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P20849

- CO9A1_HUMAN

UniProt

P20849 - CO9A1_HUMAN

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Protein
Collagen alpha-1(IX) chain
Gene
COL9A1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Structural component of hyaline cartilage and vitreous of the eye.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi213 – 2131Zinc
Metal bindingi215 – 2151Zinc
Metal bindingi253 – 2531Zinc

GO - Molecular functioni

  1. extracellular matrix structural constituent conferring tensile strength Source: BHF-UCL
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. axon guidance Source: Reactome
  2. collagen catabolic process Source: Reactome
  3. extracellular matrix disassembly Source: Reactome
  4. extracellular matrix organization Source: Reactome
  5. growth plate cartilage development Source: Ensembl
  6. organ morphogenesis Source: ProtInc
  7. tissue homeostasis Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150401. Collagen degradation.
REACT_163906. ECM proteoglycans.
REACT_16888. Signaling by PDGF.
REACT_18312. NCAM1 interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(IX) chain
Gene namesi
Name:COL9A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:2217. COL9A1.

Subcellular locationi

GO - Cellular componenti

  1. collagen type IX trimer Source: UniProtKB
  2. endoplasmic reticulum lumen Source: Reactome
  3. extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Multiple epiphyseal dysplasia 6 (EDM6) [MIM:614135]: 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.1 Publication
Stickler syndrome 4 (STL4) [MIM:614134]: 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. 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.1 Publication

Keywords - Diseasei

Deafness, Stickler syndrome

Organism-specific databases

MIMi614134. phenotype.
614135. phenotype.
Orphaneti250984. Autosomal recessive Stickler syndrome.
166002. Multiple epiphyseal dysplasia due to collagen 9 anomaly.
PharmGKBiPA26733.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323
Add
BLAST
Chaini24 – 921898Collagen alpha-1(IX) chain
PRO_0000005765Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 2421 Publication
Glycosylationi171 – 1711N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi198 ↔ 2521 Publication
Disulfide bondi411 – 411Interchain1 Publication
Disulfide bondi415 – 415Interchain1 Publication

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP20849.
PRIDEiP20849.

PTM databases

PhosphoSiteiP20849.

Expressioni

Gene expression databases

ArrayExpressiP20849.
BgeeiP20849.
GenevestigatoriP20849.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi107694. 2 interactions.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi56 – 583
Helixi59 – 624
Helixi65 – 695
Turni70 – 723
Beta strandi76 – 783
Beta strandi85 – 895
Beta strandi96 – 983
Helixi99 – 1024
Beta strandi109 – 11810
Helixi121 – 1255
Beta strandi127 – 1348
Beta strandi140 – 1478
Helixi148 – 1503
Beta strandi152 – 1598
Beta strandi164 – 1696
Helixi173 – 1753
Beta strandi177 – 1793
Beta strandi181 – 1888
Beta strandi191 – 1966
Beta strandi199 – 2057
Beta strandi215 – 22511
Beta strandi233 – 24210
Helixi246 – 2494

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2UURX-ray1.80A24-268[»]
ProteinModelPortaliP20849.
SMRiP20849. Positions 42-256.

Miscellaneous databases

EvolutionaryTraceiP20849.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 244195Laminin G-like
Add
BLAST
Domaini269 – 32456Collagen-like 1
Add
BLAST
Domaini325 – 35632Collagen-like 2
Add
BLAST
Domaini358 – 40346Collagen-like 3
Add
BLAST
Domaini416 – 47257Collagen-like 4
Add
BLAST
Domaini473 – 51644Collagen-like 5
Add
BLAST
Domaini587 – 64357Collagen-like 6
Add
BLAST
Domaini655 – 71258Collagen-like 7
Add
BLAST
Domaini713 – 75543Collagen-like 8
Add
BLAST
Domaini790 – 84758Collagen-like 9
Add
BLAST
Domaini848 – 89952Collagen-like 10
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 268245Nonhelical region (NC4)
Add
BLAST
Regioni269 – 405137Triple-helical region (COL3)
Add
BLAST
Regioni406 – 41712Nonhelical region (NC3)
Add
BLAST
Regioni418 – 756339Triple-helical region (COL2)
Add
BLAST
Regioni757 – 78630Nonhelical region (NC2)
Add
BLAST
Regioni787 – 901115Triple-helical region (COL1)
Add
BLAST
Regioni902 – 92120Nonhelical region (NC1)
Add
BLAST

Domaini

Each subunit is composed of three triple-helical domains interspersed with non-collagenous domains. The globular domain at the N-terminus of type IX collagen molecules represents the NC4 domain which may participate in electrostatic interactions with polyanionic glycosaminoglycans in cartilage.

