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P49747 (COMP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cartilage oligomeric matrix protein

Short name=COMP
Alternative name(s):
Thrombospondin-5
Short name=TSP5
Gene names
Name:COMP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length757 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 By similarity. Ref.11 Ref.12 Ref.15

Cofactor

Binds 11-14 calcium ions per subunit.

Subunit structure

Pentamer; disulfide-linked. Exists in a more compact conformation in the presence of calcium and shows a more extended conformation in the absence of calcium. Interacts with ITGB3, ITGA5 and FN1. Binding to FN1 requires the presence of divalent cations (Ca2+, Mg2+ or Mn2+). The greatest amount of binding is seen in the presence of Mn2+. Interacts with MATN1, MATN3, MATN4 and ACAN. Binds heparin, heparan sulfate and chondroitin sulfate. EDTA dimishes significantly its binding to ACAN and abolishes its binding to MATN3, MATN4 and chondroitin sulfate. Interacts with collagen I, II and IX, and interaction with these collagens is dependent on the presence of zinc ions. Interacts with ADAMTS12. Interacts with ITGA7 By similarity. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

Abundantly expressed in the chondrocyte extracellular matrix, and is also found in bone, tendon, ligament and synovium and blood vessels. Increased amounts are produced during late stages of osteoarthritis in the area adjacent to the main defect. Ref.12

Developmental stage

Present during the earliest stages of limb maturation and is later found in regions where the joints develop. Ref.12

Domain

The cell attachment motif mediates the attachment to chondrocytes. It mediates the induction of both the IAP family of survival proteins and the antiapoptotic response. Ref.15

The TSP C-terminal domain mediates interaction with FN1 and ACAN. Ref.15

Each of the eight TSP type-3 repeats binds two calcium ions. The TSP C-terminal domain binds three calcium ions. Ref.15

Involvement in disease

Multiple epiphyseal dysplasia 1 (EDM1) [MIM:132400]: 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.6 Ref.8 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.26 Ref.27

Pseudoachondroplasia (PSACH) [MIM:177170]: A skeletal dysplasia usually manifesting in the second year of life and characterized by moderate to severe disproportionate short stature, deformity of the lower limbs, brachydactyly, ligamentous laxity, and degenerative joint disease.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.7 Ref.8 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.27

Sequence similarities

Belongs to the thrombospondin family.

Contains 4 EGF-like domains.

Contains 1 TSP C-terminal (TSPC) domain.

Contains 8 TSP type-3 repeats.

Sequence caution

The sequence AAB86501.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processApoptosis
Cell adhesion
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Dwarfism
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
Heparin-binding
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular matrix organization

Traceable author statement. Source: Reactome

growth plate cartilage development

Inferred from electronic annotation. Source: Ensembl

limb development

Inferred from direct assay Ref.12. Source: UniProtKB

negative regulation of apoptotic process

Inferred from direct assay Ref.15. Source: UniProtKB

organ morphogenesis

Traceable author statement Ref.1. Source: ProtInc

skeletal system development

Traceable author statement Ref.6. Source: ProtInc

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

proteinaceous extracellular matrix

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functioncalcium ion binding

Inferred from direct assay Ref.7Ref.8. Source: UniProtKB

collagen binding

Inferred from direct assay Ref.8. Source: UniProtKB

extracellular matrix structural constituent

Traceable author statement Ref.1. Source: ProtInc

heparan sulfate proteoglycan binding

Inferred from direct assay Ref.14. Source: UniProtKB

heparin binding

Inferred from direct assay Ref.14. Source: UniProtKB

protease binding

Inferred from physical interaction PubMed 18485748. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.9Ref.10Ref.11Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACANP136082EBI-2531022,EBI-6259246From a different organism.
ADAMTS12P583973EBI-2531022,EBI-9028051

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 757737Cartilage oligomeric matrix protein
PRO_0000035857

