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Q9UMD9 (COHA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(XVII) chain
Alternative name(s):
180 kDa bullous pemphigoid antigen 2
Bullous pemphigoid antigen 2

Cleaved into the following 2 chains:

  1. 120 kDa linear IgA disease antigen
    Alternative name(s):
    120 kDa linear IgA dermatosis antigen
    Linear IgA disease antigen 1
    Short name=LAD-1
  2. 97 kDa linear IgA disease antigen
    Alternative name(s):
    97 kDa linear IgA bullous dermatosis antigen
    Short name=97 kDa LAD antigen
    Short name=97-LAD
    Linear IgA bullous disease antigen of 97 kDa
    Short name=LABD97
Gene names
Name:COL17A1
Synonyms:BP180, BPAG2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1497 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane. Ref.8 Ref.15

The 120 kDa linear IgA disease antigen is an anchoring filament component involved in dermal-epidermal cohesion. Is the target of linear IgA bullous dermatosis autoantibodies. Ref.8 Ref.15

Subunit structure

Homotrimers of alpha 1(XVII)chains. Interacts (via cytoplasmic region) with ITGB4 (via cytoplasmic region). Interacts (via cytoplasmic region) with DST isoform 3(via N-terminus). Interacts (via N-terminus) with PLEC. Interacts (via cytoplasmic region) with DSP. Ref.12 Ref.13 Ref.15

Subcellular location

Cell junctionhemidesmosome. Membrane; Single-pass type II membrane protein. Note: Localized along the plasma membrane of the hemidesmosome. Ref.1 Ref.8 Ref.10 Ref.11 Ref.15

120 kDa linear IgA disease antigen: Secretedextracellular spaceextracellular matrixbasement membrane. Note: Exclusively localized to anchoring filaments. Localized to the epidermal side of split skin. Ref.1 Ref.8 Ref.10 Ref.11 Ref.15

97 kDa linear IgA disease antigen: Secretedextracellular spaceextracellular matrixbasement membrane. Note: Localized in the lamina lucida beneath the hemidesmosomes. Ref.1 Ref.8 Ref.10 Ref.11 Ref.15

Tissue specificity

Stratified squamous epithelia. Found in hemidesmosomes. Expressed in cornea, oral mucosa, esophagus, intestine, kidney collecting ducts, ureter, bladder, urethra and thymus but is absent in lung, blood vessels, skeletal muscle and nerves. Ref.5 Ref.8

Post-translational modification

The intracellular/endo domain is disulfide-linked.

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

The ectodomain is shedded from the surface of keratinocytes resulting in a 120-kDa soluble form, also named as 120 kDa linear IgA disease antigen. The shedding is mediated by membrane-bound metalloproteases. This cleavage is inhibited by phosophorylation at Ser-544.

Involvement in disease

Generalized atrophic benign epidermolysis bullosa (GABEB) [MIM:226650]: A non-lethal, adult form of junctional epidermolysis bullosa characterized by life-long blistering of the skin, associated with hair and tooth abnormalities.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

Miscellaneous

Both the 120 kDa linear IgA disease antigen and the 97 kDa linear IgA disease antigen of COL17A1, represent major antigenic targets of autoantibodies in patients with linear IgA disease (LAD). LAD is a subepidermal blistering disorder characterized by tissue-bound and circulating IgA autoantibodies to the dermal-epidermal junction. These IgA autoantibodies preferentially react with 97 and the 120 kDa forms, but not with the full-length COL17A1, suggesting that the cleavage of the ectodomain generates novel autoantigenic epitopes.

Sequence caution

The sequence AAA35605.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH04478.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Cellular componentBasement membrane
Cell junction
Extracellular matrix
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Epidermolysis bullosa
   DomainCollagen
Repeat
Signal-anchor
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Hydroxylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell junction assembly

Traceable author statement. Source: Reactome

cell-matrix adhesion

Traceable author statement Ref.2. Source: ProtInc

collagen catabolic process

Traceable author statement. Source: Reactome

epidermis development

Traceable author statement Ref.2. Source: ProtInc

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

hemidesmosome assembly

Inferred from direct assay Ref.15. Source: UniProtKB

   Cellular_componentbasement membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell-cell junction

Traceable author statement Ref.2. Source: ProtInc

collagen trimer

Inferred from electronic annotation. Source: UniProtKB-KW

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

hemidesmosome

Inferred from direct assay Ref.15. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionprotein binding

