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Q14055 (CO9A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-2(IX) chain
Gene names
Name:COL9A2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length689 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Structural component of hyaline cartilage and vitreous of the eye.

Subunit structure

Heterotrimer of an alpha 1(IX), an alpha 2(IX) and an alpha 3(IX) chain.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Post-translational modification

Covalently linked to the telopeptides of type II collagen by lysine-derived cross-links.

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Involvement in disease

Multiple epiphyseal dysplasia 2 (EDM2) [MIM:600204]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

Intervertebral disc disease (IDD) [MIM:603932]: A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.8

Stickler syndrome 5 (STL5) [MIM:614284]: An autosomal recessive 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. STL5 is characterized by high myopia, vitreoretinal degeneration, retinal detachment, mild to moderate sensorineural hearing loss, short stature in childhood, and absence of cleft palate and Pierre Robin sequence.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Sequence similarities

Belongs to the fibril-associated collagens with interrupted helices (FACIT) family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 689666Collagen alpha-2(IX) chain
PRO_0000005837

Regions

Region27 – 163137Triple-helical region 4 (COL4)
Region164 – 18017Nonhelical region 4 (NC4)
Region181 – 519339Triple-helical region 3 (COL3)
Region520 – 54930Nonhelical region 3 (NC3)
Region550 – 63283Triple-helical region 2 (COL2)
Region633 – 6342Nonhelical region 2 (NC2)
Region635 – 66430Triple-helical region 1 (COL1)
Region665 – 68925Nonhelical region 1 (NC1)

Amino acid modifications

Glycosylation1691O-linked (Xyl...) (glycosaminoglycan) By similarity
Disulfide bond174Interchain Potential
Disulfide bond178Interchain Potential

Natural variations

Natural variant2461T → M. Ref.9
Corresponds to variant rs2228565 [ dbSNP | Ensembl ].
VAR_026465
Natural variant3261Q → R. Ref.8 Ref.9
Corresponds to variant rs2228564 [ dbSNP | Ensembl ].
VAR_012659
Natural variant3261Q → W in IDD; requires 2 nucleotide substitutions. Ref.8
VAR_012658
Natural variant3351L → V. Ref.9
Corresponds to variant rs2228567 [ dbSNP | Ensembl ].
VAR_026466
Natural variant5811V → I.
Corresponds to variant rs3737821 [ dbSNP | Ensembl ].
VAR_020014

Sequences

Sequence LengthMass (Da)Tools
Q14055 [UniParc].

Last modified May 1, 1999. Version 2.
Checksum: EB6106E02F6FA862

FASTA68965,131
        10         20         30         40         50         60 
MAAATASPRS LLVLLQVVVL ALAQIRGPPG ERGPPGPPGP PGVPGSDGID GDNGPPGKAG 

        70         80         90        100        110        120 
PPGPKGEPGK AGPDGPDGKP GIDGLTGAKG EPGPMGIPGV KGQPGLPGPP GLPGPGFAGP 

       130        140        150        160        170        180 
PGPPGPVGLP GEIGIRGPKG DPGPDGPSGP PGPPGKPGRP GTIQGLEGSA DFLCPTNCPP 

       190        200        210        220        230        240 
GMKGPPGLQG VKGHAGKRGI LGDPGHQGKP GPKGDVGASG EQGIPGPPGP QGIRGYPGMA 

       250        260        270        280        290        300 
GPKGETGPHG YKGMVGAIGA TGPPGEEGPR GPPGRAGEKG DEGSPGIRGP QGITGPKGAT 

       310        320        330        340        350        360 
GPPGINGKDG TPGTPGMKGS AGQAGQPGSP GHQGLAGVPG QPGTKGGPGD QGEPGPQGLP 

       370        380        390        400        410        420 
GFSGPPGKEG EPGPRGEIGP QGIMGQKGDQ GERGPVGQPG PQGRQGPKGE QGPPGIPGPQ 

       430        440        450        460        470        480 
GLPGVKGDKG SPGKTGPRGK VGDPGVAGLP GEKGEKGESG EPGPKGQQGV RGEPGYPGPS 

       490        500        510        520        530        540 
GDAGAPGVQG YPGPPGPRGL AGNRGVPGQP GRQGVEGRDA TDQHIVDVAL KMLQEQLAEV 

       550        560        570        580        590        600 
AVSAKREALG AVGMMGPPGP PGPPGYPGKQ GPHGHPGPRG VPGIVGAVGQ IGNTGPKGKR 

       610        620        630        640        650        660 
GEKGDPGEVG RGHPGMPGPP GIPGLPGRPG QAINGKDGDR GSPGAPGEAG RPGLPGPVGL 

       670        680 
PGFCEPAACL GASAYASARL TEPGSIKGP 

« Hide

References

« Hide 'large scale' references
[1]"Human COL9A1 and COL9A2 genes. Two genes of 90 and 15 kb code for similar polypeptides of the same collagen molecule."
Pihlajamaa T., Vuoristo M.M., Annunen S., Peraelae M., Prockop D.J., Ala-Kokko L.
Matrix Biol. 17:237-241(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Foreskin.
[2]"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].
[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 (SEP-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].
Tissue: Brain.
[5]"Molecular cloning of the human alpha 2(IX) collagen cDNA and assignment of the human COL9A2 gene to chromosome 1."
Peraelae M., Haenninen M., Haestbacka J., Elima K., Vuorio E.
FEBS Lett. 319:177-180(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 50-668.
Tissue: Cartilage.
[6]"Identification of novel pro-alpha2(IX) collagen gene mutations in two families with distinctive oligo-epiphyseal forms of multiple epiphyseal dysplasia."
Holden P., Canty E.G., Mortier G.R., Zabel B., Spranger J., Carr A., Grant M.E., Loughlin J.A., Briggs M.D.
Am. J. Hum. Genet. 65:31-38(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN EDM2.
[7]"A loss of function mutation in the COL9A2 gene causes autosomal recessive Stickler syndrome."
Baker S., Booth C., Fillman C., Shapiro M., Blair M.P., Hyland J.C., Ala-Kokko L.
Am. J. Med. Genet. A 155:1668-1672(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN STL5.
[8]"An allele of COL9A2 associated with intervertebral disc disease."
Annunen S., Paassilta P., Lohiniva J., Peraelae M., Pihlajamaa T., Karppinen J., Tervonen O., Kroeger H., Laehde S., Vanharanta H., Ryhaenen L., Goering H.H.H., Ott J., Prockop D.J., Ala-Kokko L.
Science 285:409-412(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IDD TRP-326, VARIANT ARG-326.
[9]"A mutation in COL9A1 causes multiple epiphyseal dysplasia: further evidence for locus heterogeneity."
Czarny-Ratajczak M., Lohiniva J., Rogala P., Kozlowski K., Peraelae M., Carter L., Spector T.D., Kolodziej L., Seppaenen U., Glazar R., Krolewski J., Latos-Bielenska A., Ala-Kokko L.
Am. J. Hum. Genet. 69:969-980(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MET-246; ARG-326 AND VAL-335.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF019406 Genomic DNA. Translation: AAC33512.1.
AL050341 Genomic DNA. Translation: CAB81611.1.
CH471059 Genomic DNA. Translation: EAX07229.1.
BC136326 mRNA. Translation: AAI36327.1.
BC136327 mRNA. Translation: AAI36328.1.
M95610 mRNA. Translation: AAA80977.1.
CCDSCCDS450.1.
PIRS32436.
RefSeqNP_001843.1. NM_001852.3.
XP_006710428.1. XM_006710365.1.
UniGeneHs.418012.

3D structure databases

ProteinModelPortalQ14055.
SMRQ14055. Positions 22-60.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107695. 4 interactions.
IntActQ14055. 3 interactions.
STRING9606.ENSP00000361834.

PTM databases

PhosphoSiteQ14055.

Polymorphism databases

DMDM20137328.

Proteomic databases

PaxDbQ14055.
PRIDEQ14055.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372748; ENSP00000361834; ENSG00000049089.
GeneID1298.
KEGGhsa:1298.
UCSCuc001cfh.1. human.

Organism-specific databases

CTD1298.
GeneCardsGC01M040766.
GeneReviewsCOL9A2.
H-InvDBHIX0028759.
HGNCHGNC:2218. COL9A2.
HPAHPA056316.
MIM120260. gene.
600204. phenotype.
603932. phenotype.
614284. phenotype.
neXtProtNX_Q14055.
Orphanet250984. Autosomal recessive Stickler syndrome.
166002. Multiple epiphyseal dysplasia due to collagen 9 anomaly.
PharmGKBPA26734.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000085653.
HOVERGENHBG004933.
InParanoidQ14055.
KOK08131.
OMAIKGAPGQ.
OrthoDBEOG7XSTG3.
PhylomeDBQ14055.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ14055.
BgeeQ14055.
CleanExHS_COL9A2.
GenevestigatorQ14055.

Family and domain databases

InterProIPR008160. Collagen.
[Graphical view]
PfamPF01391. Collagen. 10 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCOL9A2.
GenomeRNAi1298.
NextBio5271.
PROQ14055.
SOURCESearch...

Entry information

Entry nameCO9A2_HUMAN
AccessionPrimary (citable) accession number: Q14055
Secondary accession number(s): B2RMP9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 134 of the entry and version 2 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