Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P12107 (COBA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 166. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(XI) chain
Gene names
Name:COL11A1
Synonyms:COLL6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1806 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.

Tissue specificity

Cartilage, placenta and some tumor or virally transformed cell lines. Isoforms using exon IIA or IIB are found in the cartilage while isoforms using only exon IIB are found in the tendon.

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.

N-glycosylated By similarity.

Involvement in disease

Stickler syndrome 2 (STL2) [MIM:604841]: An autosomal dominant form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular disorders may include juvenile cataract, myopia, strabismus, vitreoretinal or chorioretinal degeneration, retinal detachment, and chronic uveitis. 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.2 Ref.8 Ref.11

Marshall syndrome (MRSHS) [MIM:154780]: An autosomal dominant disorder characterized by ocular abnormalities, deafness, craniofacial anomalies, and anhidrotic ectodermal dysplasia. Clinical features include short stature; flat or retruded midface with short, depressed nose, flat nasal bridge and anteverted nares; cleft palate with or without the Pierre Robin sequence; appearance of large eyes with ocular hypertelorism; cataracts, either congenital or juvenile; esotropia; high myopia; sensorineural hearing loss; spondyloepiphyseal abnormalities; calcification of the falx cerebri; ectodermal abnormalities, including defects in sweating and dental structures.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Fibrochondrogenesis 1 (FBCG1) [MIM:228520]: A severe short-limbed skeletal dysplasia characterized by broad long-bone metaphyses, pear-shaped vertebral bodies, and characteristic morphology of the growth plate, in which the chondrocytes have a fibroblastic appearance and there are regions of fibrous cartilage extracellular matrix. Clinical features include a flat midface with a small nose and anteverted nares, significant shortening of all limb segments but relatively normal hands and feet, and a small bell-shaped thorax with a protuberant abdomen.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

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
   DiseaseCataract
Deafness
Disease mutation
Dwarfism
Ectodermal dysplasia
Stickler syndrome
   DomainCollagen
Repeat
Signal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcartilage condensation

Inferred from electronic annotation. Source: Ensembl

chondrocyte development

Inferred from electronic annotation. Source: Ensembl

collagen catabolic process

Traceable author statement. Source: Reactome

collagen fibril organization

Non-traceable author statement Ref.6. Source: UniProtKB

detection of mechanical stimulus involved in sensory perception of sound

Inferred from mutant phenotype PubMed 10889003. Source: UniProtKB

embryonic skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Non-traceable author statement Ref.2. Source: UniProtKB

inner ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

proteoglycan metabolic process

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from mutant phenotype PubMed 10573014. Source: UniProtKB

tendon development

Inferred from electronic annotation. Source: Ensembl

ventricular cardiac muscle tissue morphogenesis

Inferred from electronic annotation. Source: Ensembl

visual perception

Inferred from mutant phenotype PubMed 10573014Ref.8. Source: UniProtKB

   Cellular_componentcollagen type XI trimer

Inferred from direct assay Ref.6. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

   Molecular_functionextracellular matrix binding

Non-traceable author statement Ref.6. Source: UniProtKB

extracellular matrix structural constituent

Non-traceable author statement Ref.2. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding, bridging

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. There is alternative usage of exon IIA or exon IIB. Transcripts containing exon IIA or IIB are present in cartilage, but exon IIB is preferentially utilized in transcripts from tendon.
Isoform A (identifier: P12107-1)

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 B (identifier: P12107-2)

The sequence of this isoform differs from the canonical sequence as follows:
     261-299: YAPEDIIEYD...VTEETIAQTE → KKKSNFKKKM...ASAKAKLGVK
Isoform C (identifier: P12107-3)

The sequence of this isoform differs from the canonical sequence as follows:
     261-299: Missing.
Isoform 4 (identifier: P12107-4)

The sequence of this isoform differs from the canonical sequence as follows:
     300-415: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Propeptide36 – 511476N-terminal propeptide Potential
PRO_0000005774
Chain512 – 15631052Collagen alpha-1(XI) chain
PRO_0000005775
Propeptide1564 – 1806243C-terminal propeptide
PRO_0000005776

Regions

Domain71 – 243173Laminin G-like
Domain442 – 49049Collagen-like 1
Domain532 – 58655Collagen-like 2
Domain583 – 64159Collagen-like 3
Domain616 – 67459Collagen-like 4
Domain643 – 69957Collagen-like 5
Domain1393 – 145058Collagen-like 6
Domain1429 – 148759Collagen-like 7
Domain1483 – 154159Collagen-like 8
Domain1577 – 1805229Fibrillar collagen NC1
Region230 – 419190Nonhelical region
Region420 – 50889Triple-helical region (interrupted)
Region509 – 5113Short nonhelical segment
Region512 – 52817Telopeptide
Region529 – 15421014Triple-helical region
Region1543 – 156321Nonhelical region (C-terminal)

