P13942 · COBA2_HUMAN

  • Protein
    Collagen alpha-2(XI) chain
  • Gene
    COL11A2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.

Features

Showing features for binding site.

117362004006008001,0001,2001,4001,600
TypeIDPosition(s)Description
Binding site1589Ca2+ (UniProtKB | ChEBI)
Binding site1591Ca2+ (UniProtKB | ChEBI)
Binding site1592Ca2+ (UniProtKB | ChEBI)
Binding site1594Ca2+ (UniProtKB | ChEBI)
Binding site1597Ca2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcollagen trimer
Cellular Componentcollagen type XI trimer
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentendoplasmic reticulum lumen
Cellular Componentextracellular region
Cellular Componentextracellular space
Molecular Functionextracellular matrix structural constituent conferring tensile strength
Molecular Functionheparin binding
Molecular Functionmetal ion binding
Molecular Functionprotein-macromolecule adaptor activity
Biological Processcartilage development
Biological Processcollagen fibril organization
Biological Processroof of mouth development
Biological Processsensory perception of sound
Biological Processskeletal system development
Biological Processsoft palate development

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Collagen alpha-2(XI) chain

Gene names

    • Name
      COL11A2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P13942
  • Secondary accessions
    • A6NLX2
    • E7ER90
    • Q07751
    • Q13271
    • Q13272

Proteomes

Organism-specific databases

Disease & Variants

Involvement in disease

Otospondylomegaepiphyseal dysplasia, autosomal dominant (OSMEDA)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An autosomal dominant form of otospondylomegaepiphyseal dysplasia, a disorder characterized by sensorineural deafness, enlarged epiphyses, mild platyspondyly, and disproportionate shortness of the limbs. Total body length is normal. Typical facial features are mid-face hypoplasia, short upturned nose and depressed nasal bridge. Most patients have Pierre Robin sequence including an opening in the roof of the mouth (cleft palate) and a small lower jaw (micrognathia). Ocular symptoms are absent. Some patients have early-onset osteoarthritis.
  • See also
    MIM:184840
Natural variants in OSMEDA
Variant IDPosition(s)ChangeDescription
VAR_013594940-948missingin OSMEDA
VAR_0135951441G>Ein OSMEDA; dbSNP:rs121912946

Otospondylomegaepiphyseal dysplasia, autosomal recessive (OSMEDB)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An autosomal recessive form of otospondylomegaepiphyseal dysplasia, a disorder characterized by sensorineural deafness, enlarged epiphyses, mild platyspondyly, and disproportionate shortness of the limbs. Total body length is normal. Typical facial features are mid-face hypoplasia, short upturned nose and depressed nasal bridge. Most patients have Pierre Robin sequence including an opening in the roof of the mouth (cleft palate) and a small lower jaw (micrognathia). Ocular symptoms are absent. Some patients have early-onset osteoarthritis.
  • See also
    MIM:215150
Natural variants in OSMEDB
Variant IDPosition(s)ChangeDescription
VAR_001907661G>Rin OSMEDB; dbSNP:rs121912945

Deafness, autosomal dominant, 13 (DFNA13)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    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.
  • See also
    MIM:601868
Natural variants in DFNA13
Variant IDPosition(s)ChangeDescription
VAR_010655808G>Ein DFNA13; dbSNP:rs121912948
VAR_0106561034R>Cin DFNA13; dbSNP:rs121912947

Deafness, autosomal recessive, 53 (DFNB53)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    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.
  • See also
    MIM:609706
Natural variants in DFNB53
Variant IDPosition(s)ChangeDescription
VAR_07273137A>Sin DFNB53; dbSNP:rs606231410
VAR_025276621P>Tin DFNB53; dbSNP:rs121912952
VAR_072732888P>Tin DFNB53; dbSNP:rs864309523

Fibrochondrogenesis 2 (FBCG2)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    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.
  • See also
    MIM:614524

