P13942 (COBA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 161.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Collagen alpha-2(XI) chain | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Reference proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 1736 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils. |
| Subunit structure | 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. |
| Domain | The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function By similarity. |
| 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. 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. |
| Involvement in disease | Stickler syndrome 3 (STL3) [MIM:184840]: 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. 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. Otospondylomegaepiphyseal dysplasia (OSMED) [MIM:215150]: A skeletal dysplasia characterized by enlarged epiphyses, disproportionate shortness of the limbs, abnormalities in vertebral bodies, and sensorineural hearing loss. Patients have typical facial features, including mid-face hypoplasia with a short upturned nose and depressed nasal bridge. Cleft palate and a small mandible are also common findings. Weissenbacher-Zweymueller syndrome (WZS) [MIM:277610]: An autosomal dominant disorder characterized by neonatal micrognathia and rhizomelic chondrodysplasia with dumbbell-shaped femora and humeri, and regression of bone changes and normal growth in later years. WZS is also referred to as heterozygous OSMED. Deafness, autosomal dominant, 13 (DFNA13) [MIM:601868]: A form of non-syndromic 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. Deafness, autosomal recessive, 53 (DFNB53) [MIM:609706]: A form of non-syndromic sensorineural deafness characterized by prelingual, profound, non-progressive 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. Fibrochondrogenesis 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. |
| Sequence similarities | Belongs to the fibrillar collagen family. Contains 8 collagen-like domains. Contains 1 fibrillar collagen NC1 domain. Contains 1 laminin G-like domain. |
Ontologies
Alternative products
| This entry describes 9 isoforms produced by alternative splicing. [Align] [Select] Note: Isoforms lack exons 6, 7 or 8 or a combination of these exons. Experimental confirmation may be lacking for some isoforms. | ||||||
| Isoform 1 (identifier: P13942-1) 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: P13942-2) The sequence of this isoform differs from the canonical sequence as follows: 267-292: Missing. | ||||||
| Isoform 3 (identifier: P13942-3) The sequence of this isoform differs from the canonical sequence as follows: 293-313: Missing. | ||||||
| Isoform 4 (identifier: P13942-4) The sequence of this isoform differs from the canonical sequence as follows: 314-373: Missing. | ||||||
| Isoform 5 (identifier: P13942-5) The sequence of this isoform differs from the canonical sequence as follows: 267-292: Missing. 293-313: Missing. | ||||||
| Isoform 6 (identifier: P13942-6) The sequence of this isoform differs from the canonical sequence as follows: 267-292: Missing. 314-373: Missing. | ||||||
| Isoform 7 (identifier: P13942-7) The sequence of this isoform differs from the canonical sequence as follows: 293-313: Missing. 314-373: Missing. | ||||||
| Isoform 8 (identifier: P13942-8) The sequence of this isoform differs from the canonical sequence as follows: 267-292: Missing. 293-313: Missing. 314-373: Missing. | ||||||