Sites

Metal binding16251Calcium By similarity
Metal binding16271Calcium By similarity
Metal binding16281Calcium; via carbonyl oxygen By similarity
Metal binding16301Calcium; via carbonyl oxygen By similarity
Metal binding16331Calcium By similarity

Amino acid modifications

Modified residue6121Allysine
Modified residue14521Allysine
Glycosylation16401N-linked (GlcNAc...) Potential
Disulfide bond61 ↔ 243 By similarity
Disulfide bond182 ↔ 236 By similarity
Disulfide bond1607 ↔ 1639 By similarity
Disulfide bond1630Interchain By similarity
Disulfide bond1648 ↔ 1803 By similarity
Disulfide bond1714 ↔ 1757 By similarity

Natural variations

Alternative sequence261 – 29939YAPED…IAQTE → KKKSNFKKKMRTVATKSKEK SKKFTPPKSEKFSSKKKKSY QASAKAKLGVK in isoform B.
VSP_001145
Alternative sequence261 – 29939Missing in isoform C.
VSP_001146
Alternative sequence300 – 415116Missing in isoform 4.
VSP_046318
Natural variant81W → G.
Corresponds to variant rs12025888 [ dbSNP | Ensembl ].
VAR_047723
Natural variant461D → E.
Corresponds to variant rs11164663 [ dbSNP | Ensembl ].
VAR_047724
Natural variant5591G → S.
Corresponds to variant rs12143815 [ dbSNP | Ensembl ].
VAR_047725
Natural variant5651G → V in STL2. Ref.11
VAR_063675
Natural variant6251G → V in STL2. Ref.8
VAR_013583
Natural variant6761G → R in STL2; overlapping phenotype with Marshall syndrome. Ref.2
VAR_013584
Natural variant7961G → R in FBCG1. Ref.10
VAR_065904
Natural variant921 – 9266Missing in STL2; overlapping phenotype with Marshall syndrome.
VAR_013585
Natural variant10271G → R in STL2. Ref.11
VAR_063676
Natural variant10421G → R in FBCG1. Ref.10
VAR_065905
Natural variant1110 – 11189Missing in STL2.
VAR_063677
Natural variant1313 – 13153Missing in STL2; overlapping phenotype with Marshall syndrome.
VAR_013586
Natural variant13231P → L. Ref.1 Ref.2 Ref.5
Corresponds to variant rs3753841 [ dbSNP | Ensembl ].
VAR_047726
Natural variant13261A → V in a breast cancer sample; somatic mutation. Ref.9
VAR_035743
Natural variant13281Q → K in a breast cancer sample; somatic mutation. Ref.9
VAR_035744
Natural variant13281Q → L in a breast cancer sample; somatic mutation. Ref.9
VAR_035745
Natural variant15131G → D in STL2. Ref.11
VAR_063678
Natural variant15161G → V in STL2; overlapping phenotype with Marshall syndrome. Ref.2 Ref.11
VAR_013587
Natural variant15351S → P. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs1676486 [ dbSNP | Ensembl ].
VAR_047727
Natural variant18051L → F.
Corresponds to variant rs1975916 [ dbSNP | Ensembl ].
VAR_047728

Experimental info

Sequence conflict941 – 9444KDGL → RMGC in AAA51891. Ref.1
Sequence conflict9861H → Y in AAA51891. Ref.1
Sequence conflict10741P → R in AAA51891. Ref.1
Sequence conflict11421D → G in AAA51891. Ref.1
Sequence conflict12181M → W in AAA51891. Ref.1
Sequence conflict17581A → T in AAA51891. Ref.1
Sequence conflict17861N → S in AAA51891. Ref.1

Sequences

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

Last modified November 25, 2008. Version 4.
Checksum: 7CBF744263321B43

FASTA1,806181,065
        10         20         30         40         50         60 
MEPWSSRWKT KRWLWDFTVT TLALTFLFQA REVRGAAPVD VLKALDFHNS PEGISKTTGF 

        70         80         90        100        110        120 
CTNRKNSKGS DTAYRVSKQA QLSAPTKQLF PGGTFPEDFS ILFTVKPKKG IQSFLLSIYN 

       130        140        150        160        170        180 
EHGIQQIGVE VGRSPVFLFE DHTGKPAPED YPLFRTVNIA DGKWHRVAIS VEKKTVTMIV 

