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P49747

- COMP_HUMAN

UniProt

P49747 - COMP_HUMAN

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Protein
Cartilage oligomeric matrix protein
Gene
COMP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Cofactori

Binds 11-14 calcium ions per subunit.

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. collagen binding Source: UniProtKB
  3. extracellular matrix structural constituent Source: ProtInc
  4. heparan sulfate proteoglycan binding Source: UniProtKB
  5. heparin binding Source: UniProtKB
  6. protease binding Source: BHF-UCL
  7. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell adhesion Source: UniProtKB-KW
  3. extracellular matrix organization Source: Reactome
  4. growth plate cartilage development Source: Ensembl
  5. limb development Source: UniProtKB
  6. negative regulation of apoptotic process Source: UniProtKB
  7. organ morphogenesis Source: ProtInc
  8. skeletal system development Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell adhesion

Keywords - Ligandi

Calcium, Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_13552. Integrin cell surface interactions.
REACT_163906. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Cartilage oligomeric matrix protein
Short name:
COMP
Alternative name(s):
Thrombospondin-5
Short name:
TSP5
Gene namesi
Name:COMP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:2227. COMP.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: BHF-UCL
  3. extracellular vesicular exosome Source: UniProt
  4. proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

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.9 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1671G → E in EDM1. 1 Publication
VAR_066789
Natural varianti276 – 2761P → R in EDM1. 2 Publications
VAR_026239
Natural varianti298 – 2981S → L in EDM1; phenotypic features overlapping with mild PSACH. 1 Publication
VAR_066792
Natural varianti311 – 3111A → D in EDM1. 1 Publication
VAR_066793
Natural varianti317 – 3171D → G in EDM1; atypical form. 1 Publication
VAR_066794
Natural varianti326 – 3261D → G in EDM1. 1 Publication
VAR_066795
Natural varianti342 – 3421D → Y in EDM1; Fairbank type. 2 Publications
VAR_007617
Natural varianti348 – 3481C → F in EDM1. 1 Publication
VAR_066798
Natural varianti361 – 3611D → V in EDM1; Fairbank type.
VAR_007619
Natural varianti361 – 3611D → Y in EDM1; binds less calcium. 2 Publications
VAR_007620
Natural varianti367 – 3682Missing in EDM1.
VAR_007621
Natural varianti371 – 3711C → S in EDM1; Fairbank type. 2 Publications
VAR_007622
Natural varianti371 – 3711C → Y in EDM1. 1 Publication
VAR_066800
Natural varianti374 – 3741D → N in EDM1. 1 Publication
VAR_066801
Natural varianti376 – 3761D → N in EDM1. 1 Publication
VAR_066802
Natural varianti385 – 3851D → N in EDM1; atypical form. 1 Publication
VAR_066804
Natural varianti385 – 3851D → Y in EDM1; atypical form. 1 Publication
VAR_066805
Natural varianti385 – 3851Missing in EDM1. 1 Publication
VAR_066806
Natural varianti397 – 3971D → H in EDM1. 1 Publication
VAR_066808
Natural varianti404 – 4041G → R in EDM1. 1 Publication
VAR_066810
Natural varianti408 – 4081D → Y in EDM1. 1 Publication
VAR_007627
Natural varianti410 – 4101C → Y in EDM1; phenotype overlapping with mild PSACH. 1 Publication
VAR_066811
Natural varianti415 – 4151N → K in EDM1. 1 Publication
VAR_066812
Natural varianti420 – 4201D → A in EDM1. 1 Publication
VAR_026240
Natural varianti427 – 4271G → E in EDM1. 1 Publication
VAR_066813
Natural varianti430 – 4323CDS → LWC in EDM1.
VAR_066814
Natural varianti453 – 4531N → S in EDM1; Fairbank type. 1 Publication
Corresponds to variant rs28936668 [ dbSNP | Ensembl ].
VAR_007630
Natural varianti457 – 4571Missing in EDM1. 1 Publication