| Isoform 9 (identifier: P13942-9) The sequence of this isoform differs from the canonical sequence as follows: 267-290: PTESLYYDYEPPYYDVMTTGTTPD → VRELGEPPSAAHPREGRHPGISPP 291-1736: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 27 | 27 | Potential | ||||||||
| Chain | 28 – 1736 | 1709 | Collagen alpha-2(XI) chain | PRO_0000005840 | |||||||
| Propeptide | 1501 – 1736 | 236 | C-terminal propeptide | PRO_0000005841 | |||||||
Regions | |||||||||||
| Domain | 57 – 228 | 172 | Laminin G-like | ||||||||
| Domain | 399 – 447 | 49 | Collagen-like 1 | ||||||||
| Domain | 487 – 545 | 59 | Collagen-like 2 | ||||||||
| Domain | 546 – 590 | 45 | Collagen-like 3 | ||||||||
| Domain | 805 – 862 | 58 | Collagen-like 4 | ||||||||
| Domain | 863 – 899 | 37 | Collagen-like 5 | ||||||||
| Domain | 1099 – 1156 | 58 | Collagen-like 6 | ||||||||
| Domain | 1157 – 1172 | 16 | Collagen-like 7 | ||||||||
| Domain | 1441 – 1499 | 59 | Collagen-like 8 | ||||||||
| Domain | 1541 – 1735 | 195 | Fibrillar collagen NC1 | ||||||||
| Region | 215 – 486 | 272 | Nonhelical region | ||||||||
| Region | 487 – 1500 | 1014 | Triple-helical region | ||||||||
| Compositional bias | 298 – 301 | 4 | Poly-Glu | ||||||||
Sites | |||||||||||
| Metal binding | 1589 | 1 | Calcium By similarity | ||||||||
| Metal binding | 1591 | 1 | Calcium By similarity | ||||||||
| Metal binding | 1592 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 1594 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 1597 | 1 | Calcium By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 1604 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 1571 ↔ 1603 | By similarity | |||||||||
| Disulfide bond | 1577 | Interchain By similarity | |||||||||
| Disulfide bond | 1594 | Interchain By similarity | |||||||||
| Disulfide bond | 1612 ↔ 1733 | By similarity | |||||||||
| Disulfide bond | 1655 ↔ 1689 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 267 – 292 | 26 | Missing in isoform 2, isoform 5, isoform 6 and isoform 8. | VSP_001167 | |||||||
| Alternative sequence | 267 – 290 | 24 | PTESL…GTTPD → VRELGEPPSAAHPREGRHPG ISPP in isoform 9. | VSP_043432 | |||||||
| Alternative sequence | 291 – 1736 | 1446 | Missing in isoform 9. | VSP_043433 | |||||||
| Alternative sequence | 293 – 313 | 21 | Missing in isoform 3, isoform 5, isoform 7 and isoform 8. | VSP_001168 | |||||||
| Alternative sequence | 314 – 373 | 60 | Missing in isoform 4, isoform 6, isoform 7 and isoform 8. | VSP_001169 | |||||||
| Natural variant | 236 | 1 | P → S. Corresponds to variant rs35116188 [ dbSNP | Ensembl ]. | VAR_048804 | |||||||
| Natural variant | 276 | 1 | E → K. Corresponds to variant rs9277934 [ dbSNP | Ensembl ]. | VAR_048805 | |||||||
| Natural variant | 593 | 1 | D → G. Ref.13 | VAR_013591 | |||||||
| Natural variant | 621 | 1 | P → T in DFNB53. Ref.17 | VAR_025276 | |||||||
| Natural variant | 661 | 1 | G → R in OSMED. Ref.12 | VAR_001907 | |||||||
| Natural variant | 808 | 1 | G → E in DFNA13. Ref.16 | VAR_010655 | |||||||
| Natural variant | 824 | 1 | E → K. Ref.13 Corresponds to variant rs1799909 [ dbSNP | Ensembl ]. | VAR_013592 | |||||||
| Natural variant | 879 | 1 | P → L. Ref.13 | VAR_013593 | |||||||
| Natural variant | 894 | 1 | L → P. Corresponds to variant rs2855430 [ dbSNP | Ensembl ]. | VAR_048806 | |||||||
| Natural variant | 940 – 948 | 9 | Missing in STL3. | VAR_013594 | |||||||
| Natural variant | 1034 | 1 | R → C in DFNA13. Ref.16 | VAR_010656 | |||||||
| Natural variant | 1316 | 1 | P → T. Ref.13 Corresponds to variant rs2229784 [ dbSNP | Ensembl ]. | VAR_013596 | |||||||
