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Protein Page:
COL11A1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
COL11A1 May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils. Defects in COL11A1 are the cause of Stickler syndrome type 2 (STL2); also known as Stickler syndrome vitreous type 2. STL2 is 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. Defects in COL11A1 are the cause of Marshall syndrome (MRSHS). It is 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. Defects in COL11A1 are the cause of fibrochondrogenesis type 1 (FBCG1). 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. Belongs to the fibrillar collagen family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Secreted, signal peptide; Extracellular matrix; Secreted
Cellular Component: collagen type XI; endoplasmic reticulum lumen; extracellular region
Molecular Function: protein binding, bridging; extracellular matrix binding; extracellular matrix structural constituent; metal ion binding
Biological Process: collagen catabolic process; proteoglycan metabolic process; extracellular matrix disassembly; inner ear morphogenesis; extracellular matrix organization and biogenesis; sensory perception of sound; collagen fibril organization; visual perception; ventricular cardiac muscle morphogenesis; chondrocyte development; detection of mechanical stimulus involved in sensory perception of sound; embryonic skeletal morphogenesis; cartilage condensation
Reference #:  P12107 (UniProtKB)
Alt. Names/Synonyms: CO11A1; COBA1; COL11A1; COLL6; Collagen alpha-1(XI) chain; collagen XI, alpha-1 polypeptide; collagen, type XI, alpha 1; STL2
Gene Symbols: COL11A1
Molecular weight: 181,065 Da
Basal Isoelectric point: 5.06  Predict pI for various phosphorylation states
Select Structure to View Below

COL11A1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 2 S67-p FCTNRKNsKGSDtAy
0 2 T72-p KNsKGSDtAyRVSKQ
0 2 Y74-p sKGSDtAyRVSKQAQ
0 2 K875-a GARGVAGkPGPRGQR
0 2 T1766-p SRKGYEKtVIEINtP
0 2 T1772-p KtVIEINtPKIDQVP
  COL11A1 iso2  
S67 FCTNRKNSKGSDTAY
T72 KNSKGSDTAYRVSKQ
Y74 SKGSDTAYRVSKQAQ
K887-a GARGVAGkPGPRGQR
T1778 SRKGYEKTVIEINTP
T1784 KTVIEINTPKIDQVP
  mouse

 
S66 FCTNRKNSKDPDVAY
V71 KNSKDPDVAYRVTEE
Y73 SKDPDVAYRVTEEAQ
K873 GARGIAGKPGPRGQR
T1764 SRKGYEKTVIEINTP
T1770 KTVIEINTPKIDQVP
  rat

 
S66 FCTSRKNSKDPDIAY
I71 KNSKDPDIAYRVTEE
Y73 SKDPDIAYRVTEEAQ
K834 GARGIAGKPGPRGQR
T1725 SRKGYEKTVIEINTP
T1731 KTVIEINTPKIDQVP
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