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Q02388

- CO7A1_HUMAN

UniProt

Q02388 - CO7A1_HUMAN

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Protein

Collagen alpha-1(VII) chain

Gene
COL7A1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei2886 – 28872Reactive bond By similarity

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. collagen catabolic process Source: Reactome
  3. epidermis development Source: ProtInc
  4. extracellular matrix disassembly Source: Reactome
  5. extracellular matrix organization Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_118779. Extracellular matrix organization.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150268. Anchoring fibril formation.
REACT_150401. Collagen degradation.
REACT_169262. Laminin interactions.

Protein family/group databases

MEROPSiI02.967.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(VII) chain
Alternative name(s):
Long-chain collagen
Short name:
LC collagen
Gene namesi
Name:COL7A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:2214. COL7A1.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: ProtInc
  2. collagen type VII trimer Source: ProtInc
  3. endoplasmic reticulum lumen Source: Reactome
  4. extracellular region Source: Reactome
  5. extracellular space Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

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) [MIM:131750]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.12 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1522 – 15221G → E in DDEB.
VAR_011162
Natural varianti1557 – 15571G → R in DDEB.
VAR_001812
Natural varianti1776 – 17761G → R in DDEB.
VAR_011167
Natural varianti2003 – 20031G → R in DDEB. 1 Publication
VAR_001815
Natural varianti2006 – 20061G → A in DDEB.
VAR_011170
Natural varianti2006 – 20061G → D in DDEB; interferes with collagen VII folding and secretion. 2 Publications
VAR_011171
Natural varianti2015 – 20151G → E in DDEB; interferes with collagen VII folding and secretion. 2 Publications
VAR_011174
Natural varianti2028 – 20281G → A in DDEB. 1 Publication
VAR_011175
Natural varianti2028 – 20281G → R in DDEB and EBP. 2 Publications
VAR_011176
Natural varianti2034 – 20341G → R in DDEB and EBDSC; interferes with collagen VII folding and secretion. 4 Publications
VAR_001818
Natural varianti2034 – 20341G → W in DDEB. 2 Publications
VAR_011178
Natural varianti2040 – 20401G → D in DDEB. 1 Publication
VAR_011180
Natural varianti2040 – 20401G → V in DDEB. 1 Publication
VAR_011181
Natural varianti2043 – 20431G → R in DDEB. 5 Publications
VAR_001820
Natural varianti2043 – 20431G → W in DDEB; localized type. 1 Publication
VAR_011182
Natural varianti2046 – 20461G → V in DDEB.
VAR_011183
Natural varianti2055 – 20551G → E in DDEB.
VAR_001822
Natural varianti2064 – 20641G → R in DDEB. 2 Publications
VAR_011184
Natural varianti2070 – 20701G → R in DDEB. 1 Publication
VAR_064997
Natural varianti2076 – 20761G → D in DDEB; also in recessive forms. 1 Publication
VAR_001826
Natural varianti2079 – 20791G → E in DDEB. 1 Publication
VAR_001827
Natural varianti2079 – 20791G → R in DDEB; associated with squamous cell carcinoma. 1 Publication
VAR_011185
Natural varianti2207 – 22071G → R in DDEB. 1 Publication
VAR_011188
Natural varianti2348 – 23481G → R in DDEB/RDEB; mild form. 1 Publication
VAR_011193
Natural varianti2713 – 27131G → D in DDEB. 1 Publication
VAR_011197
Natural varianti2791 – 27911R → W in DDEB.
Corresponds to variant rs142566193 [ dbSNP | Ensembl ].
VAR_011201
Epidermolysis bullosa dystrophica, autosomal recessive (RDEB) [MIM:226600]: A 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 to mild forms with limited and localized scarring, and less frequent extracutaneous manifestations. Mild forms include epidermolysis bullosa mitis and epidermolysis bullosa localisata.
Note: The disease is caused by mutations affecting the gene represented in this entry.10 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti142 – 1421K → R in RDEB.
VAR_001809
Natural varianti595 – 5951P → L in RDEB.
Corresponds to variant rs2228561 [ dbSNP | Ensembl ].
VAR_001810
Natural varianti1277 – 12771P → L in RDEB.
Corresponds to variant rs35761247 [ dbSNP | Ensembl ].
VAR_001811
Natural varianti1347 – 13471G → R in RDEB; localized type; mild. 1 Publication
VAR_011160
Natural varianti1604 – 16041G → R in RDEB.
VAR_011163
Natural varianti1652 – 16521G → R in RDEB; mitis type. 1 Publication
VAR_011164
Natural varianti1703 – 17031G → E in RDEB.
VAR_011165
Natural varianti1772 – 17721R → W in RDEB.
VAR_011166
Natural varianti1782 – 17821G → R in RDEB; mitis type. 1 Publication
VAR_001813
Natural varianti1812 – 18121G → R in RDEB. 1 Publication
VAR_011169
Natural varianti1845 – 18451G → R in RDEB. 1 Publication
VAR_064994
Natural varianti1981 – 19811K → R in RDEB; mild form. 1 Publication