| Natural variant | 1441 | 1 | G → E in WZS. Ref.14 | VAR_013595 | |||||||
| Natural variant | 1600 | 1 | R → Q. Ref.13 Corresponds to variant rs1799912 [ dbSNP | Ensembl ]. | VAR_013597 | |||||||
| Natural variant | 1628 | 1 | E → D. Corresponds to variant rs2229790 [ dbSNP | Ensembl ]. | VAR_033797 | |||||||
| Natural variant | 1722 | 1 | P → L. Corresponds to variant rs2229792 [ dbSNP | Ensembl ]. | VAR_048807 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 7 | 1 | C → G in AAC50213. Ref.1 | ||||||||
| Sequence conflict | 7 | 1 | C → G in AAC50214. Ref.1 | ||||||||
| Sequence conflict | 7 | 1 | C → G in AAC50215. Ref.1 | ||||||||
| Sequence conflict | 85 | 1 | S → P in AAC17464. Ref.5 | ||||||||
| Sequence conflict | 85 | 1 | S → P in AAA35498. Ref.6 | ||||||||
| Sequence conflict | 97 | 1 | Q → R in AAC17464. Ref.5 | ||||||||
| Sequence conflict | 97 | 1 | Q → R in AAA35498. Ref.6 | ||||||||
| Sequence conflict | 530 – 531 | 2 | PP → SL in AAC50213. Ref.1 | ||||||||
| Sequence conflict | 530 – 531 | 2 | PP → SL in AAC50214. Ref.1 | ||||||||
| Sequence conflict | 530 – 531 | 2 | PP → SL in AAC50215. Ref.1 | ||||||||
| Sequence conflict | 530 – 531 | 2 | PP → SL in AAC17464. Ref.5 | ||||||||
| Sequence conflict | 530 – 531 | 2 | PP → SL in AAA35498. Ref.6 | ||||||||
| Sequence conflict | 542 | 1 | A → P in AAA35498. Ref.6 | ||||||||
| Sequence conflict | 548 – 549 | 2 | MP → TL in AAA35498. Ref.6 | ||||||||
| Sequence conflict | 578 – 579 | 2 | AQ → PR in AAA35498. Ref.6 | ||||||||
| Sequence conflict | 704 – 705 | 2 | NQ → KP in AAA35498. Ref.6 | ||||||||
| Sequence conflict | 720 | 1 | R → Q in AAA35498. Ref.6 | ||||||||
| Sequence conflict | 726 | 1 | D → N in AAA35498. Ref.6 | ||||||||
| Sequence conflict | 843 – 846 | 4 | TGPR → HGST in AAA52034. Ref.7 | ||||||||
| Sequence conflict | 882 – 884 | 3 | QGP → SGS in AAA52034. Ref.7 | ||||||||
| Sequence conflict | 1031 – 1032 | 2 | PP → RQ in AAC50213. Ref.1 | ||||||||
| Sequence conflict | 1031 – 1032 | 2 | PP → RQ in AAC50214. Ref.1 | ||||||||
| Sequence conflict | 1031 – 1032 | 2 | PP → RQ in AAC50215. Ref.1 | ||||||||
| Sequence conflict | 1031 – 1032 | 2 | PP → RQ in AAA52034. Ref.7 | ||||||||
| Sequence conflict | 1091 | 1 | D → V in AAA52034. Ref.7 | ||||||||
| Sequence conflict | 1124 | 1 | A → R in AAA52034. Ref.7 | ||||||||
| Sequence conflict | 1127 – 1133 | 7 | EPGARGP → GAGGLGT in AAA52034. Ref.7 | ||||||||
| Sequence conflict | 1253 | 1 | P → A in AAC50213. Ref.1 | ||||||||
| Sequence conflict | 1253 | 1 | P → A in AAC50214. Ref.1 | ||||||||
| Sequence conflict | 1253 | 1 | P → A in AAC50215. Ref.1 | ||||||||
| Sequence conflict | 1253 | 1 | P → A in AAA52034. Ref.7 | ||||||||
| Sequence conflict | 1257 | 1 | T → Q in AAC50213. Ref.1 | ||||||||
| Sequence conflict | 1257 | 1 | T → Q in AAC50214. Ref.1 | ||||||||
| Sequence conflict | 1257 | 1 | T → Q in AAC50215. Ref.1 | ||||||||
| Sequence conflict | 1257 | 1 | T → Q in AAA52034. Ref.7 | ||||||||
| Sequence conflict | 1552 | 1 | E → R in AAA52034. Ref.7 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "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. J. Biol. Chem. 270:22873-22881(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "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., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. Beck S.Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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] (ISOFORM 9). Tissue: Skin. |