       190        200        210        220        230        240 
DCKKKTTKPL DRSERAIVDT NGITVFGTRI LDEEVFEGDI QQFLITGDPK AAYDYCEHYS 

       250        260        270        280        290        300 
PDCDSSAPKA AQAQEPQIDE YAPEDIIEYD YEYGEAEYKE AESVTEGPTV TEETIAQTEA 

       310        320        330        340        350        360 
NIVDDFQEYN YGTMESYQTE APRHVSGTNE PNPVEEIFTE EYLTGEDYDS QRKNSEDTLY 

       370        380        390        400        410        420 
ENKEIDGRDS DLLVDGDLGE YDFYEYKEYE DKPTSPPNEE FGPGVPAETD ITETSINGHG 

       430        440        450        460        470        480 
AYGEKGQKGE PAVVEPGMLV EGPPGPAGPA GIMGPPGLQG PTGPPGDPGD RGPPGRPGLP 

       490        500        510        520        530        540 
GADGLPGPPG TMLMLPFRYG GDGSKGPTIS AQEAQAQAIL QQARIALRGP PGPMGLTGRP 

       550        560        570        580        590        600 
GPVGGPGSSG AKGESGDPGP QGPRGVQGPP GPTGKPGKRG RPGADGGRGM PGEPGAKGDR 

       610        620        630        640        650        660 
GFDGLPGLPG DKGHRGERGP QGPPGPPGDD GMRGEDGEIG PRGLPGEAGP RGLLGPRGTP 

       670        680        690        700        710        720 
GAPGQPGMAG VDGPPGPKGN MGPQGEPGPP GQQGNPGPQG LPGPQGPIGP PGEKGPQGKP 

       730        740        750        760        770        780 
GLAGLPGADG PPGHPGKEGQ SGEKGALGPP GPQGPIGYPG PRGVKGADGV RGLKGSKGEK 

       790        800        810        820        830        840 
GEDGFPGFKG DMGLKGDRGE VGQIGPRGED GPEGPKGRAG PTGDPGPSGQ AGEKGKLGVP 

       850        860        870        880        890        900 
GLPGYPGRQG PKGSTGFPGF PGANGEKGAR GVAGKPGPRG QRGPTGPRGS RGARGPTGKP 

       910        920        930        940        950        960 
GPKGTSGGDG PPGPPGERGP QGPQGPVGFP GPKGPPGPPG KDGLPGHPGQ RGETGFQGKT 

       970        980        990       1000       1010       1020 
GPPGPGGVVG PQGPTGETGP IGERGHPGPP GPPGEQGLPG AAGKEGAKGD PGPQGISGKD 

      1030       1040       1050       1060       1070       1080 
GPAGLRGFPG ERGLPGAQGA PGLKGGEGPQ GPPGPVGSPG ERGSAGTAGP IGLPGRPGPQ 

      1090       1100       1110       1120       1130       1140 
GPPGPAGEKG APGEKGPQGP AGRDGVQGPV GLPGPAGPAG SPGEDGDKGE IGEPGQKGSK 

      1150       1160       1170       1180       1190       1200 
GDKGENGPPG PPGLQGPVGA PGIAGGDGEP GPRGQQGMFG QKGDEGARGF PGPPGPIGLQ 

      1210       1220       1230       1240       1250       1260 
GLPGPPGEKG ENGDVGPMGP PGPPGPRGPQ GPNGADGPQG PPGSVGSVGG VGEKGEPGEA 

      1270       1280       1290       1300       1310       1320 
GNPGPPGEAG VGGPKGERGE KGEAGPPGAA GPPGAKGPPG DDGPKGNPGP VGFPGDPGPP 

      1330       1340       1350       1360       1370       1380 
GEPGPAGQDG VGGDKGEDGD PGQPGPPGPS GEAGPPGPPG KRGPPGAAGA EGRQGEKGAK 

      1390       1400       1410       1420       1430       1440 
GEAGAEGPPG KTGPVGPQGP AGKPGPEGLR GIPGPVGEQG LPGAAGQDGP PGPMGPPGLP 

      1450       1460       1470       1480       1490       1500 
GLKGDPGSKG EKGHPGLIGL IGPPGEQGEK GDRGLPGTQG SPGAKGDGGI PGPAGPLGPP 

      1510       1520       1530       1540       1550       1560 
GPPGLPGPQG PKGNKGSTGP AGQKGDSGLP GPPGSPGPPG EVIQPLPILS SKKTRRHTEG 

      1570       1580       1590       1600       1610       1620 
MQADADDNIL DYSDGMEEIF GSLNSLKQDI EHMKFPMGTQ TNPARTCKDL QLSHPDFPDG 

      1630       1640       1650       1660       1670       1680 
EYWIDPNQGC SGDSFKVYCN FTSGGETCIY PDKKSEGVRI SSWPKEKPGS WFSEFKRGKL 

      1690       1700       1710       1720       1730       1740 
LSYLDVEGNS INMVQMTFLK LLTASARQNF TYHCHQSAAW YDVSSGSYDK ALRFLGSNDE 

      1750       1760       1770       1780       1790       1800 
EMSYDNNPFI KTLYDGCASR KGYEKTVIEI NTPKIDQVPI VDVMINDFGD QNQKFGFEVG 


PVCFLG 

« Hide

Isoform B [UniParc].

Checksum: D86BD1303BA45C99
Show »

FASTA1,818182,422
Isoform C [UniParc].

Checksum: DE451EE638FDBCA9
Show »

FASTA1,767176,619
Isoform 4 [UniParc].

Checksum: A612FE4054F2F34E
Show »

FASTA1,690167,752

References

« Hide 'large scale' references
[1]"Pro-alpha 1(XI) collagen. Structure of the amino-terminal propeptide and expression of the gene in tumor cell lines."
Yoshioka H., Ramirez F.
J. Biol. Chem. 265:6423-6426(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANTS LEU-1323 AND PRO-1535.
[2]"Splicing mutations of 54-bp exons in the COL11A1 gene cause Marshall syndrome, but other mutations cause overlapping Marshall/Stickler phenotypes."
Annunen S., Koerkkoe J., Czarny M., Warman M.L., Brunner H.G., Kaeaeriaeinen H., Mulliken J.B., Tranebjaerg L., Brooks D.G., Cox G.F., Cruysberg J.R., Curtis M.A., Davenport S.L.H., Friedrich C.A., Kaitila I., Krawczynski M.R., Latos-Bielenska A., Mukai S. expand/collapse author list , Olsen B.R., Shinno N., Somer M., Vikkula M., Zlotogora J., Prockop D.J., Ala-Kokko L.
Am. J. Hum. Genet. 65:974-983(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS A; B AND C), VARIANTS STL2/MARSHALL SYNDROME ARG-676; 921-GLN--PRO-926 DEL; 1313-PHE--GLY-1315 DEL; LEU-1323; VAL-1516 AND PRO-1535.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-1535.
[5]"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 4), VARIANTS LEU-1323 AND PRO-1535.
[6]"Cloning and sequencing of pro-alpha 1 (XI) collagen cDNA demonstrates that type XI belongs to the fibrillar class of collagens and reveals that the expression of the gene is not restricted to cartilagenous tissue."
Bernard M., Yoshioka H., Rodriguez E., van der Rest M., Kimura T., Ninomiya Y., Olsen B.R., Ramirez F.
J. Biol. Chem. 263:17159-17166(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 538-1806, PARTIAL PROTEIN SEQUENCE.
[7]"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.
Tissue: Blood.
[8]"A family with Stickler syndrome type 2 has a mutation in the COL11A1 gene resulting in the substitution of glycine 97 by valine in alpha-1(XI) collagen."
Richards A.J., Yates J.R.W., Williams R., Payne S.J., Pope F.M., Scott J.D., Snead M.P.
Hum. Mol. Genet. 5:1339-1343(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT STL2 VAL-625.
[9]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-1326; LYS-1328 AND LEU-1328.
[10]"Fibrochondrogenesis results from mutations in the COL11A1 type XI collagen gene."
Tompson S.W., Bacino C.A., Safina N.P., Bober M.B., Proud V.K., Funari T., Wangler M.F., Nevarez L., Ala-Kokko L., Wilcox W.R., Eyre D.R., Krakow D., Cohn D.H.
Am. J. Hum. Genet. 87:708-712(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FBCG1 ARG-796 AND ARG-1042.
[11]"Stickler syndrome and the vitreous phenotype: mutations in COL2A1 and COL11A1."
Richards A.J., McNinch A., Martin H., Oakhill K., Rai H., Waller S., Treacy B., Whittaker J., Meredith S., Poulson A., Snead M.P.
Hum. Mutat. 31:E1461-E1471(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS STL2 VAL-565; ARG-1027; 1110-VAL--PRO-1118 DEL; ASP-1513 AND VAL-1516.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04177 mRNA. Translation: AAA51891.1.
AF101112 expand/collapse EMBL AC list , AF101079, AF101080, AF101081, AF101082, AF101083, AF101084, AF101085, AF101086, AF101087, AF101088, AF101089, AF101090, AF101091, AF101092, AF101093, AF101094, AF101095, AF101096, AF101097, AF101098, AF101099, AF101100, AF101101, AF101102, AF101103, AF101104, AF101105, AF101106, AF101107, AF101108, AF101109, AF101110, AF101111 Genomic DNA. Translation: AAF04724.1.
AF101112 expand/collapse EMBL AC list , AF101079, AF101080, AF101081, AF101082, AF101083, AF101084, AF101085, AF101086, AF101087, AF101088, AF101089, AF101090, AF101091, AF101092, AF101093, AF101094, AF101095, AF101096, AF101097, AF101098, AF101099, AF101100, AF101101, AF101102, AF101103, AF101104, AF101105, AF101106, AF101107, AF101108, AF101109, AF101110, AF101111 Genomic DNA. Translation: AAF04725.1.
AF101112 expand/collapse EMBL AC list , AF101079, AF101080, AF101081, AF101082, AF101083, AF101084, AF101085, AF101086, AF101087, AF101088, AF101089, AF101090, AF101091, AF101092, AF101093, AF101094, AF101095, AF101096, AF101097, AF101098, AF101099, AF101100, AF101101, AF101102, AF101103, AF101104, AF101105, AF101106, AF101107, AF101108, AF101109, AF101110, AF101111 Genomic DNA. Translation: AAF04726.1.
AL627203, AC093150, AC099567 Genomic DNA. Translation: CAH73908.1.
CH471097 Genomic DNA. Translation: EAW72908.1.
CH471097 Genomic DNA. Translation: EAW72910.1.
BC117697 mRNA. Translation: AAI17698.1.
L38956 Genomic DNA. Translation: AAA79171.1.
CCDSCCDS53348.1. [P12107-3]
CCDS778.1. [P12107-1]
CCDS780.2. [P12107-4]
PIRCGHU1E. A35239.
RefSeqNP_001177638.1. NM_001190709.1. [P12107-3]
NP_001845.3. NM_001854.3. [P12107-1]
NP_542196.2. NM_080629.2. [P12107-2]
NP_542197.3. NM_080630.3. [P12107-4]
UniGeneHs.523446.

3D structure databases

ProteinModelPortalP12107.
SMRP12107. Positions 73-229, 1596-1805.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107698. 2 interactions.
STRING9606.ENSP00000351163.

Chemistry

ChEMBLCHEMBL2364188.

PTM databases

PhosphoSiteP12107.

Polymorphism databases

DMDM215274245.

Proteomic databases

MaxQBP12107.
PaxDbP12107.
PRIDEP12107.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000353414; ENSP00000302551; ENSG00000060718. [P12107-3]
ENST00000358392; ENSP00000351163; ENSG00000060718. [P12107-2]
ENST00000370096; ENSP00000359114; ENSG00000060718. [P12107-1]
ENST00000512756; ENSP00000426533; ENSG00000060718. [P12107-4]
GeneID1301.
KEGGhsa:1301.
UCSCuc001dul.3. human. [P12107-1]
uc001dum.3. human. [P12107-2]
uc001dun.3. human. [P12107-3]

Organism-specific databases

CTD1301.
GeneCardsGC01M103342.
GeneReviewsCOL11A1.
H-InvDBHIX0028847.
HGNCHGNC:2186. COL11A1.
HPAHPA052246.
MIM120280. gene.
154780. phenotype.
228520. phenotype.
604841. phenotype.
neXtProtNX_P12107.
Orphanet250984. Autosomal recessive Stickler syndrome.
2021. Fibrochondrogenesis.
560. Marshall syndrome.
90654. Stickler syndrome type 2.
PharmGKBPA26702.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG004933.
KOK06236.
OMAHPGKEGQ.
OrthoDBEOG7XPZ4W.
PhylomeDBP12107.
TreeFamTF323987.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP12107.
BgeeP12107.
CleanExHS_COL11A1.
GenevestigatorP12107.

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. 1 hit.
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

GeneWikiCollagen,_type_XI,_alpha_1.
GenomeRNAi1301.
NextBio5283.
PMAP-CutDBB1ASK7.
PROP12107.
SOURCESearch...

Entry information

Entry nameCOBA1_HUMAN
AccessionPrimary (citable) accession number: P12107
Secondary accession number(s): B1ASK7 expand/collapse secondary AC list , D3DT73, E9PCU0, Q14034, Q149N0, Q9UIT4, Q9UIT5, Q9UIT6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 166 of the entry and version 4 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 1

Human chromosome 1: entries, gene names and cross-references to MIM