VAR_064995
Natural varianti2009 – 20091G → R in RDEB. 2 Publications
VAR_011173
Natural varianti2025 – 20251G → A in RDEB; mitis type. 1 Publication
VAR_001817
Natural varianti2031 – 20311G → S in RDEB; severe phenotype. 1 Publication
VAR_011177
Natural varianti2069 – 20691R → C in RDEB. 1 Publication
VAR_064996
Natural varianti2073 – 20731G → D in RDEB; mitis type. 1 Publication
VAR_001825
Natural varianti2132 – 21321G → D in RDEB.
VAR_011186
Natural varianti2192 – 21921G → S in RDEB.
VAR_011187
Natural varianti2263 – 22631G → V in RDEB.
VAR_011190
Natural varianti2296 – 22961G → E in RDEB. 1 Publication
VAR_064999
Natural varianti2348 – 23481G → R in DDEB/RDEB; mild form. 1 Publication
VAR_011193
Natural varianti2366 – 23661G → S in RDEB; mitis type. 1 Publication
VAR_011194
Natural varianti2557 – 25571G → R in RDEB. 1 Publication
VAR_065000
Natural varianti2569 – 25691G → R in RDEB; severe and mitis type.
VAR_001830
Natural varianti2622 – 26221R → W in RDEB. 1 Publication
VAR_065001
Natural varianti2653 – 26531G → R in RDEB; mitis type.
VAR_001833
Natural varianti2671 – 26711G → V in RDEB.
VAR_001834
Natural varianti2674 – 26741G → D in RDEB.
VAR_011196
Natural varianti2674 – 26741G → R in RDEB; mitis type.
VAR_001835
Natural varianti2740 – 27401G → A in RDEB.
VAR_011199
Natural varianti2775 – 27751G → S in RDEB; mitis type. 1 Publication
VAR_011200
Epidermolysis bullosa dystrophica, Pasini type (P-DEB) [MIM:131750]: A severe, dominantly inherited form of dystrophic epidermolysis bullosa characterized by albopapuloid Pasini papule, dorsal extremity blistering, milia formation and red atrophic scarring after recurrent blisters.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2037 – 20371G → E in P-DEB. 1 Publication
VAR_011179
Natural varianti2040 – 20401G → S in P-DEB. 1 Publication
VAR_001819
Epidermolysis bullosa dystrophica, Hallopeau-Siemens type (HS-DEB) [MIM:226600]: The most severe recessive form of dystrophic epidermolysis bullosa. It manifests with mutilating scarring, joint contractures, corneal erosions, esophagus structures, and propensity to formation of cutaneous squamous cell carcinomas leading to premature demise of the affected individuals.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1982 – 19821G → W in HS-DEB. 1 Publication
VAR_001814
Natural varianti2008 – 20081R → C in HS-DEB; also in a milder localized type. 2 Publications
VAR_011172
Natural varianti2008 – 20081R → G in HS-DEB. 2 Publications
VAR_001816
Natural varianti2049 – 20491G → E in HS-DEB. 2 Publications
VAR_001821
Natural varianti2063 – 20631R → W in HS-DEB; also in a mild form. 3 Publications
VAR_001823
Natural varianti2575 – 25751G → R in HS-DEB; also in a mild form. 2 Publications
VAR_001831
Natural varianti2749 – 27491G → R in HS-DEB; also in a mild form.
Corresponds to variant rs121912853 [ dbSNP | Ensembl ].
VAR_001836
Natural varianti2798 – 27981M → K in HS-DEB; also in a mild form; the anchoring fibrils may be absent. 1 Publication
VAR_001837
Transient bullous dermolysis of the newborn (TBDN) [MIM:131705]: TBDN 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1519 – 15191G → D in TBDN; compound heterozygous with E-2251; clinically silent when heterozygous with a normal allele. 2 Publications
VAR_011161
Natural varianti2251 – 22511G → E in TBDN; compound heterozygous with D-1519; leads to isolated toenail dystrophy when heterozygous with a normal allele. 1 Publication
VAR_011189
Epidermolysis bullosa dystrophica, pretibial type (PR-DEB) [MIM:131850]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2623 – 26231G → C in PR-DEB; dominant. 1 Publication
VAR_001832
Epidermolysis bullosa dystrophica, Bart type (B-DEB) [MIM:132000]: An autosomal dominant form of dystrophic epidermolysis bullosa characterized by congenital localized absence of skin, skin fragility and deformity of nails.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Epidermolysis bullosa pruriginosa (EBP) [MIM:604129]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1791 – 17911G → E in EBP. 1 Publication
VAR_011168
Natural varianti2028 – 20281G → R in DDEB and EBP. 2 Publications
VAR_011176
Natural varianti2242 – 22421G → R in EBP. 1 Publication
VAR_001828
Natural varianti2369 – 23691G → S in EBP. 1 Publication
VAR_011195
Natural varianti2713 – 27131G → R in EBP. 1 Publication
VAR_011198
Nail disorder, non-syndromic congenital, 8 (NDNC8) [MIM:607523]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1595 – 15951G → R in NDNC8. 1 Publication
VAR_015519
Natural varianti1815 – 18151G → R in NDNC8. 1 Publication
VAR_015520
Epidermolysis bullosa dystrophica, with subcorneal cleavage (EBDSC) [MIM:131750]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2034 – 20341G → R in DDEB and EBDSC; interferes with collagen VII folding and secretion. 4 Publications
VAR_001818