Regions

Domain87 – 12640EGF-like 1
Domain127 – 17953EGF-like 2; calcium-binding Potential
Domain180 – 22243EGF-like 3; calcium-binding Potential
Domain225 – 26743EGF-like 4
Repeat268 – 30033TSP type-3 1
Repeat301 – 33636TSP type-3 2
Repeat337 – 35923TSP type-3 3
Repeat360 – 39536TSP type-3 4
Repeat396 – 41823TSP type-3 5
Repeat419 – 45638TSP type-3 6
Repeat457 – 49236TSP type-3 7
Repeat493 – 52836TSP type-3 8
Domain532 – 746215TSP C-terminal
Region22 – 8665COMP N-terminal
Region527 – 757231Mediates cell survival and induction of the IAP family of survival proteins
Motif367 – 3693Cell attachment site Potential

Amino acid modifications

Glycosylation1211N-linked (GlcNAc...) Potential
Glycosylation7421N-linked (GlcNAc...) Ref.16
Disulfide bond69Interchain Probable
Disulfide bond72Interchain Probable
Disulfide bond91 ↔ 102 By similarity
Disulfide bond96 ↔ 111 By similarity
Disulfide bond114 ↔ 125 By similarity
Disulfide bond131 ↔ 142 By similarity
Disulfide bond136 ↔ 151 By similarity
Disulfide bond154 ↔ 178 By similarity
Disulfide bond184 ↔ 197 By similarity
Disulfide bond191 ↔ 206 By similarity
Disulfide bond209 ↔ 221 By similarity
Disulfide bond229 ↔ 243 Ref.16
Disulfide bond237 ↔ 253 Ref.16
Disulfide bond255 ↔ 266 Ref.16
Disulfide bond282 ↔ 287 Ref.16
Disulfide bond292 ↔ 312 Ref.16
Disulfide bond328 ↔ 348 Ref.16
Disulfide bond351 ↔ 371 Ref.16
Disulfide bond387 ↔ 407 Ref.16
Disulfide bond410 ↔ 430 Ref.16
Disulfide bond448 ↔ 468 Ref.16
Disulfide bond484 ↔ 504 Ref.16
Disulfide bond520 ↔ 741 Ref.16