VAR_066817
Natural varianti473 – 4731D → DD in EDM1. 1 Publication
VAR_066818
Natural varianti501 – 5011G → D in EDM1. 1 Publication
VAR_066821
Natural varianti523 – 5231N → K in EDM1; Ribbing type. 2 Publications
VAR_007640
Natural varianti585 – 5851T → M in PSACH; mild form and EDM1. 2 Publications
VAR_007641
Natural varianti585 – 5851T → R in EDM1 and PSACH. 2 Publications
VAR_007642
Natural varianti718 – 7181R → P in EDM1. 1 Publication
VAR_066826
Natural varianti718 – 7181R → W in EDM1. 1 Publication
Corresponds to variant rs28936368 [ dbSNP | Ensembl ].
VAR_066827
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.12 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti234 – 2341P → S in PSACH. 1 Publication
VAR_066790
Natural varianti290 – 2901D → G in PSACH. 1 Publication
VAR_066791
Natural varianti290 – 2901D → N in PSACH; mild form.
VAR_007614
Natural varianti298 – 2981S → L in EDM1; phenotypic features overlapping with mild PSACH. 1 Publication
VAR_066792
Natural varianti299 – 2991G → R in PSACH. 1 Publication
VAR_007615
Natural varianti326 – 3261D → Y in PSACH. 1 Publication
VAR_066796
Natural varianti328 – 3281C → R in PSACH; mild form. 2 Publications
VAR_007616
Natural varianti341 – 3422Missing in PSACH.
VAR_066797
Natural varianti348 – 3481C → R in PSACH. 1 Publication
VAR_017102
Natural varianti349 – 3491D → V in PSACH; mild form.
VAR_007618
Natural varianti350 – 37223Missing in PSACH.
VAR_066799Add
BLAST
Natural varianti372 – 3721Missing in PSACH. 1 Publication
VAR_007623
Natural varianti374 – 3741Missing in PSACH; mild form.
VAR_007624
Natural varianti378 – 3781D → V in PSACH. 1 Publication
VAR_066803
Natural varianti387 – 3871C → G in PSACH; mild form.
VAR_007625
Natural varianti387 – 3871C → R in PSACH. 1 Publication
VAR_066807
Natural varianti391 – 3944PNSD → V in PSACH.
VAR_007626
Natural varianti402 – 4043GIG → VC in PSACH.
VAR_066809
Natural varianti410 – 4101C → Y in EDM1; phenotype overlapping with mild PSACH. 1 Publication
VAR_066811
Natural varianti440 – 4401G → E in PSACH; mild form.
VAR_007628
Natural varianti440 – 4401G → R in PSACH. 2 Publications
VAR_007629
Natural varianti446 – 4461D → N in PSACH. 1 Publication
VAR_066815
Natural varianti448 – 4481C → S in PSACH. 1 Publication
VAR_066816
Natural varianti459 – 4591Missing in PSACH; severe form. 2 Publications
VAR_007631
Natural varianti468 – 4681C → Y in PSACH; severe form. 2 Publications
VAR_007632
Natural varianti469 – 4691Missing 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. 3 Publications
VAR_007633
Natural varianti472 – 4721D → Y in PSACH; severe form. 2 Publications
VAR_007634
Natural varianti473 – 4731D → G in PSACH; severe form.
Corresponds to variant rs28936669 [ dbSNP | Ensembl ].
VAR_007635
Natural varianti473 – 4731D → H in PSACH. 1 Publication
VAR_066819
Natural varianti473 – 4731Missing in PSACH; severe form. 1 Publication
VAR_007636
Natural varianti475 – 4751D → N in PSACH. 1 Publication
VAR_066820
Natural varianti482 – 4821D → G in PSACH. 2 Publications
VAR_007637
Natural varianti507 – 5071D → G in PSACH. 1 Publication
VAR_066822
Natural varianti511 – 5111D → G in PSACH. 1 Publication
VAR_066823
Natural varianti513 – 5164Missing in PSACH; mild form.
VAR_007638
Natural varianti515 – 5151D → G in PSACH. 1 Publication
VAR_066824
Natural varianti518 – 5181D → N in PSACH; mild form.
VAR_007639
Natural varianti529 – 5291T → I in PSACH. 1 Publication
VAR_066825
Natural varianti585 – 5851T → M in PSACH; mild form and EDM1. 2 Publications
VAR_007641
Natural varianti585 – 5851T → R in EDM1 and PSACH. 2 Publications
VAR_007642
Natural varianti719 – 7191G → D in PSACH; severe. 1 Publication
VAR_017103
Natural varianti719 – 7191G → S in PSACH. 1 Publication
VAR_066828