Sequence similaritiesi

Contains 10 collagen-like domains.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOVERGENiHBG004933.
InParanoidiP20849.
KOiK08131.
OMAiGFCEPAS.
OrthoDBiEOG7VHSXW.
PhylomeDBiP20849.
TreeFamiTF332900.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01391. Collagen. 10 hits.
[Graphical view]
SMARTiSM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P20849-1) [UniParc]FASTAAdd to Basket

Also known as: Long

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.

« Hide

MKTCWKIPVF FFVCSFLEPW ASAAVKRRPR FPVNSNSNGG NELCPKIRIG    50
QDDLPGFDLI SQFQVDKAAS RRAIQRVVGS ATLQVAYKLG NNVDFRIPTR 100
NLYPSGLPEE YSFLTTFRMT GSTLKKNWNI WQIQDSSGKE QVGIKINGQT 150
QSVVFSYKGL DGSLQTAAFS NLSSLFDSQW HKIMIGVERS SATLFVDCNR 200
IESLPIKPRG PIDIDGFAVL GKLADNPQVS VPFELQWMLI HCDPLRPRRE 250
TCHELPARIT PSQTTDERGP PGEQGPPGPP GPPGVPGIDG IDGDRGPKGP 300
PGPPGPAGEP GKPGAPGKPG TPGADGLTGP DGSPGSIGSK GQKGEPGVPG 350
SRGFPGRGIP GPPGPPGTAG LPGELGRVGP VGDPGRRGPP GPPGPPGPRG 400
TIGFHDGDPL CPNACPPGRS GYPGLPGMRG HKGAKGEIGE PGRQGHKGEE 450
GDQGELGEVG AQGPPGAQGL RGITGIVGDK GEKGARGLDG EPGPQGLPGA 500
PGDQGQRGPP GEAGPKGDRG AEGARGIPGL PGPKGDTGLP GVDGRDGIPG 550
MPGTKGEPGK PGPPGDAGLQ GLPGVPGIPG AKGVAGEKGS TGAPGKPGQM 600
GNSGKPGQQG PPGEVGPRGP QGLPGSRGEL GPVGSPGLPG KLGSLGSPGL 650
PGLPGPPGLP GMKGDRGVVG EPGPKGEQGA SGEEGEAGER GELGDIGLPG 700
PKGSAGNPGE PGLRGPEGSR GLPGVEGPRG PPGPRGVQGE QGATGLPGVQ 750
GPPGRAPTDQ HIKQVCMRVI QEHFAEMAAS LKRPDSGATG LPGRPGPPGP 800
PGPPGENGFP GQMGIRGLPG IKGPPGALGL RGPKGDLGEK GERGPPGRGP 850
NGLPGAIGLP GDPGPASYGR NGRDGERGPP GVAGIPGVPG PPGPPGLPGF 900
CEPASCTMQA GQRAFNKGPD P 921
Length:921
Mass (Da):91,869
Last modified:May 18, 2010 - v3
Checksum:iA69BF076127283D0
GO
Isoform 2 (identifier: P20849-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1-243: Missing.
     244-267: PLRPRRETCHELPARITPSQTTDE → MAWTARDRGALGLLLLGLCLCAAQ

Show »
Length:678
Mass (Da):64,372
Checksum:iAD0E99997DF2896E
GO
Isoform 3 (identifier: P20849-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     326-328: GLT → TSP
     329-921: Missing.

Note: No experimental confirmation available.

Show »
Length:328
Mass (Da):35,509
Checksum:iBDD662939FECAD21
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti339 – 3391S → P.1 Publication
Corresponds to variant rs592121 [ dbSNP | Ensembl ].
VAR_026463
Natural varianti621 – 6211Q → R.2 Publications
Corresponds to variant rs1135056 [ dbSNP | Ensembl ].
VAR_026464
Natural varianti684 – 6841E → K.
Corresponds to variant rs35470562 [ dbSNP | Ensembl ].
VAR_055668
Natural varianti767 – 7671M → V.
Corresponds to variant rs6910140 [ dbSNP | Ensembl ].
VAR_055669
Natural varianti870 – 8701R → K.3 Publications
Corresponds to variant rs1056921 [ dbSNP | Ensembl ].
VAR_023326
Natural varianti882 – 8821V → L.3 Publications
Corresponds to variant rs1056923 [ dbSNP | Ensembl ].
VAR_023327

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 243243Missing in isoform 2.
VSP_001141Add
BLAST
Alternative sequencei244 – 26724PLRPR…QTTDE → MAWTARDRGALGLLLLGLCL CAAQ in isoform 2.
VSP_001142Add
BLAST
Alternative sequencei326 – 3283GLT → TSP in isoform 3.
VSP_015250
Alternative sequencei329 – 921593Missing in isoform 3.
VSP_015251Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti279 – 2802PP → AS in CAA38276. 1 Publication
Sequence conflicti279 – 2802PP → AS in CAA38277. 1 Publication
Sequence conflicti476 – 4761I → L in CAA38276. 1 Publication
Sequence conflicti570 – 5701Q → H in AAC33527. 1 Publication
Sequence conflicti570 – 5701Q → H in AAC33528. 1 Publication
Sequence conflicti910 – 92112AGQRA…KGPDP → LVSEHLTKGLTLERLTAAWL SA in AAA53475. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X54412 mRNA. Translation: CAA38276.1.
X54413 mRNA. Translation: CAA38277.1.
AF036130
, AF036110, AF036111, AF036112, AF036113, AF036114, AF036115, AF036116, AF036117, AF036118, AF036119, AF036120, AF036121, AF036122, AF036123, AF036124, AF036125, AF036126, AF036127, AF036128, AF036129 Genomic DNA. Translation: AAC33527.1.
AF036130
, AF036112, AF036113, AF036114, AF036115, AF036116, AF036117, AF036118, AF036119, AF036120, AF036121, AF036122, AF036123, AF036124, AF036125, AF036126, AF036127, AF036128, AF036129 Genomic DNA. Translation: AAC33528.1.
AL080275, AL160262 Genomic DNA. Translation: CAI19590.1.
AL080275 Genomic DNA. Translation: CAI19591.1.
AL160262, AL080275 Genomic DNA. Translation: CAI42321.1.
BC015409 mRNA. Translation: AAH15409.1.
BC063646 mRNA. Translation: AAH63646.1.
M32137, M32133 Genomic DNA. Translation: AAA53474.1.
M32137, M32135 Genomic DNA. Translation: AAA53475.1.
CCDSiCCDS47447.1. [P20849-2]
CCDS4971.1. [P20849-1]
PIRiS13580.
S13581.
RefSeqiNP_001842.3. NM_001851.4. [P20849-1]
NP_511040.2. NM_078485.3. [P20849-2]
UniGeneiHs.590892.

Genome annotation databases

EnsembliENST00000320755; ENSP00000315252; ENSG00000112280. [P20849-2]
ENST00000357250; ENSP00000349790; ENSG00000112280. [P20849-1]
ENST00000370496; ENSP00000359527; ENSG00000112280. [P20849-3]
GeneIDi1297.
KEGGihsa:1297.
UCSCiuc003pff.4. human. [P20849-2]
uc003pfg.4. human. [P20849-1]

Polymorphism databases

DMDMi296439373.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X54412 mRNA. Translation: CAA38276.1 .
X54413 mRNA. Translation: CAA38277.1 .
AF036130
, AF036110 , AF036111 , AF036112 , AF036113 , AF036114 , AF036115 , AF036116 , AF036117 , AF036118 , AF036119 , AF036120 , AF036121 , AF036122 , AF036123 , AF036124 , AF036125 , AF036126 , AF036127 , AF036128 , AF036129 Genomic DNA. Translation: AAC33527.1 .
AF036130
, AF036112 , AF036113 , AF036114 , AF036115 , AF036116 , AF036117 , AF036118 , AF036119 , AF036120 , AF036121 , AF036122 , AF036123 , AF036124 , AF036125 , AF036126 , AF036127 , AF036128 , AF036129 Genomic DNA. Translation: AAC33528.1 .
AL080275 , AL160262 Genomic DNA. Translation: CAI19590.1 .
AL080275 Genomic DNA. Translation: CAI19591.1 .
AL160262 , AL080275 Genomic DNA. Translation: CAI42321.1 .
BC015409 mRNA. Translation: AAH15409.1 .
BC063646 mRNA. Translation: AAH63646.1 .
M32137 , M32133 Genomic DNA. Translation: AAA53474.1 .
M32137 , M32135 Genomic DNA. Translation: AAA53475.1 .
CCDSi CCDS47447.1. [P20849-2 ]
CCDS4971.1. [P20849-1 ]
PIRi S13580.
S13581.
RefSeqi NP_001842.3. NM_001851.4. [P20849-1 ]
NP_511040.2. NM_078485.3. [P20849-2 ]
UniGenei Hs.590892.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2UUR X-ray 1.80 A 24-268 [» ]
ProteinModelPortali P20849.
SMRi P20849. Positions 42-256.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107694. 2 interactions.

PTM databases

PhosphoSitei P20849.

Polymorphism databases

DMDMi 296439373.

Proteomic databases

PaxDbi P20849.
PRIDEi P20849.

Protocols and materials databases

DNASUi 1297.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000320755 ; ENSP00000315252 ; ENSG00000112280 . [P20849-2 ]
ENST00000357250 ; ENSP00000349790 ; ENSG00000112280 . [P20849-1 ]
ENST00000370496 ; ENSP00000359527 ; ENSG00000112280 . [P20849-3 ]
GeneIDi 1297.
KEGGi hsa:1297.
UCSCi uc003pff.4. human. [P20849-2 ]
uc003pfg.4. human. [P20849-1 ]

Organism-specific databases

CTDi 1297.
GeneCardsi GC06M070924.
GeneReviewsi COL9A1.
HGNCi HGNC:2217. COL9A1.
MIMi 120210. gene.
614134. phenotype.
614135. phenotype.
neXtProti NX_P20849.
Orphaneti 250984. Autosomal recessive Stickler syndrome.
166002. Multiple epiphyseal dysplasia due to collagen 9 anomaly.
PharmGKBi PA26733.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOVERGENi HBG004933.
InParanoidi P20849.
KOi K08131.
OMAi GFCEPAS.
OrthoDBi EOG7VHSXW.
PhylomeDBi P20849.
TreeFami TF332900.

Enzyme and pathway databases

Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150401. Collagen degradation.
REACT_163906. ECM proteoglycans.
REACT_16888. Signaling by PDGF.
REACT_18312. NCAM1 interactions.

Miscellaneous databases

ChiTaRSi COL9A1. human.
EvolutionaryTracei P20849.
GeneWikii Collagen,_type_IX,_alpha_1.
GenomeRNAii 1297.
NextBioi 5265.
PROi P20849.
SOURCEi Search...

Gene expression databases

ArrayExpressi P20849.
Bgeei P20849.
Genevestigatori P20849.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR001791. Laminin_G.
[Graphical view ]
Pfami PF01391. Collagen. 10 hits.
[Graphical view ]
SMARTi SM00210. TSPN. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete primary structure of two distinct forms of human alpha 1 (IX) collagen chains."
    Muragaki Y., Kimura T., Ninomiya Y., Olsen B.R.
    Eur. J. Biochem. 192:703-708(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, VARIANTS LYS-870 AND LEU-882.
  2. "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 [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, VARIANTS ARG-621; LYS-870 AND LEU-882.
  3. "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.
    , 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].
  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] (ISOFORMS 2 AND 3).
    Tissue: Brain and Mammary gland.
  5. "Collagen type IX from human cartilage: a structural profile of intermolecular cross-linking sites."
    Diab M., Wu J.J., Eyre D.R.
    Biochem. J. 314:327-332(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 405-417 (ISOFORMS 1/2).
  6. "Molecular cloning of rat and human type IX collagen cDNA and localization of the alpha 1(IX) gene on the human chromosome 6."
    Kimura T., Mattei M.-G., Stevens J.W., Goldring M.B., Ninomiya Y., Olsen B.R.
    Eur. J. Biochem. 179:71-78(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 580-820 AND 835-884, VARIANTS LYS-870 AND LEU-882.
  7. "The alpha 1 (IX) collagen gene gives rise to two different transcripts in both mouse embryonic and human fetal RNA."
    Muragaki Y., Nishimura I., Henney A., Ninomiya Y., Olsen B.R.
    Proc. Natl. Acad. Sci. U.S.A. 87:2400-2404(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
  8. "Crystal structure of the N-terminal NC4 domain of collagen IX, a zinc binding member of the laminin-neurexin-sex hormone binding globulin (LNS) domain family."
    Leppanen V.M., Tossavainen H., Permi P., Lehtio L., Ronnholm G., Goldman A., Kilpelainen I., Pihlajamaa T.
    J. Biol. Chem. 282:23219-23230(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 24-268, DISULFIDE BONDS, ZINC-BINDING SITES.
  9. Cited for: VARIANTS PRO-339 AND ARG-621, INVOLVEMENT IN EDM6.
  10. Cited for: INVOLVEMENT IN STL4.

Entry informationi

Entry nameiCO9A1_HUMAN
AccessioniPrimary (citable) accession number: P20849
Secondary accession number(s): Q13699
, Q13700, Q5TF52, Q6P467, Q96BM8, Q99225, Q9H151, Q9H152, Q9Y6P2, Q9Y6P3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 18, 2010
Last modified: September 3, 2014
This is version 168 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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