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P16112 (PGCA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 165. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aggrecan core protein
Alternative name(s):
Cartilage-specific proteoglycan core protein
Short name=CSPCP
Chondroitin sulfate proteoglycan core protein 1
Short name=Chondroitin sulfate proteoglycan 1

Cleaved into the following chain:

  1. Aggrecan core protein 2
Gene names
Name:ACAN
Synonyms:AGC1, CSPG1, MSK16
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region.

Subunit structure

Interacts with FBLN1 By similarity. Interacts with COMP. Ref.11

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Restricted to cartilages. Ref.4

Developmental stage

Expression was detected in chondrocytes throughout the developing skeleton.

Domain

Two globular domains, G1 and G2, comprise the N-terminus of the proteoglycan, while another globular region, G3, makes up the C-terminus. G1 contains Link domains and thus consists of three disulfide-bonded loop structures designated as the A, B, B' motifs. G2 is similar to G1. The keratan sulfate (KS) and the chondroitin sulfate (CS) attachment domains lie between G2 and G3.

Post-translational modification

Contains mostly chondroitin sulfate, but also keratan sulfate chains, N-linked and O-linked oligosaccharides. The release of aggrecan fragments from articular cartilage into the synovial fluid at all stages of human osteoarthritis is the result of cleavage by aggrecanase.

Involvement in disease

Spondyloepiphyseal dysplasia type Kimberley (SEDK) [MIM:608361]: Spondyloepiphyseal dysplasias are a heterogeneous group of congenital chondrodysplasias that specifically affect epiphyses and vertebrae. The autosomal dominant SEDK is associated with premature degenerative arthropathy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Spondyloepimetaphyseal dysplasia aggrecan type (SEMD-ACAN) [MIM:612813]: A bone disease characterized by severe short stature, macrocephaly, severe midface hypoplasia, short neck, barrel chest and brachydactyly. The radiological findings comprise long bones with generalized irregular epiphyses with widened metaphyses, especially at the knees, platyspondyly, and multiple cervical-vertebral clefts.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Osteochondritis dissecans short stature and early-onset osteoarthritis (OD) [MIM:165800]: A type of osteochondritis defined as a separation of cartilage and subchondral bone from the surrounding tissue, primarily affecting the knee, ankle and elbow joints. It is clinically characterized by multiple osteochondritic lesions in knees and/or hips and/or elbows, disproportionate short stature and early-onset osteoarthritis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

Belongs to the aggrecan/versican proteoglycan family.

Contains 1 C-type lectin domain.

Contains 1 EGF-like domain.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Contains 4 Link domains.

Contains 1 Sushi (CCP/SCR) domain.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Dwarfism
   DomainEGF-like domain
Immunoglobulin domain
Repeat
Signal
Sushi
   LigandCalcium
Lectin
Metal-binding
   PTMDisulfide bond
Glycoprotein
Proteoglycan
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cell adhesion

Inferred from electronic annotation. Source: InterPro

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

keratan sulfate biosynthetic process

Traceable author statement. Source: Reactome

keratan sulfate catabolic process

Traceable author statement. Source: Reactome

keratan sulfate metabolic process

Traceable author statement. Source: Reactome

proteolysis

Non-traceable author statement Ref.3. Source: UniProtKB

skeletal system development

Non-traceable author statement Ref.3. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

lysosomal lumen

Traceable author statement. Source: Reactome

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

extracellular matrix structural constituent

Traceable author statement Ref.3. Source: UniProtKB

hyaluronic acid binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.11. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P16112-1)

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.
Isoform 2 (identifier: P16112-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2163-2200: Missing.
Isoform 3 (identifier: P16112-3)

The sequence of this isoform differs from the canonical sequence as follows:
     2163-2200: Missing.
     2330-2390: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.2
Chain17 – 24152399Aggrecan core protein
PRO_0000017505
Chain393 – 24152023Aggrecan core protein 2
PRO_0000017506

