P20849 (CO9A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-1(IX) chain

Gene names

Name:

COL9A1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	921 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular matrix By similarity.
Domain	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.
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 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. Ref.9 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. Ref.10
Sequence similarities	Belongs to the fibril-associated collagens with interrupted helices (FACIT) family. Contains 10 collagen-like domains. Contains 1 laminin G-like domain.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Deafness Stickler syndrome
Domain	Collagen Repeat Signal
Ligand	Metal-binding Zinc
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome extracellular matrix organization Traceable author statement. Source: Reactome growth plate cartilage development Inferred from electronic annotation. Source: Compara organ morphogenesis Traceable author statement PubMed 3473493. Source: ProtInc tissue homeostasis Inferred from electronic annotation. Source: Compara
Cellular_component	collagen type IX Traceable author statement Ref.2. Source: UniProtKB endoplasmic reticulum lumen Traceable author statement. Source: Reactome
Molecular_function	extracellular matrix structural constituent conferring tensile strength Inferred by curator Ref.5. Source: BHF-UCL metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P20849-1)

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.

Isoform 2 (identifier: P20849-2)

Also known as: Short;

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

Isoform 3 (identifier: P20849-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Chain

24 – 921

898

Collagen alpha-1(IX) chain

PRO_0000005765

Regions

Domain

50 – 244

195

Laminin G-like

Domain

269 – 324

56

Collagen-like 1

Domain

325 – 356

32

Collagen-like 2

Domain

358 – 403

46

Collagen-like 3

Domain

416 – 472

57

Collagen-like 4

Domain

473 – 516

44

Collagen-like 5

Domain

587 – 643

57

Collagen-like 6

Domain

655 – 712

58

Collagen-like 7

Domain

713 – 755

43

Collagen-like 8

Domain

790 – 847

58

Collagen-like 9

Domain

848 – 899

52

Collagen-like 10

Region

24 – 268

245

Nonhelical region (NC4)

Region

269 – 405

137

Triple-helical region (COL3)

Region

406 – 417

12

Nonhelical region (NC3)

Region

418 – 756

339

Triple-helical region (COL2)

Region

757 – 786

30

Nonhelical region (NC2)

Region

787 – 901

115

Triple-helical region (COL1)

Region

902 – 921

20

Nonhelical region (NC1)

Sites

Metal binding

213

1

Zinc

Metal binding

215

1

Zinc

Metal binding

253

1

Zinc

Amino acid modifications

Glycosylation

171

1

N-linked (GlcNAc...) Potential

Disulfide bond

44 ↔ 242

Ref.8

Disulfide bond

198 ↔ 252

Ref.8

Disulfide bond

411

Interchain Ref.8

Disulfide bond

415

Interchain Ref.8

Natural variations

Alternative sequence

1 – 243

243

Missing in isoform 2.

VSP_001141

Alternative sequence

244 – 267

24

PLRPR…QTTDE → MAWTARDRGALGLLLLGLCL CAAQ in isoform 2.

VSP_001142

Alternative sequence

326 – 328

3

GLT → TSP in isoform 3.

VSP_015250

Alternative sequence

329 – 921

593

Missing in isoform 3.

VSP_015251

Natural variant

339

1

S → P. Ref.9
Corresponds to variant rs592121 [ dbSNP | Ensembl ].

VAR_026463

Natural variant

621

1

Q → R. Ref.2 Ref.9
Corresponds to variant rs1135056 [ dbSNP | Ensembl ].

VAR_026464

Natural variant

684

1

E → K.
Corresponds to variant rs35470562 [ dbSNP | Ensembl ].

VAR_055668

Natural variant

767

1

M → V.
Corresponds to variant rs6910140 [ dbSNP | Ensembl ].

VAR_055669

Natural variant

870

1

R → K. Ref.1 Ref.2 Ref.6
Corresponds to variant rs1056921 [ dbSNP | Ensembl ].

VAR_023326

Natural variant

882

1

V → L. Ref.1 Ref.2 Ref.6
Corresponds to variant rs1056923 [ dbSNP | Ensembl ].

VAR_023327

Experimental info

Sequence conflict

279 – 280

2

PP → AS in CAA38276. Ref.1

Sequence conflict

279 – 280

2

PP → AS in CAA38277. Ref.1

Sequence conflict

476

1

I → L in CAA38276. Ref.1

Sequence conflict

570

1

Q → H in AAC33527. Ref.2

Sequence conflict

570

1

Q → H in AAC33528. Ref.2

Sequence conflict

910 – 921

12

AGQRA…KGPDP → LVSEHLTKGLTLERLTAAWL SA in AAA53475. Ref.1

Secondary structure

1

.

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921

Helix Strand Turn

Details...

