The human COL11A2 gene structure indicates that the gene has not evolved with the genes for the major fibrillar collagens.Vuoristo M.M., Pihlajamaa T., Vandenberg P., Prockop D.J., Ala-Kokko L.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 270:22873-22881 (1995)Cited in1Mapped to4
The DNA sequence and analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E.[...], Beck S.View abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 425:805-811 (2003)Cited in99+99+
No title available.Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H.[...], Venter J.C.Cited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (JUL-2005)Cited in99+
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project TeamView abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9)TissueSkinCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenome Res. 14:2121-2127 (2004)Cited in99+99+
The human alpha 2(XI) collagen gene (COL11A2): completion of coding information, identification of the promoter sequence, and precise localization within the major histocompatibility complex reveal overlap with the KE5 gene.Lui V.C., Ng L.J., Sat E.W., Cheah K.S.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-537CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenomics 32:401-412 (1996)Cited in11Mapped to4
Molecular cloning of PARP (proline/arginine-rich protein) from human cartilage and subsequent demonstration that PARP is a fragment of the NH2- terminal domain of the collagen alpha 2(XI) chain.Zhidkova N.I., Brewton R.G., Mayne R.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA] OF 59-807TissueCartilageCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCFEBS Lett. 326:25-28 (1993)Cited in1
The human alpha 2(XI) collagen (COL11A2) chain. Molecular cloning of cDNA and genomic DNA reveals characteristics of a fibrillar collagen with differences in genomic organization.Kimura T., Cheah K.S.E., Chan S.D.H., Lui V.C.H., Mattei M.-G., van der Rest M., Ono K., Solomon E., Ninomiya Y., Olsen B.R.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA] OF 730-1690CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 264:13910-13916 (1989)Cited in1
Alternative mRNA processing occurs in the variable region of the pro-alpha 1(XI) and pro-alpha 2(XI) collagen chains.Zhidkova N.I., Justice S.K., Mayne R.View abstractCited forALTERNATIVE SPLICINGCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 270:9486-9493 (1995)Cited in21
Autosomal recessive disorder otospondylomegaepiphyseal dysplasia is associated with loss-of-function mutations in the COL11A2 gene.Melkoniemi M., Brunner H.G., Manouvrier S., Hennekam R.C.M., Superti-Furga A., Kaeaeriaeinen H., Pauli R.M., van Essen T., Warman M.L.[...], Ala-Kokko L.View abstractCited forINVOLVEMENT IN OSMEDBCategoriesDisease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCAm. J. Hum. Genet. 66:368-377 (2000)Cited in1
Mutations in fibrillar collagens (types I, II, III, and XI), fibril- associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels.Kuivaniemi H., Tromp G., Prockop D.J.View abstractCited forREVIEW ON VARIANTSCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCHum. Mutat. 9:300-315 (1997)Cited in6Mapped to4
Dominant and recessive forms of fibrochondrogenesis resulting from mutations at a second locus, COL11A2.Tompson S.W., Faqeih E.A., Ala-Kokko L., Hecht J.T., Miki R., Funari T., Funari V.A., Nevarez L., Krakow D., Cohn D.H.View abstractCited forINVOLVEMENT IN FBCG2CategoriesDisease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCAm. J. Med. Genet. A 158:309-314 (2012)Cited in1Mapped to14
Autosomal dominant and recessive osteochondrodysplasias associated with the COL11A2 locus.Vikkula M., Mariman E.C.M., Lui V.C.H., Zhidkova N.I., Tiller G.E., Goldring M.B., van Beersum S.E.C., de Waal Malefijt M.C., van den Hoogen F.H.J.[...], Brunner H.G.View abstractCited forINVOLVEMENT IN OSMEDA, INVOLVEMENT IN OSMEDB, VARIANT OSMEDB ARG-661CategoriesSequences, Disease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell 80:431-437 (1995)Cited in1Mapped to18
Genetic mapping of ossification of the posterior longitudinal ligament of the spine.Koga H., Sakou T., Taketomi E., Hayashi K., Numasawa T., Harata S., Yone K., Matsunaga S., Otterud B.[...], Leppert M.View abstractCited forVARIANTS GLY-593; LYS-824; LEU-879; THR-1316 AND GLN-1600CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCAm. J. Hum. Genet. 62:1460-1467 (1998)Cited in1
Heterozygous glycine substitution in the COL11A2 gene in the original patient with the Weissenbacher-Zweymueller syndrome demonstrates its identity with heterozygous OSMED (nonocular Stickler syndrome).Pihlajamaa T., Prockop D.J., Faber J., Winterpacht A., Zabel B., Giedion A., Wiesbauer P., Spranger J., Ala-Kokko L.View abstractCited forINVOLVEMENT IN OSMEDA, VARIANT OSMEDA GLU-1441CategoriesSequences, Disease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCAm. J. Med. Genet. 80:115-120 (1998)Cited in1
