Linked Life Data

P13942

Source:http://identifiers.org/uniprot/P13942

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
biopax3:comment
FUNCTION: May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils. SUBUNIT: Trimers composed of three different chains: alpha 1(XI), alpha 2(XI), and alpha 3(XI). Alpha 3(XI) is a post-translational modification of alpha 1(II). Alpha 1(V) can also be found instead of alpha 3(XI)=1(II). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (By similarity). ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=9; Comment=Isoforms lack exons 6, 7 or 8 or a combination of these exons. Experimental confirmation may be lacking for some isoforms; Name=1; IsoId=P13942-1; Sequence=Displayed; Name=2; IsoId=P13942-2; Sequence=VSP_001167; Name=3; IsoId=P13942-3; Sequence=VSP_001168; Name=4; IsoId=P13942-4; Sequence=VSP_001169; Name=5; IsoId=P13942-5; Sequence=VSP_001167, VSP_001168; Name=6; IsoId=P13942-6; Sequence=VSP_001167, VSP_001169; Name=7; IsoId=P13942-7; Sequence=VSP_001168, VSP_001169; Name=8; IsoId=P13942-8; Sequence=VSP_001167, VSP_001168, VSP_001169; Name=9; IsoId=P13942-9; Sequence=VSP_043432, VSP_043433; Note=No experimental confirmation available; PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. PTM: A disulfide-bonded peptide called proline/arginine-rich protein or PARP is released from the N-terminus during extracellular processing and is subsequently retained in the cartilage matrix from which it can be isolated in significant amounts. DISEASE: Defects in COL11A2 are the cause of Stickler syndrome type 3 (STL3) [MIM:184840]. STL3 is an autosomal dominant non- ocular form of Stickler syndrome. Classical Stickler syndrome associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular symptoms are absent in STL3. Robin sequence includes an opening in the roof of the mouth (a cleft palate), a large tongue (macroglossia), and a small lower jaw (micrognathia). Bones are affected by slight platyspondylisis and large, often defective epiphyses. Juvenile joint laxity is followed by early signs of arthrosis. The degree of hearing loss varies among affected individuals and may become more severe over time. Syndrome expressivity is variable. DISEASE: Defects in COL11A2 are the cause of autosomal recessive otospondylomegaepiphyseal dysplasia (OSMED) [MIM:215150]. OSMED is a skeletal dysplasia accompanied by severe hearing loss. The phenotype overlaps that of autosomal dominant skeletal disorders (Stickler and Marshall syndromes) but can be distinguished by disproportionately short limbs and lack of ocular involvement. DISEASE: Defects in COL11A2 are the cause of Weissenbacher- Zweymueller syndrome (WZS) [MIM:277610]. WZS is an autosomal dominant disorder allelic with STL3 and OSMED. WZS is also referred to as heterozygous OSMED. DISEASE: Defects in COL11A2 are the cause of deafness autosomal dominant type 13 (DFNA13) [MIM:601868]. DFNA13 is a form of sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DISEASE: Defects in COL11A2 are the cause of deafness