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Protein

Cartilage oligomeric matrix protein

Gene

COMP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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).By similarity3 Publications

Cofactori

Ca2+Note: Binds 11-14 calcium ions per subunit.

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • collagen binding Source: UniProtKB
  • extracellular matrix structural constituent Source: ProtInc
  • heparan sulfate proteoglycan binding Source: UniProtKB
  • heparin binding Source: UniProtKB
  • protease binding Source: BHF-UCL

GO - Biological processi

  • animal organ morphogenesis Source: ProtInc
  • apoptotic process Source: UniProtKB-KW
  • cell adhesion Source: UniProtKB-KW
  • extracellular matrix organization Source: Reactome
  • growth plate cartilage development Source: Ensembl
  • limb development Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • skeletal system development Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell adhesion

Keywords - Ligandi

Calcium, Heparin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000105664-MONOMER.
ReactomeiR-HSA-216083. Integrin cell surface interactions.
R-HSA-3000178. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:2227. COMP.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Multiple epiphyseal dysplasia 1 (EDM1)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:132400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_066789167G → E in EDM1. 1 PublicationCorresponds to variant rs763887855dbSNPEnsembl.1
Natural variantiVAR_026239276P → R in EDM1. 2 Publications1
Natural variantiVAR_066792298S → L in EDM1; phenotypic features overlapping with mild PSACH. 1 Publication1
Natural variantiVAR_066793311A → D in EDM1. 1 Publication1
Natural variantiVAR_066794317D → G in EDM1; atypical form. 1 Publication1
Natural variantiVAR_066795326D → G in EDM1. 1 Publication1
Natural variantiVAR_007617342D → Y in EDM1; Fairbank type. 2 PublicationsCorresponds to variant rs137852652dbSNPEnsembl.1
Natural variantiVAR_066798348C → F in EDM1. 1 Publication1
Natural variantiVAR_007619361D → V in EDM1; Fairbank type. 1
Natural variantiVAR_007620361D → Y in EDM1; binds less calcium. 2 Publications1
Natural variantiVAR_007621367 – 368Missing in EDM1. 1 Publication2
Natural variantiVAR_007622371C → S in EDM1; Fairbank type. 2 Publications1
Natural variantiVAR_066800371C → Y in EDM1. 1 Publication1
Natural variantiVAR_066801374D → N in EDM1. 1 Publication1
Natural variantiVAR_066802376D → N in EDM1. 1 Publication1
Natural variantiVAR_066804385D → N in EDM1; atypical form. 1 Publication1
Natural variantiVAR_066805385D → Y in EDM1; atypical form. 1 Publication1
Natural variantiVAR_066806385Missing in EDM1. 1 Publication1
Natural variantiVAR_066808397D → H in EDM1. 1 Publication1
Natural variantiVAR_066810404G → R in EDM1. 1 Publication1
Natural variantiVAR_007627408D → Y in EDM1. 1 Publication1
Natural variantiVAR_066811410C → Y in EDM1; phenotype overlapping with mild PSACH. 1 Publication1
Natural variantiVAR_066812415N → K in EDM1. 1 Publication1
Natural variantiVAR_026240420D → A in EDM1. 1 Publication1
Natural variantiVAR_066813427G → E in EDM1. 1 Publication1
Natural variantiVAR_066814430 – 432CDS → LWC in EDM1. 1 Publication3
Natural variantiVAR_007630453N → S in EDM1; Fairbank type. 1 PublicationCorresponds to variant rs28936668dbSNPEnsembl.1
Natural variantiVAR_066817457Missing in EDM1. 1 Publication1
Natural variantiVAR_066818473D → DD in EDM1. 1 Publication1
Natural variantiVAR_066821501G → D in EDM1. 1 Publication1
Natural variantiVAR_007640523N → K in EDM1; Ribbing type. 2 PublicationsCorresponds to variant rs137852654dbSNPEnsembl.1
Natural variantiVAR_007641585T → M in PSACH; mild form and EDM1. 2 PublicationsCorresponds to variant rs312262900dbSNPEnsembl.1
Natural variantiVAR_007642585T → R in EDM1 and PSACH. 2 PublicationsCorresponds to variant rs312262900dbSNPEnsembl.1