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_07273137in DFNB53; dbSNP:rs606231410
Natural variantVAR_048804236in dbSNP:rs35116188
Natural variantVAR_048805276in dbSNP:rs9277934
Natural variantVAR_013591593
Natural variantVAR_025276621in DFNB53; dbSNP:rs121912952
Natural variantVAR_001907661in OSMEDB; dbSNP:rs121912945
Natural variantVAR_010655808in DFNA13; dbSNP:rs121912948
Natural variantVAR_013592824in dbSNP:rs1799909
Natural variantVAR_013593879in dbSNP:rs747883362
Natural variantVAR_072732888in DFNB53; dbSNP:rs864309523
Natural variantVAR_048806894in dbSNP:rs2855430
Natural variantVAR_013594940-948in OSMEDA
Natural variantVAR_0106561034in DFNA13; dbSNP:rs121912947
Natural variantVAR_0135961316in dbSNP:rs2229784
Natural variantVAR_0798751422in dbSNP:rs555936333
Natural variantVAR_0135951441in OSMEDA; dbSNP:rs121912946
Natural variantVAR_0135971600in dbSNP:rs1799912
Natural variantVAR_0337971628in dbSNP:rs2229790
Natural variantVAR_0488071722in dbSNP:rs2229792

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,487 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, propeptide, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-27
ChainPRO_000000584028-1736Collagen alpha-2(XI) chain
PropeptidePRO_00000058411501-1736C-terminal propeptide
Disulfide bond1571↔1603
Disulfide bond1577Interchain
Disulfide bond1594Interchain
Glycosylation1604N-linked (GlcNAc...) asparagine
Disulfide bond1612↔1733
Disulfide bond1655↔1689

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.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

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).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P13942DDR2 Q168322EBI-2515504, EBI-1381484
View interactors in UniProtKB
View CPX-1750 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain57-228Laminin G-like
Region215-486Nonhelical region
Region227-303Disordered
Compositional bias233-271Polar residues
Region330-465Disordered
Domain399-447Collagen-like 1
Region485-1538Disordered
Domain487-545Collagen-like 2
Region487-1500Triple-helical region
Domain546-590Collagen-like 3
Compositional bias727-744Basic and acidic residues
Domain805-862Collagen-like 4
Domain863-899Collagen-like 5
Compositional bias874-900Pro residues
Domain1099-1156Collagen-like 6
Domain1157-1172Collagen-like 7
Compositional bias1175-1189Pro residues
Domain1441-1499Collagen-like 8
Domain1541-1735Fibrillar collagen NC1

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).

Sequence similarities

Belongs to the fibrillar collagen family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (9)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 9 isoforms produced by Alternative splicing. Isoforms lack exons 6, 7 or 8 or a combination of these exons. Experimental confirmation may be lacking for some isoforms.

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.

  • Length
    1,736
  • Mass (Da)
    171,791
  • Last updated
    2012-01-25 v5
  • Checksum
    D687B7AAD6A7774C
MERCSRCHRLLLLLPLVLGLSAAPGWAGAPPVDVLRALRFPSLPDGVRRAKGICPADVAYRVARPAQLSAPTRQLFPGGFPKDFSLLTVVRTRPGLQAPLLTLYSAQGVRQLGLELGRPVRFLYEDQTGRPQPPSQPVFRGLSLADGKWHRVAVAVKGQSVTLIVDCKKRVTRPLPRSARPVLDTHGVIIFGARILDEEVFEGDVQELAIVPGVQAAYESCEQKELECEGGQRERPQNQQPHRAQRSPQQQPSRLHRPQNQEPQSQPTESLYYDYEPPYYDVMTTGTTPDYQDPTPGEEEEILESSLLPPLEEEQTDLQVPPTADRFQAEEYGEGGTDPPEGPYDYTYGYGDDYREETELGPALSAETAHSGAAAHGPRGLKGEKGEPAVLEPGMLVEGPPGPEGPAGLIGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGAPGPPGTSLMLPFRFGSGGGDKGPVVAAQEAQAQAILQQARLALRGPPGPMGYTGRPGPLGQPGSPGLKGESGDLGPQGPRGPQGLTGPPGKAGRRGRAGADGARGMPGDPGVKGDRGFDGLPGLPGEKGHRGDTGAQGLPGPPGEDGERGDDGEIGPRGLPGESGPRGLLGPKGPPGIPGPPGVRGMDGPQGPKGSLGPQGEPGPPGQQGTPGTQGLPGPQGAIGPHGEKGPQGKPGLPGMPGSDGPPGHPGKEGPPGTKGNQGPSGPQGPLGYPGPRGVKGVDGIRGLKGHKGEKGEDGFPGFKGDIGVKGDRGEVGVPGSRGEDGPEGPKGRTGPTGDPGPPGLMGEKGKLGVPGLPGYPGRQGPKGSLGFPGFPGASGEKGARGLSGKSGPRGERGPTGPRGQRGPRGATGKSGAKGTSGGDGPHGPPGERGLPGPQGPNGFPGPKGPLGPPGKDGLPGHPGQRGEVGFQGKTGPPGPPGVVGPQGAAGETGPMGERGHPGPPGPPGEQGLPGTAGKEGTKGDPGPPGAPGKDGPAGLRGFPGERGLPGTAGGPGLKGNEGPSGPPGPAGSPGERGAAGSGGPIGPPGRPGPQGPPGAAGEKGVPGEKGPIGPTGRDGVQGPVGLPGPAGPPGVAGEDGDKGEVGDPGQKGTKGNKGEHGPPGPPGPIGPVGQPGAAGADGEPGARGPQGHFGAKGDEGTRGFNGPPGPIGLQGLPGPSGEKGETGDVGPMGPPGPPGPRGPAGPNGADGPQGPPGGVGNLGPPGEKGEPGESGSPGIQGEPGVKGPRGERGEKGESGQPGEPGPPGPKGPTGDDGPKGNPGPVGFPGDPGPPGEGGPRGQDGAKGDRGEDGEPGQPGSPGPTGENGPPGPLGKRGPAGSPGSEGRQGGKGAKGDPGAIGAPGKTGPVGPAGPAGKPGPDGLRGLPGSVGQQGRPGATGQAGPPGPVGPPGLPGLRGDAGAKGEKGHPGLIGLIGPPGEQGEKGDRGLPGPQGSPGQKGEMGIPGASGPIGPGGPPGLPGPAGPKGAKGATGPGGPKGEKGVQGPPGHPGPPGEVIQPLPIQMPKKTRRSVDGSRLMQEDEAIPTGGAPGSPGGLEEIFGSLDSLREEIEQMRRPTGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGAARDGPLRLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFSDLGAPPRRGGVLLGPVCFMG

P13942-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P13942-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P13942-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P13942-5

P13942-6

P13942-7

P13942-8

P13942-9

  • Name
    9
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 267-290: PTESLYYDYEPPYYDVMTTGTTPD → VRELGEPPSAAHPREGRHPGISPP
    • 291-1736: Missing

Computationally mapped potential isoform sequences

There are 16 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A2AAS7A2AAS7_HUMANCOL11A2624
H0YIS1H0YIS1_HUMANCOL11A2435
A0A140T9X7A0A140T9X7_HUMANCOL11A2624
A0A140T9W8A0A140T9W8_HUMANCOL11A2597
A0A140T9N0A0A140T9N0_HUMANCOL11A2263
A0A140T9N1A0A140T9N1_HUMANCOL11A21650
A0A140T9I7A0A140T9I7_HUMANCOL11A21623
A0A140T9A1A0A140T9A1_HUMANCOL11A2290
Q4VXY6Q4VXY6_HUMANCOL11A21650
A0A140TA54A0A140TA54_HUMANCOL11A21629
A0A140TA43A0A140TA43_HUMANCOL11A21736
A0A0G2JL35A0A0G2JL35_HUMANCOL11A21736
A0A0G2JL78A0A0G2JL78_HUMANCOL11A21629
A0A0G2JI07A0A0G2JI07_HUMANCOL11A2624
A0A0C4DFS1A0A0C4DFS1_HUMANCOL11A21736
A0A0G2JHD9A0A0G2JHD9_HUMANCOL11A2333

Features

Showing features for sequence conflict, compositional bias, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict7in Ref. 1; AAC50213/AAC50214/AAC50215
Sequence conflict85in Ref. 5; AAC17464 and 6; AAA35498
Sequence conflict97in Ref. 5; AAC17464 and 6; AAA35498
Compositional bias233-271Polar residues
Alternative sequenceVSP_043432267-290in isoform 9
Alternative sequenceVSP_001167267-292in isoform 2, isoform 5, isoform 6 and isoform 8
Alternative sequenceVSP_043433291-1736in isoform 9
Alternative sequenceVSP_001168293-313in isoform 3, isoform 5, isoform 7 and isoform 8
Alternative sequenceVSP_001169314-373in isoform 4, isoform 6, isoform 7 and isoform 8
Sequence conflict530-531in Ref. 1; AAC50213/AAC50214/AAC50215, 5; AAC17464 and 6; AAA35498
Sequence conflict542in Ref. 6; AAA35498
Sequence conflict548-549in Ref. 6; AAA35498
Sequence conflict578-579in Ref. 6; AAA35498
Sequence conflict704-705in Ref. 6; AAA35498
Sequence conflict720in Ref. 6; AAA35498
Sequence conflict726in Ref. 6; AAA35498
Compositional bias727-744Basic and acidic residues
Sequence conflict843-846in Ref. 7; AAA52034
Compositional bias874-900Pro residues
Sequence conflict882-884in Ref. 7; AAA52034
Sequence conflict1031-1032in Ref. 1; AAC50213/AAC50214/AAC50215 and 7; AAA52034
Sequence conflict1091in Ref. 7; AAA52034
Sequence conflict1124in Ref. 7; AAA52034
Sequence conflict1127-1133in Ref. 7; AAA52034
Compositional bias1175-1189Pro residues
Sequence conflict1253in Ref. 1; AAC50213/AAC50214/AAC50215 and 7; AAA52034
Sequence conflict1257in Ref. 1; AAC50213/AAC50214/AAC50215 and 7; AAA52034
Sequence conflict1552in Ref. 7; AAA52034

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U32169
EMBL· GenBank· DDBJ
AAC50213.1
EMBL· GenBank· DDBJ
Genomic DNA
U32169
EMBL· GenBank· DDBJ
AAC50214.1
EMBL· GenBank· DDBJ
Genomic DNA
U32169
EMBL· GenBank· DDBJ
AAC50215.1
EMBL· GenBank· DDBJ
Genomic DNA
AL031228
EMBL· GenBank· DDBJ
CAA20240.1
EMBL· GenBank· DDBJ
Genomic DNA
AL645940
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL662824
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL844527
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL845446
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CR759733
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CR936877
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471081
EMBL· GenBank· DDBJ
EAX03676.1
EMBL· GenBank· DDBJ
Genomic DNA
BC053886
EMBL· GenBank· DDBJ
AAH53886.1
EMBL· GenBank· DDBJ
mRNA
U41069
EMBL· GenBank· DDBJ
AAC17464.1
EMBL· GenBank· DDBJ
Genomic DNA
U41065
EMBL· GenBank· DDBJ
AAC17464.1
EMBL· GenBank· DDBJ
Genomic DNA
U41066
EMBL· GenBank· DDBJ
AAC17464.1
EMBL· GenBank· DDBJ
Genomic DNA
U41067
EMBL· GenBank· DDBJ
AAC17464.1
EMBL· GenBank· DDBJ
Genomic DNA
L18987
EMBL· GenBank· DDBJ
AAA35498.1
EMBL· GenBank· DDBJ
mRNA
J04974
EMBL· GenBank· DDBJ
AAA52034.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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