Keywords - Diseasei

Disease mutation, Epidermolysis bullosa

Organism-specific databases

MIMi131705. phenotype.
131750. phenotype.
131850. phenotype.
132000. phenotype.
226600. phenotype.
604129. phenotype.
607523. phenotype.
Orphaneti158673. Acral dystrophic epidermolysis bullosa.
89841. Centripetalis recessive dystrophic epidermolysis bullosa.
89843. Dystrophic epidermolysis bullosa pruriginosa.
158676. Dystrophic epidermolysis bullosa, nails only.
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 other.
79408. Severe generalized recessive dystrophic epidermolysis bullosa.
79411. Transient bullous dermolysis of the newborn.
PharmGKBiPA26730.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616 Reviewed predictionAdd
BLAST
Chaini17 – 29442928Collagen alpha-1(VII) chainPRO_0000005761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi337 – 3371N-linked (GlcNAc...) Reviewed prediction
Glycosylationi786 – 7861N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1109 – 11091N-linked (GlcNAc...) Reviewed prediction
Modified residuei2167 – 216714-hydroxyproline
Modified residuei2176 – 217614-hydroxyproline
Modified residuei2185 – 218514-hydroxyproline
Modified residuei2188 – 218814-hydroxyproline
Modified residuei2625 – 262515-hydroxylysine; alternate
Glycosylationi2625 – 26251O-linked (Gal...); alternate
Modified residuei2631 – 263115-hydroxylysine; alternate
Glycosylationi2631 – 26311O-linked (Gal...); alternate
Disulfide bondi2634 – 2634Interchain Reviewed prediction
Modified residuei2664 – 266414-hydroxyproline
Modified residuei2667 – 266714-hydroxyproline
Modified residuei2673 – 267314-hydroxyproline
Disulfide bondi2802 – 2802Interchain Reviewed prediction
Disulfide bondi2804 – 2804Interchain Reviewed prediction
Disulfide bondi2876 ↔ 2929 By similarity
Disulfide bondi2885 ↔ 2912 By similarity
Disulfide bondi2904 ↔ 2925 By similarity

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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiQ02388.
PaxDbiQ02388.
PRIDEiQ02388.

PTM databases

PhosphoSiteiQ02388.

Expressioni

Gene expression databases

ArrayExpressiQ02388.
BgeeiQ02388.
CleanExiHS_COL7A1.
GenevestigatoriQ02388.

Organism-specific databases

HPAiCAB016357.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

BioGridi107691. 8 interactions.
IntActiQ02388. 6 interactions.
MINTiMINT-1390694.
STRINGi9606.ENSP00000332371.