Natural variantiVAR_066826718R → P in EDM1. 1 PublicationCorresponds to variant rs149551600dbSNPEnsembl.1
Natural variantiVAR_066827718R → W in EDM1. 1 PublicationCorresponds to variant rs28936368dbSNPEnsembl.1
Pseudoachondroplasia (PSACH)9 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:177170
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_066790234P → S in PSACH. 1 PublicationCorresponds to variant rs557483957dbSNPEnsembl.1
Natural variantiVAR_066791290D → G in PSACH. 1 Publication1
Natural variantiVAR_007614290D → N in PSACH; mild form. 1
Natural variantiVAR_066792298S → L in EDM1; phenotypic features overlapping with mild PSACH. 1 Publication1
Natural variantiVAR_007615299G → R in PSACH. 1 Publication1
Natural variantiVAR_066796326D → Y in PSACH. 1 Publication1
Natural variantiVAR_007616328C → R in PSACH; mild form. 2 PublicationsCorresponds to variant rs137852653dbSNPEnsembl.1
Natural variantiVAR_066797341 – 342Missing in PSACH. 1 Publication2
Natural variantiVAR_017102348C → R in PSACH. 1 PublicationCorresponds to variant rs137852656dbSNPEnsembl.1
Natural variantiVAR_007618349D → V in PSACH; mild form. 1
Natural variantiVAR_066799350 – 372Missing in PSACH. 1 PublicationAdd BLAST23
Natural variantiVAR_007623372Missing in PSACH. 1 Publication1
Natural variantiVAR_007624374Missing in PSACH; mild form. 1
Natural variantiVAR_066803378D → V in PSACH. 1 Publication1
Natural variantiVAR_007625387C → G in PSACH; mild form. 1
Natural variantiVAR_066807387C → R in PSACH. 1 Publication1
Natural variantiVAR_007626391 – 394PNSD → V in PSACH. 1 Publication4
Natural variantiVAR_066809402 – 404GIG → VC in PSACH. 1 Publication3
Natural variantiVAR_066811410C → Y in EDM1; phenotype overlapping with mild PSACH. 1 Publication1
Natural variantiVAR_007628440G → E in PSACH; mild form. 1
Natural variantiVAR_007629440G → R in PSACH. 2 Publications1
Natural variantiVAR_066815446D → N in PSACH. 1 Publication1
Natural variantiVAR_066816448C → S in PSACH. 1 Publication1
Natural variantiVAR_007631459Missing in PSACH; severe form. 2 Publications1
Natural variantiVAR_007632468C → Y in PSACH; severe form. 2 PublicationsCorresponds to variant rs137852651dbSNPEnsembl.1
Natural variantiVAR_007633469Missing 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 Publications1
Natural variantiVAR_007634472D → Y in PSACH; severe form. 2 PublicationsCorresponds to variant rs137852650dbSNPEnsembl.1
Natural variantiVAR_007635473D → G in PSACH; severe form. Corresponds to variant rs28936669dbSNPEnsembl.1
Natural variantiVAR_066819473D → H in PSACH. 1 Publication1
Natural variantiVAR_007636473Missing in PSACH; severe form. 1 Publication1
Natural variantiVAR_066820475D → N in PSACH. 1 Publication1
Natural variantiVAR_007637482D → G in PSACH. 2 Publications1
Natural variantiVAR_066822507D → G in PSACH. 1 Publication1
Natural variantiVAR_066823511D → G in PSACH. 1 Publication1
Natural variantiVAR_007638513 – 516Missing in PSACH; mild form. 1 Publication4
Natural variantiVAR_066824515D → G in PSACH. 1 Publication1
Natural variantiVAR_007639518D → N in PSACH; mild form. 1
Natural variantiVAR_066825529T → I in PSACH. 1 PublicationCorresponds to variant rs312262903dbSNPEnsembl.1
Natural variantiVAR_007641585T → M in PSACH; mild form and EDM1. 2 PublicationsCorresponds to variant rs312262900dbSNPEnsembl.1
Natural variantiVAR_007642585T → R in EDM1 and PSACH. 2 PublicationsCorresponds to variant rs312262900dbSNPEnsembl.1
Natural variantiVAR_017103719G → D in PSACH; severe. 1 PublicationCorresponds to variant rs137852655dbSNPEnsembl.1
Natural variantiVAR_066828719G → S in PSACH. 1 PublicationCorresponds to variant rs312262904dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi1311.
MalaCardsiCOMP.
MIMi132400. phenotype.
177170. phenotype.
OpenTargetsiENSG00000105664.
Orphaneti93308. Multiple epiphyseal dysplasia type 1.
750. Pseudoachondroplasia.
PharmGKBiPA26744.

