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Q02388 (CO7A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 172. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(VII) chain
Alternative name(s):
Long-chain collagen
Short name=LC collagen
Gene names
Name:COL7A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2944 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homotrimer. Interacts with MIA3/TANGO1; facilitating its loading into transport carriers and subsequent secretion. Ref.9

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane.

Post-translational modification

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

Involvement in disease

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. Ref.16 Ref.23 Ref.24 Ref.25 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32 Ref.37 Ref.38 Ref.45

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. Ref.19 Ref.20 Ref.22 Ref.23 Ref.25 Ref.26 Ref.32 Ref.39 Ref.40 Ref.45

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. Ref.14 Ref.33

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. Ref.13 Ref.18 Ref.21 Ref.25 Ref.32

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. Ref.28

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.

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. Ref.34 Ref.38

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. Ref.41

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. Ref.12 Ref.42

Sequence similarities

Contains 1 BPTI/Kunitz inhibitor domain.

Contains 9 fibronectin type-III domains.

Contains 2 VWFA domains.

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MIA3Q5JRA62EBI-724237,EBI-2291868

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q02388-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q02388-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 29442928Collagen alpha-1(VII) chain
PRO_0000005761

Regions

Domain38 – 211174VWFA 1
Domain234 – 32996Fibronectin type-III 1
Domain330 – 41687Fibronectin type-III 2
Domain417 – 50791Fibronectin type-III 3
Domain510 – 59788Fibronectin type-III 4
Domain600 – 68788Fibronectin type-III 5
Domain688 – 77588Fibronectin type-III 6
Domain778 – 86689Fibronectin type-III 7
Domain869 – 95789Fibronectin type-III 8
Domain958 – 105194Fibronectin type-III 9
Domain1054 – 1229176VWFA 2
Domain2872 – 294473BPTI/Kunitz inhibitor
Region17 – 12531237Nonhelical region (NC1)
Region1254 – 27841531Triple-helical region
Region1254 – 1477224Interrupted collagenous region
Region2785 – 2944160Nonhelical region (NC2)
Motif1170 – 11723Cell attachment site Potential
Motif1334 – 13363Cell attachment site Potential
Motif2008 – 20103Cell attachment site Potential
Motif2553 – 25553Cell attachment site Potential

Sites

Site2886 – 28872Reactive bond By similarity

Amino acid modifications

Modified residue216714-hydroxyproline
Modified residue217614-hydroxyproline
Modified residue218514-hydroxyproline
Modified residue218814-hydroxyproline
Modified residue262515-hydroxylysine; alternate
Modified residue263115-hydroxylysine; alternate
Modified residue266414-hydroxyproline
Modified residue266714-hydroxyproline
Modified residue267314-hydroxyproline
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation7861N-linked (GlcNAc...) Potential
Glycosylation11091N-linked (GlcNAc...) Potential
Glycosylation26251O-linked (Gal...); alternate
Glycosylation26311O-linked (Gal...); alternate
Disulfide bond2634Interchain Potential
Disulfide bond2802Interchain Potential
Disulfide bond2804Interchain Potential
Disulfide bond2876 ↔ 2929 By similarity
Disulfide bond2885 ↔ 2912 By similarity
Disulfide bond2904 ↔ 2925 By similarity

Natural variations

Alternative sequence1869 – 190032Missing in isoform 2.
VSP_024026
Natural variant1191T → P in a breast cancer sample; somatic mutation. Ref.43
VAR_035740
Natural variant1421K → R in RDEB.
VAR_001809
Natural variant5471V → F.
Corresponds to variant rs2229823 [ dbSNP | Ensembl ].
VAR_048765
Natural variant5951P → L in RDEB.
Corresponds to variant rs2228561 [ dbSNP | Ensembl ].
VAR_001810
Natural variant11201R → K.
Corresponds to variant rs2228563 [ dbSNP | Ensembl ].
VAR_048766
Natural variant12771P → L in RDEB.
Corresponds to variant rs35761247 [ dbSNP | Ensembl ].
VAR_001811
Natural variant13471G → R in RDEB; localized type; mild. Ref.26
VAR_011160
Natural variant13641P → T in a breast cancer sample; somatic mutation. Ref.43
VAR_035741
Natural variant13661R → W in a breast cancer sample; somatic mutation. Ref.43
VAR_035742
Natural variant15191G → D in TBDN; compound heterozygous with E-2251; clinically silent when heterozygous with a normal allele. Ref.24 Ref.28
VAR_011161
Natural variant15221G → E in DDEB.
VAR_011162
Natural variant15571G → R in DDEB.
VAR_001812
Natural variant15951G → R in NDNC8. Ref.41
VAR_015519
Natural variant16041G → R in RDEB.
VAR_011163
Natural variant16521G → R in RDEB; mitis type. Ref.22
VAR_011164
Natural variant17031G → E in RDEB.
VAR_011165
Natural variant17721R → W in RDEB.
VAR_011166
Natural variant17761G → R in DDEB.
VAR_011167
Natural variant17821G → R in RDEB; mitis type. Ref.19
VAR_001813
Natural variant17911G → E in EBP. Ref.34
VAR_011168
Natural variant18121G → R in RDEB. Ref.39
VAR_011169
Natural variant18151G → R in NDNC8. Ref.41
VAR_015520
Natural variant18451G → R in RDEB. Ref.45
VAR_064994
Natural variant19811K → R in RDEB; mild form. Ref.45
VAR_064995
Natural variant19821G → W in HS-DEB. Ref.21
VAR_001814
Natural variant20031G → R in DDEB. Ref.45
VAR_001815
Natural variant20061G → A in DDEB.
VAR_011170
Natural variant20061G → D in DDEB; interferes with collagen VII folding and secretion. Ref.24 Ref.32
VAR_011171
Natural variant20081R → C in HS-DEB; also in a milder localized type. Ref.25 Ref.32
VAR_011172
Natural variant20081R → G in HS-DEB. Ref.21 Ref.32
VAR_001816
Natural variant20091G → R in RDEB. Ref.23 Ref.32
VAR_011173
Natural variant20151G → E in DDEB; interferes with collagen VII folding and secretion. Ref.24 Ref.32
VAR_011174
Natural variant20251G → A in RDEB; mitis type. Ref.21
VAR_001817
Natural variant20281G → A in DDEB. Ref.38
VAR_011175
Natural variant20281G → R in DDEB and EBP. Ref.37 Ref.38
VAR_011176
Natural variant20311G → S in RDEB; severe phenotype. Ref.40
VAR_011177
Natural variant20341G → R in DDEB and EBDSC; interferes with collagen VII folding and secretion. Ref.12 Ref.24 Ref.32 Ref.42
VAR_001818
Natural variant20341G → W in DDEB. Ref.27 Ref.32
VAR_011178
Natural variant20371G → E in P-DEB. Ref.33
VAR_011179
Natural variant20401G → D in DDEB. Ref.45
VAR_011180
Natural variant20401G → S in P-DEB. Ref.14
VAR_001819
Natural variant20401G → V in DDEB. Ref.27
VAR_011181
Natural variant20431G → R in DDEB. Ref.16 Ref.23 Ref.27 Ref.32 Ref.45
VAR_001820
Natural variant20431G → W in DDEB; localized type. Ref.32
VAR_011182
Natural variant20461G → V in DDEB.
VAR_011183
Natural variant20491G → E in HS-DEB. Ref.21 Ref.45
VAR_001821
Natural variant20551G → E in DDEB.
VAR_001822
Natural variant20631R → W in HS-DEB; also in a mild form. Ref.21 Ref.29 Ref.45
VAR_001823
Natural variant20641G → R in DDEB. Ref.27 Ref.45
VAR_011184
Natural variant20691R → C in RDEB. Ref.45
VAR_064996
Natural variant20701G → R in DDEB. Ref.45
VAR_064997
Natural variant20731G → D in RDEB; mitis type. Ref.20
VAR_001825
Natural variant20761G → D in DDEB; also in recessive forms. Ref.45
VAR_001826
Natural variant20791G → E in DDEB. Ref.29
VAR_001827
Natural variant20791G → R in DDEB; associated with squamous cell carcinoma. Ref.31
VAR_011185
Natural variant21321G → D in RDEB.
VAR_011186
Natural variant21921G → S in RDEB.
VAR_011187
Natural variant22071G → R in DDEB. Ref.25
VAR_011188
Natural variant22211G → A in a patient with recessive dystrophic epidermolysis bullosa. Ref.44
VAR_064998
Natural variant22421G → R in EBP. Ref.34
VAR_001828
Natural variant22511G → E in TBDN; compound heterozygous with D-1519; leads to isolated toenail dystrophy when heterozygous with a normal allele. Ref.28
VAR_011189
Natural variant22631G → V in RDEB.
VAR_011190
Natural variant22871G → 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. Ref.35
VAR_011191
Natural variant22961G → E in RDEB. Ref.45
VAR_064999
Natural variant23161G → R in a compound heterozygote affected by moderately severe dystrophic epidermolysis bullosa; in combination with R-2287. Ref.35
VAR_011192
Natural variant23481G → R in DDEB/RDEB; mild form. Ref.30
VAR_011193
Natural variant23511G → R in a patient with dystrophic epidermolysis bullosa; mitis type.
Corresponds to variant rs1800013 [ dbSNP | Ensembl ].
VAR_001829
Natural variant23661G → S in RDEB; mitis type. Ref.29
VAR_011194
Natural variant23691G → S in EBP. Ref.34
VAR_011195
Natural variant24291P → L.
Corresponds to variant rs2229822 [ dbSNP | Ensembl ].
VAR_033786
Natural variant25571G → R in RDEB. Ref.45
VAR_065000
Natural variant25691G → R in RDEB; severe and mitis type.
VAR_001830
Natural variant25751G → R in HS-DEB; also in a mild form. Ref.18 Ref.21
VAR_001831
Natural variant26221R → W in RDEB. Ref.45
VAR_065001
Natural variant26231G → C in PR-DEB; dominant. Ref.15
VAR_001832
Natural variant26531G → R in RDEB; mitis type.
VAR_001833
Natural variant26711G → V in RDEB.
VAR_001834
Natural variant26741G → D in RDEB.
VAR_011196
Natural variant26741G → R in RDEB; mitis type.
VAR_001835
Natural variant27131G → D in DDEB. Ref.27
VAR_011197
Natural variant27131G → R in EBP. Ref.34
VAR_011198
Natural variant27401G → A in RDEB.
VAR_011199
Natural variant27491G → R in HS-DEB; also in a mild form.
Corresponds to variant rs121912853 [ dbSNP | Ensembl ].
VAR_001836
Natural variant27751G → S in RDEB; mitis type. Ref.25
VAR_011200
Natural variant27911R → W in DDEB.
Corresponds to variant rs142566193 [ dbSNP | Ensembl ].
VAR_011201
Natural variant27981M → K in HS-DEB; also in a mild form; the anchoring fibrils may be absent. Ref.13
VAR_001837

