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P13942 (COBA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-2(XI) chain
Gene names
Name:COL11A2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1736 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 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

Secretedextracellular spaceextracellular 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.15

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.12

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.14

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.16

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.17

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.11

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

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDeafness
Disease mutation
Dwarfism
Non-syndromic deafness
Stickler syndrome
   DomainCollagen
Repeat
Signal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcartilage development

Inferred from mutant phenotype PubMed 9188673. Source: UniProtKB

collagen catabolic process

Traceable author statement. Source: Reactome

collagen fibril organization

Inferred from direct assay PubMed 9188673. Source: UniProtKB

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

palate development

Inferred from mutant phenotype PubMed 12673280. Source: UniProtKB

sensory perception of sound

Inferred from mutant phenotype Ref.9Ref.17PubMed 9188673. Source: UniProtKB

skeletal system development

Inferred from mutant phenotype Ref.9. Source: UniProtKB

soft palate development

Inferred from mutant phenotype Ref.9. Source: UniProtKB

   Cellular_componentcollagen type XI trimer

Non-traceable author statement Ref.12Ref.5. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

   Molecular_functionextracellular matrix structural constituent conferring tensile strength

Non-traceable author statement Ref.12Ref.5. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 17703188. Source: IntAct

protein binding, bridging

Non-traceable author statement Ref.9. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DDR2Q168322EBI-2515504,EBI-1381484

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 17361709Collagen alpha-2(XI) chain
PRO_0000005840
Propeptide1501 – 1736236C-terminal propeptide
PRO_0000005841

Regions

Domain57 – 228172Laminin G-like
Domain399 – 44749Collagen-like 1
Domain487 – 54559Collagen-like 2
Domain546 – 59045Collagen-like 3
Domain805 – 86258Collagen-like 4
Domain863 – 89937Collagen-like 5
Domain1099 – 115658Collagen-like 6
Domain1157 – 117216Collagen-like 7
Domain1441 – 149959Collagen-like 8
Domain1541 – 1735195Fibrillar collagen NC1
Region215 – 486272Nonhelical region
Region487 – 15001014Triple-helical region
Compositional bias298 – 3014Poly-Glu

Sites

Metal binding15891Calcium By similarity
Metal binding15911Calcium By similarity
Metal binding15921Calcium; via carbonyl oxygen By similarity
Metal binding15941Calcium; via carbonyl oxygen By similarity
Metal binding15971Calcium By similarity

Amino acid modifications

Glycosylation16041N-linked (GlcNAc...) Potential
Disulfide bond1571 ↔ 1603 By similarity
Disulfide bond1577Interchain By similarity
Disulfide bond1594Interchain By similarity
Disulfide bond1612 ↔ 1733 By similarity
Disulfide bond1655 ↔ 1689 By similarity

Natural variations

Alternative sequence267 – 29226Missing in isoform 2, isoform 5, isoform 6 and isoform 8.
VSP_001167
Alternative sequence267 – 29024PTESL…GTTPD → VRELGEPPSAAHPREGRHPG ISPP in isoform 9.
VSP_043432
Alternative sequence291 – 17361446Missing in isoform 9.
VSP_043433
Alternative sequence293 – 31321Missing in isoform 3, isoform 5, isoform 7 and isoform 8.
VSP_001168
Alternative sequence314 – 37360Missing in isoform 4, isoform 6, isoform 7 and isoform 8.
VSP_001169
Natural variant2361P → S.
Corresponds to variant rs35116188 [ dbSNP | Ensembl ].
VAR_048804
Natural variant2761E → K.
Corresponds to variant rs9277934 [ dbSNP | Ensembl ].
VAR_048805
Natural variant5931D → G. Ref.13
VAR_013591
Natural variant6211P → T in DFNB53. Ref.17
VAR_025276
Natural variant6611G → R in OSMED. Ref.12
VAR_001907
Natural variant8081G → E in DFNA13. Ref.16
VAR_010655
Natural variant8241E → K. Ref.13
Corresponds to variant rs1799909 [ dbSNP | Ensembl ].
VAR_013592
Natural variant8791P → L. Ref.13
VAR_013593
Natural variant8941L → P.
Corresponds to variant rs2855430 [ dbSNP | Ensembl ].
VAR_048806
Natural variant940 – 9489Missing in STL3.
VAR_013594
Natural variant10341R → C in DFNA13. Ref.16
VAR_010656
Natural variant13161P → T. Ref.13
Corresponds to variant rs2229784 [ dbSNP | Ensembl ].
VAR_013596
Natural variant14411G → E in WZS. Ref.14
VAR_013595
Natural variant16001R → Q. Ref.13
Corresponds to variant rs1799912 [ dbSNP | Ensembl ].
VAR_013597
Natural variant16281E → D.
Corresponds to variant rs2229790 [ dbSNP | Ensembl ].
VAR_033797
Natural variant17221P → L.
Corresponds to variant rs2229792 [ dbSNP | Ensembl ].
VAR_048807

Experimental info

Sequence conflict71C → G in AAC50213. Ref.1
Sequence conflict71C → G in AAC50214. Ref.1
Sequence conflict71C → G in AAC50215. Ref.1
Sequence conflict851S → P in AAC17464. Ref.5
Sequence conflict851S → P in AAA35498. Ref.6
Sequence conflict971Q → R in AAC17464. Ref.5
Sequence conflict971Q → R in AAA35498. Ref.6
Sequence conflict530 – 5312PP → SL in AAC50213. Ref.1
Sequence conflict530 – 5312PP → SL in AAC50214. Ref.1
Sequence conflict530 – 5312PP → SL in AAC50215. Ref.1
Sequence conflict530 – 5312PP → SL in AAC17464. Ref.5
Sequence conflict530 – 5312PP → SL in AAA35498. Ref.6
Sequence conflict5421A → P in AAA35498. Ref.6
Sequence conflict548 – 5492MP → TL in AAA35498. Ref.6
Sequence conflict578 – 5792AQ → PR in AAA35498. Ref.6
Sequence conflict704 – 7052NQ → KP in AAA35498. Ref.6
Sequence conflict7201R → Q in AAA35498. Ref.6
Sequence conflict7261D → N in AAA35498. Ref.6
Sequence conflict843 – 8464TGPR → HGST in AAA52034. Ref.7
Sequence conflict882 – 8843QGP → SGS in AAA52034. Ref.7
Sequence conflict1031 – 10322PP → RQ in AAC50213. Ref.1
Sequence conflict1031 – 10322PP → RQ in AAC50214. Ref.1
Sequence conflict1031 – 10322PP → RQ in AAC50215. Ref.1
Sequence conflict1031 – 10322PP → RQ in AAA52034. Ref.7
Sequence conflict10911D → V in AAA52034. Ref.7
Sequence conflict11241A → R in AAA52034. Ref.7
Sequence conflict1127 – 11337EPGARGP → GAGGLGT in AAA52034. Ref.7
Sequence conflict12531P → A in AAC50213. Ref.1
Sequence conflict12531P → A in AAC50214. Ref.1
Sequence conflict12531P → A in AAC50215. Ref.1
Sequence conflict12531P → A in AAA52034. Ref.7
Sequence conflict12571T → Q in AAC50213. Ref.1
Sequence conflict12571T → Q in AAC50214. Ref.1
Sequence conflict12571T → Q in AAC50215. Ref.1
Sequence conflict12571T → Q in AAA52034. Ref.7
Sequence conflict15521E → R in AAA52034. Ref.7

Sequences

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

Last modified January 25, 2012. Version 5.
Checksum: D687B7AAD6A7774C

FASTA1,736171,791
        10         20         30         40         50         60 
MERCSRCHRL LLLLPLVLGL SAAPGWAGAP PVDVLRALRF PSLPDGVRRA KGICPADVAY 

        70         80         90        100        110        120 
RVARPAQLSA PTRQLFPGGF PKDFSLLTVV RTRPGLQAPL LTLYSAQGVR QLGLELGRPV 

       130        140        150        160        170        180 
RFLYEDQTGR PQPPSQPVFR GLSLADGKWH RVAVAVKGQS VTLIVDCKKR VTRPLPRSAR 

       190        200        210        220        230        240 
PVLDTHGVII FGARILDEEV FEGDVQELAI VPGVQAAYES CEQKELECEG GQRERPQNQQ 

       250        260        270        280        290        300 
PHRAQRSPQQ QPSRLHRPQN QEPQSQPTES LYYDYEPPYY DVMTTGTTPD YQDPTPGEEE 

       310        320        330        340        350        360 
EILESSLLPP LEEEQTDLQV PPTADRFQAE EYGEGGTDPP EGPYDYTYGY GDDYREETEL 

       370        380        390        400        410        420 
GPALSAETAH SGAAAHGPRG LKGEKGEPAV LEPGMLVEGP PGPEGPAGLI GPPGIQGNPG 

       430        440        450        460        470        480 
PVGDPGERGP PGRAGLPGSD GAPGPPGTSL MLPFRFGSGG GDKGPVVAAQ EAQAQAILQQ 

       490        500        510        520        530        540 
ARLALRGPPG PMGYTGRPGP LGQPGSPGLK GESGDLGPQG PRGPQGLTGP PGKAGRRGRA 

       550        560        570        580        590        600 
GADGARGMPG DPGVKGDRGF DGLPGLPGEK GHRGDTGAQG LPGPPGEDGE RGDDGEIGPR 

       610        620        630        640        650        660 
GLPGESGPRG LLGPKGPPGI PGPPGVRGMD GPQGPKGSLG PQGEPGPPGQ QGTPGTQGLP 

       670        680        690        700        710        720 
GPQGAIGPHG EKGPQGKPGL PGMPGSDGPP GHPGKEGPPG TKGNQGPSGP QGPLGYPGPR 

       730        740        750        760        770        780 
GVKGVDGIRG LKGHKGEKGE DGFPGFKGDI GVKGDRGEVG VPGSRGEDGP EGPKGRTGPT 

       790        800        810        820        830        840 
GDPGPPGLMG EKGKLGVPGL PGYPGRQGPK GSLGFPGFPG ASGEKGARGL SGKSGPRGER 

       850        860        870        880        890        900 
GPTGPRGQRG PRGATGKSGA KGTSGGDGPH GPPGERGLPG PQGPNGFPGP KGPLGPPGKD 

       910        920        930        940        950        960 
GLPGHPGQRG EVGFQGKTGP PGPPGVVGPQ GAAGETGPMG ERGHPGPPGP PGEQGLPGTA 

       970        980        990       1000       1010       1020 
GKEGTKGDPG PPGAPGKDGP AGLRGFPGER GLPGTAGGPG LKGNEGPSGP PGPAGSPGER 

      1030       1040       1050       1060       1070       1080 
GAAGSGGPIG PPGRPGPQGP PGAAGEKGVP GEKGPIGPTG RDGVQGPVGL PGPAGPPGVA 

      1090       1100       1110       1120       1130       1140 
GEDGDKGEVG DPGQKGTKGN KGEHGPPGPP GPIGPVGQPG AAGADGEPGA RGPQGHFGAK 

      1150       1160       1170       1180       1190       1200 
GDEGTRGFNG PPGPIGLQGL PGPSGEKGET GDVGPMGPPG PPGPRGPAGP NGADGPQGPP 

      1210       1220       1230       1240       1250       1260 
GGVGNLGPPG EKGEPGESGS PGIQGEPGVK GPRGERGEKG ESGQPGEPGP PGPKGPTGDD 

      1270       1280       1290       1300       1310       1320 
GPKGNPGPVG FPGDPGPPGE GGPRGQDGAK GDRGEDGEPG QPGSPGPTGE NGPPGPLGKR 

      1330       1340       1350       1360       1370       1380 
GPAGSPGSEG RQGGKGAKGD PGAIGAPGKT GPVGPAGPAG KPGPDGLRGL PGSVGQQGRP 

      1390       1400       1410       1420       1430       1440 
GATGQAGPPG PVGPPGLPGL RGDAGAKGEK GHPGLIGLIG PPGEQGEKGD RGLPGPQGSP 

      1450       1460       1470       1480       1490       1500 
GQKGEMGIPG ASGPIGPGGP PGLPGPAGPK GAKGATGPGG PKGEKGVQGP PGHPGPPGEV 

      1510       1520       1530       1540       1550       1560 
IQPLPIQMPK KTRRSVDGSR LMQEDEAIPT GGAPGSPGGL EEIFGSLDSL REEIEQMRRP 

      1570       1580       1590       1600       1610       1620 
TGTQDSPART CQDLKLCHPE LPDGEYWVDP NQGCARDAFR VFCNFTAGGE TCVTPRDDVT 

      1630       1640       1650       1660       1670       1680 
QFSYVDSEGS PVGVVQLTFL RLLSVSAHQD VSYPCSGAAR DGPLRLRGAN EDELSPETSP 

      1690       1700       1710       1720       1730 
YVKEFRDGCQ TQQGRTVLEV RTPVLEQLPV LDASFSDLGA PPRRGGVLLG PVCFMG 

« Hide

Isoform 2 [UniParc].

Checksum: A2EDA1C81EEA9D22
Show »

FASTA1,710168,698
Isoform 3 [UniParc].

Checksum: 2362B2D6508A0C24
Show »

FASTA1,715169,485
Isoform 4 [UniParc].

Checksum: A87540ED78D3E198
Show »

FASTA1,676165,293
Isoform 5 [UniParc].