Polymorphism and mutation databases

BioMutaiCOMP.
DMDMi209572601.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000003585721 – 757Cartilage oligomeric matrix proteinAdd BLAST737

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi69Interchain1 Publication
Disulfide bondi72Interchain1 Publication
Disulfide bondi91 ↔ 102PROSITE-ProRule annotation
Disulfide bondi96 ↔ 111PROSITE-ProRule annotation
Disulfide bondi114 ↔ 125PROSITE-ProRule annotation
Glycosylationi121N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi131 ↔ 142PROSITE-ProRule annotation
Disulfide bondi136 ↔ 151PROSITE-ProRule annotation
Disulfide bondi154 ↔ 178PROSITE-ProRule annotation
Disulfide bondi184 ↔ 197PROSITE-ProRule annotation
Disulfide bondi191 ↔ 206PROSITE-ProRule annotation
Disulfide bondi209 ↔ 221PROSITE-ProRule annotation
Disulfide bondi229 ↔ 243PROSITE-ProRule annotation1 Publication
Disulfide bondi237 ↔ 253PROSITE-ProRule annotation1 Publication
Disulfide bondi255 ↔ 266PROSITE-ProRule annotation1 Publication
Disulfide bondi282 ↔ 287PROSITE-ProRule annotation1 Publication
Disulfide bondi292 ↔ 312PROSITE-ProRule annotation1 Publication
Disulfide bondi328 ↔ 348PROSITE-ProRule annotation1 Publication
Disulfide bondi351 ↔ 371PROSITE-ProRule annotation1 Publication
Disulfide bondi387 ↔ 407PROSITE-ProRule annotation1 Publication
Disulfide bondi410 ↔ 430PROSITE-ProRule annotation1 Publication
Disulfide bondi448 ↔ 468PROSITE-ProRule annotation1 Publication
Disulfide bondi484 ↔ 504PROSITE-ProRule annotation1 Publication
Disulfide bondi520 ↔ 741PROSITE-ProRule annotation1 Publication
Glycosylationi742N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP49747.
PeptideAtlasiP49747.
PRIDEiP49747.

PTM databases

PhosphoSitePlusiP49747.

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

BgeeiENSG00000105664.
CleanExiHS_COMP.
ExpressionAtlasiP49747. baseline and differential.
GenevisibleiP49747. HS.

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ACANP136082EBI-2531022,EBI-6259246From a different organism.
ADAMTS12P583973EBI-2531022,EBI-9028051
OTX1P322425EBI-2531022,EBI-740446

GO - Molecular functioni

  • collagen binding Source: UniProtKB
  • protease binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi107706. 1 interactor.
IntActiP49747. 11 interactors.
STRINGi9606.ENSP00000222271.

Structurei

Secondary structure

1757
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi232 – 234Combined sources3
Beta strandi241 – 245Combined sources5
Beta strandi251 – 255Combined sources5
Beta strandi259 – 265Combined sources7
Beta strandi272 – 274Combined sources3
Helixi285 – 287Combined sources3
Beta strandi291 – 295Combined sources5
Beta strandi306 – 308Combined sources3
Helixi310 – 312Combined sources3
Turni314 – 317Combined sources4
Beta strandi319 – 321Combined sources3
Helixi323 – 325Combined sources3
Beta strandi327 – 331Combined sources5
Beta strandi342 – 344Combined sources3
Helixi346 – 348Combined sources3
Beta strandi364 – 367Combined sources4
Helixi369 – 371Combined sources3
Beta strandi378 – 380Combined sources3
Beta strandi401 – 403Combined sources3
Helixi405 – 407Combined sources3
Beta strandi424 – 426Combined sources3
Turni428 – 430Combined sources3
Helixi443 – 445Combined sources3
Beta strandi462 – 464Combined sources3
Turni466 – 468Combined sources3
Beta strandi470 – 473Combined sources4
Beta strandi475 – 477Combined sources3
Helixi479 – 481Combined sources3
Beta strandi495 – 500Combined sources6
Turni503 – 506Combined sources4
Beta strandi511 – 513Combined sources3
Helixi515 – 517Combined sources3
Beta strandi532 – 540Combined sources9
Beta strandi551 – 553Combined sources3
Turni555 – 557Combined sources3
Beta strandi560 – 562Combined sources3
Beta strandi567 – 588Combined sources22
Beta strandi596 – 605Combined sources10
Beta strandi608 – 617Combined sources10
Beta strandi625 – 627Combined sources3
Beta strandi636 – 641Combined sources6
Helixi648 – 655Combined sources8
Beta strandi656 – 658Combined sources3
Turni661 – 663Combined sources3
Beta strandi664 – 669Combined sources6
Beta strandi681 – 689Combined sources9
Helixi690 – 692Combined sources3
Beta strandi694 – 701Combined sources8
Beta strandi704 – 708Combined sources5
Beta strandi716 – 728Combined sources13
Beta strandi732 – 741Combined sources10
Helixi748 – 754Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FBYX-ray3.15A/B/C225-757[»]
ProteinModelPortaliP49747.
SMRiP49747.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49747.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini87 – 126EGF-like 1PROSITE-ProRule annotationAdd BLAST40
Domaini127 – 179EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST53
Domaini180 – 222EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini225 – 267EGF-like 4PROSITE-ProRule annotationAdd BLAST43
Repeati268 – 300TSP type-3 1Add BLAST33
Repeati301 – 336TSP type-3 2Add BLAST36
Repeati337 – 359TSP type-3 3Add BLAST23
Repeati360 – 395TSP type-3 4Add BLAST36
Repeati396 – 418TSP type-3 5Add BLAST23
Repeati419 – 456TSP type-3 6Add BLAST38
Repeati457 – 492TSP type-3 7Add BLAST36
Repeati493 – 528TSP type-3 8Add BLAST36
Domaini532 – 746TSP C-terminalPROSITE-ProRule annotationAdd BLAST215

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 86COMP N-terminalAdd BLAST65
Regioni527 – 757Mediates cell survival and induction of the IAP family of survival proteinsAdd BLAST231

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi367 – 369Cell attachment siteSequence analysis3

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.Curated
Contains 4 EGF-like domains.PROSITE-ProRule annotation
Contains 1 TSP C-terminal (TSPC) domain.PROSITE-ProRule annotation
Contains 8 TSP type-3 repeats.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IFQQ. Eukaryota.
ENOG410XQKE. LUCA.
GeneTreeiENSGT00850000132273.
HOGENOMiHOG000007542.
HOVERGENiHBG000636.
InParanoidiP49747.
KOiK04659.
OMAiDVDHDFV.
OrthoDBiEOG091G00TV.
PhylomeDBiP49747.
TreeFamiTF324917.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR024665. Thbs/COMP_coiled-coil.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR028974. TSP_type-3_rpt.
[Graphical view]
PfamiPF11598. COMP. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 3 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. AlignAdd to basket

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

        10         20         30         40         50
MVPDTACVLL LTLAALGASG QGQSPLGSDL GPQMLRELQE TNAALQDVRE
60 70 80 90 100
LLRQQVREIT FLKNTVMECD ACGMQQSVRT GLPSVRPLLH CAPGFCFPGV
110 120 130 140 150
ACIQTESGAR CGPCPAGFTG NGSHCTDVNE CNAHPCFPRV RCINTSPGFR
160 170 180 190 200
CEACPPGYSG PTHQGVGLAF AKANKQVCTD INECETGQHN CVPNSVCINT
210 220 230 240 250
RGSFQCGPCQ PGFVGDQASG CQRRAQRFCP DGSPSECHEH ADCVLERDGS
260 270 280 290 300
RSCVCAVGWA GNGILCGRDT DLDGFPDEKL RCPERQCRKD NCVTVPNSGQ
310 320 330 340 350
EDVDRDGIGD ACDPDADGDG VPNEKDNCPL VRNPDQRNTD EDKWGDACDN
360 370 380 390 400
CRSQKNDDQK DTDQDGRGDA CDDDIDGDRI RNQADNCPRV PNSDQKDSDG
410 420 430 440 450
DGIGDACDNC PQKSNPDQAD VDHDFVGDAC DSDQDQDGDG HQDSRDNCPT
460 470 480 490 500
VPNSAQEDSD HDGQGDACDD DDDNDGVPDS RDNCRLVPNP GQEDADRDGV
510 520 530 540 550
GDVCQDDFDA DKVVDKIDVC PENAEVTLTD FRAFQTVVLD PEGDAQIDPN
560 570 580 590 600
WVVLNQGREI VQTMNSDPGL AVGYTAFNGV DFEGTFHVNT VTDDDYAGFI
610 620 630 640 650
FGYQDSSSFY VVMWKQMEQT YWQANPFRAV AEPGIQLKAV KSSTGPGEQL
660 670 680 690 700
RNALWHTGDT ESQVRLLWKD PRNVGWKDKK SYRWFLQHRP QVGYIRVRFY
710 720 730 740 750
EGPELVADSN VVLDTTMRGG RLGVFCFSQE NIIWANLRYR CNDTIPEDYE

