Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
COL1A1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
COL1A1 Type I collagen is a member of group I collagen (fibrillar forming collagen). Defects in COL1A1 are the cause of Caffey disease (CAFFD); also known as infantile cortical hyperostosis. Caffey disease is characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age. Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1); also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome. Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A); also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations. Defects in COL1A1 are a cause of osteogenesis imperfecta type 1 (OI1). A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta. Defects in COL1A1 are a cause of osteogenesis imperfecta type 2 (OI2); also known as osteogenesis imperfecta congenita. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. Defects in COL1A1 are a cause of osteogenesis imperfecta type 3 (OI3). A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta. Defects in COL1A1 are a cause of osteogenesis imperfecta type 4 (OI4); also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. Genetic variations in COL1A1 are a cause of susceptibility to osteoporosis (OSTEOP); also known as involutional or senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mass, disruption of bone microarchitecture without alteration in the composition of bone. Osteoporotic bones are more at risk of fracture. A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF. Belongs to the fibrillar collagen family. Note: This description may include information from UniProtKB.
Protein type: Secreted, signal peptide; Secreted; Extracellular matrix
Cellular Component: extracellular matrix; extracellular space; endoplasmic reticulum lumen; extracellular region; collagen type I
Molecular Function: identical protein binding; protein binding; metal ion binding; extracellular matrix structural constituent; platelet-derived growth factor binding
Biological Process: response to peptide hormone stimulus; extracellular matrix organization and biogenesis; intramembranous ossification; response to cAMP; collagen fibril organization; positive regulation of transcription, DNA-dependent; embryonic skeletal development; response to estradiol stimulus; response to corticosteroid stimulus; extracellular matrix disassembly; protein transport; sensory perception of sound; visual perception; collagen biosynthetic process; skeletal development; response to nutrient; endochondral ossification; blood vessel development; platelet activation; skin morphogenesis; osteoblast differentiation; collagen catabolic process; response to hydrogen peroxide; blood coagulation; leukocyte migration; positive regulation of cell migration
Reference #:  P02452 (UniProtKB)
Alt. Names/Synonyms: Alpha-1 type I collagen; CO1A1; COL1A1; collagen alpha 1 chain type I; Collagen alpha-1(I) chain; collagen of skin, tendon and bone, alpha-1 chain; collagen, type I, alpha 1; OI4; pro-alpha-1 collagen type 1
Gene Symbols: COL1A1
Molecular weight: 138,942 Da
Basal Isoelectric point: 5.6  Predict pI for various phosphorylation states
Select Structure to View Below

COL1A1

Protein Structure Not Found.


STRING  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


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

 
0 1 K277-ac FSGLDGAkGDAGPAG
0 1 K277 FSGLDGAKGDAGPAG
0 1 T478-ga ARGEPGPtGLPGPPG
0 1 K505-ac ADGVAGPkGPAGERG
0 1 K520-ac SPGPAGPkGSPGEAG
1 1 S543-p GAKGLTGsPGsPGPD
1 1 S546-p GLTGsPGsPGPDGKT
0 5 K759-ac GADGSPGkDGVRGLT
0 1 S867-p GAKGARGsAGPPGAT
0 1 S889-p RVGPPGPsGNAGPPG
0 1 S1023-p GAPGAEGsPGRDGSP
0 1 S1125-p GPPGPPGsPGEQGPS
0 1 T1234-ga RDLEVDTtLKSLSQQ
0 1 K1385 DQQTGNLKKALLLQG
  mouse

 
K266 FSGLDGAKGDAGPAG
K266-sc FSGLDGAkGDAGPAG
S467 ARGEPGPSGLPGPPG
K494 ADGVAGPKGPSGERG
K509 APGPAGPKGSPGEAG
S532 GAKGLTGSPGSPGPD
S535 GLTGSPGSPGPDGKT
K748 GADGSPGKDGARGLT
A856 GPKGPRGAAGPPGAT
S878 RVGPPGPSGNAGPPG
S1012 GSPGAEGSPGRDGAP
S1114 GPPGSPGSPGEQGPS
T1223 RDLEVDTTLKSLSQQ
K1374-ac DQQTGNLkKALLLQG
  rat

 
K266 FSGLDGAKGDTGPAG
K266 FSGLDGAKGDTGPAG
S467 ARGEPGPSGLPGPPG
K494 ADGVAGPKGPAGERG
K509 SPGPAGPKGSPGEAG
S532 GAKGLTGSPGSPGPD
S535 GLTGSPGSPGPDGKT
K748 GADGSPGKDGVRGLT
A856 GPKGSRGAAGPPGAT
S878 RVGPPGPSGNAGPPG
S1012 GSPGAEGSPGRDGAP
S1114 GPPGSPGSPGEQGPS
T1223 RDLEVDTTLKSLSQQ
K1374 DQQTGNLKKSLLLQG
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.