Structurei

3D structure databases

ProteinModelPortaliQ02388.
SMRiQ02388. Positions 38-215, 233-1041, 1051-1237, 2876-2933.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 211174VWFA 1Add
BLAST
Domaini234 – 32996Fibronectin type-III 1Add
BLAST
Domaini330 – 41687Fibronectin type-III 2Add
BLAST
Domaini417 – 50791Fibronectin type-III 3Add
BLAST
Domaini510 – 59788Fibronectin type-III 4Add
BLAST
Domaini600 – 68788Fibronectin type-III 5Add
BLAST
Domaini688 – 77588Fibronectin type-III 6Add
BLAST
Domaini778 – 86689Fibronectin type-III 7Add
BLAST
Domaini869 – 95789Fibronectin type-III 8Add
BLAST
Domaini958 – 105194Fibronectin type-III 9Add
BLAST
Domaini1054 – 1229176VWFA 2Add
BLAST
Domaini2872 – 294473BPTI/Kunitz inhibitorAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni17 – 12531237Nonhelical region (NC1)Add
BLAST
Regioni1254 – 27841531Triple-helical regionAdd
BLAST
Regioni1254 – 1477224Interrupted collagenous regionAdd
BLAST
Regioni2785 – 2944160Nonhelical region (NC2)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1170 – 11723Cell attachment site Reviewed prediction
Motifi1334 – 13363Cell attachment site Reviewed prediction
Motifi2008 – 20103Cell attachment site Reviewed prediction
Motifi2553 – 25553Cell attachment site Reviewed prediction

Sequence similaritiesi

Contains 2 VWFA domains.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000111866.
HOVERGENiHBG051053.
InParanoidiQ02388.
KOiK16628.
OMAiWHSGHGP.
OrthoDBiEOG7CG6Z4.
PhylomeDBiQ02388.
TreeFamiTF351645.

Family and domain databases

Gene3Di2.60.40.10. 9 hits.
3.40.50.410. 2 hits.
4.10.410.10. 1 hit.
InterProiIPR008160. Collagen.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01391. Collagen. 18 hits.
PF00041. fn3. 9 hits.
PF00014. Kunitz_BPTI. 1 hit.
PF00092. VWA. 2 hits.
[Graphical view]
PRINTSiPR00759. BASICPTASE.
SMARTiSM00060. FN3. 9 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 5 hits.
SSF53300. SSF53300. 2 hits.
SSF57362. SSF57362. 1 hit.
PROSITEiPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
PS50853. FN3. 9 hits.
PS50234. VWFA. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

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.

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MTLRLLVAAL CAGILAEAPR VRAQHRERVT CTRLYAADIV FLLDGSSSIG     50
RSNFREVRSF LEGLVLPFSG AASAQGVRFA TVQYSDDPRT EFGLDALGSG 100
GDVIRAIREL SYKGGNTRTG AAILHVADHV FLPQLARPGV PKVCILITDG 150
KSQDLVDTAA QRLKGQGVKL FAVGIKNADP EELKRVASQP TSDFFFFVND 200
FSILRTLLPL VSRRVCTTAG GVPVTRPPDD STSAPRDLVL SEPSSQSLRV 250
QWTAASGPVT GYKVQYTPLT GLGQPLPSER QEVNVPAGET SVRLRGLRPL 300
TEYQVTVIAL YANSIGEAVS GTARTTALEG PELTIQNTTA HSLLVAWRSV 350
PGATGYRVTW RVLSGGPTQQ QELGPGQGSV LLRDLEPGTD YEVTVSTLFG 400
RSVGPATSLM ARTDASVEQT LRPVILGPTS ILLSWNLVPE ARGYRLEWRR 450
ETGLEPPQKV VLPSDVTRYQ LDGLQPGTEY RLTLYTLLEG HEVATPATVV 500
PTGPELPVSP VTDLQATELP GQRVRVSWSP VPGATQYRII VRSTQGVERT 550
LVLPGSQTAF DLDDVQAGLS YTVRVSARVG PREGSASVLT VRREPETPLA 600
VPGLRVVVSD ATRVRVAWGP VPGASGFRIS WSTGSGPESS QTLPPDSTAT 650
DITGLQPGTT YQVAVSVLRG REEGPAAVIV ARTDPLGPVR TVHVTQASSS 700
SVTITWTRVP GATGYRVSWH SAHGPEKSQL VSGEATVAEL DGLEPDTEYT 750
VHVRAHVAGV DGPPASVVVR TAPEPVGRVS RLQILNASSD VLRITWVGVT 800
GATAYRLAWG RSEGGPMRHQ ILPGNTDSAE IRGLEGGVSY SVRVTALVGD 850
REGTPVSIVV TTPPEAPPAL GTLHVVQRGE HSLRLRWEPV PRAQGFLLHW 900
QPEGGQEQSR VLGPELSSYH LDGLEPATQY RVRLSVLGPA GEGPSAEVTA 950
RTESPRVPSI ELRVVDTSID SVTLAWTPVS RASSYILSWR PLRGPGQEVP 1000
GSPQTLPGIS SSQRVTGLEP GVSYIFSLTP VLDGVRGPEA SVTQTPVCPR 1050
GLADVVFLPH ATQDNAHRAE ATRRVLERLV LALGPLGPQA VQVGLLSYSH 1100
RPSPLFPLNG SHDLGIILQR IRDMPYMDPS GNNLGTAVVT AHRYMLAPDA 1150
PGRRQHVPGV MVLLVDEPLR GDIFSPIREA QASGLNVVML GMAGADPEQL 1200
RRLAPGMDSV QTFFAVDDGP SLDQAVSGLA TALCQASFTT QPRPEPCPVY 1250
CPKGQKGEPG EMGLRGQVGP PGDPGLPGRT GAPGPQGPPG SATAKGERGF 1300
PGADGRPGSP GRAGNPGTPG APGLKGSPGL PGPRGDPGER GPRGPKGEPG 1350
APGQVIGGEG PGLPGRKGDP GPSGPPGPRG PLGDPGPRGP PGLPGTAMKG 1400
DKGDRGERGP PGPGEGGIAP GEPGLPGLPG SPGPQGPVGP PGKKGEKGDS 1450
EDGAPGLPGQ PGSPGEQGPR GPPGAIGPKG DRGFPGPLGE AGEKGERGPP 1500
GPAGSRGLPG VAGRPGAKGP EGPPGPTGRQ GEKGEPGRPG DPAVVGPAVA 1550
GPKGEKGDVG PAGPRGATGV QGERGPPGLV LPGDPGPKGD PGDRGPIGLT 1600
GRAGPPGDSG PPGEKGDPGR PGPPGPVGPR GRDGEVGEKG DEGPPGDPGL 1650
PGKAGERGLR GAPGVRGPVG EKGDQGDPGE DGRNGSPGSS GPKGDRGEPG 1700
PPGPPGRLVD TGPGAREKGE PGDRGQEGPR GPKGDPGLPG APGERGIEGF 1750
RGPPGPQGDP GVRGPAGEKG DRGPPGLDGR SGLDGKPGAA GPSGPNGAAG 1800
KAGDPGRDGL PGLRGEQGLP GPSGPPGLPG KPGEDGKPGL NGKNGEPGDP 1850
GEDGRKGEKG DSGASGREGR DGPKGERGAP GILGPQGPPG LPGPVGPPGQ 1900
GFPGVPGGTG PKGDRGETGS KGEQGLPGER GLRGEPGSVP NVDRLLETAG 1950
IKASALREIV ETWDESSGSF LPVPERRRGP KGDSGEQGPP GKEGPIGFPG 2000
ERGLKGDRGD PGPQGPPGLA LGERGPPGPS GLAGEPGKPG IPGLPGRAGG 2050
VGEAGRPGER GERGEKGERG EQGRDGPPGL PGTPGPPGPP GPKVSVDEPG 2100
PGLSGEQGPP GLKGAKGEPG SNGDQGPKGD RGVPGIKGDR GEPGPRGQDG 2150
NPGLPGERGM AGPEGKPGLQ GPRGPPGPVG GHGDPGPPGA PGLAGPAGPQ 2200
GPSGLKGEPG ETGPPGRGLT GPTGAVGLPG PPGPSGLVGP QGSPGLPGQV 2250
GETGKPGAPG RDGASGKDGD RGSPGVPGSP GLPGPVGPKG EPGPTGAPGQ 2300
AVVGLPGAKG EKGAPGGLAG DLVGEPGAKG DRGLPGPRGE KGEAGRAGEP 2350
GDPGEDGQKG APGPKGFKGD PGVGVPGSPG PPGPPGVKGD LGLPGLPGAP 2400
GVVGFPGQTG PRGEMGQPGP SGERGLAGPP GREGIPGPLG PPGPPGSVGP 2450
PGASGLKGDK GDPGVGLPGP RGERGEPGIR GEDGRPGQEG PRGLTGPPGS 2500
RGERGEKGDV GSAGLKGDKG DSAVILGPPG PRGAKGDMGE RGPRGLDGDK 2550
GPRGDNGDPG DKGSKGEPGD KGSAGLPGLR GLLGPQGQPG AAGIPGDPGS 2600
PGKDGVPGIR GEKGDVGFMG PRGLKGERGV KGACGLDGEK GDKGEAGPPG 2650
RPGLAGHKGE MGEPGVPGQS GAPGKEGLIG PKGDRGFDGQ PGPKGDQGEK 2700
GERGTPGIGG FPGPSGNDGS AGPPGPPGSV GPRGPEGLQG QKGERGPPGE 2750
RVVGAPGVPG APGERGEQGR PGPAGPRGEK GEAALTEDDI RGFVRQEMSQ 2800
HCACQGQFIA SGSRPLPSYA ADTAGSQLHA VPVLRVSHAE EEERVPPEDD 2850
EYSEYSEYSV EEYQDPEAPW DSDDPCSLPL DEGSCTAYTL RWYHRAVTGS 2900
TEACHPFVYG GCGGNANRFG TREACERRCP PRVVQSQGTG TAQD 2944
Length:2,944
Mass (Da):295,220
Last modified:February 1, 1996 - v2
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

Sequence cautioni

The sequence BAA02853.1 differs from that shown. Reason: Frameshift at positions 275, 282, 476, 494, 523, 541 and 543.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti119 – 1191T → P in a breast cancer sample; somatic mutation. 1 Publication
VAR_035740
Natural varianti142 – 1421K → R in RDEB.
VAR_001809
Natural varianti547 – 5471V → F.
Corresponds to variant rs2229823 [ dbSNP | Ensembl ].
VAR_048765
Natural varianti595 – 5951P → L in RDEB.
Corresponds to variant rs2228561 [ dbSNP | Ensembl ].
VAR_001810
Natural varianti1120 – 11201R → K.
Corresponds to variant rs2228563 [ dbSNP | Ensembl ].
VAR_048766
Natural varianti1277 – 12771P → L in RDEB.
Corresponds to variant rs35761247 [ dbSNP | Ensembl ].
VAR_001811
Natural varianti1347 – 13471G → R in RDEB; localized type; mild. 1 Publication
VAR_011160
Natural varianti1364 – 13641P → T in a breast cancer sample; somatic mutation. 1 Publication
VAR_035741
Natural varianti1366 – 13661R → W in a breast cancer sample; somatic mutation. 1 Publication
VAR_035742
Natural varianti1519 – 15191G → D in TBDN; compound heterozygous with E-2251; clinically silent when heterozygous with a normal allele. 2 Publications
VAR_011161
Natural varianti1522 – 15221G → E in DDEB.
VAR_011162
Natural varianti1557 – 15571G → R in DDEB.
VAR_001812
Natural varianti1595 – 15951G → R in NDNC8. 1 Publication
VAR_015519
Natural varianti1604 – 16041G → R in RDEB.
VAR_011163
Natural varianti1652 – 16521G → R in RDEB; mitis type. 1 Publication
VAR_011164
Natural varianti1703 – 17031G → E in RDEB.
VAR_011165
Natural varianti1772 – 17721R → W in RDEB.
VAR_011166
Natural varianti1776 – 17761G → R in DDEB.
VAR_011167
Natural varianti1782 – 17821G → R in RDEB; mitis type. 1 Publication
VAR_001813
Natural varianti1791 – 17911G → E in EBP. 1 Publication
VAR_011168
Natural varianti1812 – 18121G → R in RDEB. 1 Publication
VAR_011169
Natural varianti1815 – 18151G → R in NDNC8. 1 Publication
VAR_015520
Natural varianti1845 – 18451G → R in RDEB. 1 Publication
VAR_064994
Natural varianti1981 – 19811K → R in RDEB; mild form. 1 Publication
VAR_064995
Natural varianti1982 – 19821G → W in HS-DEB. 1 Publication
VAR_001814
Natural varianti2003 – 20031G → R in DDEB. 1 Publication
VAR_001815
Natural varianti2006 – 20061G → A in DDEB.
VAR_011170
Natural varianti2006 – 20061G → D in DDEB; interferes with collagen VII folding and secretion. 2 Publications
VAR_011171
Natural varianti2008 – 20081R → C in HS-DEB; also in a milder localized type. 2 Publications
VAR_011172
Natural varianti2008 – 20081R → G in HS-DEB. 2 Publications
VAR_001816
Natural varianti2009 – 20091G → R in RDEB. 2 Publications
VAR_011173
Natural varianti2015 – 20151G → E in DDEB; interferes with collagen VII folding and secretion. 2 Publications
VAR_011174
Natural varianti2025 – 20251G → A in RDEB; mitis type. 1 Publication
VAR_001817
Natural varianti2028 – 20281G → A in DDEB. 1 Publication
VAR_011175
Natural varianti2028 – 20281G → R in DDEB and EBP. 2 Publications
VAR_011176
Natural varianti2031 – 20311G → S in RDEB; severe phenotype. 1 Publication
VAR_011177
Natural varianti2034 – 20341G → R in DDEB and EBDSC; interferes with collagen VII folding and secretion. 4 Publications
VAR_001818
Natural varianti2034 – 20341G → W in DDEB. 2 Publications
VAR_011178
Natural varianti2037 – 20371G → E in P-DEB. 1 Publication
VAR_011179
Natural varianti2040 – 20401G → D in DDEB. 1 Publication
VAR_011180
Natural varianti2040 – 20401G → S in P-DEB. 1 Publication
VAR_001819
Natural varianti2040 – 20401G → V in DDEB. 1 Publication
VAR_011181
Natural varianti2043 – 20431G → R in DDEB. 5 Publications
VAR_001820
Natural varianti2043 – 20431G → W in DDEB; localized type. 1 Publication
VAR_011182
Natural varianti2046 – 20461G → V in DDEB.
VAR_011183
Natural varianti2049 – 20491G → E in HS-DEB. 2 Publications
VAR_001821
Natural varianti2055 – 20551G → E in DDEB.
VAR_001822
Natural varianti2063 – 20631R → W in HS-DEB; also in a mild form. 3 Publications
VAR_001823
Natural varianti2064 – 20641G → R in DDEB. 2 Publications
VAR_011184
Natural varianti2069 – 20691R → C in RDEB. 1 Publication
VAR_064996
Natural varianti2070 – 20701G → R in DDEB. 1 Publication
VAR_064997
Natural varianti2073 – 20731G → D in RDEB; mitis type. 1 Publication
VAR_001825
Natural varianti2076 – 20761G → D in DDEB; also in recessive forms. 1 Publication
VAR_001826
Natural varianti2079 – 20791G → E in DDEB. 1 Publication
VAR_001827
Natural varianti2079 – 20791G → R in DDEB; associated with squamous cell carcinoma. 1 Publication
VAR_011185
Natural varianti2132 – 21321G → D in RDEB.
VAR_011186
Natural varianti2192 – 21921G → S in RDEB.
VAR_011187
Natural varianti2207 – 22071G → R in DDEB. 1 Publication
VAR_011188
Natural varianti2221 – 22211G → A in a patient with recessive dystrophic epidermolysis bullosa. 1 Publication
VAR_064998
Natural varianti2242 – 22421G → R in EBP. 1 Publication
VAR_001828
Natural varianti2251 – 22511G → E in TBDN; compound heterozygous with D-1519; leads to isolated toenail dystrophy when heterozygous with a normal allele. 1 Publication
VAR_011189
Natural varianti2263 – 22631G → V in RDEB.
VAR_011190
Natural varianti2287 – 22871G → R in a compound heterozygote affected by moderately severe dystrophic epidermolysis bullosa; in combination with R-2316; leads to isolated toenail dystrophy when heterozygous with a normal allele. 1 Publication
VAR_011191
Natural varianti2296 – 22961G → E in RDEB. 1 Publication
VAR_064999
Natural varianti2316 – 23161G → R in a compound heterozygote affected by moderately severe dystrophic epidermolysis bullosa; in combination with R-2287. 1 Publication
VAR_011192
Natural varianti2348 – 23481G → R in DDEB/RDEB; mild form. 1 Publication
VAR_011193
Natural varianti2351 – 23511G → R in a patient with dystrophic epidermolysis bullosa; mitis type.
Corresponds to variant rs1800013 [ dbSNP | Ensembl ].
VAR_001829
Natural varianti2366 – 23661G → S in RDEB; mitis type. 1 Publication
VAR_011194
Natural varianti2369 – 23691G → S in EBP. 1 Publication
VAR_011195
Natural varianti2429 – 24291P → L.
Corresponds to variant rs2229822 [ dbSNP | Ensembl ].
VAR_033786
Natural varianti2557 – 25571G → R in RDEB. 1 Publication
VAR_065000
Natural varianti2569 – 25691G → R in RDEB; severe and mitis type.
VAR_001830
Natural varianti2575 – 25751G → R in HS-DEB; also in a mild form. 2 Publications
VAR_001831
Natural varianti2622 – 26221R → W in RDEB. 1 Publication
VAR_065001
Natural varianti2623 – 26231G → C in PR-DEB; dominant. 1 Publication
VAR_001832
Natural varianti2653 – 26531G → R in RDEB; mitis type.
VAR_001833
Natural varianti2671 – 26711G → V in RDEB.
VAR_001834
Natural varianti2674 – 26741G → D in RDEB.
VAR_011196
Natural varianti2674 – 26741G → R in RDEB; mitis type.
VAR_001835
Natural varianti2713 – 27131G → D in DDEB. 1 Publication
VAR_011197
Natural varianti2713 – 27131G → R in EBP. 1 Publication
VAR_011198
Natural varianti2740 – 27401G → A in RDEB.
VAR_011199
Natural varianti2749 – 27491G → R in HS-DEB; also in a mild form.
Corresponds to variant rs121912853 [ dbSNP | Ensembl ].
VAR_001836
Natural varianti2775 – 27751G → S in RDEB; mitis type. 1 Publication
VAR_011200
Natural varianti2791 – 27911R → W in DDEB.
Corresponds to variant rs142566193 [ dbSNP | Ensembl ].
VAR_011201
Natural varianti2798 – 27981M → K in HS-DEB; also in a mild form; the anchoring fibrils may be absent. 1 Publication
VAR_001837

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1869 – 190032Missing in isoform 2. VSP_024026Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1973FFF → EFR in BAA02853. 1 Publication
Sequence conflicti369 – 3713QQQ → EFR in AAA36357. 1 Publication
Sequence conflicti369 – 3713QQQ → EFR in AAB24637. 1 Publication
Sequence conflicti518 – 5192EL → DV in AAA36357. 1 Publication
Sequence conflicti518 – 5192EL → DV in AAB24637. 1 Publication
Sequence conflicti529 – 5291S → C in BAA02853. 1 Publication
Sequence conflicti541 – 5411V → W in AAA36357. 1 Publication
Sequence conflicti541 – 5411V → W in AAB24637. 1 Publication
Sequence conflicti851 – 8511R → H in BAA02853. 1 Publication
Sequence conflicti893 – 8931A → E in AAA58965. 1 Publication
Sequence conflicti893 – 8931A → E in BAA02853. 1 Publication
Sequence conflicti893 – 8931A → E in AAA96439. 1 Publication
Sequence conflicti1122 – 11221R → L in BAA02853. 1 Publication
Sequence conflicti1463 – 14642SP → LR AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
UniGeneiHs.476218.