Regions

Domain34 – 147114Ig-like V-type
Domain153 – 24896Link 1
Domain254 – 35097Link 2
Domain478 – 57396Link 3
Domain579 – 67496Link 4
Repeat772 – 77761-1
Repeat778 – 78361-2
Repeat784 – 78961-3
Repeat790 – 79561-4
Repeat796 – 80161-5
Repeat802 – 80761-6
Repeat808 – 81361-7; approximate
Repeat814 – 81961-8; approximate
Repeat820 – 82561-9
Repeat826 – 83161-10; approximate
Repeat832 – 83761-11
Repeat838 – 84361-12
Repeat941 – 959192-1
Repeat960 – 978192-2
Repeat979 – 997192-3
Repeat998 – 1016192-4
Repeat1017 – 1035192-5
Repeat1036 – 1054192-6
Repeat1055 – 1073192-7
Repeat1074 – 1092192-8
Repeat1093 – 1111192-9
Repeat1112 – 1130192-10
Repeat1131 – 1149192-11
Repeat1150 – 1168192-12
Repeat1169 – 1187192-13
Repeat1188 – 1206192-14
Repeat1207 – 1225192-15
Repeat1226 – 1244192-16
Repeat1245 – 1263192-17
Repeat1264 – 1282192-18
Repeat1283 – 1301192-19
Repeat1302 – 1320192-20
Repeat1321 – 1339192-21
Repeat1340 – 1358192-22
Repeat1360 – 1378192-23
Repeat1379 – 1397192-24
Repeat1398 – 1416192-25
Repeat1418 – 1436192-26
Repeat1439 – 1457192-27; approximate
Repeat1459 – 1477192-28
Repeat1479 – 1497192-29
Domain2164 – 219936EGF-like
Domain2201 – 2327127C-type lectin
Domain2330 – 239061Sushi
Region48 – 14194G1-A
Region152 – 24796G1-B
Region253 – 34997G1-B'
Region477 – 57195G2-B
Region578 – 67295G2-B'
Region676 – 848173KS
Region772 – 8437212 X 6 AA approximate tandem repeats of E-[GVE]-P-[SFY]-[APT]-[TSP]
Region851 – 1497647CS-1
Region941 – 149755729 X 19 AA approximate tandem repeats of E-[IVDG]-[LV]-[EV]-[GTI]-[STA]-[ATV]-[SP]-[GA]-[VIFAD]-[GEDL]-[DE]-[LVI]-[SG]-[GERK]-[LV]-P-S-G
Region1498 – 2162665CS-2
Region2163 – 2415253G3

Sites

Metal binding22661Calcium 1 By similarity
Metal binding22701Calcium 1 By similarity
Metal binding22701Calcium 3 By similarity
Metal binding22901Calcium 2 By similarity
Metal binding22921Calcium 2 By similarity
Metal binding22931Calcium 1 By similarity
Metal binding22991Calcium 1; via carbonyl oxygen By similarity
Metal binding22991Calcium 2 By similarity
Metal binding23001Calcium 1 By similarity
Metal binding23001Calcium 3 By similarity
Metal binding23131Calcium 2 By similarity
Metal binding23141Calcium 2 By similarity
Metal binding23141Calcium 2; via carbonyl oxygen By similarity
Site392 – 3932Cleavage; by aggrecanase

Amino acid modifications

Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential
Glycosylation3711O-linked (Xyl...) (keratan sulfate) Probable
Glycosylation3761O-linked (Xyl...) (keratan sulfate) Probable
Glycosylation3871N-linked (GlcNAc...) Potential
Glycosylation4341N-linked (GlcNAc...) Potential
Glycosylation6021N-linked (GlcNAc...) Potential
Glycosylation6571N-linked (GlcNAc...) Ref.10
Glycosylation7371N-linked (GlcNAc...) Potential
Glycosylation18981N-linked (GlcNAc...) Potential
Disulfide bond51 ↔ 133 By similarity
Disulfide bond175 ↔ 246 By similarity
Disulfide bond199 ↔ 220 By similarity
Disulfide bond273 ↔ 348 By similarity
Disulfide bond297 ↔ 318 By similarity
Disulfide bond500 ↔ 571 By similarity
Disulfide bond524 ↔ 545 By similarity
Disulfide bond598 ↔ 672 By similarity
Disulfide bond621 ↔ 642 By similarity
Disulfide bond2168 ↔ 2178 By similarity
Disulfide bond2173 ↔ 2187 By similarity
Disulfide bond2189 ↔ 2198 By similarity
Disulfide bond2205 ↔ 2216 By similarity
Disulfide bond2233 ↔ 2325 By similarity
Disulfide bond2301 ↔ 2317 By similarity
Disulfide bond2332 ↔ 2375 By similarity
Disulfide bond2361 ↔ 2388 By similarity