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi132400. phenotype.
177170. phenotype.
Orphaneti93308. Multiple epiphyseal dysplasia type 1.
750. Pseudoachondroplasia.
PharmGKBiPA26744.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed prediction
Add
BLAST
Chaini21 – 757737Cartilage oligomeric matrix protein
PRO_0000035857Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi69 – 69Interchain Inferred
Disulfide bondi72 – 72Interchain Inferred
Disulfide bondi91 ↔ 102 By similarity
Disulfide bondi96 ↔ 111 By similarity
Disulfide bondi114 ↔ 125 By similarity
Glycosylationi121 – 1211N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi131 ↔ 142 By similarity
Disulfide bondi136 ↔ 151 By similarity
Disulfide bondi154 ↔ 178 By similarity
Disulfide bondi184 ↔ 197 By similarity
Disulfide bondi191 ↔ 206 By similarity
Disulfide bondi209 ↔ 221 By similarity
Disulfide bondi229 ↔ 2431 Publication
Disulfide bondi237 ↔ 2531 Publication
Disulfide bondi255 ↔ 2661 Publication
Disulfide bondi282 ↔ 2871 Publication
Disulfide bondi292 ↔ 3121 Publication
Disulfide bondi328 ↔ 3481 Publication
Disulfide bondi351 ↔ 3711 Publication
Disulfide bondi387 ↔ 4071 Publication
Disulfide bondi410 ↔ 4301 Publication
Disulfide bondi448 ↔ 4681 Publication
Disulfide bondi484 ↔ 5041 Publication
Disulfide bondi520 ↔ 7411 Publication
Glycosylationi742 – 7421N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP49747.
PaxDbiP49747.
PRIDEiP49747.

PTM databases

PhosphoSiteiP49747.

Miscellaneous databases

PMAP-CutDBP49747.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

Present during the earliest stages of limb maturation and is later found in regions where the joints develop.1 Publication

Gene expression databases

ArrayExpressiP49747.
BgeeiP49747.
CleanExiHS_COMP.
GenevestigatoriP49747.

Interactioni

Subunit structurei

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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACANP136082EBI-2531022,EBI-6259246From a different organism.
ADAMTS12P583973EBI-2531022,EBI-9028051

Protein-protein interaction databases

IntActiP49747. 4 interactions.
STRINGi9606.ENSP00000222271.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi232 – 2343
Beta strandi241 – 2455
Beta strandi251 – 2555
Beta strandi259 – 2657
Beta strandi272 – 2743
Helixi285 – 2873
Beta strandi291 – 2955
Beta strandi306 – 3083
Helixi310 – 3123
Turni314 – 3174
Beta strandi319 – 3213
Helixi323 – 3253
Beta strandi327 – 3315
Beta strandi342 – 3443
Helixi346 – 3483
Beta strandi364 – 3674
Helixi369 – 3713
Beta strandi378 – 3803
Beta strandi401 – 4033
Helixi405 – 4073
Beta strandi424 – 4263
Turni428 – 4303
Helixi443 – 4453
Beta strandi462 – 4643
Turni466 – 4683
Beta strandi470 – 4734
Beta strandi475 – 4773
Helixi479 – 4813
Beta strandi495 – 5006
Turni503 – 5064
Beta strandi511 – 5133
Helixi515 – 5173
Beta strandi532 – 5409
Beta strandi551 – 5533
Turni555 – 5573
Beta strandi560 – 5623
Beta strandi567 – 58822
Beta strandi596 – 60510
Beta strandi608 – 61710
Beta strandi625 – 6273
Beta strandi636 – 6416
Helixi648 – 6558
Beta strandi656 – 6583
Turni661 – 6633
Beta strandi664 – 6696
Beta strandi681 – 6899
Helixi690 – 6923
Beta strandi694 – 7018
Beta strandi704 – 7085
Beta strandi716 – 72813
Beta strandi732 – 74110
Helixi748 – 7547

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FBYX-ray3.15A/B/C225-757[»]
ProteinModelPortaliP49747.
SMRiP49747. Positions 29-72, 91-757.