Natural variations

Natural variant501E → D. Ref.1 Ref.2
VAR_016254
Natural variant511L → W. Ref.1 Ref.2
VAR_016255
Natural variant1091A → G. Ref.1 Ref.2
VAR_016257
Natural variant1671G → E in EDM1. Ref.27
VAR_066789
Natural variant2241R → G. Ref.1 Ref.2
VAR_016258
Natural variant2341P → S in PSACH. Ref.27
VAR_066790
Natural variant2761P → R in EDM1. Ref.26 Ref.27
VAR_026239
Natural variant2851R → P. Ref.1 Ref.2
VAR_016261
Natural variant2901D → G in PSACH. Ref.27
VAR_066791
Natural variant2901D → N in PSACH; mild form.
VAR_007614
Natural variant2981S → L in EDM1; phenotypic features overlapping with mild PSACH. Ref.27
VAR_066792
Natural variant2991G → R in PSACH. Ref.27
VAR_007615
Natural variant3111A → D in EDM1. Ref.27
VAR_066793
Natural variant3171D → G in EDM1; atypical form. Ref.27
VAR_066794
Natural variant3261D → G in EDM1. Ref.27
VAR_066795
Natural variant3261D → Y in PSACH. Ref.27
VAR_066796
Natural variant3281C → R in PSACH; mild form. Ref.6 Ref.22
VAR_007616
Natural variant341 – 3422Missing in PSACH.
VAR_066797
Natural variant3421D → Y in EDM1; Fairbank type. Ref.6 Ref.22
VAR_007617
Natural variant3481C → F in EDM1. Ref.27
VAR_066798
Natural variant3481C → R in PSACH. Ref.24
VAR_017102
Natural variant3491D → V in PSACH; mild form.
VAR_007618
Natural variant350 – 37223Missing in PSACH.
VAR_066799
Natural variant3611D → V in EDM1; Fairbank type.
VAR_007619
Natural variant3611D → Y in EDM1; binds less calcium. Ref.8 Ref.22
VAR_007620
Natural variant367 – 3682Missing in EDM1.
VAR_007621
Natural variant3711C → S in EDM1; Fairbank type. Ref.19 Ref.27
VAR_007622
Natural variant3711C → Y in EDM1. Ref.27
VAR_066800
Natural variant3721Missing in PSACH. Ref.22
VAR_007623
Natural variant3741D → N in EDM1. Ref.27
VAR_066801
Natural variant3741Missing in PSACH; mild form.
VAR_007624
Natural variant3761D → N in EDM1. Ref.27
VAR_066802
Natural variant3781D → V in PSACH. Ref.27
VAR_066803
Natural variant3811R → C.
Corresponds to variant rs3179763 [ dbSNP | Ensembl ].
VAR_046796
Natural variant3851D → N in EDM1; atypical form. Ref.27
VAR_066804
Natural variant3851D → Y in EDM1; atypical form. Ref.27
VAR_066805
Natural variant3851Missing in EDM1. Ref.27
VAR_066806
Natural variant3871C → G in PSACH; mild form.
VAR_007625
Natural variant3871C → R in PSACH. Ref.27
VAR_066807
Natural variant391 – 3944PNSD → V in PSACH.
VAR_007626
Natural variant3971D → H in EDM1. Ref.27
VAR_066808
Natural variant402 – 4043GIG → VC in PSACH.
VAR_066809
Natural variant4041G → R in EDM1. Ref.27
VAR_066810
Natural variant4081D → Y in EDM1. Ref.22
VAR_007627
Natural variant4101C → Y in EDM1; phenotype overlapping with mild PSACH. Ref.27
VAR_066811
Natural variant4151N → K in EDM1. Ref.27
VAR_066812
Natural variant4201D → A in EDM1. Ref.26
VAR_026240
Natural variant4271G → E in EDM1. Ref.27
VAR_066813
Natural variant430 – 4323CDS → LWC in EDM1.
VAR_066814
Natural variant4401G → E in PSACH; mild form.
VAR_007628
Natural variant4401G → R in PSACH. Ref.22 Ref.27
VAR_007629
Natural variant4461D → N in PSACH. Ref.27
VAR_066815
Natural variant4481C → S in PSACH. Ref.27
VAR_066816
Natural variant4531N → S in EDM1; Fairbank type. Ref.20
Corresponds to variant rs28936668 [ dbSNP | Ensembl ].
VAR_007630
Natural variant4571Missing in EDM1. Ref.27
VAR_066817
Natural variant4591Missing in PSACH; severe form. Ref.17 Ref.22
VAR_007631
Natural variant4681C → Y in PSACH; severe form. Ref.17 Ref.22
VAR_007632
Natural variant4691Missing in PSACH; severe form; MUT3 mutant; most common mutation; binds less calcium and causes misfolding of the protein; greatly reduced interaction with ACAN; reduced interaction with collagen. Ref.7 Ref.8 Ref.22
VAR_007633
Natural variant4721D → Y in PSACH; severe form. Ref.17 Ref.22
VAR_007634
Natural variant4731D → DD in EDM1. Ref.27
VAR_066818
Natural variant4731D → G in PSACH; severe form.
Corresponds to variant rs28936669 [ dbSNP | Ensembl ].
VAR_007635
Natural variant4731D → H in PSACH. Ref.27
VAR_066819
Natural variant4731Missing in PSACH; severe form. Ref.27
VAR_007636
Natural variant4751D → N in PSACH. Ref.27
VAR_066820
Natural variant4821D → G in PSACH. Ref.23 Ref.27
VAR_007637
Natural variant5011G → D in EDM1. Ref.27
VAR_066821
Natural variant5071D → G in PSACH. Ref.27
VAR_066822
Natural variant5111D → G in PSACH. Ref.27
VAR_066823
Natural variant513 – 5164Missing in PSACH; mild form.
VAR_007638
Natural variant5151D → G in PSACH. Ref.27
VAR_066824
Natural variant5181D → N in PSACH; mild form.
VAR_007639
Natural variant5231N → K in EDM1; Ribbing type. Ref.18 Ref.27
VAR_007640
Natural variant5291T → I in PSACH. Ref.27
VAR_066825
Natural variant5851T → M in PSACH; mild form and EDM1. Ref.26 Ref.27
VAR_007641
Natural variant5851T → R in EDM1 and PSACH. Ref.20 Ref.27
VAR_007642
Natural variant7181R → P in EDM1. Ref.27
VAR_066826
Natural variant7181R → W in EDM1. Ref.27
Corresponds to variant rs28936368 [ dbSNP | Ensembl ].
VAR_066827
Natural variant7191G → D in PSACH; severe. Ref.25
VAR_017103
Natural variant7191G → S in PSACH. Ref.27
VAR_066828
Natural variant7561Q → R in a patient with multiple epiphyseal dysplasia. Ref.27
Corresponds to variant rs61752496 [ dbSNP | Ensembl ].
VAR_066829