Natural variations

Alternative sequence2163 – 220038Missing in isoform 2 and isoform 3.
VSP_003074
Alternative sequence2330 – 239061Missing in isoform 3.
VSP_003075
Natural variant1021D → E.
Corresponds to variant rs16942318 [ dbSNP | Ensembl ].
VAR_056152
Natural variant2751R → Q.
Corresponds to variant rs34949187 [ dbSNP | Ensembl ].
VAR_056153
Natural variant19431P → L.
Corresponds to variant rs35061438 [ dbSNP | Ensembl ].
VAR_056154
Natural variant20051S → R.
Corresponds to variant rs34153007 [ dbSNP | Ensembl ].
VAR_056155
Natural variant22661D → N in SEMD-ACAN; creates a functional N-glycosylation site; does not adversely affect protein trafficking and secretion. Ref.12
VAR_063053
Natural variant23031V → M in OD. Ref.13
VAR_063765

Experimental info

Sequence conflict7661E → A in AAC60643. Ref.6
Sequence conflict8471E → V in AAC60643. Ref.6
Sequence conflict19281E → A in CAA35463. Ref.7
Sequence conflict19641I → V in CAA35463. Ref.7
Sequence conflict19641I → V in AAA35726. Ref.8
Sequence conflict20701P → A in AAA35726. Ref.8
Sequence conflict23911A → P in CAA35463. Ref.7
Sequence conflict23911A → P in AAA35726. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: 1288937E1B98C6B6

FASTA2,415250,193
        10         20         30         40         50         60 
MTTLLWVFVT LRVITAAVTV ETSDHDNSLS VSIPQPSPLR VLLGTSLTIP CYFIDPMHPV 

        70         80         90        100        110        120 
TTAPSTAPLA PRIKWSRVSK EKEVVLLVAT EGRVRVNSAY QDKVSLPNYP AIPSDATLEV 

       130        140        150        160        170        180 
QSLRSNDSGV YRCEVMHGIE DSEATLEVVV KGIVFHYRAI STRYTLDFDR AQRACLQNSA 

       190        200        210        220        230        240 
IIATPEQLQA AYEDGFHQCD AGWLADQTVR YPIHTPREGC YGDKDEFPGV RTYGIRDTNE 

       250        260        270        280        290        300 
TYDVYCFAEE MEGEVFYATS PEKFTFQEAA NECRRLGARL ATTGHVYLAW QAGMDMCSAG 

       310        320        330        340        350        360 
WLADRSVRYP ISKARPNCGG NLLGVRTVYV HANQTGYPDP SSRYDAICYT GEDFVDIPEN 

       370        380        390        400        410        420 
FFGVGGEEDI TVQTVTWPDM ELPLPRNITE GEARGSVILT VKPIFEVSPS PLEPEEPFTF 

       430        440        450        460        470        480 
APEIGATAFA EVENETGEAT RPWGFPTPGL GPATAFTSED LVVQVTAVPG QPHLPGGVVF 

       490        500        510        520        530        540 
HYRPGPTRYS LTFEEAQQAC PGTGAVIASP EQLQAAYEAG YEQCDAGWLR DQTVRYPIVS 

       550        560        570        580        590        600 
PRTPCVGDKD SSPGVRTYGV RPSTETYDVY CFVDRLEGEV FFATRLEQFT FQEALEFCES 

       610        620        630        640        650        660 
HNATATTGQL YAAWSRGLDK CYAGWLADGS LRYPIVTPRP ACGGDKPGVR TVYLYPNQTG 