Miscellaneous databases

EvolutionaryTraceiP49747.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 12640EGF-like 1
Add
BLAST
Domaini127 – 17953EGF-like 2; calcium-binding Reviewed prediction
Add
BLAST
Domaini180 – 22243EGF-like 3; calcium-binding Reviewed prediction
Add
BLAST
Domaini225 – 26743EGF-like 4
Add
BLAST
Repeati268 – 30033TSP type-3 1
Add
BLAST
Repeati301 – 33636TSP type-3 2
Add
BLAST
Repeati337 – 35923TSP type-3 3
Add
BLAST
Repeati360 – 39536TSP type-3 4
Add
BLAST
Repeati396 – 41823TSP type-3 5
Add
BLAST
Repeati419 – 45638TSP type-3 6
Add
BLAST
Repeati457 – 49236TSP type-3 7
Add
BLAST
Repeati493 – 52836TSP type-3 8
Add
BLAST
Domaini532 – 746215TSP C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 8665COMP N-terminal
Add
BLAST
Regioni527 – 757231Mediates cell survival and induction of the IAP family of survival proteins
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi367 – 3693Cell attachment site Reviewed prediction

Domaini

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.1 Publication
The TSP C-terminal domain mediates interaction with FN1 and ACAN.1 Publication
Each of the eight TSP type-3 repeats binds two calcium ions. The TSP C-terminal domain binds three calcium ions.1 Publication

Sequence similaritiesi

Belongs to the thrombospondin family.
Contains 4 EGF-like domains.
Contains 8 TSP type-3 repeats.

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000007542.
HOVERGENiHBG000636.
InParanoidiP49747.
KOiK04659.
OMAiPEDYETQ.
PhylomeDBiP49747.
TreeFamiTF324917.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProiIPR028492. 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]
PANTHERiPTHR10199:SF81. PTHR10199:SF81. 1 hit.
PfamiPF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view]
SUPFAMiSSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS01186. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P49747-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MVPDTACVLL LTLAALGASG QGQSPLGSDL GPQMLRELQE TNAALQDVRE    50
LLRQQVREIT FLKNTVMECD ACGMQQSVRT GLPSVRPLLH CAPGFCFPGV 100
ACIQTESGAR CGPCPAGFTG NGSHCTDVNE CNAHPCFPRV RCINTSPGFR 150
CEACPPGYSG PTHQGVGLAF AKANKQVCTD INECETGQHN CVPNSVCINT 200
RGSFQCGPCQ PGFVGDQASG CQRRAQRFCP DGSPSECHEH ADCVLERDGS 250
RSCVCAVGWA GNGILCGRDT DLDGFPDEKL RCPERQCRKD NCVTVPNSGQ 300
EDVDRDGIGD ACDPDADGDG VPNEKDNCPL VRNPDQRNTD EDKWGDACDN 350
CRSQKNDDQK DTDQDGRGDA CDDDIDGDRI RNQADNCPRV PNSDQKDSDG 400
DGIGDACDNC PQKSNPDQAD VDHDFVGDAC DSDQDQDGDG HQDSRDNCPT 450
VPNSAQEDSD HDGQGDACDD DDDNDGVPDS RDNCRLVPNP GQEDADRDGV 500
GDVCQDDFDA DKVVDKIDVC PENAEVTLTD FRAFQTVVLD PEGDAQIDPN 550
WVVLNQGREI VQTMNSDPGL AVGYTAFNGV DFEGTFHVNT VTDDDYAGFI 600
FGYQDSSSFY VVMWKQMEQT YWQANPFRAV AEPGIQLKAV KSSTGPGEQL 650
RNALWHTGDT ESQVRLLWKD PRNVGWKDKK SYRWFLQHRP QVGYIRVRFY 700
EGPELVADSN VVLDTTMRGG RLGVFCFSQE NIIWANLRYR CNDTIPEDYE 750
THQLRQA 757
Length:757
Mass (Da):82,860
Last modified:October 14, 2008 - v2
Checksum:iA0B73AADB39FBC7B
GO
Isoform 2 (identifier: P49747-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     129-181: Missing.

