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Protein Page:
COL1A2 (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
COL1A2 Type I collagen is a member of group I collagen (fibrillar forming collagen). Defects in COL1A2 are the cause of Ehlers-Danlos syndrome type 7B (EDS7B). EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7B is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations. Defects in COL1A2 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 COL1A2 are a cause of osteogenesis imperfecta type 2 (OI2); also known as osteogenesis imperfecta congenita (OIC) or lethal perinatal. 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 COL1A2 are the cause of Ehlers-Danlos syndrome autosomal recessive cardiac valvular form (EDSCV). A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. In addition to joint laxity, skin hyperextensibility and friability, and abnormal scar formation, patients have mitral valve prolapse and insufficiency, mitral regurgitation, and aortic insufficiency. Defects in COL1A2 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 COL1A2 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. A chromosomal aberration involving COL1A2 may be a cause of lipoblastomas, which are benign tumors resulting from transformation of adipocytes, usually diagnosed in children. Translocation t(7;8)(p22;q13) with PLAG1. Belongs to the fibrillar collagen family. Note: This description may include information from UniProtKB.
Protein type: Secreted; Secreted, signal peptide
Cellular Component: extracellular matrix; extracellular space; endoplasmic reticulum lumen; extracellular region; collagen type I
Molecular Function: protein binding, bridging; identical protein binding; protein binding; platelet-derived growth factor binding; extracellular matrix structural constituent; metal ion binding; SMAD binding
Biological Process: blood vessel development; platelet activation; extracellular matrix organization and biogenesis; collagen fibril organization; skin morphogenesis; Rho protein signal transduction; odontogenesis; extracellular matrix disassembly; collagen catabolic process; transforming growth factor beta receptor signaling pathway; regulation of blood pressure; blood coagulation; leukocyte migration; skeletal development
Reference #:  P08123 (UniProtKB)
Alt. Names/Synonyms: alpha 2(I)-collagen; Alpha-2 type I collagen; CO1A2; COL1A2; Collagen alpha-2(I) chain; collagen I, alpha-2 polypeptide; collagen of skin, tendon and bone, alpha-2 chain; collagen, type I, alpha 2; OI4; type I procollagen
Gene Symbols: COL1A2
Molecular weight: 129,314 Da
Basal Isoelectric point: 9.08  Predict pI for various phosphorylation states
Select Structure to View Below

COL1A2

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

 
0 1 K198-ac QPGAPGVkGEPGAPG
0 1 S251-p GPAGPIGsAGPPGFP
0 1 S291 EVGLPGLSGPVGPPG
0 1 T306 NPGANGLTGAKGAAG
0 1 S389-p GPNGEAGsAGPPGPP
0 1 S401-p GPPGLRGsPGsRGLP
0 1 S404-p GLRGsPGsRGLPGAD
0 1 R671 GEIGNPGRDGARGAP
0 1 S710-p GPAGPRGsPGERGEV
0 1 T981-p KHGNRGEtGPSGPVG
0 2 K1064-ac GPSGPAGkDGRTGHP
0 1 K1064 GPSGPAGKDGRTGHP
0 1 T1073-p GRTGHPGtVGPAGIR
0 1 S1104-p PPGPPGVsGGGYDFG
0 1 T1138-p KDYEVDAtLKsLNNQ
0 1 T1138-ga KDYEVDAtLKsLNNQ
0 1 S1141-p EVDAtLKsLNNQIEt
0 1 T1148-p sLNNQIEtLLTPEGs
0 1 S1155-p tLLTPEGsRKNPART
0 1 S1295-p KAVILQGsNDVELVA
  mouse

 
K204 QPGAQGVKGEPGAPG
S257 GPAGPIGSAGPPGFP
S297-p EVGLPGLsGPVGPPG
T312-p NPGTNGLtGAKGATG
S395 GSPGEAGSAGPAGPP
S407 GPPGLRGSPGSRGLP
S410 GLRGSPGSRGLPGAD
R677-m1 GDTGNTGrDGARGIP
S716 GPAGPRGSPGERGEV
P987 KHGNRGEPGPAGSVG
K1070 GPSGPVGKDGRSGQP
K1070-sc GPSGPVGkDGRSGQP
P1079 GRSGQPGPVGPAGVR
S1110 PPGPPGVSGGGYDFG
T1144 KDYEVDATLKSLNNQ
T1144 KDYEVDATLKSLNNQ
S1147 EVDATLKSLNNQIET
T1154 SLNNQIETLLTPEGS
S1161 TLLTPEGSRKNPART
S1301 KAVLLQGSNDVELVA
  rat

 
K204 QPGAQGVKGEPGAPG
S257 GPAGPIGSAGPPGFP
S297 EAGLPGLSGPVGPPG
T312 NPGANGLTGAKGATG
S395 GSPGEPGSAGPAGPP
S407 GPPGLRGSPGSRGLP
S410 GLRGSPGSRGLPGAD
R677 GEIGNPGRDGARGAP
S716 GPAGPRGSPGERGEV
P987 KHGNRGEPGPAGSVG
K1070-ac GPSGPIGkDGRSGHP
K1070 GPSGPIGKDGRSGHP
P1079 GRSGHPGPVGPAGVR
S1110 PPGPPGVSGGGYDFG
T1144 KDYEVDATLKSLNNQ
T1144 KDYEVDATLKSLNNQ
S1147 EVDATLKSLNNQIET
T1154 SLNNQIETLLTPEGS
S1161 TLLTPEGSRKNPART
S1301 KAVILQGSNDVELVA
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