Experimental info

Sequence conflict195 – 1973FFF → EFR in BAA02853. Ref.4
Sequence conflict369 – 3713QQQ → EFR in AAA36357. Ref.5
Sequence conflict369 – 3713QQQ → EFR in AAB24637. Ref.5
Sequence conflict518 – 5192EL → DV in AAA36357. Ref.5
Sequence conflict518 – 5192EL → DV in AAB24637. Ref.5
Sequence conflict5291S → C in BAA02853. Ref.4
Sequence conflict5411V → W in AAA36357. Ref.5
Sequence conflict5411V → W in AAB24637. Ref.5
Sequence conflict8511R → H in BAA02853. Ref.4
Sequence conflict8931A → E in AAA58965. Ref.1
Sequence conflict8931A → E in BAA02853. Ref.4
Sequence conflict8931A → E in AAA96439. Ref.6
Sequence conflict11221R → L in BAA02853. Ref.4
Sequence conflict1463 – 14642SP → LR AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 96D8BF6D0FD387DB

FASTA2,944295,220
        10         20         30         40         50         60 
MTLRLLVAAL CAGILAEAPR VRAQHRERVT CTRLYAADIV FLLDGSSSIG RSNFREVRSF 

        70         80         90        100        110        120 
LEGLVLPFSG AASAQGVRFA TVQYSDDPRT EFGLDALGSG GDVIRAIREL SYKGGNTRTG 

       130        140        150        160        170        180 
AAILHVADHV FLPQLARPGV PKVCILITDG KSQDLVDTAA QRLKGQGVKL FAVGIKNADP 