Inferred from physical interaction Ref.15. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UMD9-1)

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: Q9UMD9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     922-966: Missing.
     1170-1207: GSEFRGIVGPPGPPGPPGIPGNVWSSISVEDLSSYLHT → A
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14971497Collagen alpha-1(XVII) chain
PRO_0000059406
Chain524 – 1497974120 kDa linear IgA disease antigen
PRO_0000342555
Chain531 – ?97 kDa linear IgA disease antigenPRO_0000342556

Regions

Topological domain1 – 467467Cytoplasmic Potential
Transmembrane468 – 48821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain489 – 14971009Extracellular Potential
Region1 – 566566Nonhelical region (NC16)
Region145 – 23086Necessary for interaction with DST and for the recruitment of DST to hemidesmosome
Region567 – 1482916Triple-helical region
Region1483 – 149715Nonhelical region (NC1)

Amino acid modifications

Modified residue5441Phosphoserine; by CK2 Ref.16
Glycosylation14211N-linked (GlcNAc...) Ref.12

Natural variations

Alternative sequence922 – 96645Missing in isoform 2.
VSP_024940
Alternative sequence1170 – 120738GSEFR…SYLHT → A in isoform 2.
VSP_024941
Natural variant41T → A.
Corresponds to variant rs17116471 [ dbSNP | Ensembl ].
VAR_048781
Natural variant2101T → M. Ref.4
Corresponds to variant rs805708 [ dbSNP | Ensembl ].
VAR_017593
Natural variant2311M → I. Ref.2 Ref.22
Corresponds to variant rs1054113 [ dbSNP | Ensembl ].
VAR_017594
Natural variant2381M → T. Ref.2
VAR_017595
Natural variant2651S → C in GABEB. Ref.22
VAR_017596
Natural variant4281G → S. Ref.1 Ref.2
Corresponds to variant rs805698 [ dbSNP | Ensembl ].
VAR_017597
Natural variant6271G → V in GABEB. Ref.18 Ref.20
VAR_017598
Natural variant6331G → D in GABEB. Ref.21
VAR_017599
Natural variant7031M → V. Ref.2
Corresponds to variant rs805722 [ dbSNP | Ensembl ].
VAR_017600
Natural variant13031R → Q in GABEB. Ref.19
Corresponds to variant rs121912771 [ dbSNP | Ensembl ].
VAR_017601
Natural variant13701D → G. Ref.2
Corresponds to variant rs17116350 [ dbSNP | Ensembl ].
VAR_017602

Experimental info

Sequence conflict8561Q → P in AAA51839. Ref.5
Sequence conflict9051S → F in AAA35605. Ref.1
Sequence conflict9051S → F in AAB51499. Ref.2

Sequences

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

Last modified May 1, 2007. Version 3.
Checksum: E01027005F3AE843

FASTA1,497150,419
        10         20         30         40         50         60 
MDVTKKNKRD GTEVTERIVT ETVTTRLTSL PPKGGTSNGY AKTASLGGGS RLEKQSLTHG 

        70         80         90        100        110        120 
SSGYINSTGS TRGHASTSSY RRAHSPASTL PNSPGSTFER KTHVTRHAYE GSSSGNSSPE 

       130        140        150        160        170        180 
YPRKEFASSS TRGRSQTRES EIRVRLQSAS PSTRWTELDD VKRLLKGSRS ASVSPTRNSS 

       190        200        210        220        230        240 
NTLPIPKKGT VETKIVTASS QSVSGTYDAT ILDANLPSHV WSSTLPAGSS MGTYHNNMTT 

       250        260        270        280        290        300 
QSSSLLNTNA YSAGSVFGVP NNMASCSPTL HPGLSTSSSV FGMQNNLAPS LTTLSHGTTT 

       310        320        330        340        350        360 
TSTAYGVKKN MPQSPAAVNT GVSTSAACTT SVQSDDLLHK DCKFLILEKD NTPAKKEMEL 

       370        380        390        400        410        420 
LIMTKDSGKV FTASPASIAA TSFSEDTLKK EKQAAYNADS GLKAEANGDL KTVSTKGKTT 

       430        440        450        460        470        480 
TADIHSYGSS GGGGSGGGGG VGGAGGGPWG PAPAWCPCGS CCSWWKWLLG LLLTWLLLLG 