THQLRQA
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 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti256A → R in AAA57253 (PubMed:7713493).Curated1
Sequence conflicti256A → R in BAC53888 (Ref. 2) Curated1
Sequence conflicti340D → Y in AAB35270 (PubMed:7670472).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01625450E → D.2 Publications1
Natural variantiVAR_01625551L → W.2 Publications1
Natural variantiVAR_016257109A → G.2 Publications1
Natural variantiVAR_066789167G → E in EDM1. 1 PublicationCorresponds to variant rs763887855dbSNPEnsembl.1
Natural variantiVAR_016258224R → G.2 Publications1
Natural variantiVAR_066790234P → S in PSACH. 1 PublicationCorresponds to variant rs557483957dbSNPEnsembl.1
Natural variantiVAR_026239276P → R in EDM1. 2 Publications1
Natural variantiVAR_016261285R → P.2 Publications1
Natural variantiVAR_066791290D → G in PSACH. 1 Publication1
Natural variantiVAR_007614290D → N in PSACH; mild form. 1
Natural variantiVAR_066792298S → L in EDM1; phenotypic features overlapping with mild PSACH. 1 Publication1
Natural variantiVAR_007615299G → R in PSACH. 1 Publication1
Natural variantiVAR_066793311A → D in EDM1. 1 Publication1
Natural variantiVAR_066794317D → G in EDM1; atypical form. 1 Publication1
Natural variantiVAR_066795326D → G in EDM1. 1 Publication1
Natural variantiVAR_066796326D → Y in PSACH. 1 Publication1
Natural variantiVAR_007616328C → R in PSACH; mild form. 2 PublicationsCorresponds to variant rs137852653dbSNPEnsembl.1
Natural variantiVAR_066797341 – 342Missing in PSACH. 1 Publication2
Natural variantiVAR_007617342D → Y in EDM1; Fairbank type. 2 PublicationsCorresponds to variant rs137852652dbSNPEnsembl.1
Natural variantiVAR_066798348C → F in EDM1. 1 Publication1
Natural variantiVAR_017102348C → R in PSACH. 1 PublicationCorresponds to variant rs137852656dbSNPEnsembl.1
Natural variantiVAR_007618349D → V in PSACH; mild form. 1
Natural variantiVAR_066799350 – 372Missing in PSACH. 1 PublicationAdd BLAST23
Natural variantiVAR_007619361D → V in EDM1; Fairbank type. 1
Natural variantiVAR_007620361D → Y in EDM1; binds less calcium. 2 Publications1
Natural variantiVAR_007621367 – 368Missing in EDM1. 1 Publication2
Natural variantiVAR_007622371C → S in EDM1; Fairbank type. 2 Publications1
Natural variantiVAR_066800371C → Y in EDM1. 1 Publication1
Natural variantiVAR_007623372Missing in PSACH. 1 Publication1
Natural variantiVAR_066801374D → N in EDM1. 1 Publication1
Natural variantiVAR_007624374Missing in PSACH; mild form. 1
Natural variantiVAR_066802376D → N in EDM1. 1 Publication1
Natural variantiVAR_066803378D → V in PSACH. 1 Publication1
Natural variantiVAR_046796381R → C.Corresponds to variant rs3179763dbSNPEnsembl.1
Natural variantiVAR_066804385D → N in EDM1; atypical form. 1 Publication1
Natural variantiVAR_066805385D → Y in EDM1; atypical form. 1 Publication1
Natural variantiVAR_066806385Missing in EDM1. 1 Publication1
Natural variantiVAR_007625387C → G in PSACH; mild form. 1
Natural variantiVAR_066807387C → R in PSACH. 1 Publication1
Natural variantiVAR_007626391 – 394PNSD → V in PSACH. 1 Publication4
Natural variantiVAR_066808397D → H in EDM1. 1 Publication1
Natural variantiVAR_066809402 – 404GIG → VC in PSACH. 1 Publication3
Natural variantiVAR_066810404G → R in EDM1. 1 Publication1
Natural variantiVAR_007627408D → Y in EDM1. 1 Publication1
Natural variantiVAR_066811410C → Y in EDM1; phenotype overlapping with mild PSACH. 1 Publication1
Natural variantiVAR_066812415N → K in EDM1. 1 Publication1
Natural variantiVAR_026240420D → A in EDM1. 1 Publication1
Natural variantiVAR_066813427G → E in EDM1. 1 Publication1
Natural variantiVAR_066814430 – 432CDS → LWC in EDM1. 1 Publication3
Natural variantiVAR_007628440G → E in PSACH; mild form. 1
Natural variantiVAR_007629440G → R in PSACH. 2 Publications1
Natural variantiVAR_066815446D → N in PSACH. 1 Publication1
Natural variantiVAR_066816448C → S in PSACH. 1 Publication1
Natural variantiVAR_007630453N → S in EDM1; Fairbank type. 1 PublicationCorresponds to variant rs28936668dbSNPEnsembl.1
Natural variantiVAR_066817457Missing in EDM1. 1 Publication1
Natural variantiVAR_007631459Missing in PSACH; severe form. 2 Publications1
Natural variantiVAR_007632468C → Y in PSACH; severe form. 2 PublicationsCorresponds to variant rs137852651dbSNPEnsembl.1
Natural variantiVAR_007633469Missing 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 Publications1
Natural variantiVAR_007634472D → Y in PSACH; severe form. 2 PublicationsCorresponds to variant rs137852650dbSNPEnsembl.1
Natural variantiVAR_066818473D → DD in EDM1. 1 Publication1
Natural variantiVAR_007635473D → G in PSACH; severe form. Corresponds to variant rs28936669dbSNPEnsembl.1
Natural variantiVAR_066819473D → H in PSACH. 1 Publication1
Natural variantiVAR_007636473Missing in PSACH; severe form. 1 Publication1
Natural variantiVAR_066820475D → N in PSACH. 1 Publication1
Natural variantiVAR_007637482D → G in PSACH. 2 Publications1
Natural variantiVAR_066821501G → D in EDM1. 1 Publication1
Natural variantiVAR_066822507D → G in PSACH. 1 Publication1
Natural variantiVAR_066823511D → G in PSACH. 1 Publication1
Natural variantiVAR_007638513 – 516Missing in PSACH; mild form. 1 Publication4
Natural variantiVAR_066824515D → G in PSACH. 1 Publication1
Natural variantiVAR_007639518D → N in PSACH; mild form. 1
Natural variantiVAR_007640523N → K in EDM1; Ribbing type. 2 PublicationsCorresponds to variant rs137852654dbSNPEnsembl.1
Natural variantiVAR_066825529T → I in PSACH. 1 PublicationCorresponds to variant rs312262903dbSNPEnsembl.1
Natural variantiVAR_007641585T → M in PSACH; mild form and EDM1. 2 PublicationsCorresponds to variant rs312262900dbSNPEnsembl.1
Natural variantiVAR_007642585T → R in EDM1 and PSACH. 2 PublicationsCorresponds to variant rs312262900dbSNPEnsembl.1
Natural variantiVAR_066826718R → P in EDM1. 1 PublicationCorresponds to variant rs149551600dbSNPEnsembl.1
Natural variantiVAR_066827718R → W in EDM1. 1 PublicationCorresponds to variant rs28936368dbSNPEnsembl.1
Natural variantiVAR_017103719G → D in PSACH; severe. 1 PublicationCorresponds to variant rs137852655dbSNPEnsembl.1
Natural variantiVAR_066828719G → S in PSACH. 1 Publication