Note: No experimental confirmation available.

Show »
Length:704
Mass (Da):77,214
Checksum:i1126EE4088275D29
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501E → D.2 Publications
VAR_016254
Natural varianti51 – 511L → W.2 Publications
VAR_016255
Natural varianti109 – 1091A → G.2 Publications
VAR_016257
Natural varianti167 – 1671G → E in EDM1. 1 Publication
VAR_066789
Natural varianti224 – 2241R → G.2 Publications
VAR_016258
Natural varianti234 – 2341P → S in PSACH. 1 Publication
VAR_066790
Natural varianti276 – 2761P → R in EDM1. 2 Publications
VAR_026239
Natural varianti285 – 2851R → P.2 Publications
VAR_016261
Natural varianti290 – 2901D → G in PSACH. 1 Publication
VAR_066791
Natural varianti290 – 2901D → N in PSACH; mild form.
VAR_007614
Natural varianti298 – 2981S → L in EDM1; phenotypic features overlapping with mild PSACH. 1 Publication
VAR_066792
Natural varianti299 – 2991G → R in PSACH. 1 Publication
VAR_007615
Natural varianti311 – 3111A → D in EDM1. 1 Publication
VAR_066793
Natural varianti317 – 3171D → G in EDM1; atypical form. 1 Publication
VAR_066794
Natural varianti326 – 3261D → G in EDM1. 1 Publication
VAR_066795
Natural varianti326 – 3261D → Y in PSACH. 1 Publication
VAR_066796
Natural varianti328 – 3281C → R in PSACH; mild form. 2 Publications
VAR_007616
Natural varianti341 – 3422Missing in PSACH.
VAR_066797
Natural varianti342 – 3421D → Y in EDM1; Fairbank type. 2 Publications
VAR_007617
Natural varianti348 – 3481C → F in EDM1. 1 Publication
VAR_066798
Natural varianti348 – 3481C → R in PSACH. 1 Publication
VAR_017102
Natural varianti349 – 3491D → V in PSACH; mild form.
VAR_007618
Natural varianti350 – 37223Missing in PSACH.
VAR_066799Add
BLAST
Natural varianti361 – 3611D → V in EDM1; Fairbank type.
VAR_007619
Natural varianti361 – 3611D → Y in EDM1; binds less calcium. 2 Publications
VAR_007620
Natural varianti367 – 3682Missing in EDM1.
VAR_007621
Natural varianti371 – 3711C → S in EDM1; Fairbank type. 2 Publications
VAR_007622
Natural varianti371 – 3711C → Y in EDM1. 1 Publication
VAR_066800
Natural varianti372 – 3721Missing in PSACH. 1 Publication
VAR_007623
Natural varianti374 – 3741D → N in EDM1. 1 Publication
VAR_066801
Natural varianti374 – 3741Missing in PSACH; mild form.
VAR_007624
Natural varianti376 – 3761D → N in EDM1. 1 Publication
VAR_066802
Natural varianti378 – 3781D → V in PSACH. 1 Publication
VAR_066803
Natural varianti381 – 3811R → C.
Corresponds to variant rs3179763 [ dbSNP | Ensembl ].
VAR_046796
Natural varianti385 – 3851D → N in EDM1; atypical form. 1 Publication
VAR_066804
Natural varianti385 – 3851D → Y in EDM1; atypical form. 1 Publication
VAR_066805
Natural varianti385 – 3851Missing in EDM1. 1 Publication
VAR_066806
Natural varianti387 – 3871C → G in PSACH; mild form.
VAR_007625
Natural varianti387 – 3871C → R in PSACH. 1 Publication
VAR_066807
Natural varianti391 – 3944PNSD → V in PSACH.
VAR_007626
Natural varianti397 – 3971D → H in EDM1. 1 Publication
VAR_066808
Natural varianti402 – 4043GIG → VC in PSACH.
VAR_066809
Natural varianti404 – 4041G → R in EDM1. 1 Publication
VAR_066810
Natural varianti408 – 4081D → Y in EDM1. 1 Publication
VAR_007627
Natural varianti410 – 4101C → Y in EDM1; phenotype overlapping with mild PSACH. 1 Publication
VAR_066811
Natural varianti415 – 4151N → K in EDM1. 1 Publication