       490        500        510        520        530        540 
LLFGLIALAE EVRKLKARVD ELERIRRSIL PYGDSMDRIE KDRLQGMAPA AGADLDKIGL 

       550        560        570        580        590        600 
HSDSQEELWM FVRKKLMMEQ ENGNLRGSPG PKGDMGSPGP KGDRGFPGTP GIPGPLGHPG 

       610        620        630        640        650        660 
PQGPKGQKGS VGDPGMEGPM GQRGREGPMG PRGEAGPPGS GEKGERGAAG EPGPHGPPGV 

       670        680        690        700        710        720 
PGSVGPKGSS GSPGPQGPPG PVGLQGLRGE VGLPGVKGDK GPMGPPGPKG DQGEKGPRGL 

       730        740        750        760        770        780 
TGEPGMRGLP GAVGEPGAKG AMGPAGPDGH QGPRGEQGLT GMPGIRGPPG PSGDPGKPGL 

       790        800        810        820        830        840 
TGPQGPQGLP GTPGRPGIKG EPGAPGKIVT SEGSSMLTVP GPPGPPGAMG PPGPPGAPGP 

       850        860        870        880        890        900 
AGPAGLPGHQ EVLNLQGPPG PPGPRGPPGP SIPGPPGPRG PPGEGLPGPP GPPGSFLSNS 

       910        920        930        940        950        960 
ETFLSGPPGP PGPPGPKGDQ GPPGPRGHQG EQGLPGFSTS GSSSFGLNLQ GPPGPPGPQG 

       970        980        990       1000       1010       1020 
PKGDKGDPGV PGALGIPSGP SEGGSSSTMY VSGPPGPPGP PGPPGSISSS GQEIQQYISE 

      1030       1040       1050       1060       1070       1080 
YMQSDSIRSY LSGVQGPPGP PGPPGPVTTI TGETFDYSEL ASHVVSYLRT SGYGVSLFSS 

      1090       1100       1110       1120       1130       1140 
SISSEDILAV LQRDDVRQYL RQYLMGPRGP PGPPGASGDG SLLSLDYAEL SSRILSYMSS 

      1150       1160       1170       1180       1190       1200 
SGISIGLPGP PGPPGLPGTS YEELLSLLRG SEFRGIVGPP GPPGPPGIPG NVWSSISVED 

      1210       1220       1230       1240       1250       1260 
LSSYLHTAGL SFIPGPPGPP GPPGPRGPPG VSGALATYAA ENSDSFRSEL ISYLTSPDVR 

      1270       1280       1290       1300       1310       1320 
SFIVGPPGPP GPQGPPGDSR LLSTDASHSR GSSSSSHSSS VRRGSSYSSS MSTGGGGAGS 

      1330       1340       1350       1360       1370       1380 
LGAGGAFGEA AGDRGPYGTD IGPGGGYGAA AEGGMYAGNG GLLGADFAGD LDYNELAVRV 

      1390       1400       1410       1420       1430       1440 
SESMQRQGLL QGMAYTVQGP PGQPGPQGPP GISKVFSAYS NVTADLMDFF QTYGAIQGPP 

      1450       1460       1470       1480       1490 
GQKGEMGTPG PKGDRGPAGP PGHPGPPGPR GHKGEKGDKG DQVYAGRRRR RSIAVKP 

« Hide

Isoform 2 [UniParc].

Checksum: 51434477730EC017
Show »