Genome annotation databases

EnsembliENST00000328333; ENSP00000332371; ENSG00000114270. [Q02388-1]
ENST00000454817; ENSP00000412569; ENSG00000114270. [Q02388-2]
GeneIDi1294.
KEGGihsa:1294.
UCSCiuc003ctz.2. human. [Q02388-1]

Polymorphism databases

DMDMi1345650.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2773.1. [Q02388-1 ]
PIRi A54849.
RefSeqi NP_000085.1. NM_000094.3. [Q02388-1 ]
UniGenei Hs.476218.

3D structure databases

ProteinModelPortali Q02388.
SMRi Q02388. Positions 38-215, 233-1041, 1051-1237, 2876-2933.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107691. 8 interactions.
IntActi Q02388. 6 interactions.
MINTi MINT-1390694.
STRINGi 9606.ENSP00000332371.

Protein family/group databases

MEROPSi I02.967.

PTM databases

PhosphoSitei Q02388.

Polymorphism databases

DMDMi 1345650.

Proteomic databases

MaxQBi Q02388.
PaxDbi Q02388.
PRIDEi Q02388.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000328333 ; ENSP00000332371 ; ENSG00000114270 . [Q02388-1 ]
ENST00000454817 ; ENSP00000412569 ; ENSG00000114270 . [Q02388-2 ]
GeneIDi 1294.
KEGGi hsa:1294.
UCSCi uc003ctz.2. human. [Q02388-1 ]

Organism-specific databases

CTDi 1294.
GeneCardsi GC03M048576.
GeneReviewsi COL7A1.
HGNCi HGNC:2214. COL7A1.
HPAi CAB016357.
MIMi 120120. gene.
131705. phenotype.
131750. phenotype.
131850. phenotype.
132000. phenotype.
226600. phenotype.
604129. phenotype.
607523. phenotype.
neXtProti NX_Q02388.
Orphaneti 158673. Acral dystrophic epidermolysis bullosa.
89841. Centripetalis recessive dystrophic epidermolysis bullosa.
89843. Dystrophic epidermolysis bullosa pruriginosa.
158676. Dystrophic epidermolysis bullosa, nails only.
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 other.
79408. Severe generalized recessive dystrophic epidermolysis bullosa.
79411. Transient bullous dermolysis of the newborn.
PharmGKBi PA26730.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000111866.
HOVERGENi HBG051053.
InParanoidi Q02388.
KOi K16628.
OMAi WHSGHGP.
OrthoDBi EOG7CG6Z4.
PhylomeDBi Q02388.
TreeFami TF351645.

Enzyme and pathway databases

Reactomei REACT_118779. Extracellular matrix organization.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150268. Anchoring fibril formation.
REACT_150401. Collagen degradation.
REACT_169262. Laminin interactions.

Miscellaneous databases

ChiTaRSi COL7A1. human.
GeneWikii Collagen,_type_VII,_alpha_1.
GenomeRNAii 1294.
NextBioi 5251.
PROi Q02388.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q02388.
Bgeei Q02388.
CleanExi HS_COL7A1.
Genevestigatori Q02388.

Family and domain databases

Gene3Di 2.60.40.10. 9 hits.
3.40.50.410. 2 hits.
4.10.410.10. 1 hit.
InterProi IPR008160. Collagen.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
IPR002035. VWF_A.
[Graphical view ]
Pfami PF01391. Collagen. 18 hits.
PF00041. fn3. 9 hits.
PF00014. Kunitz_BPTI. 1 hit.
PF00092. VWA. 2 hits.
[Graphical view ]
PRINTSi PR00759. BASICPTASE.
SMARTi SM00060. FN3. 9 hits.
SM00327. VWA. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 5 hits.
SSF53300. SSF53300. 2 hits.
SSF57362. SSF57362. 1 hit.
PROSITEi PS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
PS50853. FN3. 9 hits.
PS50234. VWFA. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural organization of the human type VII collagen gene (COL7A1), composed of more exons than any previously characterized gene."
    Christiano A.M., Hoffman G.G., Chung-Honet L.C., Lee S., Cheng W., Uitto J., Greenspan D.S.
    Genomics 21:169-179(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
    Tissue: Placenta.
  2. "Cloning of human type VII collagen. Complete primary sequence of the alpha 1(VII) chain and identification of intragenic polymorphisms."
    Christiano A.M., Greenspan D.S., Lee S., Uitto J.
    J. Biol. Chem. 269:20256-20262(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The large non-collagenous domain (NC-1) of type VII collagen is amino-terminal and chimeric. Homology to cartilage matrix protein, the type III domains of fibronectin and the A domains of von Willebrand factor."
    Christiano A.M., Rosenbaum L.M., Chung-Honet L.C., Parente M.G., Woodley D.T., Pan T.C., Zhang R.Z., Chu M.-L., Burgeson R.E., Uitto J.
    Hum. Mol. Genet. 1:475-481(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 128-1493, PARTIAL PROTEIN SEQUENCE.
  4. "Molecular cloning and characterization of type VII collagen cDNA."
    Tanaka T., Takahashi K., Furukawa F., Imamura S.
    Biochem. Biophys. Res. Commun. 183:958-963(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 195-1275.
    Tissue: Keratinocyte.
  5. "Noncollagenous (NC1) domain of collagen VII resembles multidomain adhesion proteins involved in tissue-specific organization of extracellular matrix."
    Gammon W.R., Abernethy M.L., Padilla K.M., Prisayanh P.S., Cook M.E., Wright J., Briggaman R.A., Hunt S.W. III
    J. Invest. Dermatol. 99:691-696(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 369-1255.
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 815-1439.
  7. "The carboxyl-terminal half of type VII collagen, including the non-collagenous NC-2 domain and intron/exon organization of the corresponding region of the COL7A1 gene."
    Greenspan D.S.
    Hum. Mol. Genet. 2:273-278(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2395-2944.
  8. "Cleavage of type VII collagen by interstitial collagenase and type IV collagenase (gelatinase) derived from human skin."
    Seltzer J.L., Eisen A.Z., Bauer E.A., Morris N.P., Glanville R.W., Burgeson R.E.
    J. Biol. Chem. 264:3822-3826(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, HYDROXYLATION.
  9. "TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites."
    Saito K., Chen M., Bard F., Chen S., Zhou H., Woodley D., Polischuk R., Schekman R., Malhotra V.
    Cell 136:891-902(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MIA3.
  10. "Molecular basis of dystrophic epidermolysis bullosa: mutations in the type VII collagen gene (COL7A1)."
    Jaervikallio A., Pulkkinen L., Uitto J.
    Hum. Mutat. 10:338-347(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Epidermolysis bullosa simplex superficialis. A new variant of epidermolysis bullosa characterized by subcorneal skin cleavage mimicking peeling skin syndrome."
    Fine J.-D., Johnson L., Wright T.
    Arch. Dermatol. 125:633-638(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EBDSC ARG-2034.
  13. "A missense mutation in type VII collagen in two affected siblings with recessive dystrophic epidermolysis bullosa."
    Christiano A.M., Greenspan D.S., Hoffman G.G., Zhang X., Tamai Y., Lin A.N., Dietz H.C., Hovnanian A., Uitto J.
    Nat. Genet. 4:62-66(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HS-DEB LYS-2798.
  14. "Dominant dystrophic epidermolysis bullosa: identification of a Gly-->Ser substitution in the triple-helical domain of type VII collagen."
    Christiano A.M., Ryynaenen M., Uitto J.
    Proc. Natl. Acad. Sci. U.S.A. 91:3549-3553(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT P-DEB SER-2040.
  15. "Pretibial epidermolysis bullosa: genetic linkage to COL7A1 and identification of a glycine-to-cysteine substitution in the triple-helical domain of type VII collagen."
    Christiano A.M., Lee J.Y.-Y., Chen W.J., Laforgia S., Uitto J.
    Hum. Mol. Genet. 4:1579-1583(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PR-DEB CYS-2623.
  16. "A glycine-to-arginine substitution in the triple-helical domain of type VII collagen in a family with dominant dystrophic epidermolysis bullosa."
    Christiano A.M., Morricone A., Paradisi M., Angelo C., Mazzanti C., Cavalieri R., Uitto J.
    J. Invest. Dermatol. 104:438-440(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DDEB ARG-2043.
  17. "Glycine substitutions in the triple-helical region of type VII collagen result in a spectrum of dystrophic epidermolysis bullosa phenotypes and patterns of inheritance."
    Christiano A.M., McGrath J.A., Tan K.C., Uitto J.
    Am. J. Hum. Genet. 58:671-681(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DEB.
  18. "Molecular basis of recessive dystrophic epidermolysis bullosa: genotype/phenotype correlation in a case of moderate clinical severity."
    Shimizu H., McGrath J.A., Christiano A.M., Nishikawa T., Uitto J.
    J. Invest. Dermatol. 106:119-124(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HS-DEB ARG-2575.
  19. "Influence of the second COL7A1 mutation in determining the phenotypic severity of recessive dystrophic epidermolysis bullosa."
    Christiano A.M., McGrath J.A., Uitto J.
    J. Invest. Dermatol. 106:766-770(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RDEB ARG-1782.
  20. "Clinicopathological correlations of compound heterozygous COL7A1 mutations in recessive dystrophic epidermolysis bullosa."
    Dunnill M.G.S., McGrath J.A., Richards A.J., Christiano A.M., Uitto J., Pope F.M., Eady R.A.J.
    J. Invest. Dermatol. 107:171-177(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RDEB ASP-2073.
  21. "Characterization of 18 new mutations in COL7A1 in recessive dystrophic epidermolysis bullosa provides evidence for distinct molecular mechanisms underlying defective anchoring fibril formation."
    Hovnanian A., Rochat A., Bodemer C., Petit E., Rivers C.A., Prost C., Fraitag S., Christiano A.M., Uitto J., Lathrop M., Barrandon Y., de Prost Y.
    Am. J. Hum. Genet. 61:599-610(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HS-DEB TRP-1982; GLY-2008; ALA-2025; GLU-2049; TRP-2063 AND ARG-2575.
  22. "Identification of a glycine substitution and a splice site mutation in the type VII collagen gene in a proband with mitis recessive dystrophic epidermolysis bullosa."
    Cserhalmi-Friedman P.B., Karpati S., Horvath A., Christiano A.M.
    Arch. Dermatol. Res. 289:640-645(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RDEB ARG-1652.
  23. "Modulation of disease severity of dystrophic epidermolysis bullosa by a splice site mutation in combination with a missense mutation in the COL7A1 gene."
    Winberg J.-O., Hammami-Hauasli N., Nilssen O., Anton-Lamprecht I., Naylor S.L., Kerbacher K., Zimmermann M., Krajci P., Gedde-Dahl T. Jr., Bruckner-Tuderman L.
    Hum. Mol. Genet. 6:1125-1135(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RDEB ARG-2009, VARIANT DDEB ARG-2043.
  24. "Some, but not all, glycine substitution mutations in COL7A1 result in intracellular accumulation of collagen VII, loss of anchoring fibrils, and skin blistering."