VAR_066812
Natural varianti420 – 4201D → A in EDM1. 1 Publication
VAR_026240
Natural varianti427 – 4271G → E in EDM1. 1 Publication
VAR_066813
Natural varianti430 – 4323CDS → LWC in EDM1.
VAR_066814
Natural varianti440 – 4401G → E in PSACH; mild form.
VAR_007628
Natural varianti440 – 4401G → R in PSACH. 2 Publications
VAR_007629
Natural varianti446 – 4461D → N in PSACH. 1 Publication
VAR_066815
Natural varianti448 – 4481C → S in PSACH. 1 Publication
VAR_066816
Natural varianti453 – 4531N → S in EDM1; Fairbank type. 1 Publication
Corresponds to variant rs28936668 [ dbSNP | Ensembl ].
VAR_007630
Natural varianti457 – 4571Missing in EDM1. 1 Publication
VAR_066817
Natural varianti459 – 4591Missing in PSACH; severe form. 2 Publications
VAR_007631
Natural varianti468 – 4681C → Y in PSACH; severe form. 2 Publications
VAR_007632
Natural varianti469 – 4691Missing 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. 3 Publications
VAR_007633
Natural varianti472 – 4721D → Y in PSACH; severe form. 2 Publications
VAR_007634
Natural varianti473 – 4731D → DD in EDM1. 1 Publication
VAR_066818
Natural varianti473 – 4731D → G in PSACH; severe form.
Corresponds to variant rs28936669 [ dbSNP | Ensembl ].
VAR_007635
Natural varianti473 – 4731D → H in PSACH. 1 Publication
VAR_066819
Natural varianti473 – 4731Missing in PSACH; severe form. 1 Publication
VAR_007636
Natural varianti475 – 4751D → N in PSACH. 1 Publication
VAR_066820
Natural varianti482 – 4821D → G in PSACH. 2 Publications
VAR_007637
Natural varianti501 – 5011G → D in EDM1. 1 Publication
VAR_066821
Natural varianti507 – 5071D → G in PSACH. 1 Publication
VAR_066822
Natural varianti511 – 5111D → G in PSACH. 1 Publication
VAR_066823
Natural varianti513 – 5164Missing in PSACH; mild form.
VAR_007638
Natural varianti515 – 5151D → G in PSACH. 1 Publication
VAR_066824
Natural varianti518 – 5181D → N in PSACH; mild form.
VAR_007639
Natural varianti523 – 5231N → K in EDM1; Ribbing type. 2 Publications
VAR_007640
Natural varianti529 – 5291T → I in PSACH. 1 Publication
VAR_066825
Natural varianti585 – 5851T → M in PSACH; mild form and EDM1. 2 Publications
VAR_007641
Natural varianti585 – 5851T → R in EDM1 and PSACH. 2 Publications
VAR_007642
Natural varianti718 – 7181R → P in EDM1. 1 Publication
VAR_066826
Natural varianti718 – 7181R → W in EDM1. 1 Publication
Corresponds to variant rs28936368 [ dbSNP | Ensembl ].
VAR_066827
Natural varianti719 – 7191G → D in PSACH; severe. 1 Publication
VAR_017103
Natural varianti719 – 7191G → S in PSACH. 1 Publication
VAR_066828
Natural varianti756 – 7561Q → R in a patient with multiple epiphyseal dysplasia. 1 Publication
Corresponds to variant rs61752496 [ dbSNP | Ensembl ].
VAR_066829

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei129 – 18153Missing in isoform 2.
VSP_055758Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti256 – 2561A → R in AAA57253. 1 Publication
Sequence conflicti256 – 2561A → R in BAC53888. 1 Publication
Sequence conflicti340 – 3401D → Y in AAB35270. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L32137 mRNA. Translation: AAA57253.1.
AB086984 mRNA. Translation: BAC53888.1.
AK296586 mRNA. Translation: BAG59205.1.
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.
CCDSiCCDS12385.1.
RefSeqiNP_000086.2. NM_000095.2.
UniGeneiHs.1584.