| [5] | "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. Genomics 32:401-412(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-537. |
| [6] | "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. FEBS Lett. 326:25-28(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-807. Tissue: Cartilage. |
| [7] | "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. J. Biol. Chem. 264:13910-13916(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 730-1690. |
| [8] | "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. J. Biol. Chem. 270:9486-9493(1995) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING. |
| [9] | "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., Bonaventure J., Miny P., Ala-Kokko L. Am. J. Hum. Genet. 66:368-377(2000) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE. |
| [10] | "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. Hum. Mutat. 9:300-315(1997) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS. |
| [11] | "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. Am. J. Med. Genet. A 158:309-314(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN FBCG2. |
| [12] | "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., Ropers H.-H., Mayne R., Cheah K.S.E., Olsen B.R., Warman M.L., Brunner H.G. Cell 80:431-437(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OSMED ARG-661. |
| [13] | "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., Inoue I., Leppert M. Am. J. Hum. Genet. 62:1460-1467(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLY-593; LYS-824; LEU-879; THR-1316 AND GLN-1600. |
| [14] | "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. Am. J. Med. Genet. 80:115-120(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT WZS GLU-1441. |
| [15] | "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. J. Pediatr. 132:368-371(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT STL3 940-GLY--PRO-948 DEL. |
| [16] | "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., Lynch E., King M.-C., Brunner H.G., Cremers C.W.R.J., Takanosu M., Li S.-W., Arita M., Mayne R., Prockop D.J., Van Camp G., Smith R.J.H. Nat. Genet. 23:413-419(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 1031-1032, VARIANTS DFNA13 GLU-808 AND CYS-1034. |
| [17] | "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. J. Med. Genet. 42:E61-E61(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DFNB53 THR-621. |
| + | Additional computationally mapped references. |
Web resources
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U32169 Genomic DNA. Translation: AAC50213.1. U32169 Genomic DNA. Translation: AAC50214.1. U32169 Genomic DNA. Translation: AAC50215.1. AL031228 Genomic DNA. Translation: CAA20240.1. AL645940 Genomic DNA. Translation: CAI18063.2. AL662824 Genomic DNA. No translation available. AL844527 Genomic DNA. Translation: CAM25784.1. AL844527, AL845446 Genomic DNA. Translation: CAI41834.1. AL845446, AL844527 Genomic DNA. Translation: CAI95551.1. CR759733 Genomic DNA. Translation: CAQ10294.1. CR759733 Genomic DNA. Translation: CAQ10296.1. CR936877 Genomic DNA. Translation: CAQ09060.1. CR936877 Genomic DNA. Translation: CAQ09062.1. CH471081 Genomic DNA. Translation: EAX03676.1. BC053886 mRNA. Translation: AAH53886.1. U41069 U41067 Genomic DNA. Translation: AAC17464.1.L18987 mRNA. Translation: AAA35498.1. J04974 mRNA. Translation: AAA52034.1. |
| IPI | IPI00011283. IPI00219922. IPI00219923. IPI00219924. IPI00219925. IPI00219927. IPI00413940. IPI00748259. IPI00937105. |
| PIR | CGHU2E. S34790. |
| RefSeq | NP_001157243.1. NM_001163771.1. NP_542411.2. NM_080680.2. NP_542412.2. NM_080681.2. |