FASTA1,415142,344

References

« Hide 'large scale' references
[1]"Cloning and primary structural analysis of the bullous pemphigoid autoantigen, BP180."
Giudice G.J., Emery D.J., Diaz L.A.
J. Invest. Dermatol. 99:243-250(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, VARIANT SER-428.
Tissue: Foreskin.
[2]"Cloning of the human type XVII collagen gene (COL17A1), and detection of novel mutations in generalized atrophic benign epidermolysis bullosa."
Gatalica B., Pulkkinen L., Li K., Kuokkanen K., Ryynaenen M., McGrath J.A., Uitto J.
Am. J. Hum. Genet. 60:352-365(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS ILE-231; THR-238; SER-428; VAL-703 AND GLY-1370.
[3]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-390, VARIANT MET-210.
Tissue: Pancreas.
[5]"Genomic organization of collagenous domains and chromosomal assignment of human 180-kDa bullous pemphigoid antigen-2, a novel collagen of stratified squamous epithelium."
Li K.H., Sawamura D., Giudice G.J., Diaz L.A., Mattei M.-G., Chu M.-L., Uitto J.
J. Biol. Chem. 266:24064-24069(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 508-856, TISSUE SPECIFICITY.
[6]"The 97-kDa (LABD97) and 120-kDa (LAD-1) fragments of bullous pemphigoid antigen 180/type XVII collagen have different N-termini."
Hirako Y., Nishizawa Y., Sitaru C., Opitz A., Marcus K., Meyer H.E., Butt E., Owaribe K., Zillikens D.
J. Invest. Dermatol. 121:1554-1556(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 524-535.
[7]"The 97 kDa linear IgA bullous disease antigen is identical to a portion of the extracellular domain of the 180 kDa bullous pemphigoid antigen, BPAg2."
Zone J.J., Taylor T.B., Meyer L.J., Petersen M.J.
J. Invest. Dermatol. 110:207-210(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 531-546; 554-565; 585-605; 647-666; 680-688; 689-703; 755-765; 842-860; 880-891; 1016-1028; 1062-1069; 1102-1108; 1134-1142; 1227-1247 AND 1248-1260.
[8]"LAD-1, the linear IgA bullous dermatosis autoantigen, is a novel 120-kDa anchoring filament protein synthesized by epidermal cells."
Marinkovich M.P., Taylor T.B., Keene D.R., Burgeson R.E., Zone J.J.
J. Invest. Dermatol. 106:734-738(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY.
[9]Erratum
Marinkovich M.P., Taylor T.B., Keene D.R., Burgeson R.E., Zone J.J.
J. Invest. Dermatol. 106:1343-1343(1996)
[10]"97-kDa linear IgA bullous dermatosis (LAD) antigen localizes to the lamina lucida of the epidermal basement membrane."
Ishiko A., Shimizu H., Masunaga T., Hashimoto T., Dmochowski M., Wojnarowska F., Bhogal B.S., Black M.M., Nishikawa T.
J. Invest. Dermatol. 106:739-743(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Evidence that the 180-kD bullous pemphigoid antigen is a transmembrane collagen, type XVII, in a triple-helical conformation and in type II transmembrane topography."
Limardo M., Arffman A., Aho S., Utto J.
J. Invest. Dermatol. 106:860-860(1996)
Cited for: SUBCELLULAR LOCATION.
[12]"Two forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomain."
Schaecke H., Schumann H., Hammami-Hauasli N., Raghunath M., Bruckner-Tuderman L.
J. Biol. Chem. 273:25937-25943(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, PROTEOLYTIC PROCESSING, GLYCOSYLATION AT ASN-1421, DOMAINS.
[13]"The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmosome."
Hopkinson S.B., Jones J.C.
Mol. Biol. Cell 11:277-286(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DSP.
[14]"Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs."
Franzke C.-W., Tasanen K., Schaecke H., Zhou Z., Tryggvason K., Mauch C., Zigrino P., Sunnarborg S., Lee D.C., Fahrenholz F., Bruckner-Tuderman L.
EMBO J. 21:5026-5035(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SHEDDING.
[15]"Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly."
Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.
J. Cell Sci. 116:387-399(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DSP; DST; ITGB4 AND PLEC, SUBCELLULAR LOCATION.
[16]"Extracellular phosphorylation of collagen XVII by ecto-casein kinase 2 inhibits ectodomain shedding."
Zimina E.P., Fritsch A., Schermer B., Bakulina A.Y., Bashkurov M., Benzing T., Bruckner-Tuderman L.
J. Biol. Chem. 282:22737-22746(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-544.
[17]"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].
[18]"Compound heterozygosity for a dominant glycine substitution and a recessive internal duplication mutation in the type XVII collagen gene results in junctional epidermolysis bullosa and abnormal dentition."
McGrath J.A., Gatalica B., Li K., Dunnill M.G.S., McMillan J.R., Christiano A.M., Eady R.A.J., Uitto J.
Am. J. Pathol. 148:1787-1796(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GABEB VAL-627.
[19]"Three novel homozygous point mutations and a new polymorphism in the COL17A1 gene: relation to biological and clinical phenotypes of junctional epidermolysis bullosa."
Schumann H., Hammami-Hauasli N., Pulkkinen L., Mauviel A., Kuester W., Luethi U., Owaribe K., Uitto J., Bruckner-Tuderman L.
Am. J. Hum. Genet. 60:1344-1353(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GABEB GLN-1303.
[20]"Collagen XVII is destabilized by a glycine substitution mutation in the cell adhesion domain Col15."
Tasanen K., Eble J.A., Aumailley M., Schumann H., Baetge J., Tu H., Bruckner P., Bruckner-Tuderman L.
J. Biol. Chem. 275:3093-3099(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GABEB VAL-627.
[21]"Hemizygosity for a glycine substitution in collagen XVII: unfolding and degradation of the ectodomain."
Tasanen K., Floeth M., Schumann H., Bruckner-Tuderman L.
J. Invest. Dermatol. 115:207-212(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GABEB ASP-633.
[22]"A novel homozygous point mutation in the COL17A1 gene in a Chinese family with generalized atrophic benign epidermolysis bullosa."
Wu Y., Li G., Zhu X.
J. Dermatol. Sci. 28:181-186(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GABEB CYS-265, VARIANT ILE-231.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M91669 mRNA. Translation: AAA35605.1. Different initiation.
U76604 expand/collapse EMBL AC list , U76565, U76566, U76567, U76568, U76569, U76570, U76571, U76572, U76573, U76574, U76575, U76576, U76577, U76578, U76579, U76580, U76581, U76582, U76583, U76584, U76585, U76586, U76587, U76588, U76589, U76590, U76591, U76592, U76593, U76594, U76595, U76596, U76597, U76598, U76599, U76600, U76601, U76602, U76603 Genomic DNA. Translation: AAB51499.1.
AL138761 Genomic DNA. Translation: CAC00589.1.
AL138761 Genomic DNA. Translation: CAI12398.1.
BC004478 mRNA. Translation: AAH04478.1. Sequence problems.
M63730 mRNA. Translation: AAA51839.1.
CCDSCCDS7554.1. [Q9UMD9-1]
PIRA61262. I56325.
RefSeqNP_000485.3. NM_000494.3. [Q9UMD9-1]
UniGeneHs.117938.
Hs.732773.