Checksum: D53384E69D99D454
Show »

FASTA1,689166,393
Isoform 6 [UniParc].

Checksum: 1ECC3F4C92956F3F
Show »

FASTA1,650162,201
Isoform 7 [UniParc].

Checksum: 125F75A575246E2E
Show »

FASTA1,655162,988
Isoform 8 [UniParc].

Checksum: 9E095488C4B3C32F
Show »

FASTA1,629159,895
Isoform 9 [UniParc].

Checksum: 7E59579056D3640F
Show »

FASTA29031,960

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. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., 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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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 expand/collapse EMBL AC list , U41065, U41066, U41067 Genomic DNA. Translation: AAC17464.1.
L18987 mRNA. Translation: AAA35498.1.
J04974 mRNA. Translation: AAA52034.1.
CCDSCCDS43452.1. [P13942-6]
CCDS54992.1. [P13942-9]
PIRCGHU2E. S34790.
RefSeqNP_001157243.1. NM_001163771.1. [P13942-9]
NP_542411.2. NM_080680.2.
NP_542412.2. NM_080681.2.
UniGeneHs.390171.

3D structure databases

ProteinModelPortalP13942.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107699. 4 interactions.
IntActP13942. 5 interactions.
MINTMINT-5222373.
STRING9606.ENSP00000414605.

Chemistry

ChEMBLCHEMBL2364188.

PTM databases

PhosphoSiteP13942.

Polymorphism databases

DMDM374095517.

Proteomic databases

PaxDbP13942.
PRIDEP13942.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341947; ENSP00000339915; ENSG00000204248.
ENST00000383087; ENSP00000372565; ENSG00000227801. [P13942-6]
ENST00000383088; ENSP00000372566; ENSG00000206290. [P13942-9]
ENST00000395194; ENSP00000378620; ENSG00000204248. [P13942-9]
ENST00000439039; ENSP00000410284; ENSG00000227801. [P13942-9]
ENST00000447741; ENSP00000400813; ENSG00000235708. [P13942-9]
ENST00000452937; ENSP00000406347; ENSG00000230930. [P13942-9]
ENST00000547261; ENSP00000450150; ENSG00000227801. [P13942-7]
ENST00000547999; ENSP00000446903; ENSG00000227801. [P13942-3]
ENST00000549289; ENSP00000448643; ENSG00000227801. [P13942-4]
ENST00000549381; ENSP00000448464; ENSG00000227801. [P13942-5]
ENST00000549811; ENSP00000449275; ENSG00000227801. [P13942-1]
ENST00000550561; ENSP00000449393; ENSG00000227801. [P13942-2]
ENST00000551542; ENSP00000447864; ENSG00000227801. [P13942-8]
ENST00000551758; ENSP00000447062; ENSG00000230930.
GeneID1302.
KEGGhsa:1302.
UCSCuc003ocx.1. human. [P13942-1]
uc003oda.3. human. [P13942-9]

Organism-specific databases

CTD1302.
GeneCardsGC06M033130.
GC06Mj33052.
GC06Mk33108.
GC06Mm33300.
GC06Mn33059.
GeneReviewsCOL11A2.
H-InvDBHIX0033301.
HIX0166403.
HIX0166658.
HIX0166919.
HIX0167181.
HIX0167416.
HIX0184201.
HIX0207630.
HGNCHGNC:2187. COL11A2.
MIM120290. gene.
184840. phenotype.
215150. phenotype.
277610. phenotype.
601868. phenotype.
609706. phenotype.
614524. phenotype.
neXtProtNX_P13942.
Orphanet90635. 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.
PharmGKBPA26703.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000205337.
HOVERGENHBG004933.
InParanoidP13942.
KOK06236.
OMACAYAGAS.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP13942.
BgeeP13942.
CleanExHS_COL11A2.
GenevestigatorP13942.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view]
PfamPF01410. COLFI. 2 hits.
PF01391. Collagen. 8 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS51461. NC1_FIB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCOL11A2_(gene).
GenomeRNAi1302.
NextBio5291.
PROP13942.
SOURCESearch...

Entry information

Entry nameCOBA2_HUMAN
AccessionPrimary (citable) accession number: P13942
Secondary accession number(s): A6NLX2 expand/collapse secondary AC list , E7ER90, Q07751, Q13271, Q13272, Q13273, Q5JP94, Q5SUI8, Q7Z6C3, Q99866, Q9UIP9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 25, 2012
Last modified: July 9, 2014
This is version 173 of the entry and version 5 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

SIMILARITY comments

Index of protein domains and families

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 6

Human chromosome 6: entries, gene names and cross-references to MIM