       670        680        690        700        710        720 
LPDPLSRHHA FCFRGISAVP SPGEEEGGTP TSPSGVEEWI VTQVVPGVAA VPVEEETTAV 

       730        740        750        760        770        780 
PSGETTAILE FTTEPENQTE WEPAYTPVGT SPLPGILPTW PPTGAETEES TEGPSATEVP 

       790        800        810        820        830        840 
SASEEPSPSE VPFPSEEPSP SEEPFPSVRP FPSVELFPSE EPFPSKEPSP SEEPSASEEP 

       850        860        870        880        890        900 
YTPSPPEPSW TELPSSGEES GAPDVSGDFT GSGDVSGHLD FSGQLSGDRA SGLPSGDLDS 

       910        920        930        940        950        960 
SGLTSTVGSG LTVESGLPSG DEERIEWPST PTVGELPSGA EILEGSASGV GDLSGLPSGE 

       970        980        990       1000       1010       1020 
VLETSASGVG DLSGLPSGEV LETTAPGVED ISGLPSGEVL ETTAPGVEDI SGLPSGEVLE 

      1030       1040       1050       1060       1070       1080 
TTAPGVEDIS GLPSGEVLET TAPGVEDISG LPSGEVLETT APGVEDISGL PSGEVLETAA 

      1090       1100       1110       1120       1130       1140 
PGVEDISGLP SGEVLETAAP GVEDISGLPS GEVLETAAPG VEDISGLPSG EVLETAAPGV 

      1150       1160       1170       1180       1190       1200 
EDISGLPSGE VLETAAPGVE DISGLPSGEV LETAAPGVED ISGLPSGEVL ETAAPGVEDI 

      1210       1220       1230       1240       1250       1260 
SGLPSGEVLE TAAPGVEDIS GLPSGEVLET AAPGVEDISG LPSGEVLETA APGVEDISGL 

      1270       1280       1290       1300       1310       1320 
PSGEVLETAA PGVEDISGLP SGEVLETTAP GVEEISGLPS GEVLETTAPG VDEISGLPSG 

      1330       1340       1350       1360       1370       1380 
EVLETTAPGV EEISGLPSGE VLETSTSAVG DLSGLPSGGE VLEISVSGVE DISGLPSGEV 

      1390       1400       1410       1420       1430       1440 
VETSASGIED VSELPSGEGL ETSASGVEDL SRLPSGEEVL EISASGFGDL SGVPSGGEGL 

      1450       1460       1470       1480       1490       1500 
ETSASEVGTD LSGLPSGREG LETSASGAED LSGLPSGKED LVGSASGDLD LGKLPSGTLG 

      1510       1520       1530       1540       1550       1560 
SGQAPETSGL PSGFSGEYSG VDLGSGPPSG LPDFSGLPSG FPTVSLVDST LVEVVTASTA 

      1570       1580       1590       1600       1610       1620 
SELEGRGTIG ISGAGEISGL PSSELDISGR ASGLPSGTEL SGQASGSPDV SGEIPGLFGV 

      1630       1640       1650       1660       1670       1680 
SGQPSGFPDT SGETSGVTEL SGLSSGQPGV SGEASGVLYG TSQPFGITDL SGETSGVPDL 

      1690       1700       1710       1720       1730       1740 
SGQPSGLPGF SGATSGVPDL VSGTTSGSGE SSGITFVDTS LVEVAPTTFK EEEGLGSVEL 

      1750       1760       1770       1780       1790       1800 
SGLPSGEADL SGKSGMVDVS GQFSGTVDSS GFTSQTPEFS GLPSGIAEVS GESSRAEIGS 

      1810       1820       1830       1840       1850       1860 
SLPSGAYYGS GTPSSFPTVS LVDRTLVESV TQAPTAQEAG EGPSGILELS GAHSGAPDMS 

      1870       1880       1890       1900       1910       1920 
GEHSGFLDLS GLQSGLIEPS GEPPGTPYFS GDFASTTNVS GESSVAMGTS GEASGLPEVT 

      1930       1940       1950       1960       1970       1980 
LITSEFVEGV TEPTISQELG QRPPVTHTPQ LFESSGKVST AGDISGATPV LPGSGVEVSS 