| UniGene | Hs.390171. |
3D structure databases | |
| ProteinModelPortal | P13942. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P13942. 1 interaction. |
| MINT | MINT-5222373. |
| STRING | 9606.ENSP00000414605. |
PTM databases | |
| PhosphoSite | P13942. |
Polymorphism databases | |
| DMDM | 116241308. |
Proteomic databases | |
| PaxDb | P13942. |
| PRIDE | P13942. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000341947; ENSP00000339915; ENSG00000204248. ENST00000383087; ENSP00000372565; ENSG00000227801. ENST00000383088; ENSP00000372566; ENSG00000206290. ENST00000395194; ENSP00000378620; ENSG00000204248. ENST00000439039; ENSP00000410284; ENSG00000227801. ENST00000447741; ENSP00000400813; ENSG00000235708. ENST00000452937; ENSP00000406347; ENSG00000230930. ENST00000547261; ENSP00000450150; ENSG00000227801. ENST00000547999; ENSP00000446903; ENSG00000227801. ENST00000549289; ENSP00000448643; ENSG00000227801. ENST00000549381; ENSP00000448464; ENSG00000227801. ENST00000549811; ENSP00000449275; ENSG00000227801. ENST00000550561; ENSP00000449393; ENSG00000227801. ENST00000551542; ENSP00000447864; ENSG00000227801. ENST00000551758; ENSP00000447062; ENSG00000230930. |
| GeneID | 1302. |
| KEGG | hsa:1302. |
| UCSC | uc003ocx.1. human. uc003ocy.1. human. uc003ocz.1. human. |
Organism-specific databases | |
| CTD | 1302. |
| GeneCards | GC06M033130. |
| H-InvDB | HIX0033301. HIX0166403. HIX0166658. HIX0166919. HIX0167181. HIX0167416. HIX0184201. HIX0207630. |
| HGNC | HGNC:2187. COL11A2. |
| MIM | 120290. gene. 184840. phenotype. 215150. phenotype. 277610. phenotype. 601868. phenotype. 609706. phenotype. 614524. phenotype. |
| neXtProt | NX_P13942. |
| Orphanet | 90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA. 90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB. 2021. Fibrochondrogenesis. 1427. Otospondylomegaepiphyseal dysplasia. 166100. Stickler syndrome type 3. 3450. Weissenbacher- Zweymuller syndrome. |
| PharmGKB | PA26703. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | NOG12793. |
| HOGENOM | HOG000205337. |
| HOVERGEN | HBG004933. |
| InParanoid | P13942. |
| KO | K06236. |
Enzyme and pathway databases | |
| Reactome | REACT_118779. Extracellular matrix organization. |
Gene expression databases | |
| ArrayExpress | P13942. |
| Bgee | P13942. |
| CleanEx | HS_COL11A2. |
| Genevestigator | P13942. |
| GermOnline | ENSG00000204248. Homo sapiens. |
Family and domain databases | |
| Gene3D | 2.60.120.200. 1 hit. |
| InterPro | IPR008160. Collagen. IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR000885. Fib_collagen_C. IPR001791. Laminin_G. [Graphical view] |
| Pfam | PF01410. COLFI. 2 hits. PF01391. Collagen. 8 hits. PF02210. Laminin_G_2. 1 hit. [Graphical view] |
| ProDom | PD002078. Fib_collagen_C. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00038. COLFI. 1 hit. SM00282. LamG. 1 hit. SM00210. TSPN. 1 hit. [Graphical view] |
| SUPFAM | SSF49899. ConA_like_lec_gl. 1 hit. |
| PROSITE | PS50025. LAM_G_DOMAIN. False negative. PS51461. NC1_FIB. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| GenomeRNAi | 1302. |
| NextBio | 5291. |
| SOURCE | Search... |
Entry information
| Entry name | COBA2_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P13942 Secondary accession number(s): A6NLX2 Q9UIP9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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
| Human chromosome 6 Human chromosome 6: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