       190        200        210        220        230        240 
EELKRVASQP TSDFFFFVND FSILRTLLPL VSRRVCTTAG GVPVTRPPDD STSAPRDLVL 

       250        260        270        280        290        300 
SEPSSQSLRV QWTAASGPVT GYKVQYTPLT GLGQPLPSER QEVNVPAGET SVRLRGLRPL 

       310        320        330        340        350        360 
TEYQVTVIAL YANSIGEAVS GTARTTALEG PELTIQNTTA HSLLVAWRSV PGATGYRVTW 

       370        380        390        400        410        420 
RVLSGGPTQQ QELGPGQGSV LLRDLEPGTD YEVTVSTLFG RSVGPATSLM ARTDASVEQT 

       430        440        450        460        470        480 
LRPVILGPTS ILLSWNLVPE ARGYRLEWRR ETGLEPPQKV VLPSDVTRYQ LDGLQPGTEY 

       490        500        510        520        530        540 
RLTLYTLLEG HEVATPATVV PTGPELPVSP VTDLQATELP GQRVRVSWSP VPGATQYRII 

       550        560        570        580        590        600 
VRSTQGVERT LVLPGSQTAF DLDDVQAGLS YTVRVSARVG PREGSASVLT VRREPETPLA 

       610        620        630        640        650        660 
VPGLRVVVSD ATRVRVAWGP VPGASGFRIS WSTGSGPESS QTLPPDSTAT DITGLQPGTT 

       670        680        690        700        710        720 
YQVAVSVLRG REEGPAAVIV ARTDPLGPVR TVHVTQASSS SVTITWTRVP GATGYRVSWH 

       730        740        750        760        770        780 
SAHGPEKSQL VSGEATVAEL DGLEPDTEYT VHVRAHVAGV DGPPASVVVR TAPEPVGRVS 

       790        800        810        820        830        840 
RLQILNASSD VLRITWVGVT GATAYRLAWG RSEGGPMRHQ ILPGNTDSAE IRGLEGGVSY 

       850        860        870        880        890        900 
SVRVTALVGD REGTPVSIVV TTPPEAPPAL GTLHVVQRGE HSLRLRWEPV PRAQGFLLHW 

       910        920        930        940        950        960 
QPEGGQEQSR VLGPELSSYH LDGLEPATQY RVRLSVLGPA GEGPSAEVTA RTESPRVPSI 

       970        980        990       1000       1010       1020 
ELRVVDTSID SVTLAWTPVS RASSYILSWR PLRGPGQEVP GSPQTLPGIS SSQRVTGLEP 

      1030       1040       1050       1060       1070       1080 
GVSYIFSLTP VLDGVRGPEA SVTQTPVCPR GLADVVFLPH ATQDNAHRAE ATRRVLERLV 

      1090       1100       1110       1120       1130       1140 
LALGPLGPQA VQVGLLSYSH RPSPLFPLNG SHDLGIILQR IRDMPYMDPS GNNLGTAVVT 

      1150       1160       1170       1180       1190       1200 
AHRYMLAPDA PGRRQHVPGV MVLLVDEPLR GDIFSPIREA QASGLNVVML GMAGADPEQL 

      1210       1220       1230       1240       1250       1260 
RRLAPGMDSV QTFFAVDDGP SLDQAVSGLA TALCQASFTT QPRPEPCPVY CPKGQKGEPG 

      1270       1280       1290       1300       1310       1320 
EMGLRGQVGP PGDPGLPGRT GAPGPQGPPG SATAKGERGF PGADGRPGSP GRAGNPGTPG 

      1330       1340       1350       1360       1370       1380 
APGLKGSPGL PGPRGDPGER GPRGPKGEPG APGQVIGGEG PGLPGRKGDP GPSGPPGPRG 

      1390       1400       1410       1420       1430       1440 
PLGDPGPRGP PGLPGTAMKG DKGDRGERGP PGPGEGGIAP GEPGLPGLPG SPGPQGPVGP 

      1450       1460       1470       1480       1490       1500 
PGKKGEKGDS EDGAPGLPGQ PGSPGEQGPR GPPGAIGPKG DRGFPGPLGE AGEKGERGPP 

      1510       1520       1530       1540       1550       1560 
GPAGSRGLPG VAGRPGAKGP EGPPGPTGRQ GEKGEPGRPG DPAVVGPAVA GPKGEKGDVG 

      1570       1580       1590       1600       1610       1620 
PAGPRGATGV QGERGPPGLV LPGDPGPKGD PGDRGPIGLT GRAGPPGDSG PPGEKGDPGR 

      1630       1640       1650       1660       1670       1680 
PGPPGPVGPR GRDGEVGEKG DEGPPGDPGL PGKAGERGLR GAPGVRGPVG EKGDQGDPGE 

      1690       1700       1710       1720       1730       1740 
DGRNGSPGSS GPKGDRGEPG PPGPPGRLVD TGPGAREKGE PGDRGQEGPR GPKGDPGLPG 

      1750       1760       1770       1780       1790       1800 
APGERGIEGF RGPPGPQGDP GVRGPAGEKG DRGPPGLDGR SGLDGKPGAA GPSGPNGAAG 

      1810       1820       1830       1840       1850       1860 
KAGDPGRDGL PGLRGEQGLP GPSGPPGLPG KPGEDGKPGL NGKNGEPGDP GEDGRKGEKG 

      1870       1880       1890       1900       1910       1920 
DSGASGREGR DGPKGERGAP GILGPQGPPG LPGPVGPPGQ GFPGVPGGTG PKGDRGETGS 

      1930       1940       1950       1960       1970       1980 
KGEQGLPGER GLRGEPGSVP NVDRLLETAG IKASALREIV ETWDESSGSF LPVPERRRGP 

      1990       2000       2010       2020       2030       2040 
KGDSGEQGPP GKEGPIGFPG ERGLKGDRGD PGPQGPPGLA LGERGPPGPS GLAGEPGKPG 

      2050       2060       2070       2080       2090       2100 
IPGLPGRAGG VGEAGRPGER GERGEKGERG EQGRDGPPGL PGTPGPPGPP GPKVSVDEPG 

      2110       2120       2130       2140       2150       2160 
PGLSGEQGPP GLKGAKGEPG SNGDQGPKGD RGVPGIKGDR GEPGPRGQDG NPGLPGERGM 

      2170       2180       2190       2200       2210       2220 
AGPEGKPGLQ GPRGPPGPVG GHGDPGPPGA PGLAGPAGPQ GPSGLKGEPG ETGPPGRGLT 

      2230       2240       2250       2260       2270       2280 
GPTGAVGLPG PPGPSGLVGP QGSPGLPGQV GETGKPGAPG RDGASGKDGD RGSPGVPGSP 

      2290       2300       2310       2320       2330       2340 
GLPGPVGPKG EPGPTGAPGQ AVVGLPGAKG EKGAPGGLAG DLVGEPGAKG DRGLPGPRGE 

      2350       2360       2370       2380       2390       2400 
KGEAGRAGEP GDPGEDGQKG APGPKGFKGD PGVGVPGSPG PPGPPGVKGD LGLPGLPGAP 

      2410       2420       2430       2440       2450       2460 
GVVGFPGQTG PRGEMGQPGP SGERGLAGPP GREGIPGPLG PPGPPGSVGP PGASGLKGDK 

      2470       2480       2490       2500       2510       2520 
GDPGVGLPGP RGERGEPGIR GEDGRPGQEG PRGLTGPPGS RGERGEKGDV GSAGLKGDKG 

      2530       2540       2550       2560       2570       2580 
DSAVILGPPG PRGAKGDMGE RGPRGLDGDK GPRGDNGDPG DKGSKGEPGD KGSAGLPGLR 

      2590       2600       2610       2620       2630       2640 
GLLGPQGQPG AAGIPGDPGS PGKDGVPGIR GEKGDVGFMG PRGLKGERGV KGACGLDGEK 

      2650       2660       2670       2680       2690       2700 
GDKGEAGPPG RPGLAGHKGE MGEPGVPGQS GAPGKEGLIG PKGDRGFDGQ PGPKGDQGEK 

      2710       2720       2730       2740       2750       2760 
GERGTPGIGG FPGPSGNDGS AGPPGPPGSV GPRGPEGLQG QKGERGPPGE RVVGAPGVPG 

      2770       2780       2790       2800       2810       2820 
APGERGEQGR PGPAGPRGEK GEAALTEDDI RGFVRQEMSQ HCACQGQFIA SGSRPLPSYA 

      2830       2840       2850       2860       2870       2880 
ADTAGSQLHA VPVLRVSHAE EEERVPPEDD EYSEYSEYSV EEYQDPEAPW DSDDPCSLPL 

      2890       2900       2910       2920       2930       2940 
DEGSCTAYTL RWYHRAVTGS TEACHPFVYG GCGGNANRFG TREACERRCP PRVVQSQGTG 


TAQD 

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Isoform 2 [UniParc].

Checksum: C206B8957E4333A2
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FASTA2,912292,267

References

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[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]"Human type VII collagen: cDNA cloning and chromosomal mapping of the gene."
Parente M.G., Chung L.C., Ryynaenen J., Woodley D.T., Wynn K.W., Bauer E.A., Mattei M.-G., Chu M.-L., Uitto J.
Proc. Natl. Acad. Sci. U.S.A. 88:6931-6935(1991) [PubMed] [Europe PMC] [Abstract]
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.
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Allelic heterogeneity of dominant and recessive COL7A1 mutations underlying epidermolysis bullosa pruriginosa."
Mellerio J.E., Ashton G.H.S., Mohammedi R., Lyon C.C., Kirby B., Harman K.E., Salas-Alanis J.C., Atherton D.J., Harrison P.V., Griffiths W.A.D., Black M.M., Eady R.A.J., McGrath J.A.
J. Invest. Dermatol. 112:984-987(1999) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2773.1. [Q02388-1]
PIRA54849.
RefSeqNP_000085.1. NM_000094.3. [Q02388-1]
UniGeneHs.476218.

3D structure databases

ProteinModelPortalQ02388.
SMRQ02388. Positions 38-215, 233-1041, 1051-1237, 2876-2933.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107691. 8 interactions.
IntActQ02388. 6 interactions.
MINTMINT-1390694.
STRING9606.ENSP00000332371.

Protein family/group databases

MEROPSI02.967.

PTM databases

PhosphoSiteQ02388.

Polymorphism databases

DMDM1345650.

Proteomic databases

MaxQBQ02388.
PaxDbQ02388.
PRIDEQ02388.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328333; ENSP00000332371; ENSG00000114270. [Q02388-1]
ENST00000454817; ENSP00000412569; ENSG00000114270. [Q02388-2]
GeneID1294.
KEGGhsa:1294.
UCSCuc003ctz.2. human. [Q02388-1]

Organism-specific databases

CTD1294.
GeneCardsGC03M048576.
GeneReviewsCOL7A1.
HGNCHGNC:2214. COL7A1.
HPACAB016357.
MIM120120. gene.
131705. phenotype.
131750. phenotype.
131850. phenotype.
132000. phenotype.
226600. phenotype.
604129. phenotype.
607523. phenotype.
neXtProtNX_Q02388.
Orphanet158673. 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.
PharmGKBPA26730.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000111866.
HOVERGENHBG051053.
InParanoidQ02388.
KOK16628.
OMAWHSGHGP.
OrthoDBEOG7CG6Z4.
PhylomeDBQ02388.
TreeFamTF351645.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ02388.
BgeeQ02388.
CleanExHS_COL7A1.
GenevestigatorQ02388.

Family and domain databases

Gene3D2.60.40.10. 9 hits.
3.40.50.410. 2 hits.
4.10.410.10. 1 hit.
InterProIPR008160. Collagen.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
IPR002035. VWF_A.
[Graphical view]
PfamPF01391. Collagen. 18 hits.
PF00041. fn3. 9 hits.
PF00014. Kunitz_BPTI. 1 hit.
PF00092. VWA. 2 hits.
[Graphical view]
PRINTSPR00759. BASICPTASE.
SMARTSM00060. FN3. 9 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 5 hits.
SSF53300. SSF53300. 2 hits.
SSF57362. SSF57362. 1 hit.
PROSITEPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
PS50853. FN3. 9 hits.
PS50234. VWFA. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL7A1. human.
GeneWikiCollagen,_type_VII,_alpha_1.
GenomeRNAi1294.
NextBio5251.
PROQ02388.
SOURCESearch...

Entry information

Entry nameCO7A1_HUMAN
AccessionPrimary (citable) accession number: Q02388
Secondary accession number(s): Q14054, Q16507
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 172 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM