COL9A1
entrez
1297
canonical
uniprot
P20849
canonical
ensembl
ENSG00000112280
resolver
ensp
ENSP00000315252
resolver
ensp
ENSP00000349790
resolver
ensp
ENSP00000359527
resolver
ensp
ENSP00000506990
resolver
ensp
ENSP00000508147
resolver
enst
ENST00000683980
resolver
genesymbol
COL9A1
resolver
hgnc
HGNC:2217
resolver
uniprot
A0A804HIB6
resolver
uniprot
Q13699
resolver
uniprot
Q13700
resolver
uniprot
Q5TF52
resolver
uniprot
Q6P467
resolver
uniprot
Q96BM8
resolver
uniprot
Q99225
resolver
uniprot
Q9H151
resolver
uniprot
Q9H152
resolver
uniprot
Q9Y6P2
resolver
uniprot
Q9Y6P3
resolver
uniprot_entry
A0A804HIB6_HUMAN
resolver
uniprot_entry
CO9A1_HUMAN
resolver
uniprot_sec
Q13699
resolver
uniprot_sec
Q13700
resolver
uniprot_sec
Q5TF52
resolver
uniprot_sec
Q6P467
resolver
uniprot_sec
Q96BM8
resolver
uniprot_sec
Q99225
resolver
uniprot_sec
Q9H151
resolver
uniprot_sec
Q9H152
resolver
uniprot_sec
Q9Y6P2
resolver
uniprot_sec
Q9Y6P3
resolver
amino_acid_sequence
MKTCWKIPVFFFVCSFLEPWASAAVKRRPRFPVNSNSNGGNELCPKIRIGQDDLPGFDLISQFQVDKAASRRAIQRVVGSATLQVAYKLGNNVDFRIPTRNLYPSGLPEEYSFLTTFRMTGSTLKKNWNIWQIQDSSGKEQVGIKINGQTQSVVFSYKGLDGSLQTAAFSNLSSLFDSQWHKIMIGVERSSATLFVDCNRIESLPIKPRGPIDIDGFAVLGKLADNPQVSVPFELQWMLIHCDPLRPRRETCHELPARITPSQTTDERGPPGEQGPPGPPGPPGVPGIDGIDGDRGPKGPPGPPGPAGEPGKPGAPGKPGTPGADGLTGPDGSPGSIGSKGQKGEPGVPGSRGFPGRGIPGPPGPPGTAGLPGELGRVGPVGDPGRRGPPGPPGPPGPRGTIGFHDGDPLCPNACPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGTKGEPGKPGPPGDAGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKLGSLGSPGLPGLPGPPGLPGMKGDRGVVGEPGPKGEQGASGEEGEAGERGELGDIGLPGPKGSAGNPGEPGLRGPEGSRGLPGVEGPRGPPGPRGVQGEQGATGLPGVQGPPGRAPTDQHIKQVCMRVIQEHFAEMAASLKRPDSGATGLPGRPGPPGPPGPPGENGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPPGRGPNGLPGAIGLPGDPGPASYGRNGRDGERGPPGVAGIPGVPGPPGPPGLPGFCEPASCTMQAGQRAFNKGPDP
uniprot
proteins
disease_involvement
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. {ECO:0000269|PubMed:11565064}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: 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. Pierre 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. {ECO:0000269|PubMed:16909383, ECO:0000269|PubMed:21421862, ECO:0000269|PubMed:31090205}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Structural component of hyaline cartilage and vitreous of the eye.
uniprot
proteins
mass_dalton
91869
uniprot
proteins
post_translational_modification
PTM: Covalently linked to the telopeptides of type II collagen by lysine-derived cross-links.; PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
uniprot
proteins
protein_family
Fibril-associated collagens with interrupted helices (FACIT) family
uniprot
proteins
pubmed
11565064
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1690886
uniprot
proteins
pubmed
16909383
uniprot
proteins
pubmed
17553797
uniprot
proteins
pubmed
21421862
uniprot
proteins
pubmed
2209617
uniprot
proteins
pubmed
2465149
uniprot
proteins
pubmed
31090205
uniprot
proteins
pubmed
8660302
uniprot
proteins
pubmed
9707347
uniprot
proteins
sequence_length
921
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
uniprot
proteins