autosomal recessive type 53 (DFNB53) [MIM:609706]. DISEASE: Defects in COL11A2 are the cause of fibrochondrogenesis type 2 (FBCG2) [MIM:614524]. A severe skeletal dysplasia characterized by a flat midface, short long bones, short ribs with broad metaphyses, and vertebral bodies that show distinctive hypoplastic posterior ends and rounded anterior ends, giving the vertebral bodies a pinched appearance on lateral radiographic views. The chest is small, causing perinatal respiratory problems which usually, but not always, result in lethality. Affected individuals who survive the neonatal period have high myopia, mild to moderate hearing loss, and severe skeletal dysplasia. SIMILARITY: Belongs to the fibrillar collagen family. SIMILARITY: Contains 8 collagen-like domains. SIMILARITY: Contains 1 fibrillar collagen NC1 domain. SIMILARITY: Contains 1 laminin G-like domain. WEB RESOURCE: Name=Hereditary hearing loss homepage; Note=Gene page; URL="http://webhost.ua.ac.be/hhh/"; WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/COL11A2"; GENE SYNONYMS:COL11A2. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License., SEQUENCE 1736 AA; 171791 MW; D687B7AAD6A7774C CRC64;
biopax3:xref
biopax3:displayName
COBA2_HUMAN
biopax3:name
COL11A2
biopax3:organism
biopax3:sequence
MERCSRCHRLLLLLPLVLGLSAAPGWAGAPPVDVLRALRFPSLPDGVRRAKGICPADVAYRVARPAQLSAPTRQLFPGGFPKDFSLLTVVRTRPGLQAPLLTLYSAQGVRQLGLELGRPVRFLYEDQTGRPQPPSQPVFRGLSLADGKWHRVAVAVKGQSVTLIVDCKKRVTRPLPRSARPVLDTHGVIIFGARILDEEVFEGDVQELAIVPGVQAAYESCEQKELECEGGQRERPQNQQPHRAQRSPQQQPSRLHRPQNQEPQSQPTESLYYDYEPPYYDVMTTGTTPDYQDPTPGEEEEILESSLLPPLEEEQTDLQVPPTADRFQAEEYGEGGTDPPEGPYDYTYGYGDDYREETELGPALSAETAHSGAAAHGPRGLKGEKGEPAVLEPGMLVEGPPGPEGPAGLIGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGAPGPPGTSLMLPFRFGSGGGDKGPVVAAQEAQAQAILQQARLALRGPPGPMGYTGRPGPLGQPGSPGLKGESGDLGPQGPRGPQGLTGPPGKAGRRGRAGADGARGMPGDPGVKGDRGFDGLPGLPGEKGHRGDTGAQGLPGPPGEDGERGDDGEIGPRGLPGESGPRGLLGPKGPPGIPGPPGVRGMDGPQGPKGSLGPQGEPGPPGQQGTPGTQGLPGPQGAIGPHGEKGPQGKPGLPGMPGSDGPPGHPGKEGPPGTKGNQGPSGPQGPLGYPGPRGVKGVDGIRGLKGHKGEKGEDGFPGFKGDIGVKGDRGEVGVPGSRGEDGPEGPKGRTGPTGDPGPPGLMGEKGKLGVPGLPGYPGRQGPKGSLGFPGFPGASGEKGARGLSGKSGPRGERGPTGPRGQRGPRGATGKSGAKGTSGGDGPHGPPGERGLPGPQGPNGFPGPKGPLGPPGKDGLPGHPGQRGEVGFQGKTGPPGPPGVVGPQGAAGETGPMGERGHPGPPGPPGEQGLPGTAGKEGTKGDPGPPGAPGKDGPAGLRGFPGERGLPGTAGGPGLKGNEGPSGPPGPAGSPGERGAAGSGGPIGPPGRPGPQGPPGAAGEKGVPGEKGPIGPTGRDGVQGPVGLPGPAGPPGVAGEDGDKGEVGDPGQKGTKGNKGEHGPPGPPGPIGPVGQPGAAGADGEPGARGPQGHFGAKGDEGTRGFNGPPGPIGLQGLPGPSGEKGETGDVGPMGPPGPPGPRGPAGPNGADGPQGPPGGVGNLGPPGEKGEPGESGSPGIQGEPGVKGPRGERGEKGESGQPGEPGPPGPKGPTGDDGPKGNPGPVGFPGDPGPPGEGGPRGQDGAKGDRGEDGEPGQPGSPGPTGENGPPGPLGKRGPAGSPGSEGRQGGKGAKGDPGAIGAPGKTGPVGPAGPAGKPGPDGLRGLPGSVGQQGRPGATGQAGPPGPVGPPGLPGLRGDAGAKGEKGHPGLIGLIGPPGEQGEKGDRGLPGPQGSPGQKGEMGIPGASGPIGPGGPPGLPGPAGPKGAKGATGPGGPKGEKGVQGPPGHPGPPGEVIQPLPIQMPKKTRRSVDGSRLMQEDEAIPTGGAPGSPGGLEEIFGSLDSLREEIEQMRRPTGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGAARDGPLRLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFSDLGAPPRRGGVLLGPVCFMG
biopax3:standardName
Collagen alpha-2(XI) chain