Stickler syndrome without eye involvement is caused by mutations in COL11A2, the gene encoding the alpha-2(XI) chain of type XI collagen.Sirko-Osadsa D.A., Murray M.A., Scott J.A., Lavery M.A., Warman M.L., Robin N.H.View abstractCited forINVOLVEMENT IN OSMEDA, VARIANT OSMEDA 940-GLY--PRO-948 DELCategoriesSequences, Disease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Pediatr. 132:368-371 (1998)Cited in1
Mutations in COL11A2 cause non-syndromic hearing loss (DFNA13).McGuirt W.T., Prasad S.D., Griffith A.J., Kunst H.P.M., Green G.E., Shpargel K.B., Runge C., Huybrechts C., Mueller R.F.[...], Smith R.J.H.View abstractCited forSEQUENCE REVISION TO 1031-1032, VARIANTS DFNA13 GLU-808 AND CYS-1034CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Genet. 23:413-419 (1999)Cited in1Mapped to4
Mutation of COL11A2 causes autosomal recessive non-syndromic hearing loss at the DFNB53 locus.Chen W., Kahrizi K., Meyer N.C., Riazalhosseini Y., Van Camp G., Najmabadi H., Smith R.J.H.View abstractCited forVARIANT DFNB53 THR-621CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Med. Genet. 42:E61-E61 (2005)Cited in1Mapped to14
Targeted massive parallel sequencing: the effective detection of novel causative mutations associated with hearing loss in small families.Baek J.I., Oh S.K., Kim D.B., Choi S.Y., Kim U.K., Lee K.Y., Lee S.H.View abstractCited forVARIANT LEU-1422CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCOrphanet J. Rare Dis. 7:60-60 (2012)Cited in7
Novel mutations confirm that COL11A2 is responsible for autosomal recessive non-syndromic hearing loss DFNB53.Chakchouk I., Grati M., Bademci G., Bensaid M., Ma Q., Chakroun A., Foster J. II, Yan D., Duman D.[...], Liu X.Z.View abstractCited forVARIANTS DFNB53 SER-37 AND THR-888CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Genet. Genomics 290:1327-1334 (2015)Cited in1Mapped to14
An orphan receptor tyrosine kinase family whose members serve as nonintegrin collagen receptors.Shrivastava A., Radziejewski C., Campbell E., Kovac L., McGlynn M., Ryan T.E., Davis S., Goldfarb M.P., Glass D.J.[...], Yancopoulos G.D.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-2152267, Reactome: R-HSA-2192863, Reactome: R-HSA-2192865, Reactome: R-HSA-2192866, Reactome: R-HSA-2192867, Reactome: R-HSA-2192868, Reactome: R-HSA-2192869, Reactome: R-HSA-2192871, Reactome: R-HSA-2192872, Reactome: R-HSA-2192873, Reactome: R-HSA-2192882, Reactome: R-HSA-2192883PubMedEurope PMCMol Cell 1:25-34 (1997)Mapped to18
The discoidin domain receptor tyrosine kinases are activated by collagen.Vogel W., Gish G.D., Alves F., Pawson T.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-2152267, Reactome: R-HSA-2192863, Reactome: R-HSA-2192865, Reactome: R-HSA-2192866, Reactome: R-HSA-2192867, Reactome: R-HSA-2192868, Reactome: R-HSA-2192869, Reactome: R-HSA-2192871, Reactome: R-HSA-2192872, Reactome: R-HSA-2192873, Reactome: R-HSA-2192882, Reactome: R-HSA-2192883PubMedEurope PMCMol. Cell 1:13-23 (1997)Cited in2Mapped to15
Cloning and characterization of a novel matrix metalloproteinase (MMP), CMMP, from chicken embryo fibroblasts. CMMP, Xenopus XMMP, and human MMP19 have a conserved unique cysteine in the catalytic domain.Yang M., Kurkinen M.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-2470589, Reactome: R-HSA-2470596, Reactome: R-HSA-2470599, Reactome: R-HSA-2470602, Reactome: R-HSA-2470604, Reactome: R-HSA-2470607, Reactome: R-HSA-2470609, Reactome: R-HSA-2470610, Reactome: R-HSA-2470611, Reactome: R-HSA-2470612, Reactome: R-HSA-2470613, Reactome: R-HSA-2470619, Reactome: R-HSA-2470621, Reactome: R-HSA-2470622, Reactome: R-HSA-2470625, Reactome: R-HSA-2470628, Reactome: R-HSA-2470629, Reactome: R-HSA-2470631, Reactome: R-HSA-2470634, Reactome: R-HSA-2470635, Reactome: R-HSA-2470637, Reactome: R-HSA-2470638, Reactome: R-HSA-2470639, Reactome: R-HSA-2470641PubMedEurope PMCJ Biol Chem 273:17893-17900 (1998)Mapped to24
Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3).Valtavaara M., Szpirer C., Szpirer J., Myllylae R.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-2179197, Reactome: R-HSA-2179215, Reactome: R-HSA-2179217, Reactome: R-HSA-2179218, Reactome: R-HSA-2179225, Reactome: R-HSA-2179229PubMedEurope PMCJ. Biol. Chem. 273:12881-12886 (1998)Cited in1Mapped to46
Thiol-independent interaction of protein disulphide isomerase with type X collagen during intra-cellular folding and assembly.McLaughlin S.H., Bulleid N.J.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-2179197PubMedEurope PMCBiochem J 331:793-800 (1998)Mapped to45
Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen.Wilson R., Lees J.F., Bulleid N.J.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-2179197PubMedEurope PMCJ Biol Chem 273:9637-9643 (1998)Mapped to45