Experimental info

Sequence conflict2561A → R in AAA57253. Ref.1
Sequence conflict2561A → R in BAC53888. Ref.2
Sequence conflict3401D → Y in AAB35270. Ref.6

Secondary structure

...................................................................................................... 757
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49747 [UniParc].

Last modified October 14, 2008. Version 2.
Checksum: A0B73AADB39FBC7B

FASTA75782,860
        10         20         30         40         50         60 
MVPDTACVLL LTLAALGASG QGQSPLGSDL GPQMLRELQE TNAALQDVRE LLRQQVREIT 

        70         80         90        100        110        120 
FLKNTVMECD ACGMQQSVRT GLPSVRPLLH CAPGFCFPGV ACIQTESGAR CGPCPAGFTG 

       130        140        150        160        170        180 
NGSHCTDVNE CNAHPCFPRV RCINTSPGFR CEACPPGYSG PTHQGVGLAF AKANKQVCTD 

       190        200        210        220        230        240 
INECETGQHN CVPNSVCINT RGSFQCGPCQ PGFVGDQASG CQRRAQRFCP DGSPSECHEH 

       250        260        270        280        290        300 
ADCVLERDGS RSCVCAVGWA GNGILCGRDT DLDGFPDEKL RCPERQCRKD NCVTVPNSGQ 

       310        320        330        340        350        360 
EDVDRDGIGD ACDPDADGDG VPNEKDNCPL VRNPDQRNTD EDKWGDACDN CRSQKNDDQK 

       370        380        390        400        410        420 
DTDQDGRGDA CDDDIDGDRI RNQADNCPRV PNSDQKDSDG DGIGDACDNC PQKSNPDQAD 

       430        440        450        460        470        480 
VDHDFVGDAC DSDQDQDGDG HQDSRDNCPT VPNSAQEDSD HDGQGDACDD DDDNDGVPDS 

       490        500        510        520        530        540 
RDNCRLVPNP GQEDADRDGV GDVCQDDFDA DKVVDKIDVC PENAEVTLTD FRAFQTVVLD 

       550        560        570        580        590        600 
PEGDAQIDPN WVVLNQGREI VQTMNSDPGL AVGYTAFNGV DFEGTFHVNT VTDDDYAGFI 

       610        620        630        640        650        660 
FGYQDSSSFY VVMWKQMEQT YWQANPFRAV AEPGIQLKAV KSSTGPGEQL RNALWHTGDT 

       670        680        690        700        710        720 
ESQVRLLWKD PRNVGWKDKK SYRWFLQHRP QVGYIRVRFY EGPELVADSN VVLDTTMRGG 