Genome annotation databases

EnsembliENST00000222271; ENSP00000222271; ENSG00000105664.
ENST00000425807; ENSP00000403792; ENSG00000105664.
GeneIDi1311.
KEGGihsa:1311.
UCSCiuc002nkd.3. human.

Polymorphism databases

DMDMi209572601.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L32137 mRNA. Translation: AAA57253.1 .
AB086984 mRNA. Translation: BAC53888.1 .
AK296586 mRNA. Translation: BAG59205.1 .
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 .
CCDSi CCDS12385.1.
RefSeqi NP_000086.2. NM_000095.2.
UniGenei Hs.1584.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3FBY X-ray 3.15 A/B/C 225-757 [» ]
ProteinModelPortali P49747.
SMRi P49747. Positions 29-72, 91-757.
ModBasei Search...

Protein-protein interaction databases

IntActi P49747. 4 interactions.
STRINGi 9606.ENSP00000222271.

PTM databases

PhosphoSitei P49747.

Polymorphism databases

DMDMi 209572601.

Proteomic databases

MaxQBi P49747.
PaxDbi P49747.
PRIDEi P49747.

Protocols and materials databases

DNASUi 1311.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000222271 ; ENSP00000222271 ; ENSG00000105664 .
ENST00000425807 ; ENSP00000403792 ; ENSG00000105664 .
GeneIDi 1311.
KEGGi hsa:1311.
UCSCi uc002nkd.3. human.

Organism-specific databases

CTDi 1311.
GeneCardsi GC19M018894.
GeneReviewsi COMP.
H-InvDB HIX0014925.
HGNCi HGNC:2227. COMP.
MIMi 132400. phenotype.
177170. phenotype.
600310. gene.
neXtProti NX_P49747.
Orphaneti 93308. Multiple epiphyseal dysplasia type 1.
750. Pseudoachondroplasia.
PharmGKBi PA26744.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000007542.
HOVERGENi HBG000636.
InParanoidi P49747.
KOi K04659.
OMAi PEDYETQ.
PhylomeDBi P49747.
TreeFami TF324917.

Enzyme and pathway databases

Reactomei REACT_13552. Integrin cell surface interactions.
REACT_163906. ECM proteoglycans.

Miscellaneous databases

ChiTaRSi COMP. human.
EvolutionaryTracei P49747.
GeneWikii Cartilage_oligomeric_matrix_protein.
GenomeRNAii 1311.
NextBioi 5361.
PMAP-CutDB P49747.
PROi P49747.
SOURCEi Search...

Gene expression databases

ArrayExpressi P49747.
Bgeei P49747.
CleanExi HS_COMP.
Genevestigatori P49747.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProi IPR028492. 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 ]
PANTHERi PTHR10199:SF81. PTHR10199:SF81. 1 hit.
Pfami PF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view ]
SMARTi SM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
[Graphical view ]
SUPFAMi SSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEi PS01186. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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] (ISOFORM 1), VARIANTS ASP-50; TRP-51; GLY-109; GLY-224 AND PRO-285.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  4. "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.
    , 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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Ovary.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.
  23. "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.
  24. "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.
  25. "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.
  26. "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.
  27. Cited for: VARIANTS EDM1 ARG-276; ALA-420 AND MET-585.
  28. "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.

Entry informationi

Entry nameiCOMP_HUMAN
AccessioniPrimary (citable) accession number: P49747
Secondary accession number(s): B4DKJ3
, O14592, Q16388, Q16389, Q2NL86, Q8N4T2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 14, 2008
Last modified: September 3, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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