Beta strand

56 – 58

3

Helix

59 – 62

4

Helix

65 – 69

5

Turn

70 – 72

3

Beta strand

76 – 78

3

Beta strand

85 – 89

5

Beta strand

96 – 98

3

Helix

99 – 102

4

Beta strand

109 – 118

10

Helix

121 – 125

5

Beta strand

127 – 134

8

Beta strand

140 – 147

8

Helix

148 – 150

3

Beta strand

152 – 159

8

Beta strand

164 – 169

6

Helix

173 – 175

3

Beta strand

177 – 179

3

Beta strand

181 – 188

8

Beta strand

191 – 196

6

Beta strand

199 – 205

7

Beta strand

215 – 225

11

Beta strand

233 – 242

10

Helix

246 – 249

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified May 18, 2010. Version 3. Checksum: A69BF076127283D0	FASTA	921	91,869
	10 20 30 40 50 60 MKTCWKIPVF FFVCSFLEPW ASAAVKRRPR FPVNSNSNGG NELCPKIRIG QDDLPGFDLI 70 80 90 100 110 120 SQFQVDKAAS RRAIQRVVGS ATLQVAYKLG NNVDFRIPTR NLYPSGLPEE YSFLTTFRMT 130 140 150 160 170 180 GSTLKKNWNI WQIQDSSGKE QVGIKINGQT QSVVFSYKGL DGSLQTAAFS NLSSLFDSQW 190 200 210 220 230 240 HKIMIGVERS SATLFVDCNR IESLPIKPRG PIDIDGFAVL GKLADNPQVS VPFELQWMLI 250 260 270 280 290 300 HCDPLRPRRE TCHELPARIT PSQTTDERGP PGEQGPPGPP GPPGVPGIDG IDGDRGPKGP 310 320 330 340 350 360 PGPPGPAGEP GKPGAPGKPG TPGADGLTGP DGSPGSIGSK GQKGEPGVPG SRGFPGRGIP 370 380 390 400 410 420 GPPGPPGTAG LPGELGRVGP VGDPGRRGPP GPPGPPGPRG TIGFHDGDPL CPNACPPGRS 430 440 450 460 470 480 GYPGLPGMRG HKGAKGEIGE PGRQGHKGEE GDQGELGEVG AQGPPGAQGL RGITGIVGDK 490 500 510 520 530 540 GEKGARGLDG EPGPQGLPGA PGDQGQRGPP GEAGPKGDRG AEGARGIPGL PGPKGDTGLP 550 560 570 580 590 600 GVDGRDGIPG MPGTKGEPGK PGPPGDAGLQ GLPGVPGIPG AKGVAGEKGS TGAPGKPGQM 610 620 630 640 650 660 GNSGKPGQQG PPGEVGPRGP QGLPGSRGEL GPVGSPGLPG KLGSLGSPGL PGLPGPPGLP 670 680 690 700 710 720 GMKGDRGVVG EPGPKGEQGA SGEEGEAGER GELGDIGLPG PKGSAGNPGE PGLRGPEGSR 730 740 750 760 770 780 GLPGVEGPRG PPGPRGVQGE QGATGLPGVQ GPPGRAPTDQ HIKQVCMRVI QEHFAEMAAS 790 800 810 820 830 840 LKRPDSGATG LPGRPGPPGP PGPPGENGFP GQMGIRGLPG IKGPPGALGL RGPKGDLGEK 850 860 870 880 890 900 GERGPPGRGP NGLPGAIGLP GDPGPASYGR NGRDGERGPP GVAGIPGVPG PPGPPGLPGF 910 920 CEPASCTMQA GQRAFNKGPD P
	Isoform 2 (Short) [UniParc]. Checksum: AD0E99997DF2896E	FASTA	678	64,372
	10 20 30 40 50 60 MAWTARDRGA LGLLLLGLCL CAAQRGPPGE QGPPGPPGPP GVPGIDGIDG DRGPKGPPGP 70 80 90 100 110 120 PGPAGEPGKP GAPGKPGTPG ADGLTGPDGS PGSIGSKGQK GEPGVPGSRG FPGRGIPGPP 130 140 150 160 170 180 GPPGTAGLPG ELGRVGPVGD PGRRGPPGPP GPPGPRGTIG FHDGDPLCPN ACPPGRSGYP 190 200 210 220 230 240 GLPGMRGHKG AKGEIGEPGR QGHKGEEGDQ GELGEVGAQG PPGAQGLRGI TGIVGDKGEK 250 260 270 280 290 300 GARGLDGEPG PQGLPGAPGD QGQRGPPGEA GPKGDRGAEG ARGIPGLPGP KGDTGLPGVD 310 320 330 340 350 360 GRDGIPGMPG TKGEPGKPGP PGDAGLQGLP GVPGIPGAKG VAGEKGSTGA PGKPGQMGNS 370 380 390 400 410 420 GKPGQQGPPG EVGPRGPQGL PGSRGELGPV GSPGLPGKLG SLGSPGLPGL PGPPGLPGMK 430 440 450 460 470 480 GDRGVVGEPG PKGEQGASGE EGEAGERGEL GDIGLPGPKG SAGNPGEPGL RGPEGSRGLP 490 500 510 520 530 540 GVEGPRGPPG PRGVQGEQGA TGLPGVQGPP GRAPTDQHIK QVCMRVIQEH FAEMAASLKR 550 560 570 580 590 600 PDSGATGLPG RPGPPGPPGP PGENGFPGQM GIRGLPGIKG PPGALGLRGP KGDLGEKGER 610 620 630 640 650 660 GPPGRGPNGL PGAIGLPGDP GPASYGRNGR DGERGPPGVA GIPGVPGPPG PPGLPGFCEP 670 ASCTMQAGQR AFNKGPDP
	Isoform 3 [UniParc]. Checksum: BDD662939FECAD21	FASTA	328	35,509
	10 20 30 40 50 60 MKTCWKIPVF FFVCSFLEPW ASAAVKRRPR FPVNSNSNGG NELCPKIRIG QDDLPGFDLI 70 80 90 100 110 120 SQFQVDKAAS RRAIQRVVGS ATLQVAYKLG NNVDFRIPTR NLYPSGLPEE YSFLTTFRMT 130 140 150 160 170 180 GSTLKKNWNI WQIQDSSGKE QVGIKINGQT QSVVFSYKGL DGSLQTAAFS NLSSLFDSQW 190 200 210 220 230 240 HKIMIGVERS SATLFVDCNR IESLPIKPRG PIDIDGFAVL GKLADNPQVS VPFELQWMLI 250 260 270 280 290 300 HCDPLRPRRE TCHELPARIT PSQTTDERGP PGEQGPPGPP GPPGVPGIDG IDGDRGPKGP 310 320 PGPPGPAGEP GKPGAPGKPG TPGADTSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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 PRO-339 AND ARG-621, INVOLVEMENT IN EDM6.
[10]	"A new autosomal recessive form of Stickler syndrome is caused by a mutation in the COL9A1 gene." Van Camp G., Snoeckx R.L., Hilgert N., van den Ende J., Fukuoka H., Wagatsuma M., Suzuki H., Smets R.M., Vanhoenacker F., Declau F., Van de Heyning P., Usami S. Am. J. Hum. Genet. 79:449-457(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN STL4.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00295999.
IPI00645204.
IPI00874229.