      1990       2000       2010       2020       2030       2040 
VPESSSETSA YPEAGFGASA APEASREDSG SPDLSETTSA FHEANLERSS GLGVSGSTLT 

      2050       2060       2070       2080       2090       2100 
FQEGEASAAP EVSGESTTTS DVGTEAPGLP SATPTASGDR TEISGDLSGH TSQLGVVIST 

      2110       2120       2130       2140       2150       2160 
SIPESEWTQQ TQRPAETHLE IESSSLLYSG EETHTVETAT SPTDASIPAS PEWKRESEST 

      2170       2180       2190       2200       2210       2220 
AAAPARSCAE EPCGAGTCKE TEGHVICLCP PGYTGEHCNI DQEVCEEGWN KYQGHCYRHF 

      2230       2240       2250       2260       2270       2280 
PDRETWVDAE RRCREQQSHL SSIVTPEEQE FVNNNAQDYQ WIGLNDRTIE GDFRWSDGHP 

      2290       2300       2310       2320       2330       2340 
MQFENWRPNQ PDNFFAAGED CVVMIWHEKG EWNDVPCNYH LPFTCKKGTV ACGEPPVVEH 

      2350       2360       2370       2380       2390       2400 
ARTFGQKKDR YEINSLVRYQ CTEGFVQRHM PTIRCQPSGH WEEPRITCTD ATTYKRRLQK 

      2410 
RSSRHPRRSR PSTAH 

« Hide

Isoform 2 [UniParc].

Checksum: CC3F3E0D74B00DAD
Show »

FASTA2,377246,306
Isoform 3 [UniParc].

Checksum: 44ABD9AF85CC3612
Show »

FASTA2,316239,235

References

« Hide 'large scale' references
[1]"Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. Human-specific repeats, and additional alternatively spliced forms."
Doege K.J., Sasaki M., Kimura T., Yamada Y.
J. Biol. Chem. 266:894-902(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Chondrocyte.
[2]"Catabolism of aggrecan by explant cultures of human articular cartilage in the presence of retinoic acid."
Ilic M.Z., Mok M.T., Williamson O.D., Campbell M.A., Hughes C.E., Handley C.J.
Arch. Biochem. Biophys. 322:22-30(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-27 AND 393-403, PROTEOLYTIC PROCESSING BY AGGRECANASE.
[3]"The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain."
Sandy J.D., Flannery C.R., Neame P.J., Lohmander L.S.
J. Clin. Invest. 89:1512-1516(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 361-373 AND 393-409, PROTEOLYTIC PROCESSING, GLYCOSYLATION AT THR-371 AND THR-376.
[4]"Analysis of aggrecan and tenascin gene expression in mouse skeletal tissues by northern and in situ hybridization using species specific cDNA probes."
Glumoff V., Savontaus M., Vehanen J., Vuorio E.
Biochim. Biophys. Acta 1219:613-622(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 380-497, TISSUE SPECIFICITY.
[5]"The structure of aggrecan fragments in human synovial fluid. Evidence that aggrecanase mediates cartilage degradation in inflammatory joint disease, joint injury, and osteoarthritis."
Lohmander L.S., Neame P.J., Sandy J.D.
Arthritis Rheum. 36:1214-1222(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 393-409.
Tissue: Synovial fluid.
[6]"Length variation in the keratan sulfate domain of mammalian aggrecan."
Barry F.P., Neame P.J., Sasse J., Pearson D.
Matrix Biol. 14:323-328(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 764-864.
Tissue: Blood.
[7]"Age-related changes in the content of the C-terminal region of aggrecan in human articular cartilage."
Dudhia J., Davidson C.M., Wells T.M., Vynios D.H., Hardingham T.E., Bayliss M.T.
Biochem. J. 313:933-940(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1778-2415 (ISOFORM 2).
Tissue: Chondrocyte.
[8]"A new epidermal growth factor-like domain in the human core protein for the large cartilage-specific proteoglycan. Evidence for alternative splicing of the domain."
Baldwin C.T., Reginato A.M., Prockop D.J.
J. Biol. Chem. 264:15747-15750(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1936-2415 (ISOFORM 1).
[9]"A mutation in the variable repeat region of the aggrecan gene (AGC1) causes a form of spondyloepiphyseal dysplasia associated with severe, premature osteoarthritis."
Gleghorn L., Ramesar R., Beighton P., Wallis G.
Am. J. Hum. Genet. 77:484-490(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SEDK.
[10]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-657.
Tissue: Plasma.
[11]"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 COMP.
[12]"A recessive skeletal dysplasia, SEMD aggrecan type, results from a missense mutation affecting the C-type lectin domain of aggrecan."
Tompson S.W., Merriman B., Funari V.A., Fresquet M., Lachman R.S., Rimoin D.L., Nelson S.F., Briggs M.D., Cohn D.H., Krakow D.
Am. J. Hum. Genet. 84:72-79(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SEMD-ACAN ASN-2266, CHARACTERIZATION OF VARIANT SEMD-ACAN ASN-2266.
[13]"A missense mutation in the aggrecan C-type lectin domain disrupts extracellular matrix interactions and causes dominant familial osteochondritis dissecans."
Stattin E.L., Wiklund F., Lindblom K., Onnerfjord P., Jonsson B.A., Tegner Y., Sasaki T., Struglics A., Lohmander S., Dahl N., Heinegard D., Aspberg A.
Am. J. Hum. Genet. 86:126-137(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OD MET-2303, DETECTION OF VARIANT OD MET-2303 BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55172 mRNA. Translation: AAA62824.1.
X80278 mRNA. No translation available.
S74659 Genomic DNA. Translation: AAC60643.2.
X17406 mRNA. Translation: CAA35463.1.
J05062 mRNA. Translation: AAA35726.1.
PIRA39086.
UniGeneHs.2159.
Hs.616395.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4MD4X-ray1.95C89-103[»]
ProteinModelPortalP16112.
SMRP16112. Positions 36-150, 154-247, 263-349, 479-572, 588-673, 2161-2200, 2203-2328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP16112. 1 interaction.
STRING9606.ENSP00000268134.