       730        740        750 
RLGVFCFSQE NIIWANLRYR CNDTIPEDYE THQLRQA 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of human and mouse cartilage oligomeric matrix protein."
Newton G., Weremowicz S., Morton C.C., Copeland N.G., Gilbert D.J., Jenkins N.A., Lawler J.
Genomics 24:435-439(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASP-50; TRP-51; GLY-109; GLY-224 AND PRO-285.
Tissue: Cartilage.
[2]"Human comp cDNA with 5 SNIPs."
Hashimoto Y., Mori H.
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASP-50; TRP-51; GLY-109; GLY-224 AND PRO-285.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Ovary.
[6]"Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene."
Briggs M.D., Hoffman S.M.G., King L.M., Olsen A.S., Mohrenweiser H., Leroy J.G., Mortier G.R., Rimoin D.L., Lachman R.S., Gaines E.S., Cekleniak J.A., Knowlton R.G., Cohn D.H.
Nat. Genet. 10:330-336(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 326-344, VARIANT EDM1 TYR-342, VARIANT PSACH ARG-328.
[7]"Cartilage oligomeric matrix protein is a calcium-binding protein, and a mutation in its type 3 repeats causes conformational changes."
Chen H., Deere M., Hecht J.T., Lawler J.
J. Biol. Chem. 275:26538-26544(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 80-89, SUBUNIT, CALCIUM-BINDING, CHARACTERIZATION OF VARIANT PSACH ASP-469 DEL.
[8]"Mutations in cartilage oligomeric matrix protein causing pseudoachondroplasia and multiple epiphyseal dysplasia affect binding of calcium and collagen I, II, and IX."
Thur J., Rosenberg K., Nitsche D.P., Pihlajamaa T., Ala-Kokko L., Heinegaard D., Paulsson M., Maurer P.
J. Biol. Chem. 276:6083-6092(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, CALCIUM-BINDING, INTERACTION WITH COLLAGEN I; COLLAGEN II AND COLLAGEN IX, CHARACTERIZATION OF VARIANT PSACH ASP-469 DEL, CHARACTERIZATION OF VARIANT EDM1 TYR-361.
[9]"Matrix-matrix interaction of cartilage oligomeric matrix protein and fibronectin."
Di Cesare P.E., Chen F.S., Moergelin M., Carlson C.S., Leslie M.P., Perris R., Fang C.
Matrix Biol. 21:461-470(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FN1.
[10]"Interactions between the cartilage oligomeric matrix protein and matrilins. Implications for matrix assembly and the pathogenesis of chondrodysplasias."
Mann H.H., Oezbek S., Engel J., Paulsson M., Wagener R.
J. Biol. Chem. 279:25294-25298(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MATN1; MATN3 AND MATN4.
[11]"Cartilage oligomeric matrix protein/thrombospondin 5 supports chondrocyte attachment through interaction with integrins."
Chen F.-H., Thomas A.O., Hecht J.T., Goldring M.B., Lawler J.
J. Biol. Chem. 280:32655-32661(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ITGB3 AND ITGA5.
[12]"Cartilage oligomeric matrix protein is involved in human limb development and in the pathogenesis of osteoarthritis."
Koelling S., Clauditz T.S., Kaste M., Miosge N.
Arthritis Res. Ther. 8:R56-R56(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[13]"ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein."
Liu C.-J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E.
J. Biol. Chem. 281:15800-15808(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADAMTS12.
[14]"Interaction of cartilage oligomeric matrix protein/thrombospondin 5 with aggrecan."
Chen F.-H., Herndon M.E., Patel N., Hecht J.T., Tuan R.S., Lawler J.
J. Biol. Chem. 282:24591-24598(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACAN; HEPARIN; HEPARAN SULFATE AND CHONDROITIN SULFATE.
[15]"Cartilage oligomeric matrix protein protects cells against death by elevating members of the IAP family of survival proteins."
Gagarina V., Carlberg A.L., Pereira-Mouries L., Hall D.J.
J. Biol. Chem. 283:648-659(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAINS.
[16]"The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin binding."
Tan K., Duquette M., Joachimiak A., Lawler J.
FASEB J. 23:2490-2501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 225-757 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS, GLYCOSYLATION AT ASN-742.
[17]"Mutations in exon 17B of cartilage oligomeric matrix protein (COMP) cause pseudoachondroplasia."
Hecht J.T., Nelson L.D., Crowder E., Wang Y., Elder F.F.B., Harrison W.R., Francomano C.A., Prange C.K., Lennon G.G., Deere M., Lawler J.
Nat. Genet. 10:325-329(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSACH SER-459 DEL; TYR-468 AND TYR-472.
[18]"Multiple epiphyseal dysplasia, ribbing type: a novel point mutation in the COMP gene in a South African family."
Ballo R., Briggs M.D., Cohn D.H., Knowlton R.G., Beighton P.H., Ramesar R.S.