PIR

S13580.
S13581.

RefSeq

NP_001842.3. NM_001851.4.
NP_511040.2. NM_078485.3.

UniGene

Hs.590892.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2UUR	X-ray	1.80	A	24-268	[»]

ProteinModelPortal

P20849.

SMR

P20849. Positions 42-256.

ModBase

Search...

PTM databases

PhosphoSite

P20849.

Polymorphism databases

DMDM

296439373.

Proteomic databases

PaxDb

P20849.

PRIDE

P20849.

Protocols and materials databases

DNASU

1297.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000320755; ENSP00000315252; ENSG00000112280.
ENST00000357250; ENSP00000349790; ENSG00000112280.
ENST00000370496; ENSP00000359527; ENSG00000112280.

GeneID

1297.

KEGG

hsa:1297.

UCSC

uc003pff.4. human.
uc003pfg.4. human.

Organism-specific databases

CTD

1297.

GeneCards

GC06M070924.

HGNC

HGNC:2217. COL9A1.

MIM

120210. gene.
614134. phenotype.
614135. phenotype.

neXtProt

NX_P20849.

Orphanet

250984. Autosomal recessive Stickler syndrome.
166002. Multiple epiphyseal dysplasia due to collagen 9 anomaly.

PharmGKB

PA26733.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOVERGEN

HBG004933.

InParanoid

P20849.

KO

K08131.

OMA

GFCEPAS.

OrthoDB

EOG4P2Q36.

PhylomeDB

P20849.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpress

P20849.

Bgee

P20849.

Genevestigator

P20849.

GermOnline

ENSG00000112280. Homo sapiens.

Family and domain databases

Gene3D

2.60.120.200. 1 hit.

InterPro

IPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR001791. Laminin_G.
[Graphical view]

Pfam

PF01391. Collagen. 10 hits.
[Graphical view]

SMART

SM00210. TSPN. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS50025. LAM_G_DOMAIN. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

COL9A1. human.

EvolutionaryTrace

P20849.

GenomeRNAi

1297.

NextBio

5265.

SOURCE

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Entry information

Entry name

CO9A1_HUMAN

Accession

Primary (citable) accession number: P20849
Secondary accession number(s): Q13699 , Q13700, Q5TF52, Q6P467, Q96BM8, Q99225, Q9H151, Q9H152, Q9Y6P2, Q9Y6P3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 155 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.