PTM databases

PhosphoSiteP16112.

Polymorphism databases

DMDM129886.

Proteomic databases

PaxDbP16112.
PRIDEP16112.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GeneCardsGC15P089346.
H-InvDBHIX0026812.
HGNCHGNC:319. ACAN.
HPACAB016377.
MIM155760. gene.
165800. phenotype.
608361. phenotype.
612813. phenotype.
neXtProtNX_P16112.
Orphanet251262. Familial osteochondritis dissecans.
171866. Spondyloepimetaphyseal dysplasia, aggrecan type.
93283. Spondyloepiphyseal dysplasia, Kimberley type.
PharmGKBPA24616.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000168421.
HOVERGENHBG007982.
InParanoidP16112.
PhylomeDBP16112.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.

Gene expression databases

CleanExHS_ACAN.
GenevestigatorP16112.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.10.100.10. 5 hits.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR000538. Link.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 1 hit.
PF07686. V-set. 1 hit.
PF00193. Xlink. 4 hits.
[Graphical view]
PRINTSPR01265. LINKMODULE.
SMARTSM00032. CCP. 1 hit.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
SM00409. IG. 1 hit.
SM00445. LINK. 4 hits.
[Graphical view]
SUPFAMSSF56436. SSF56436. 5 hits.
SSF57535. SSF57535. 1 hit.
PROSITEPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS50835. IG_LIKE. 1 hit.
PS00290. IG_MHC. 1 hit.
PS01241. LINK_1. 3 hits.
PS50963. LINK_2. 4 hits.
PS50923. SUSHI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACAN. human.
PMAP-CutDBP16112.
PROP16112.
SOURCESearch...

Entry information

Entry namePGCA_HUMAN
AccessionPrimary (citable) accession number: P16112
Secondary accession number(s): Q13650 expand/collapse secondary AC list , Q9UCD3, Q9UCP4, Q9UCP5, Q9UDE0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: August 1, 1992
Last modified: June 11, 2014
This is version 165 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 15

Human chromosome 15: entries, gene names and cross-references to MIM