Am. J. Med. Genet. 68:396-400(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EDM1 LYS-523.
[19]"Multiple epiphyseal dysplasia and pseudoachondroplasia due to novel mutations in the calmodulin-like repeats of cartilage oligomeric matrix protein."
Susic S., McGrory J., Ahier J., Cole W.G.
Clin. Genet. 51:219-224(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EDM1 SER-371, VARIANT PSACH 513-VAL--LYS-516 DEL.
[20]"Diverse mutations in the gene for cartilage oligomeric matrix protein in the pseudoachondroplasia-multiple epiphyseal dysplasia disease spectrum."
Briggs M.D., Mortier G.R., Cole W.G., King L.M., Golik S.S., Bonaventure J., Nuytinck L., de Paepe A., Leroy J.G., Biesecker L., Lipson M., Wilcox W.R., Lachman R.S., Rimoin D.L., Knowlton R.G., Cohn D.H.
Am. J. Hum. Genet. 62:311-319(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSACH, VARIANTS EDM1 SER-453 AND ARG-585.
[21]"Novel and recurrent COMP (cartilage oligomeric matrix protein) mutations in pseudoachondroplasia and multiple epiphyseal dysplasia."
Ikegawa S., Ohashi H., Nishimura G., Kim K.C., Sannohe A., Kimizuka M., Fukushima Y., Nagai T., Nakamura Y.
Hum. Genet. 103:633-638(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSACH AND EDM1.
[22]"Identification of five novel mutations in cartilage oligomeric matrix protein gene in pseudoachondroplasia and multiple epiphyseal dysplasia."
Loughlin J., Irven C., Mustafa Z., Briggs M.D., Carr A., Lynch S.-A., Knowlton R.G., Cohn D.H., Sykes B.
Hum. Mutat. Suppl. 1:S10-S17(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSACH ARG-328; ASP-372 DEL; 391-PRO--ASP-394 DELINS VAL; ARG-440; SER-459 DEL; TYR-468; ASP-469 DEL AND TYR-472, VARIANTS EDM1 TYR-342; TYR-361; 367-ARG-GLY-368 DEL AND TYR-408.
[23]"Pseudoachondroplasia due to the substitution of the highly conserved Asp482 by Gly in the seventh calmodulin-like repeat of cartilage oligomeric matrix protein."
Susic S., Ahier J., Cole W.G.
Hum. Mutat. Suppl. 1:S125-S127(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PSACH GLY-482.
[24]"Double heterozygosity for pseudoachondroplasia and spondyloepiphyseal dysplasia congenita."
Unger S., Koerkkoe J., Krakow D., Lachman R.S., Rimoin D.L., Cohn D.H.
Am. J. Med. Genet. 104:140-146(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PSACH ARG-348.
[25]"Novel mutation in exon 18 of the cartilage oligomeric matrix protein gene causes a severe pseudoachondroplasia."
Mabuchi A., Haga N., Ikeda T., Manabe N., Ohashi H., Takatori Y., Nakamura K., Ikegawa S.
Am. J. Med. Genet. 104:135-139(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PSACH ASP-719.
[26]"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 EDM1 ARG-276; ALA-420 AND MET-585.
[27]"Pseudoachondroplasia and multiple epiphyseal dysplasia: A 7-year comprehensive analysis of the known disease genes identify novel and recurrent mutations and provides an accurate assessment of their relative contribution."
Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R., Spranger J., Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M., Offiah A., Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C., Elles R., Bonafe L., Superti-Furga A., Unger S., Zankl A., Briggs M.D.
Hum. Mutat. 33:144-157(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSACH SER-234; GLY-290; ARG-299; TYR-326; 341-GLU-ASP-342 DEL; 350-ASN--ASP-372 DEL; VAL-378; ARG-387; 402-GLY--GLY-404 DELINS VAL-CYS; ARG-440; ASN-446; SER-448; ASP-473 DEL; HIS-473; ASN-475; GLY-482; GLY-507; GLY-511; GLY-515; ILE-529; ARG-585 AND SER-719, VARIANTS EDM1 GLU-167; ARG-276; LEU-298; ASP-311; GLY-317; GLY-326; PHE-348; SER-371; TYR-371; ASN-374; ASN-376; ASN-385; ASP-385 DEL; TYR-385; HIS-397; ARG-404; TYR-410; LYS-415; GLU-427; 430-CYS--SER-432 DELINS LEU-TRP-CYS; GLU-457 DEL; ASP-473 INS; ASP-501; LYS-523; MET-585; PRO-718 AND TRP-718, VARIANT ARG-756.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L32137 mRNA. Translation: AAA57253.1.
AB086984 mRNA. Translation: BAC53888.1.
AC003107 Genomic DNA. Translation: AAB86501.1. Sequence problems.
CH471106 Genomic DNA. Translation: EAW84737.1.
BC110847 mRNA. Translation: AAI10848.1.
BC125092 mRNA. Translation: AAI25093.1.
S79499 Genomic DNA. Translation: AAB35269.1.
S79500 Genomic DNA. Translation: AAB35270.1.
CCDSCCDS12385.1.
RefSeqNP_000086.2. NM_000095.2.
UniGeneHs.1584.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FBYX-ray3.15A/B/C225-757[»]
ProteinModelPortalP49747.
SMRP49747. Positions 29-72, 91-757.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP49747. 4 interactions.
STRING9606.ENSP00000222271.