3D structure databases

ProteinModelPortalQ9UMD9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107704. 8 interactions.
IntActQ9UMD9. 1 interaction.
MINTMINT-119869.
STRING9606.ENSP00000340937.

Protein family/group databases

Allergome8213. Hom s BP180.
8226. Hom s BP180.0101.

PTM databases

PhosphoSiteQ9UMD9.

Polymorphism databases

DMDM146345399.

Proteomic databases

MaxQBQ9UMD9.
PaxDbQ9UMD9.
PRIDEQ9UMD9.

Protocols and materials databases

DNASU1308.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000353479; ENSP00000340937; ENSG00000065618. [Q9UMD9-1]
ENST00000369733; ENSP00000358748; ENSG00000065618. [Q9UMD9-2]
GeneID1308.
KEGGhsa:1308.
UCSCuc001kxr.3. human. [Q9UMD9-1]

Organism-specific databases

CTD1308.
GeneCardsGC10M105781.
GeneReviewsCOL17A1.
H-InvDBHIX0035327.
HGNCHGNC:2194. COL17A1.
HPAHPA043673.
MIM113811. gene.
226650. phenotype.
neXtProtNX_Q9UMD9.
Orphanet79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
79406. Late-onset junctional epidermolysis bullosa.
251393. Localized junctional epidermolysis bullosa, non-Herlitz type.
PharmGKBPA26710.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG309396.
HOGENOMHOG000111885.
HOVERGENHBG051065.
InParanoidQ9UMD9.
KOK07603.
OMALLHKDCK.
OrthoDBEOG76QFJV.
PhylomeDBQ9UMD9.
TreeFamTF332289.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ9UMD9.
BgeeQ9UMD9.
CleanExHS_COL17A1.
GenevestigatorQ9UMD9.

Family and domain databases

InterProIPR008160. Collagen.
[Graphical view]
PfamPF01391. Collagen. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCollagen,_type_XVII,_alpha_1.
GenomeRNAi1308.
NextBio5353.
PMAP-CutDBQ9UMD9.
PROQ9UMD9.
SOURCESearch...

Entry information

Entry nameCOHA1_HUMAN
AccessionPrimary (citable) accession number: Q9UMD9
Secondary accession number(s): Q02802 expand/collapse secondary AC list , Q5JV36, Q99018, Q9NQK9, Q9UC14
Entry history
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 131 of the entry and version 3 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

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 10

Human chromosome 10: entries, gene names and cross-references to MIM