

Polymorphism and mutation databases

BioMutaiCOL7A1
DMDMi1345650

Proteomic databases

EPDiQ02388
jPOSTiQ02388
MaxQBiQ02388
PaxDbiQ02388
PeptideAtlasiQ02388
PRIDEiQ02388
ProteomicsDBi58086
58087 [Q02388-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000328333; ENSP00000332371; ENSG00000114270 [Q02388-1]
GeneIDi1294
KEGGihsa:1294
UCSCiuc003ctz.3 human [Q02388-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1294
DisGeNETi1294
EuPathDBiHostDB:ENSG00000114270.15

GeneCards: human genes, protein and diseases

More...
GeneCardsi
COL7A1
GeneReviewsiCOL7A1
HGNCiHGNC:2214 COL7A1
HPAiCAB016357
HPA042420
MalaCardsiCOL7A1
MIMi120120 gene
131705 phenotype
131750 phenotype
131850 phenotype
132000 phenotype
226600 phenotype
604129 phenotype
607523 phenotype
neXtProtiNX_Q02388
OpenTargetsiENSG00000114270
Orphaneti158673 Acral dystrophic epidermolysis bullosa
89841 Centripetalis recessive dystrophic epidermolysis bullosa
158676 Dominant dystrophic epidermolysis bullosa, nails only
89843 Dystrophic epidermolysis bullosa pruriginosa
89839 Epidermolysis bullosa simplex superficialis
231568 Generalized dominant dystrophic epidermolysis bullosa
79410 Pretibial dystrophic epidermolysis bullosa
79409 Recessive dystrophic epidermolysis bullosa inversa
89842 Recessive dystrophic epidermolysis bullosa, generalized intermediate
79408 Severe generalized recessive dystrophic epidermolysis bullosa
79411 Transient bullous dermolysis of the newborn
PharmGKBiPA26730

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG410XNMM LUCA
GeneTreeiENSGT00940000154865
HOGENOMiHOG000111866
HOVERGENiHBG051053
InParanoidiQ02388
KOiK16628
OMAiYRVSWHS
OrthoDBi67372at2759
PhylomeDBiQ02388
TreeFamiTF351645

Enzyme and pathway databases

ReactomeiR-HSA-1442490 Collagen degradation
R-HSA-1474244 Extracellular matrix organization
R-HSA-1650814 Collagen biosynthesis and modifying enzymes
R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures
R-HSA-204005 COPII-mediated vesicle transport
R-HSA-216083 Integrin cell surface interactions
R-HSA-2214320 Anchoring fibril formation
R-HSA-3000157 Laminin interactions
R-HSA-5694530 Cargo concentration in the ER
R-HSA-8948216 Collagen chain trimerization
SIGNORiQ02388

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
COL7A1 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Collagen,_type_VII,_alpha_1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
1294

Protein Ontology

More...
PROi
PR:Q02388

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000114270 Expressed in 211 organ(s), highest expression level in skin of abdomen
ExpressionAtlasiQ02388 baseline and differential
GenevisibleiQ02388 HS

Family and domain databases

CDDicd00063 FN3, 9 hits
cd00109 KU, 1 hit
Gene3Di2.60.40.10, 9 hits
3.40.50.410, 2 hits
4.10.410.10, 1 hit
InterProiView protein in InterPro
IPR008160 Collagen
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR013783 Ig-like_fold
IPR002223 Kunitz_BPTI
IPR036880 Kunitz_BPTI_sf
IPR020901 Prtase_inh_Kunz-CS
IPR002035 VWF_A
IPR036465 vWFA_dom_sf
PfamiView protein in Pfam
PF01391 Collagen, 15 hits
PF00041 fn3, 8 hits
PF00014 Kunitz_BPTI, 1 hit
PF00092 VWA, 2 hits
PRINTSiPR00759 BASICPTASE
SMARTiView protein in SMART
SM00060 FN3, 9 hits
SM00327 VWA, 1 hit
SUPFAMiSSF49265 SSF49265, 5 hits
SSF53300 SSF53300, 2 hits
SSF57362 SSF57362, 1 hit
PROSITEiView protein in PROSITE
PS00280 BPTI_KUNITZ_1, 1 hit
PS50279 BPTI_KUNITZ_2, 1 hit
PS50853 FN3, 9 hits
PS50234 VWFA, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCO7A1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q02388
Secondary accession number(s): Q14054, Q16507
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1996
Last modified: February 13, 2019
This is version 220 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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