    Hammami-Hauasli N., Schumann H., Raghunath M., Kilgus O., Luethi U., Luger T., Bruckner-Tuderman L.
    J. Biol. Chem. 273:19228-19234(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DDEB ASP-1519; ASP-2006; GLU-2015 AND ARG-2034.
  25. "Novel COL7A1 mutations in dystrophic forms of epidermolysis bullosa."
    Kon A., Pulkkinen L., Ishida-Yamamoto A., Hashimoto I., Uitto J.
    J. Invest. Dermatol. 111:534-537(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HS-DEB CYS-2008, VARIANT DDEB ARG-2207, VARIANT RDEB SER-2775.
  26. "Compound heterozygosity for a recessive glycine substitution and a splice site mutation in the COL7A1 gene causes an unusually mild form of localized recessive dystrophic epidermolysis bullosa."
    Terracina M., Posteraro P., Schubert M., Sonego G., Atzori F., Zambruno G., Bruckner-Tuderman L., Castiglia D.
    J. Invest. Dermatol. 111:744-750(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RDEB ARG-1347.
  27. "Novel and de novo glycine substitution mutations in the type VII collagen gene (COL7A1) in dystrophic epidermolysis bullosa: implications for genetic counseling."
    Rouan F., Pulkkinen L., Jonkman M.F., Bauer J.W., Cserhalmi-Friedman P.B., Christiano A.M., Uitto J.
    J. Invest. Dermatol. 111:1210-1213(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DDEB TRP-2034; VAL-2040; ARG-2043; ARG-2064 AND ASP-2713.
  28. "Transient bullous dermolysis of the newborn associated with compound heterozygosity for recessive and dominant COL7A1 mutations."
    Hammami-Hauasli N., Raghunath M., Kuester W., Bruckner-Tuderman L.
    J. Invest. Dermatol. 111:1214-1219(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TBDN ASP-1519 AND GLU-2251.
  29. "Diagnostic dilemma of 'sporadic' cases of dystrophic epidermolysis bullosa: a new dominant or mitis recessive mutation?"
    Hashimoto I., Kon A., Tamai K., Uitto J.
    Exp. Dermatol. 8:140-142(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DDEB/RDEB TRP-2063 AND SER-2366, VARIANT DDEB GLU-2079.
  30. "Identification of a de novo glycine substitution in the type VII collagen gene in a proband with mild dystrophic epidermolysis bullosa."
    Cserhalmi-Friedman P.B., Grossman J., Karpati S., Ahmad W., Horvath A., Christiano A.M.
    Exp. Dermatol. 8:143-145(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DDEB/RDEB ARG-2348.
  31. "Squamous cell carcinoma in a family with dominant dystrophic epidermolysis bullosa: a molecular genetic study."
    Christiano A.M., Crollick J., Pincus S., Uitto J.
    Exp. Dermatol. 8:146-152(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DDEB ARG-2079.
  32. "Clustering of COL7A1 mutations in exon 73: implications for mutation analysis in dystrophic epidermolysis bullosa."
    Mecklenbeck S., Hammami-Hauasli N., Hoepfner B., Schumann H., Kramer A., Kuester W., Bruckner-Tuderman L.
    J. Invest. Dermatol. 112:398-400(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DDEB ASP-2006; GLU-2015; ARG-2034; TRP-2034; ARG-2043 AND TRP-2043, VARIANTS HS-DEB CYS-2008 AND GLY-2008, VARIANT RDEB ARG-2009.
  33. "Dominant dystrophic epidermolysis bullosa (Pasini) caused by a novel glycine substitution mutation in the type VII collagen gene (COL7A1)."
    Jonkman M.F., Moreno G., Rouan F., Oranje A.P., Pulkkinen L., Uitto J.
    J. Invest. Dermatol. 112:815-817(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT P-DEB GLU-2037.
  34. Cited for: VARIANTS EBP GLU-1791; ARG-2242; SER-2369 AND ARG-2713.
  35. "Compound heterozygosity for silent and dominant glycine substitution mutations in COL7A1 leads to a marked transient intracytoplasmic retention of procollagen VII and a moderately severe dystrophic epidermolysis bullosa phenotype."
    Shimizu H., Hammami-Hauasli N., Hatta N., Nishikawa T., Bruckner-Tuderman L.
    J. Invest. Dermatol. 113:419-421(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARG-2287 AND ARG-2316.
  36. "Comparative mutation detection screening of the type VII collagen gene (COL7A1) using the protein truncation test, fluorescent chemical cleavage of mismatch, and conformation sensitive gel electrophoresis."
    Whittock N.V., Ashton G.H.S., Mohammedi R., Mellerio J.E., Mathew C.G., Abbs S.J., Eady R.A.J., McGrath J.A.
    J. Invest. Dermatol. 113:673-686(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DEB.
  37. "A de novo glycine substitution mutation in the collagenous domain of COL7A1 in dominant dystrophic epidermolysis bullosa."
    Lee J.Y.-Y., Li C., Chao S.-C., Pulkkinen L., Uitto J.
    Arch. Dermatol. Res. 292:159-163(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DDEB ARG-2028.
  38. "Glycine substitution mutations by different amino acids in the same codon of COL7A1 lead to heterogeneous clinical phenotypes of dominant dystrophic epidermolysis bullosa."
    Murata T., Masunaga T., Shimizu H., Takizawa Y., Ishiko A., Hatta N., Nishikawa T.
    Arch. Dermatol. Res. 292:477-481(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DDEB ALA-2028, VARIANT EBP ARG-2028.
  39. "Combination of novel premature termination codon and glycine substitution mutations in COL7A1 leads to moderately severe recessive dystrophic epidermolysis bullosa."
    Masunaga T., Shimizu H., Takizawa Y., Uitto J., Nishikawa T.
    J. Invest. Dermatol. 114:204-205(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RDEB ARG-1812.
  40. "Generalized dystrophic epidermolysis bullosa: identification of a novel, homozygous glycine substitution, G2031S, in exon 73 of COL7A1 in monozygous triplets."
    Nordal E.J., Mecklenbeck S., Hausser I., Skranes J., Bruckner-Tuderman L., Gedde-Dahl T. Jr.
    Br. J. Dermatol. 144:151-157(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RDEB SER-2031.
  41. "Toenail dystrophy with COL7A1 glycine substitution mutations segregates as an autosomal dominant trait in 2 families with dystrophic epidermolysis bullosa."
    Sato-Matsumura K.C., Yasukawa K., Tomita Y., Shimizu H.
    Arch. Dermatol. 138:269-271(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS NDNC8 ARG-1595 AND ARG-1815.
  42. "EB simplex superficialis resulting from a mutation in the type VII collagen gene."
    Martinez-Mir A., Liu J., Gordon D., Weiner M.S., Ahmad W., Fine J.D., Ott J., Gilliam T.C., Christiano A.M.
    J. Invest. Dermatol. 118:547-549(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EBDSC ARG-2034.
  43. Cited for: VARIANTS [LARGE SCALE ANALYSIS] PRO-119; THR-1364 AND TRP-1366.
  44. "Novel human pathological mutations. Gene symbol: COL7A1. Disease: Epidermolysis bullosa dystrophica."
    Garcia M., Escamez M.J., Cuadrado-Corrales N., Sanchez-Jimeno C., Illera N., Lopez-Martinez M.A., Trujillo-Tiebas M.J., Ayuso C., Del Rio M.
    Hum. Genet. 127:116-117(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ALA-2221.
  45. "Analysis of the COL7A1 gene in Czech patients with dystrophic epidermolysis bullosa reveals novel and recurrent mutations."
    Jerabkova B., Kopeckova L., Buckova H., Vesely K., Valickova J., Fajkusova L.
    J. Dermatol. Sci. 59:136-140(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS RDEB ARG-1845; ARG-1981; GLU-2049; TRP-2063; CYS-2069; GLU-2296; ARG-2557 AND TRP-2622, VARIANTS DDEB ARG-2003; ASP-2040; ARG-2043; ARG-2064; ARG-2070 AND ASP-2076.

Entry informationi

Entry nameiCO7A1_HUMAN
AccessioniPrimary (citable) accession number: Q02388
Secondary accession number(s): Q14054, Q16507
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 173 of the entry and version 2 of the sequence. [Complete history]
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.

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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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