PTM databases

PhosphoSiteP49747.

Polymorphism databases

DMDM209572601.

Proteomic databases

MaxQBP49747.
PaxDbP49747.
PRIDEP49747.

Protocols and materials databases

DNASU1311.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222271; ENSP00000222271; ENSG00000105664.
GeneID1311.
KEGGhsa:1311.
UCSCuc002nkd.3. human.

Organism-specific databases

CTD1311.
GeneCardsGC19M018894.
GeneReviewsCOMP.
H-InvDBHIX0014925.
HGNCHGNC:2227. COMP.
MIM132400. phenotype.
177170. phenotype.
600310. gene.
neXtProtNX_P49747.
Orphanet93308. Multiple epiphyseal dysplasia type 1.
750. Pseudoachondroplasia.
PharmGKBPA26744.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000007542.
HOVERGENHBG000636.
InParanoidP49747.
KOK04659.
OMAPEDYETQ.
PhylomeDBP49747.
TreeFamTF324917.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP49747.
BgeeP49747.
CleanExHS_COMP.
GenevestigatorP49747.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProIPR028492. Comp.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR024665. Thbs/COMP_coiled-coil.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR028974. TSP_type-3_rpt.
[Graphical view]
PANTHERPTHR10199:SF81. PTHR10199:SF81. 1 hit.
PfamPF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view]
SMARTSM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view]
SUPFAMSSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEPS01186. EGF_2. 1 hit.
PS50026. EGF_3. 3 hits.
PS01187. EGF_CA. 2 hits.
PS51234. TSP3. 8 hits.
PS51236. TSP_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOMP. human.
EvolutionaryTraceP49747.
GeneWikiCartilage_oligomeric_matrix_protein.
GenomeRNAi1311.
NextBio5361.
PMAP-CutDBP49747.
PROP49747.
SOURCESearch...

Entry information

Entry nameCOMP_HUMAN
AccessionPrimary (citable) accession number: P49747
Secondary accession number(s): O14592 expand/collapse secondary AC list , Q16388, Q16389, Q2NL86, Q8N4T2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM